ion trap mass spectrometer Search Results


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  • 99
    Thermo Fisher lcq ion trap mass spectrometer
    Mass spectral analysis of Fhit. ( A-C ) MALDI-TOF spectra of unphosphorylated, monophosphorylated, and diphosphorylated forms of Fhit, respectively, were acquired on an Applied Biosystems Voyager Elite as described in Materials and Methods . The m/z values shown in bold represent the average of three spectra obtained from the same sample spot on the MALDI target. The lower intensity peaks in each panel represent matrix adducts. ( D and E ) <t>ESI</t> tandem mass spectra were acquired on a Thermo Finnigan <t>LCQ</t> Classic spectrometer as described in Materials and Methods . ( D ) Tandem mass spectrum of the 2+ ion ( m/z 619.8) of tryptic peptide 109-118 from unphosphorylated Fhit. ( E ) Tandem mass spectrum from the 2+ ion ( m/z ). Identification of the site of phosphorylation was obtained by comparison of the y -series ions in the two spectra.
    Lcq Ion Trap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 776 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lcq ion trap mass spectrometer/product/Thermo Fisher
    Average 99 stars, based on 776 article reviews
    Price from $9.99 to $1999.99
    lcq ion trap mass spectrometer - by Bioz Stars, 2020-04
    99/100 stars
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    99
    Thermo Fisher ion trap mass spectrometer
    Mass spectral analysis of Fhit. ( A-C ) MALDI-TOF spectra of unphosphorylated, monophosphorylated, and diphosphorylated forms of Fhit, respectively, were acquired on an Applied Biosystems Voyager Elite as described in Materials and Methods . The m/z values shown in bold represent the average of three spectra obtained from the same sample spot on the MALDI target. The lower intensity peaks in each panel represent matrix adducts. ( D and E ) <t>ESI</t> tandem mass spectra were acquired on a Thermo Finnigan <t>LCQ</t> Classic spectrometer as described in Materials and Methods . ( D ) Tandem mass spectrum of the 2+ ion ( m/z 619.8) of tryptic peptide 109-118 from unphosphorylated Fhit. ( E ) Tandem mass spectrum from the 2+ ion ( m/z ). Identification of the site of phosphorylation was obtained by comparison of the y -series ions in the two spectra.
    Ion Trap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1868 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ion trap mass spectrometer/product/Thermo Fisher
    Average 99 stars, based on 1868 article reviews
    Price from $9.99 to $1999.99
    ion trap mass spectrometer - by Bioz Stars, 2020-04
    99/100 stars
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    96
    Agilent technologies ion trap mass spectrometer
    Mass spectral analysis of Fhit. ( A-C ) MALDI-TOF spectra of unphosphorylated, monophosphorylated, and diphosphorylated forms of Fhit, respectively, were acquired on an Applied Biosystems Voyager Elite as described in Materials and Methods . The m/z values shown in bold represent the average of three spectra obtained from the same sample spot on the MALDI target. The lower intensity peaks in each panel represent matrix adducts. ( D and E ) <t>ESI</t> tandem mass spectra were acquired on a Thermo Finnigan <t>LCQ</t> Classic spectrometer as described in Materials and Methods . ( D ) Tandem mass spectrum of the 2+ ion ( m/z 619.8) of tryptic peptide 109-118 from unphosphorylated Fhit. ( E ) Tandem mass spectrum from the 2+ ion ( m/z ). Identification of the site of phosphorylation was obtained by comparison of the y -series ions in the two spectra.
    Ion Trap Mass Spectrometer, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 96/100, based on 391 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ion trap mass spectrometer/product/Agilent technologies
    Average 96 stars, based on 391 article reviews
    Price from $9.99 to $1999.99
    ion trap mass spectrometer - by Bioz Stars, 2020-04
    96/100 stars
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    97
    Bruker Corporation ion trap mass spectrometer
    Mass spectral analysis of Fhit. ( A-C ) MALDI-TOF spectra of unphosphorylated, monophosphorylated, and diphosphorylated forms of Fhit, respectively, were acquired on an Applied Biosystems Voyager Elite as described in Materials and Methods . The m/z values shown in bold represent the average of three spectra obtained from the same sample spot on the MALDI target. The lower intensity peaks in each panel represent matrix adducts. ( D and E ) <t>ESI</t> tandem mass spectra were acquired on a Thermo Finnigan <t>LCQ</t> Classic spectrometer as described in Materials and Methods . ( D ) Tandem mass spectrum of the 2+ ion ( m/z 619.8) of tryptic peptide 109-118 from unphosphorylated Fhit. ( E ) Tandem mass spectrum from the 2+ ion ( m/z ). Identification of the site of phosphorylation was obtained by comparison of the y -series ions in the two spectra.
    Ion Trap Mass Spectrometer, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 97/100, based on 553 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ion trap mass spectrometer/product/Bruker Corporation
    Average 97 stars, based on 553 article reviews
    Price from $9.99 to $1999.99
    ion trap mass spectrometer - by Bioz Stars, 2020-04
    97/100 stars
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    90
    Varian Medical ion trap mass spectrometer
    Mass spectral analysis of Fhit. ( A-C ) MALDI-TOF spectra of unphosphorylated, monophosphorylated, and diphosphorylated forms of Fhit, respectively, were acquired on an Applied Biosystems Voyager Elite as described in Materials and Methods . The m/z values shown in bold represent the average of three spectra obtained from the same sample spot on the MALDI target. The lower intensity peaks in each panel represent matrix adducts. ( D and E ) <t>ESI</t> tandem mass spectra were acquired on a Thermo Finnigan <t>LCQ</t> Classic spectrometer as described in Materials and Methods . ( D ) Tandem mass spectrum of the 2+ ion ( m/z 619.8) of tryptic peptide 109-118 from unphosphorylated Fhit. ( E ) Tandem mass spectrum from the 2+ ion ( m/z ). Identification of the site of phosphorylation was obtained by comparison of the y -series ions in the two spectra.
    Ion Trap Mass Spectrometer, supplied by Varian Medical, used in various techniques. Bioz Stars score: 90/100, based on 39 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ion trap mass spectrometer/product/Varian Medical
    Average 90 stars, based on 39 article reviews
    Price from $9.99 to $1999.99
    ion trap mass spectrometer - by Bioz Stars, 2020-04
    90/100 stars
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    99
    Thermo Fisher ltq ion trap mass spectrometer
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    Ltq Ion Trap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 3047 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ltq ion trap mass spectrometer/product/Thermo Fisher
    Average 99 stars, based on 3047 article reviews
    Price from $9.99 to $1999.99
    ltq ion trap mass spectrometer - by Bioz Stars, 2020-04
    99/100 stars
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    96
    Thermo Fisher ion trap
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    Ion Trap, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 96/100, based on 388 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ion trap/product/Thermo Fisher
    Average 96 stars, based on 388 article reviews
    Price from $9.99 to $1999.99
    ion trap - by Bioz Stars, 2020-04
    96/100 stars
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    94
    Amazon ion trap mass spectrometer
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    Ion Trap Mass Spectrometer, supplied by Amazon, used in various techniques. Bioz Stars score: 94/100, based on 189 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ion trap mass spectrometer/product/Amazon
    Average 94 stars, based on 189 article reviews
    Price from $9.99 to $1999.99
    ion trap mass spectrometer - by Bioz Stars, 2020-04
    94/100 stars
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    92
    Waters Corporation ion trap mass spectrometer
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    Ion Trap Mass Spectrometer, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 92/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ion trap mass spectrometer/product/Waters Corporation
    Average 92 stars, based on 19 article reviews
    Price from $9.99 to $1999.99
    ion trap mass spectrometer - by Bioz Stars, 2020-04
    92/100 stars
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    85
    GE Healthcare ion trap mass spectrometers
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    Ion Trap Mass Spectrometers, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 85/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ion trap mass spectrometers/product/GE Healthcare
    Average 85 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    ion trap mass spectrometers - by Bioz Stars, 2020-04
    85/100 stars
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    92
    Shimadzu Corporation ion trap mass spectrometers
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    Ion Trap Mass Spectrometers, supplied by Shimadzu Corporation, used in various techniques. Bioz Stars score: 92/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ion trap mass spectrometers/product/Shimadzu Corporation
    Average 92 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    ion trap mass spectrometers - by Bioz Stars, 2020-04
    92/100 stars
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    94
    Bruker Corporation hct ion trap mass spectrometer
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    Hct Ion Trap Mass Spectrometer, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 94/100, based on 72 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hct ion trap mass spectrometer/product/Bruker Corporation
    Average 94 stars, based on 72 article reviews
    Price from $9.99 to $1999.99
    hct ion trap mass spectrometer - by Bioz Stars, 2020-04
    94/100 stars
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    92
    Shimadzu Corporation ion trap tof mass spectrometer
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    Ion Trap Tof Mass Spectrometer, supplied by Shimadzu Corporation, used in various techniques. Bioz Stars score: 92/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ion trap tof mass spectrometer/product/Shimadzu Corporation
    Average 92 stars, based on 17 article reviews
    Price from $9.99 to $1999.99
    ion trap tof mass spectrometer - by Bioz Stars, 2020-04
    92/100 stars
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    86
    Bruker Corporation 3000plus ion trap mass spectrometer
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    3000plus Ion Trap Mass Spectrometer, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 86/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/3000plus ion trap mass spectrometer/product/Bruker Corporation
    Average 86 stars, based on 15 article reviews
    Price from $9.99 to $1999.99
    3000plus ion trap mass spectrometer - by Bioz Stars, 2020-04
    86/100 stars
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    95
    Agilent technologies 1100 ion trap mass spectrometer
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    1100 Ion Trap Mass Spectrometer, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 95/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/1100 ion trap mass spectrometer/product/Agilent technologies
    Average 95 stars, based on 21 article reviews
    Price from $9.99 to $1999.99
    1100 ion trap mass spectrometer - by Bioz Stars, 2020-04
    95/100 stars
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    90
    Thermo Fisher polarisq ion trap mass spectrometer
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    Polarisq Ion Trap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 61 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 90 stars, based on 61 article reviews
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    polarisq ion trap mass spectrometer - by Bioz Stars, 2020-04
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    93
    Agilent technologies 6330 ion trap mass spectrometer
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    6330 Ion Trap Mass Spectrometer, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 93/100, based on 72 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    6330 ion trap mass spectrometer - by Bioz Stars, 2020-04
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    93
    Bruker Corporation sl ion trap mass spectrometer
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    Sl Ion Trap Mass Spectrometer, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 93/100, based on 79 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sl ion trap mass spectrometer/product/Bruker Corporation
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    sl ion trap mass spectrometer - by Bioz Stars, 2020-04
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    94
    SCIEX ion trap quadrupole mass spectrometer
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    Ion Trap Quadrupole Mass Spectrometer, supplied by SCIEX, used in various techniques. Bioz Stars score: 94/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ion trap quadrupole mass spectrometer - by Bioz Stars, 2020-04
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    94
    SCIEX quadrupole ion trap mass spectrometer
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    Quadrupole Ion Trap Mass Spectrometer, supplied by SCIEX, used in various techniques. Bioz Stars score: 94/100, based on 31 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    quadrupole ion trap mass spectrometer - by Bioz Stars, 2020-04
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    85
    Shimadzu Corporation linear ion trap mass spectrometer
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    Linear Ion Trap Mass Spectrometer, supplied by Shimadzu Corporation, used in various techniques. Bioz Stars score: 85/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/linear ion trap mass spectrometer/product/Shimadzu Corporation
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    linear ion trap mass spectrometer - by Bioz Stars, 2020-04
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    95
    Bruker Corporation edt ion trap mass spectrometer
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    Edt Ion Trap Mass Spectrometer, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 95/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/edt ion trap mass spectrometer/product/Bruker Corporation
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    91
    Bruker Corporation esquire3000plus ion trap mass spectrometer
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    Esquire3000plus Ion Trap Mass Spectrometer, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 91/100, based on 46 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/esquire3000plus ion trap mass spectrometer/product/Bruker Corporation
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    93
    Bruker Corporation etd ion trap mass spectrometer
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    Etd Ion Trap Mass Spectrometer, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 93/100, based on 84 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/etd ion trap mass spectrometer/product/Bruker Corporation
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    etd ion trap mass spectrometer - by Bioz Stars, 2020-04
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    93
    Bruker Corporation hctultra ion trap mass spectrometer
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    Hctultra Ion Trap Mass Spectrometer, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 93/100, based on 92 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hctultra ion trap mass spectrometer/product/Bruker Corporation
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    hctultra ion trap mass spectrometer - by Bioz Stars, 2020-04
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    94
    Agilent technologies ion trap xct mass spectrometer
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    Ion Trap Xct Mass Spectrometer, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 94/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ion trap xct mass spectrometer - by Bioz Stars, 2020-04
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    94
    Agilent technologies 6310 ion trap mass spectrometer
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    6310 Ion Trap Mass Spectrometer, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 94/100, based on 60 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    6310 ion trap mass spectrometer - by Bioz Stars, 2020-04
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    86
    Agilent technologies sl ion trap mass spectrometer
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    Sl Ion Trap Mass Spectrometer, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 86/100, based on 45 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    sl ion trap mass spectrometer - by Bioz Stars, 2020-04
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    86
    Thermo Fisher finnigan ion trap mass spectrometer
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    Finnigan Ion Trap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Bruker Corporation quadruple ion trap mass spectrometer
    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method <t>(SIMAC,</t> TiO 2 and IMAC) coupled to R3/C18 and <t>MSA-LTQ</t> ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.
    Quadruple Ion Trap Mass Spectrometer, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Thermo Fisher electrospray ion trap mass spectrometer
    <t>HPLC-electrospray</t> ionization MS analysis of inactivated clindamycin. (A) HPLC chromatogram showing a major peak eluting at 10.8 min. (B) Full MS analysis of the 10.8-min-eluted fraction reveals the dominance of a 754.1-amu compound and its Na adduct (+22
    Electrospray Ion Trap Mass Spectrometer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 137 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Mass spectral analysis of Fhit. ( A-C ) MALDI-TOF spectra of unphosphorylated, monophosphorylated, and diphosphorylated forms of Fhit, respectively, were acquired on an Applied Biosystems Voyager Elite as described in Materials and Methods . The m/z values shown in bold represent the average of three spectra obtained from the same sample spot on the MALDI target. The lower intensity peaks in each panel represent matrix adducts. ( D and E ) ESI tandem mass spectra were acquired on a Thermo Finnigan LCQ Classic spectrometer as described in Materials and Methods . ( D ) Tandem mass spectrum of the 2+ ion ( m/z 619.8) of tryptic peptide 109-118 from unphosphorylated Fhit. ( E ) Tandem mass spectrum from the 2+ ion ( m/z ). Identification of the site of phosphorylation was obtained by comparison of the y -series ions in the two spectra.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Fhit is a physiological target of the protein kinase Src

    doi: 10.1073/pnas.0400481101

    Figure Lengend Snippet: Mass spectral analysis of Fhit. ( A-C ) MALDI-TOF spectra of unphosphorylated, monophosphorylated, and diphosphorylated forms of Fhit, respectively, were acquired on an Applied Biosystems Voyager Elite as described in Materials and Methods . The m/z values shown in bold represent the average of three spectra obtained from the same sample spot on the MALDI target. The lower intensity peaks in each panel represent matrix adducts. ( D and E ) ESI tandem mass spectra were acquired on a Thermo Finnigan LCQ Classic spectrometer as described in Materials and Methods . ( D ) Tandem mass spectrum of the 2+ ion ( m/z 619.8) of tryptic peptide 109-118 from unphosphorylated Fhit. ( E ) Tandem mass spectrum from the 2+ ion ( m/z ). Identification of the site of phosphorylation was obtained by comparison of the y -series ions in the two spectra.

    Article Snippet: HPLC-electrospray ionization (ESI) tandem mass spectra were acquired on a Thermo Finnigan LCQ Classic ion trap mass spectrometer connected via a home-built microspray interface to a Michrom BioResources MAGIC 2002 micro HPLC.

    Techniques:

    Plots of target PSM hits for the seven datasets validated under a series of FDRs for De-Noise, PeptideProphet, and Percolator. The number of target peptide hits is plotted for a FDR range from 0.01 to 0.1. (A) Gcn4 LCQ (B) UPS1 LTQ (C) Tal08 LTQ-Orbitrap XL MiPS (D) PBMC LTQ-Orbitrap XL MiPS (E) PBMC LTQ-Orbitrap XL MiPS-off (F) PBMC LTQ-Orbitrap Velos MiPS (G) PBMC LTQ-Orbitrap Velos MiPS-off.

    Journal: Journal of proteome research

    Article Title: A Novel Algorithm for Validating Peptide Identification from a Shotgun Proteomics Search Engine

    doi: 10.1021/pr300631t

    Figure Lengend Snippet: Plots of target PSM hits for the seven datasets validated under a series of FDRs for De-Noise, PeptideProphet, and Percolator. The number of target peptide hits is plotted for a FDR range from 0.01 to 0.1. (A) Gcn4 LCQ (B) UPS1 LTQ (C) Tal08 LTQ-Orbitrap XL MiPS (D) PBMC LTQ-Orbitrap XL MiPS (E) PBMC LTQ-Orbitrap XL MiPS-off (F) PBMC LTQ-Orbitrap Velos MiPS (G) PBMC LTQ-Orbitrap Velos MiPS-off.

    Article Snippet: Affinity preparation of the S. cerevisiae Gcn4 complex and its MudPIT analysis using an LCQ quadrupole ion trap mass spectrometer (Thermofisher) have been previously described .

    Techniques:

    ROC curves for the seven datasets showing the validation performance of De-Noise, PeptideProphet, and Percolator. (A) Gcn4 LCQ (B) UPS1 LTQ (C) Tal08 LTQ-Orbitrap XL MiPS-off (D) PBMC LTQ Orbitrap XL MiPS (E) PBMC LTQ-Orbitrap XL MiPS-off (F) PBMC LTQ-Orbitrap Velos MiPS (G) PBMC LTQ-Orbitrap Velos MiPS-off.

    Journal: Journal of proteome research

    Article Title: A Novel Algorithm for Validating Peptide Identification from a Shotgun Proteomics Search Engine

    doi: 10.1021/pr300631t

    Figure Lengend Snippet: ROC curves for the seven datasets showing the validation performance of De-Noise, PeptideProphet, and Percolator. (A) Gcn4 LCQ (B) UPS1 LTQ (C) Tal08 LTQ-Orbitrap XL MiPS-off (D) PBMC LTQ Orbitrap XL MiPS (E) PBMC LTQ-Orbitrap XL MiPS-off (F) PBMC LTQ-Orbitrap Velos MiPS (G) PBMC LTQ-Orbitrap Velos MiPS-off.

    Article Snippet: Affinity preparation of the S. cerevisiae Gcn4 complex and its MudPIT analysis using an LCQ quadrupole ion trap mass spectrometer (Thermofisher) have been previously described .

    Techniques:

    Predicted bombinin HL sequence from selected rp-HPLC fraction using LCQ-Fleet. Thermoquest LCQ™ fragment scan spectrum derived from ions corresponding to bombinin HL ( a ) and electrospray ion-trap MS/MS fragmentation dataset ( b ) Expected single- and double-charged b- and y-ions arising from MS/MS fragmentation were predicted using the MS Product program through Protein Prospector online. Truly observed ions are indicated in bold typeface and underlined.

    Journal: Bioscience Reports

    Article Title: The synergistic antimicrobial effects of novel bombinin and bombinin H peptides from the skin secretion of Bombinaorientalis

    doi: 10.1042/BSR20170967

    Figure Lengend Snippet: Predicted bombinin HL sequence from selected rp-HPLC fraction using LCQ-Fleet. Thermoquest LCQ™ fragment scan spectrum derived from ions corresponding to bombinin HL ( a ) and electrospray ion-trap MS/MS fragmentation dataset ( b ) Expected single- and double-charged b- and y-ions arising from MS/MS fragmentation were predicted using the MS Product program through Protein Prospector online. Truly observed ions are indicated in bold typeface and underlined.

    Article Snippet: Fractions containing peptides with molecular masses coincident with predicted mature peptides from ‘shotgun’ cloning were infused into the LCQ Fleet™ ion-trap electrospray mass spectrometer for analysis (Thermo Quest, San Jose, CA, U.S.A.).

    Techniques: Sequencing, High Performance Liquid Chromatography, Derivative Assay, Mass Spectrometry

    Predicted BHL-bombinin sequence from selected rp-HPLC fraction using LCQ-Fleet. Thermoquest LCQ™ fragment scan spectrum derived from ions corresponding to BHL-bombinin ( a ) and electrospray ion-trap MS/MS fragmentation dataset ( b ). Expected single- and double-charged b- and y-ions arising from MS/MS fragmentation were predicted using the MS Product program through Protein Prospector online. Truly observed ions are indicated in bold typeface and underlined.

    Journal: Bioscience Reports

    Article Title: The synergistic antimicrobial effects of novel bombinin and bombinin H peptides from the skin secretion of Bombinaorientalis

    doi: 10.1042/BSR20170967

    Figure Lengend Snippet: Predicted BHL-bombinin sequence from selected rp-HPLC fraction using LCQ-Fleet. Thermoquest LCQ™ fragment scan spectrum derived from ions corresponding to BHL-bombinin ( a ) and electrospray ion-trap MS/MS fragmentation dataset ( b ). Expected single- and double-charged b- and y-ions arising from MS/MS fragmentation were predicted using the MS Product program through Protein Prospector online. Truly observed ions are indicated in bold typeface and underlined.

    Article Snippet: Fractions containing peptides with molecular masses coincident with predicted mature peptides from ‘shotgun’ cloning were infused into the LCQ Fleet™ ion-trap electrospray mass spectrometer for analysis (Thermo Quest, San Jose, CA, U.S.A.).

    Techniques: Sequencing, High Performance Liquid Chromatography, Derivative Assay, Mass Spectrometry

    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method (SIMAC, TiO 2 and IMAC) coupled to R3/C18 and MSA-LTQ ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.

    Journal: Journal of Clinical Bioinformatics

    Article Title: Discovering and validating unknown phospho-sites from p38 and HuR protein kinases in vitro by Phosphoproteomic and Bioinformatic tools

    doi: 10.1186/2043-9113-1-16

    Figure Lengend Snippet: The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method (SIMAC, TiO 2 and IMAC) coupled to R3/C18 and MSA-LTQ ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.

    Article Snippet: In fact, multistage activation resulted in more information for the suite of phosphopeptides studied (Table ) (see an example of the spectrum of an identified phosphorylated peptide when using SIMAC coupled to MSA in the LTQ ion Trap mass spectrometer and Mascot, Figure ).

    Techniques: Purification, Mass Spectrometry, Isolation, RNA Binding Assay, Activation Assay

    MS spectra of permethylated N -linked glycans in the serum of patients with CCA compared with healthy controls, as detected using NSI-MS. Glycans released from the serum of patients with CCA and healthy controls were permethylated and analyzed. MS spectra present the predominance of the complex type and high-mannose type oligosaccharides in (A) healthy sera vs. (B) CCA sera. The glycan profiles (A vs. B) demonstrate similar glycan patterns, but they differ in their relative quantities. Glycans were detected as doubly [2+] and triply charged species [3+]. The graphical representation of monosaccharide residues are defined in the figure and are consistent with the suggested nomenclature of the Consortium for Functional Glycomics ( http://glycomics.scripps.edu/CFGnomenclature.pdf ). MS, mass spectrometry; CCA, cholangiocarcinoma; NSI-MS, nanospray ionization-linear ion trap mass spectrometry; m / z , mass/charge ratio; Glc, N-acetylglucosamine.

    Journal: Oncology Letters

    Article Title: Increased expression of the high-mannose M6N2 and NeuAc3H3N3M3N2F tri-antennary N-glycans in cholangiocarcinoma

    doi: 10.3892/ol.2017.7384

    Figure Lengend Snippet: MS spectra of permethylated N -linked glycans in the serum of patients with CCA compared with healthy controls, as detected using NSI-MS. Glycans released from the serum of patients with CCA and healthy controls were permethylated and analyzed. MS spectra present the predominance of the complex type and high-mannose type oligosaccharides in (A) healthy sera vs. (B) CCA sera. The glycan profiles (A vs. B) demonstrate similar glycan patterns, but they differ in their relative quantities. Glycans were detected as doubly [2+] and triply charged species [3+]. The graphical representation of monosaccharide residues are defined in the figure and are consistent with the suggested nomenclature of the Consortium for Functional Glycomics ( http://glycomics.scripps.edu/CFGnomenclature.pdf ). MS, mass spectrometry; CCA, cholangiocarcinoma; NSI-MS, nanospray ionization-linear ion trap mass spectrometry; m / z , mass/charge ratio; Glc, N-acetylglucosamine.

    Article Snippet: Briefly, permethylated glycans were dissolved in 1 mM NaOH in 50% methanol and infused directly into a linear ion trap mass spectrometer (LTQ Orbitrap Discovery; Thermo Fisher Scientific, Inc., Waltham, MA, USA) using a Thermo Fisher Scientific™ nanospray ion source (Thermo Fisher Scientific, Inc.).

    Techniques: Mass Spectrometry, Functional Assay, Gas Chromatography

    Quantification of calcium-dependent regulation of phosphorylation sites of Toxoplasma invasion motor complex components. A ) Work flow to identify individual phosphorylation sites and quantitatively assess their responsiveness to calcium signals using a SILAC-based proteomics approach. A 1∶1 mixture of Triton X-100 lysates from “Heavy” (H; Arg4/Lys8)-labeled ethanol-stimulated tachyzoites or

    Journal: PLoS Pathogens

    Article Title: Quantitative in vivo Analyses Reveal Calcium-dependent Phosphorylation Sites and Identifies a Novel Component of the Toxoplasma Invasion Motor Complex

    doi: 10.1371/journal.ppat.1002222

    Figure Lengend Snippet: Quantification of calcium-dependent regulation of phosphorylation sites of Toxoplasma invasion motor complex components. A ) Work flow to identify individual phosphorylation sites and quantitatively assess their responsiveness to calcium signals using a SILAC-based proteomics approach. A 1∶1 mixture of Triton X-100 lysates from “Heavy” (H; Arg4/Lys8)-labeled ethanol-stimulated tachyzoites or "Light" (L; Arg0/Lys0)-labeled non-stimulated parasites was generated, and a TiO 2 -enriched phosphopeptide sample of H/L-labeled Toxoplasma invasion motor complexes was prepared and analysed by LC-MS/MS on an LTQ-Orbitrap instrument. Mascot and MaxQuant search engines facilitated subsequent manual identification, phosphosite localization and quantification of proteins or peptides as detailed in materials and mathods. B ) Sypro Ruby-stained SDS-PAGE separation of the relative amounts of light (lane 1) or heavy (lane 2) Triton X-100 whole protein extracts are shown. Intact tachyzoite invasion motor complexes comprising the five major components MyoA, GAP50, GAP45 and MLC1 were precipitated from a 1∶1 H/L mixture by GAP45-specific immuno-affinity chromatography (lane 3).

    Article Snippet: Individual TiO2 -bound phosphopeptide fractions were analyzed by multi-dimensional LC-MS/MS on an LTQ linear ion trap mass spectrometer (Thermo Scientific), according to published protocols .

    Techniques: Flow Cytometry, Labeling, Generated, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, Staining, SDS Page, Affinity Chromatography

    Workflow of label free quantitative shotgun proteomic analysis. Proteins extracted from rice leaves were separated by SDS-PAGE. After trypsin digestion, the resulting peptides were analysed by nanoLC-MS/MS on an LTQ-XL linear ion trap mass spectrometer. The raw files acquired from the mass spectrometer were converted into mzXML files and searched against the rice database using the GPM software. The outputs from the GPM search were further processed using the Scrappy software package to calculate normalized spectral abundance factors. The Gene ontology (GO) annotation of differentially expressed proteins was extracted from the UniProt database and matched to the list of reproducibly identified proteins using PloGo.

    Journal: Data in Brief

    Article Title: Label-free and isobaric tandem mass tag (TMT) multiplexed quantitative proteomic data of two contrasting rice cultivars exposed to drought stress and recovery

    doi: 10.1016/j.dib.2018.12.041

    Figure Lengend Snippet: Workflow of label free quantitative shotgun proteomic analysis. Proteins extracted from rice leaves were separated by SDS-PAGE. After trypsin digestion, the resulting peptides were analysed by nanoLC-MS/MS on an LTQ-XL linear ion trap mass spectrometer. The raw files acquired from the mass spectrometer were converted into mzXML files and searched against the rice database using the GPM software. The outputs from the GPM search were further processed using the Scrappy software package to calculate normalized spectral abundance factors. The Gene ontology (GO) annotation of differentially expressed proteins was extracted from the UniProt database and matched to the list of reproducibly identified proteins using PloGo.

    Article Snippet: The resulting peptides were analysed by nanoflow LC-MS/MS (nanoLC-MS/MS) using a LTQ-XL ion-trap mass spectrometer (Thermo, CA, USA).

    Techniques: SDS Page, Mass Spectrometry, Software

    Negative ion nanoelectrospray spectra of the V. fischeri lipid A mixture. A , sample run on an LTQ XL linear ion trap mass spectrometer with spray conditions producing multiply charged ions. This spectrum highlights the diphosphorylated lipid A species. B , sample run on an LCQ Deca quadrupole ion trap instrument, where singly charged, monophosphorylated lipid A species predominate. The ion clusters tentatively labeled as “ hexaacyl ” and “ heptaacyl ” were ultimately found to contain primarily pentaacyl and hexaacyl species, respectively (see “Results”).

    Journal: The Journal of Biological Chemistry

    Article Title: The Lipid A from Vibrio fischeri Lipopolysaccharide

    doi: 10.1074/jbc.M111.239475

    Figure Lengend Snippet: Negative ion nanoelectrospray spectra of the V. fischeri lipid A mixture. A , sample run on an LTQ XL linear ion trap mass spectrometer with spray conditions producing multiply charged ions. This spectrum highlights the diphosphorylated lipid A species. B , sample run on an LCQ Deca quadrupole ion trap instrument, where singly charged, monophosphorylated lipid A species predominate. The ion clusters tentatively labeled as “ hexaacyl ” and “ heptaacyl ” were ultimately found to contain primarily pentaacyl and hexaacyl species, respectively (see “Results”).

    Article Snippet: The V. fischeri lipid A sample, dissolved in CHCl3 /CH3 OH (1:2, v/v) at a concentration of ∼0.1–0.5 μg/μl, was analyzed by static or dynamic nanoelectrospray using either a LCQDeca quadrupole ion trap or an LTQ XL linear ion trap mass spectrometer (both instruments from Thermo Scientific, San Jose, CA).

    Techniques: Mass Spectrometry, Labeling

    The ETD MS 2 spectrum of the K14acK23acK27me3 species from f analyzed in a parallel experiment on an LTQ-Orbitrap equipped with ETD fragmentation. The inset accurate mass error analysis of the z25 ion (−1.4 ppm for me3 versus 11.8 ppm for

    Journal:

    Article Title: High Throughput Characterization of Combinatorial Histone Codes *

    doi: 10.1074/mcp.M900238-MCP200

    Figure Lengend Snippet: The ETD MS 2 spectrum of the K14acK23acK27me3 species from f analyzed in a parallel experiment on an LTQ-Orbitrap equipped with ETD fragmentation. The inset accurate mass error analysis of the z25 ion (−1.4 ppm for me3 versus 11.8 ppm for

    Article Snippet: Several other buffer systems for the B mobile phase were tried during method development as noted under “Results.” The column eluent was introduced into an LTQ-ETD ion trap mass spectrometer (Thermo Scientific, Waltham, MA) or an LTQ-Orbitrap XL (Thermo Scientific) (data in only) by nanoelectrospray ionization.

    Techniques: Mass Spectrometry

    Comparison of samples making up each dataset. For each, on the left ( a , c , e , g ) is the principal component analysis, plotting PC1 (93–98% of variance, as indicated) against PC2 (1–5% of variance); on the right ( b , d , f , h ) are box plots showing relative molar abundance (im) values for all proteins in the indicated samples. ( a , b ) Chick LTQ. ( c , d ) Chick Velos. ( e , f ) Rat LTQ. ( g , h ) Mouse Velos.

    Journal: Scientific Data

    Article Title: Hair-bundle proteomes of avian and mammalian inner-ear utricles

    doi: 10.1038/sdata.2015.74

    Figure Lengend Snippet: Comparison of samples making up each dataset. For each, on the left ( a , c , e , g ) is the principal component analysis, plotting PC1 (93–98% of variance, as indicated) against PC2 (1–5% of variance); on the right ( b , d , f , h ) are box plots showing relative molar abundance (im) values for all proteins in the indicated samples. ( a , b ) Chick LTQ. ( c , d ) Chick Velos. ( e , f ) Rat LTQ. ( g , h ) Mouse Velos.

    Article Snippet: Peptides were separated with a Waters nanoAcquity LC system, and then delivered to an LTQ Velos linear ion trap mass spectrometer (Thermo Scientific) using electrospray ionization with a Microm Captivespray source fitted with a 20 μm taper spray tip and 1.0 kV source voltage.

    Techniques:

    ESI-MS/MS spectra of acetylated peptides of H3.3 protein obtained from MCF7 cells treated with TSA (A) Peptide sequence of H3.3 showing acetylated lysine residues in red with 100% amino acid sequence coverage obtained from MS/MS. (B) MS/MS spectrum of acetylated peptide QTARK(Ac)STGGK(Ac)APRK. (C) MS/MS spectrum of the acetylated peptide STGGK(Ac)APRK(Ac)QLATK. (D) MS/MS spectrum of the acetylated peptide QLATK(Ac)AARK(Ac)SAPSTGGVK. (E) MS/MS spectrum of the peptide TDLRFQSAAIGALQEASE showing amino acids marked in red color unique to H3.3. Spectral images were obtained using Tandem data base where y-type immonium ions represented by red peaks. All the MS/MS data were acquired using Thermo Scientific Velos Pro ion trap mass spectrometer. Acetylation at K residues were highlighted in yellow. Amino acids which characterized H3.3 in the sequence are shown in red. Results are representative of three independent experiments.

    Journal: Biochimica et biophysica acta. Gene regulatory mechanisms

    Article Title: Interaction of Positive Coactivator 4 with Histone 3.3 Protein is Essential for Transcriptional Activation of the Luteinizing Hormone Receptor Gene

    doi: 10.1016/j.bbagrm.2018.09.002

    Figure Lengend Snippet: ESI-MS/MS spectra of acetylated peptides of H3.3 protein obtained from MCF7 cells treated with TSA (A) Peptide sequence of H3.3 showing acetylated lysine residues in red with 100% amino acid sequence coverage obtained from MS/MS. (B) MS/MS spectrum of acetylated peptide QTARK(Ac)STGGK(Ac)APRK. (C) MS/MS spectrum of the acetylated peptide STGGK(Ac)APRK(Ac)QLATK. (D) MS/MS spectrum of the acetylated peptide QLATK(Ac)AARK(Ac)SAPSTGGVK. (E) MS/MS spectrum of the peptide TDLRFQSAAIGALQEASE showing amino acids marked in red color unique to H3.3. Spectral images were obtained using Tandem data base where y-type immonium ions represented by red peaks. All the MS/MS data were acquired using Thermo Scientific Velos Pro ion trap mass spectrometer. Acetylation at K residues were highlighted in yellow. Amino acids which characterized H3.3 in the sequence are shown in red. Results are representative of three independent experiments.

    Article Snippet: The resulting reaction mixture was analyzed by LC-MS/MS, using an Easy nanoLC II HPLC system (Thermo) interfaced via electrospray ionization (ESI) to a dual pressure linear ion trap mass spectrometer (LTQ velos, Thermo Fisher).

    Techniques: Mass Spectrometry, Sequencing

    HPLC-electrospray ionization MS analysis of inactivated clindamycin. (A) HPLC chromatogram showing a major peak eluting at 10.8 min. (B) Full MS analysis of the 10.8-min-eluted fraction reveals the dominance of a 754.1-amu compound and its Na adduct (+22

    Journal:

    Article Title: Lincomycin Resistance Gene lnu(D) in Streptococcus uberis ▿

    doi: 10.1128/AAC.01126-07

    Figure Lengend Snippet: HPLC-electrospray ionization MS analysis of inactivated clindamycin. (A) HPLC chromatogram showing a major peak eluting at 10.8 min. (B) Full MS analysis of the 10.8-min-eluted fraction reveals the dominance of a 754.1-amu compound and its Na adduct (+22

    Article Snippet: Samples were analyzed by using an electrospray ion trap mass spectrometer (MS) (LCQ Deca XP; Thermo Finnigan, San Jose, CA) coupled online with high-performance liquid chromatography (HPLC; Surveyor LC).

    Techniques: High Performance Liquid Chromatography, Mass Spectrometry