Thermo Fisher
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Waters Corporation
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ESI 05 is an inhibitor of exchange protein activated by cAMP 2 Epac2 that inhibits cAMP induced Epac2 guanine nucleotide exchange factor GEF activity with an IC value of 0
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Image Search Results

Journal: bioRxiv
Article Title: Covalent Protein Painting Reveals Structural Changes in the Proteome in Alzheimer Disease
doi: 10.1101/2020.01.31.929117
Figure Lengend Snippet: Schematic of the CPP method. CPP includes in vivo chemical methylation of lysine residues at the surface of proteins and its detection with mass spectrometry. The flow chart shows each labeling step and the resultant relative measurement of surface accessibility for chemical modification based on mass spectrometric quantification of isotope labeled peptides. Proteins are labeled with isotope defined reagents at solvent exposed lysine residues (K) with two methyl moieties ( 13 CD 3 , heavy) in vivo . Protein are then digested in peptides with the endoproteinase Chymotrypsin, and all newly accessible primary amines labeled with two methyl moieties (CH 3 , light). Peptides are separated by liquid chromatography (LC) and transferred into gas phase by electrospray ionization (nano ESI). High mass resolution (Orbitrap) mass spectra (MS) and fragment ion mass spectra (MS/MS) are acquired. Peptides are identified with a database search using ProLuCID and quantified with Census. The “surfaces of all protein complexes” (SoPaX) algorithm within ProteinClusterQuant (PCQ) determines and compares the relative surface accessibility of lysine residues.
Article Snippet: Following chromatographic separation, peptides were transferred into an Orbitrap Lumos mass spectrometer by
Techniques: In Vivo, Methylation, Mass Spectrometry, Labeling, Modification, Liquid Chromatography, Tandem Mass Spectroscopy
![Annotations of lipids by MS2Analyzer. (a) QTOF MS/MS of digalactosyldiacylglycerol 18:3/16:0 in positive electrospray mode, indicating the neutral loss of the DGDG headgroup from the [M + NH 4 ] + adduct precursor ion as well as m / z differences for product ions indicating both acyl side chains. Note that positional isomers of acyl groups cannot be determined with this method. (b) QTOF MS/MS of phosphatidylglycerol 16:0/16:0 in negative electrospray mode, indicating the characteristic product ions of the phosphatidylglycerol headgroup ( m / z 152.995) and the acyl side chains ( m / z 255.233).](https://storage.googleapis.com/bioz_article_images/PMC4222628/ac-2014-02818e_0003.jpg)
Journal: Analytical Chemistry
Article Title: MS2Analyzer: A Software for Small Molecule Substructure Annotations from Accurate Tandem Mass Spectra
doi: 10.1021/ac502818e
Figure Lengend Snippet: Annotations of lipids by MS2Analyzer. (a) QTOF MS/MS of digalactosyldiacylglycerol 18:3/16:0 in positive electrospray mode, indicating the neutral loss of the DGDG headgroup from the [M + NH 4 ] + adduct precursor ion as well as m / z differences for product ions indicating both acyl side chains. Note that positional isomers of acyl groups cannot be determined with this method. (b) QTOF MS/MS of phosphatidylglycerol 16:0/16:0 in negative electrospray mode, indicating the characteristic product ions of the phosphatidylglycerol headgroup ( m / z 152.995) and the acyl side chains ( m / z 255.233).
Article Snippet: In order to reduce the impact from different instruments, ionizations, and adducts, only [M + H]+ spectra acquired under positive
Techniques: Mass Spectrometry

Journal: Journal of the American Society for Mass Spectrometry
Article Title: Monitoring Copopulated Conformational States During Protein Folding Events Using Electrospray Ionization-Ion Mobility Spectrometry-Mass Spectrometry
doi: 10.1016/j.jasms.2007.09.017
Figure Lengend Snippet: ( a )–( c ): ESI-IMS-MS Driftscope plots showing drift time (x axis) versus m/z (y axis) for β 2 m and variants at pH 6.8. ( a ) wild-type β 2 m, ( b ) single mutant I7A, and ( c ) double mutant I7A/P32G. Insets at the right hand side: the summed, full scan m/z spectra of each protein showing the charge state ions detected.
Article Snippet: ESI-IMS-MS Analyses Samples were infused into the
Techniques: Mass Spectrometry, Mutagenesis

Journal: Journal of the American Society for Mass Spectrometry
Article Title: Monitoring Copopulated Conformational States During Protein Folding Events Using Electrospray Ionization-Ion Mobility Spectrometry-Mass Spectrometry
doi: 10.1016/j.jasms.2007.09.017
Figure Lengend Snippet: ESI-IMS-MS Driftscope plots showing drift time (x axis) versus m/z (y axis) for wild-type β 2 m analyzed at ( a ) pH 6.23, ( b ) pH 4.28, ( c ) pH 3.54, and ( d ) pH 2.60. The number of conformeric species observed for each individual charge state can be seen. Insets at the right hand side of each plot: the summed, full scan m/z spectra of wild-type β 2 m for each data acquisition showing the charge state ions detected.
Article Snippet: ESI-IMS-MS Analyses Samples were infused into the
Techniques: Mass Spectrometry

Journal: Journal of the American Society for Mass Spectrometry
Article Title: Monitoring Copopulated Conformational States During Protein Folding Events Using Electrospray Ionization-Ion Mobility Spectrometry-Mass Spectrometry
doi: 10.1016/j.jasms.2007.09.017
Figure Lengend Snippet: ( a ) The summed m/z spectrum from an ESI-IMS-MS data acquisition of cytochrome c analyzed in 50 mM aqueous ammonium acetate solution acidified to pH 3 showing a charge state distribution from +6 to +20 ions consistent with monomeric protein (12,359.4 Da). ( b ) ESI-IMS-MS Driftscope plot showing drift time (x axis) versus m/z (y axis) for the analysis of cytochrome c in 50 mM aqueous ammonium acetate solution acidified to pH 3. ( c ) ESI-IMS-MS drift time versus intensity graphs for the m/z 1237.0 (+10 ions; upper), m/z 1374.4 (+9 ions; middle), and m/z 1546.0 (+8 ions; lower) signals detected during the analysis of cytochrome c in 50 mM aqueous ammonium acetate solution acidified to pH 3.
Article Snippet: ESI-IMS-MS Analyses Samples were infused into the
Techniques: Mass Spectrometry

Journal: Journal of Clinical Microbiology
Article Title: Broad-Range PCR Coupled with Electrospray Ionization Time of Flight Mass Spectrometry for Detection of Bacteremia and Fungemia in Patients with Neutropenic Fever
doi: 10.1128/JCM.01066-16
Figure Lengend Snippet: Assessment of factors influencing performance of PCR/ESI-MS.
Article Snippet: Episodes with polymicrobial infection, where
Techniques: Polymerase Chain Reaction, Mass Spectrometry

Journal: Journal of Clinical Microbiology
Article Title: Broad-Range PCR Coupled with Electrospray Ionization Time of Flight Mass Spectrometry for Detection of Bacteremia and Fungemia in Patients with Neutropenic Fever
doi: 10.1128/JCM.01066-16
Figure Lengend Snippet: PCR/ESI-MS and blood culture results by specimen.
Article Snippet: Episodes with polymicrobial infection, where
Techniques: Polymerase Chain Reaction, Mass Spectrometry

Journal: Journal of Clinical Microbiology
Article Title: Broad-Range PCR Coupled with Electrospray Ionization Time of Flight Mass Spectrometry for Detection of Bacteremia and Fungemia in Patients with Neutropenic Fever
doi: 10.1128/JCM.01066-16
Figure Lengend Snippet: Results of blood cultures (BC) and PCR/ESI-MS in the 105 cases of neutropenic fever. Bloodstream infection (BSI) included both definite and probable BSI based on BC and/or PCR/ESI-MS. MO, microorganism; +, positive result; −, negative result;
Article Snippet: Episodes with polymicrobial infection, where
Techniques: Polymerase Chain Reaction, Mass Spectrometry, Infection

Journal: Frontiers in Immunology
Article Title: Alterations of Gut Microbiome and Metabolite Profiling in Mice Infected by Schistosoma japonicum
doi: 10.3389/fimmu.2020.569727
Figure Lengend Snippet: Three-dimensional score plots of partial least squares-discriminatory analysis from healthy mice and infected mice at different time points. Each point represents an individual. (A) Serum samples in positive electrospray ionization (ESI+) mode. (B) Urine samples in ESI+ mode. (C) Liver aqueous extracts in negative electrospray ionization (ESI-) mode. (D) Serum samples in ESI- mode. (E) Urine samples in ESI- mode. (F) Colon aqueous extracts in ESI- mode.
Article Snippet: Quadrupole-Time-of-Flight Mass Spectrometry Conditions Mass spectrometry data were collected by a SYNAPT G2-Si High-Definition Mass Spectrometer with an
Techniques: Mouse Assay, Infection

Journal: Frontiers in Immunology
Article Title: Alterations of Gut Microbiome and Metabolite Profiling in Mice Infected by Schistosoma japonicum
doi: 10.3389/fimmu.2020.569727
Figure Lengend Snippet: Three-dimensional score plots of principal component analysis from healthy mice and infected mice at different time points. Each point represents an individual. (A) Serum samples in positive electrospray ionization (ESI+) mode. (B) Urine samples in ESI+ mode. (C) Liver aqueous extracts in negative electrospray ionization (ESI-) mode. (D) Serum samples in ESI- mode. (E) Urine samples in ESI- mode. (F) Colon aqueous extracts in ESI- mode.
Article Snippet: Quadrupole-Time-of-Flight Mass Spectrometry Conditions Mass spectrometry data were collected by a SYNAPT G2-Si High-Definition Mass Spectrometer with an
Techniques: Mouse Assay, Infection

Journal: Toxins
Article Title: Anti-Breast Cancer Activity of Latroeggtoxin-V Mined from the Transcriptome of Spider Latrodectus tredecimguttatus Eggs
doi: 10.3390/toxins10110451
Figure Lengend Snippet: Purification and identification of rLatroeggtoxin-V. ( A ) Chromatogram of RP-HPLC purification of rLatroeggtoxin-V. ( B ) Molecular weight determination of rLatroeggtoxin-V by electrospray ionization mass spectrometry. The m / z value and the number of charges for each rLatroeggtoxin-V ion peak were labeled.
Article Snippet: The molecular weight of the components in each elution peak was determined by
Techniques: Purification, High Performance Liquid Chromatography, Molecular Weight, Mass Spectrometry, Labeling

Journal: Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
Article Title: Amino acid variability in the peptide composition of a suite of amphiphilic peptide siderophores from an open ocean Vibrio species
doi: 10.1007/s00775-013-0995-3
Figure Lengend Snippet: Electrospray ionization-tandem mass spectrum of moanachelin gly-D (C14:0).
Article Snippet: The masses of the siderophores and the siderophore fragments were determined by
Techniques:

Journal: Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
Article Title: Amino acid variability in the peptide composition of a suite of amphiphilic peptide siderophores from an open ocean Vibrio species
doi: 10.1007/s00775-013-0995-3
Figure Lengend Snippet: Electrospray ionization-tandem mass spectrum of moanachelin ala-D (C14:0).
Article Snippet: The masses of the siderophores and the siderophore fragments were determined by
Techniques:

Journal: Scientific Reports
Article Title: Efficient biosynthesis of a Cecropin A-melittin mutant in Bacillus subtilis WB700
doi: 10.1038/srep40587
Figure Lengend Snippet: Identification of CAM-W produced by recombinant B. subtilis WB 700. ( A ) Analysis of tricine-SDS-PAGE (a) cropped from Supplementary Figure 1 and western blots (b and c) cropped from Supplementary Figures 2 and 3 of the total extracellular proteins from B. subtilis WB700 harboring pDM031 induced without maltose (lane 1) or with maltose (lane 2). These gels were run under the same experimental conditions. The EDDIE and CAM-W bands are indicated by (←) and (← ← ). The bands present in (a) lane 2 were confirmed by western blotting, as shown in (b) and (c). The marker lane contained a broad range protein marker (#P7702, New England Biolabs, USA). ( B ) RP-HPLC analysis of purified CAM-W. ( C ) Electrospray ionization mass spectrometry analysis of purified recombinant CAM-W.
Article Snippet: The molecular weight of the purified CAM-W was measured using
Techniques: Chick Chorioallantoic Membrane Assay, Produced, Recombinant, Western Blot, SDS Page, Marker, High Performance Liquid Chromatography, Purification, Mass Spectrometry