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  • 94
    Thermo Fisher rabbit polyclonal anti dsn1
    Rabbit Polyclonal Anti Dsn1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti dsn1/product/Thermo Fisher
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    99
    Millipore α dsn1 ps100 antibody
    Aurora B phosphorylates <t>Dsn1</t> and strengthens the CCAN–KMN interaction. (A) Lysates (Input), α-Mis12C IP (Mis12C), and IgG IP of mitotic HeLa cells treated with nocodazole and MG132 in the presence or absence of ZM447439 were blotted with the indicated antibodies. The asterisk indicates the IgG heavy chain in the IP samples. Dsn1 migrated as multiple bands due to phosphorylation. Mis12 and Nnf1 co-migrated. (B) Mis12C was incubated with Aurora B–INCENP and γ-[ 32 P]ATP, separated by SDS-PAGE, and analyzed by Coomassie brilliant blue (CBB) staining (left) or with a phosphorimager (right). Mis12 and Nnf1 co-migrated. Nsl1 underwent proteolysis. Myelin basic protein (MBP) was used as a positive control. (C) Mis12C containing Dsn1-WT or Dsn1-EE was incubated with Aurora B–INCENP with (+) or without (–) cold ATP. Samples were separated by SDS-PAGE and blotted with the indicated antibodies. Dsn1-EE was recognized by <t>α-pS100</t> Dsn1. Black lines indicate that intervening lanes have been spliced out. (D) HeLa cells were arrested in prometaphase with nocodazole and incubated with MG132 alone or with MG132 and ZM447439, and then stained with DAPI (blue in the merge), CREST (red), and α-pS100 Dsn1 (green). The boxed regions were magnified and shown in the rightmost column. (E) Cells stably expressing Dsn1-WT, S100E/S109E (EE), or S100A/S109A (AA)-GFP were transfected with siDsn1, treated as in D, and stained with the indicated antibodies. Boxed regions in merged images were magnified and shown in the rightmost column. The normalized kinetochore intensities (mean ± SD, n = 400) of Dsn1-GFP and Knl1of cells were quantified and shown. Bars, 5 µm (1 µm for magnified images).
    α Dsn1 Ps100 Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Hornung dsn1
    Hrr25 phosphorylates <t>Dsn1</t> Phos‐tag gels showing phosphorylation of purified S. cerevisiae Mtw1 complex by Hrr25 1–394 and Hrr25 1–394 :Mam1 87–191 . Asterisks denote N‐terminal proteolytic cleavage products of Dsn1, with the red asterisk denoting a previously characterized product lacking the first 171 residues (Hornung et al ). Model of the intact monopolin complex. Four copies of Csm1 (blue) and two of Lrs4 (green) form the core “V”‐shaped kinetochore‐binding complex (Corbett et al ), which in turn recruits one copy of Hrr25 (blue/green). Thirty‐one residues of Mam1 (192–222) separate the protein's Hrr25‐binding and Csm1‐binding domains, which when fully extended could reach as far as ˜120 Å.
    Dsn1, supplied by Hornung, used in various techniques. Bioz Stars score: 90/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    dsn1  (Abcam)
    90
    Abcam dsn1
    Knockdown of SKA3 reduces cell growth HT29 and HCT116 cells were transfected with control siRNA or target siRNA. A typical result is shown; each data point represents mean ± SD of cell indexes conducted in triplicate. A-F. Knockdown of SKA3, SKA1, or SKA2 reduced growth rates in HT29 and HCT116 cells. G-H. Knockdown of <t>DSN1</t> did not affect cell growth rate in either HT29 or HCT116 cells. (** p
    Dsn1, supplied by Abcam, used in various techniques. Bioz Stars score: 90/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dsn1/product/Abcam
    Average 90 stars, based on 11 article reviews
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    91
    Cell Signaling Technology Inc dsn1
    Proper Chromosome Alignment and Ndc80 Phosphorylation Require Centromeric CPC ( A ) Upper panel: Representative images of spindles formed in WT and ΔCPC extracts with indicated CPC conditions. Chromatin was stained with Hoechst (blue), and rhodamine-labeled tubulin was added (red). Lower panel: Representative IF images of metaphase spindles stained for <t>Dsn1</t> (green). ( B ) Mean of inter-kinetochore distances observed in ΔCPC extracts with indicated CPC conditions +/− nocodazole. n = 100 kinetochores. ( C ) Mean percent of bipolar spindles observed in (B) which contained multiple misaligned kinetochores. n = 75 total spindle structures per condition. ( D ) Mean integrated fluorescence intensities of Ndc80S40ph in metaphase spindles in WT and activated CPC ΔCEN .
    Dsn1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 91/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Proteintech rabbit dsn1 polyclonal
    Proper Chromosome Alignment and Ndc80 Phosphorylation Require Centromeric CPC ( A ) Upper panel: Representative images of spindles formed in WT and ΔCPC extracts with indicated CPC conditions. Chromatin was stained with Hoechst (blue), and rhodamine-labeled tubulin was added (red). Lower panel: Representative IF images of metaphase spindles stained for <t>Dsn1</t> (green). ( B ) Mean of inter-kinetochore distances observed in ΔCPC extracts with indicated CPC conditions +/− nocodazole. n = 100 kinetochores. ( C ) Mean percent of bipolar spindles observed in (B) which contained multiple misaligned kinetochores. n = 75 total spindle structures per condition. ( D ) Mean integrated fluorescence intensities of Ndc80S40ph in metaphase spindles in WT and activated CPC ΔCEN .
    Rabbit Dsn1 Polyclonal, supplied by Proteintech, used in various techniques. Bioz Stars score: 90/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    21st Century Biochemicals phosphorylated dsn1
    Proper Chromosome Alignment and Ndc80 Phosphorylation Require Centromeric CPC ( A ) Upper panel: Representative images of spindles formed in WT and ΔCPC extracts with indicated CPC conditions. Chromatin was stained with Hoechst (blue), and rhodamine-labeled tubulin was added (red). Lower panel: Representative IF images of metaphase spindles stained for <t>Dsn1</t> (green). ( B ) Mean of inter-kinetochore distances observed in ΔCPC extracts with indicated CPC conditions +/− nocodazole. n = 100 kinetochores. ( C ) Mean percent of bipolar spindles observed in (B) which contained multiple misaligned kinetochores. n = 75 total spindle structures per condition. ( D ) Mean integrated fluorescence intensities of Ndc80S40ph in metaphase spindles in WT and activated CPC ΔCEN .
    Phosphorylated Dsn1, supplied by 21st Century Biochemicals, used in various techniques. Bioz Stars score: 86/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    Covalab polyclonal rabbit anti dsn1
    Proper Chromosome Alignment and Ndc80 Phosphorylation Require Centromeric CPC ( A ) Upper panel: Representative images of spindles formed in WT and ΔCPC extracts with indicated CPC conditions. Chromatin was stained with Hoechst (blue), and rhodamine-labeled tubulin was added (red). Lower panel: Representative IF images of metaphase spindles stained for <t>Dsn1</t> (green). ( B ) Mean of inter-kinetochore distances observed in ΔCPC extracts with indicated CPC conditions +/− nocodazole. n = 100 kinetochores. ( C ) Mean percent of bipolar spindles observed in (B) which contained multiple misaligned kinetochores. n = 75 total spindle structures per condition. ( D ) Mean integrated fluorescence intensities of Ndc80S40ph in metaphase spindles in WT and activated CPC ΔCEN .
    Polyclonal Rabbit Anti Dsn1, supplied by Covalab, used in various techniques. Bioz Stars score: 84/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Aurora B phosphorylates Dsn1 and strengthens the CCAN–KMN interaction. (A) Lysates (Input), α-Mis12C IP (Mis12C), and IgG IP of mitotic HeLa cells treated with nocodazole and MG132 in the presence or absence of ZM447439 were blotted with the indicated antibodies. The asterisk indicates the IgG heavy chain in the IP samples. Dsn1 migrated as multiple bands due to phosphorylation. Mis12 and Nnf1 co-migrated. (B) Mis12C was incubated with Aurora B–INCENP and γ-[ 32 P]ATP, separated by SDS-PAGE, and analyzed by Coomassie brilliant blue (CBB) staining (left) or with a phosphorimager (right). Mis12 and Nnf1 co-migrated. Nsl1 underwent proteolysis. Myelin basic protein (MBP) was used as a positive control. (C) Mis12C containing Dsn1-WT or Dsn1-EE was incubated with Aurora B–INCENP with (+) or without (–) cold ATP. Samples were separated by SDS-PAGE and blotted with the indicated antibodies. Dsn1-EE was recognized by α-pS100 Dsn1. Black lines indicate that intervening lanes have been spliced out. (D) HeLa cells were arrested in prometaphase with nocodazole and incubated with MG132 alone or with MG132 and ZM447439, and then stained with DAPI (blue in the merge), CREST (red), and α-pS100 Dsn1 (green). The boxed regions were magnified and shown in the rightmost column. (E) Cells stably expressing Dsn1-WT, S100E/S109E (EE), or S100A/S109A (AA)-GFP were transfected with siDsn1, treated as in D, and stained with the indicated antibodies. Boxed regions in merged images were magnified and shown in the rightmost column. The normalized kinetochore intensities (mean ± SD, n = 400) of Dsn1-GFP and Knl1of cells were quantified and shown. Bars, 5 µm (1 µm for magnified images).

    Journal: The Journal of Cell Biology

    Article Title: Multiple assembly mechanisms anchor the KMN spindle checkpoint platform at human mitotic kinetochores

    doi: 10.1083/jcb.201407074

    Figure Lengend Snippet: Aurora B phosphorylates Dsn1 and strengthens the CCAN–KMN interaction. (A) Lysates (Input), α-Mis12C IP (Mis12C), and IgG IP of mitotic HeLa cells treated with nocodazole and MG132 in the presence or absence of ZM447439 were blotted with the indicated antibodies. The asterisk indicates the IgG heavy chain in the IP samples. Dsn1 migrated as multiple bands due to phosphorylation. Mis12 and Nnf1 co-migrated. (B) Mis12C was incubated with Aurora B–INCENP and γ-[ 32 P]ATP, separated by SDS-PAGE, and analyzed by Coomassie brilliant blue (CBB) staining (left) or with a phosphorimager (right). Mis12 and Nnf1 co-migrated. Nsl1 underwent proteolysis. Myelin basic protein (MBP) was used as a positive control. (C) Mis12C containing Dsn1-WT or Dsn1-EE was incubated with Aurora B–INCENP with (+) or without (–) cold ATP. Samples were separated by SDS-PAGE and blotted with the indicated antibodies. Dsn1-EE was recognized by α-pS100 Dsn1. Black lines indicate that intervening lanes have been spliced out. (D) HeLa cells were arrested in prometaphase with nocodazole and incubated with MG132 alone or with MG132 and ZM447439, and then stained with DAPI (blue in the merge), CREST (red), and α-pS100 Dsn1 (green). The boxed regions were magnified and shown in the rightmost column. (E) Cells stably expressing Dsn1-WT, S100E/S109E (EE), or S100A/S109A (AA)-GFP were transfected with siDsn1, treated as in D, and stained with the indicated antibodies. Boxed regions in merged images were magnified and shown in the rightmost column. The normalized kinetochore intensities (mean ± SD, n = 400) of Dsn1-GFP and Knl1of cells were quantified and shown. Bars, 5 µm (1 µm for magnified images).

    Article Snippet: The α-Dsn1-pS100 antibody was produced at an in-house facility by immunizing rabbits with a mixture of the pS100 peptide (SWRRApSMKETNC) and the pS109 peptide (TNRRKpSLHPIHC) coupled to hemocyanin (Sigma-Aldrich).

    Techniques: Incubation, SDS Page, Staining, Positive Control, Stable Transfection, Expressing, Transfection

    Hrr25 phosphorylates Dsn1 Phos‐tag gels showing phosphorylation of purified S. cerevisiae Mtw1 complex by Hrr25 1–394 and Hrr25 1–394 :Mam1 87–191 . Asterisks denote N‐terminal proteolytic cleavage products of Dsn1, with the red asterisk denoting a previously characterized product lacking the first 171 residues (Hornung et al ). Model of the intact monopolin complex. Four copies of Csm1 (blue) and two of Lrs4 (green) form the core “V”‐shaped kinetochore‐binding complex (Corbett et al ), which in turn recruits one copy of Hrr25 (blue/green). Thirty‐one residues of Mam1 (192–222) separate the protein's Hrr25‐binding and Csm1‐binding domains, which when fully extended could reach as far as ˜120 Å.

    Journal: The EMBO Journal

    Article Title: Structure of the Saccharomyces cerevisiae Hrr25:Mam1 monopolin subcomplex reveals a novel kinase regulator

    doi: 10.15252/embj.201694082

    Figure Lengend Snippet: Hrr25 phosphorylates Dsn1 Phos‐tag gels showing phosphorylation of purified S. cerevisiae Mtw1 complex by Hrr25 1–394 and Hrr25 1–394 :Mam1 87–191 . Asterisks denote N‐terminal proteolytic cleavage products of Dsn1, with the red asterisk denoting a previously characterized product lacking the first 171 residues (Hornung et al ). Model of the intact monopolin complex. Four copies of Csm1 (blue) and two of Lrs4 (green) form the core “V”‐shaped kinetochore‐binding complex (Corbett et al ), which in turn recruits one copy of Hrr25 (blue/green). Thirty‐one residues of Mam1 (192–222) separate the protein's Hrr25‐binding and Csm1‐binding domains, which when fully extended could reach as far as ˜120 Å.

    Article Snippet: In order to cross‐link two kinetochores, a single monopolin complex must bind at least one Dsn1 from each of two separate kinetochores, rather than binding multiple copies of Dsn1 within a single kinetochore.

    Techniques: Purification, Binding Assay

    Knockdown of SKA3 reduces cell growth HT29 and HCT116 cells were transfected with control siRNA or target siRNA. A typical result is shown; each data point represents mean ± SD of cell indexes conducted in triplicate. A-F. Knockdown of SKA3, SKA1, or SKA2 reduced growth rates in HT29 and HCT116 cells. G-H. Knockdown of DSN1 did not affect cell growth rate in either HT29 or HCT116 cells. (** p

    Journal: Oncotarget

    Article Title: Over-expression of AURKA, SKA3 and DSN1 contributes to colorectal adenoma to carcinoma progression

    doi: 10.18632/oncotarget.9960

    Figure Lengend Snippet: Knockdown of SKA3 reduces cell growth HT29 and HCT116 cells were transfected with control siRNA or target siRNA. A typical result is shown; each data point represents mean ± SD of cell indexes conducted in triplicate. A-F. Knockdown of SKA3, SKA1, or SKA2 reduced growth rates in HT29 and HCT116 cells. G-H. Knockdown of DSN1 did not affect cell growth rate in either HT29 or HCT116 cells. (** p

    Article Snippet: The processed sections were incubated with primary antibody overnight at 4°C at the following dilutions: Aurora A: 1:250, SKA3: 1:800, DSN1: 1:3000 (Abcam, Cambridge, MA, USA).

    Techniques: Transfection

    Knockdown of SKA3 or DSN1 inhibits migration, invasion, and anchorage-independent growth Transwell migration, invasion, and soft agar colony assays were conducted with HT29 and HCT116 cells transfected with control siRNA or target siRNA. Knockdown of SKA3 or DSN1 inhibited cell migration and invasion in both cell lines A-D. Relative percentages of migrated and invaded cells are presented as mean ± SD. Depletion of SKA3 or DSN1 decreased colony formation in E. HT29 cells and F. HCT116 cells. Representative images of colony formation following each treatment are shown on the left and quantification results are shown on the right. Numbers of colonies are presented as mean ± SD. (* p

    Journal: Oncotarget

    Article Title: Over-expression of AURKA, SKA3 and DSN1 contributes to colorectal adenoma to carcinoma progression

    doi: 10.18632/oncotarget.9960

    Figure Lengend Snippet: Knockdown of SKA3 or DSN1 inhibits migration, invasion, and anchorage-independent growth Transwell migration, invasion, and soft agar colony assays were conducted with HT29 and HCT116 cells transfected with control siRNA or target siRNA. Knockdown of SKA3 or DSN1 inhibited cell migration and invasion in both cell lines A-D. Relative percentages of migrated and invaded cells are presented as mean ± SD. Depletion of SKA3 or DSN1 decreased colony formation in E. HT29 cells and F. HCT116 cells. Representative images of colony formation following each treatment are shown on the left and quantification results are shown on the right. Numbers of colonies are presented as mean ± SD. (* p

    Article Snippet: The processed sections were incubated with primary antibody overnight at 4°C at the following dilutions: Aurora A: 1:250, SKA3: 1:800, DSN1: 1:3000 (Abcam, Cambridge, MA, USA).

    Techniques: Migration, Transfection

    Protein expression of candidate genes in tissues A. Representative immunoblotting analysis of Aurora A, SKA3, UBE2C, and DSN1 in tri-part samples from four patients (CRC01, CRC06, CRC08, and CRC09). Ratios normalized to GAPDH are shown under each lane. (N, non-neoplastic tissue; A, polyp; C, carcinoma) B. Aurora A, SKA3, and DSN1 protein levels in paired adenoma and carcinoma samples. Fold change in protein levels was normalized to paired non-neoplastic samples. (* p

    Journal: Oncotarget

    Article Title: Over-expression of AURKA, SKA3 and DSN1 contributes to colorectal adenoma to carcinoma progression

    doi: 10.18632/oncotarget.9960

    Figure Lengend Snippet: Protein expression of candidate genes in tissues A. Representative immunoblotting analysis of Aurora A, SKA3, UBE2C, and DSN1 in tri-part samples from four patients (CRC01, CRC06, CRC08, and CRC09). Ratios normalized to GAPDH are shown under each lane. (N, non-neoplastic tissue; A, polyp; C, carcinoma) B. Aurora A, SKA3, and DSN1 protein levels in paired adenoma and carcinoma samples. Fold change in protein levels was normalized to paired non-neoplastic samples. (* p

    Article Snippet: The processed sections were incubated with primary antibody overnight at 4°C at the following dilutions: Aurora A: 1:250, SKA3: 1:800, DSN1: 1:3000 (Abcam, Cambridge, MA, USA).

    Techniques: Expressing

    ROC analysis of Aurora A, SKA3, and DSN1 for discriminating carcinoma from adenoma ROC curves show the specificity and sensitivity of each protein by comparing polyps to non-neoplastic tissues (left panel), carcinomas to non-neoplastic tissues (middle panel), and carcinomas to polyps (right panel). The AUC values are indicated in each graph.

    Journal: Oncotarget

    Article Title: Over-expression of AURKA, SKA3 and DSN1 contributes to colorectal adenoma to carcinoma progression

    doi: 10.18632/oncotarget.9960

    Figure Lengend Snippet: ROC analysis of Aurora A, SKA3, and DSN1 for discriminating carcinoma from adenoma ROC curves show the specificity and sensitivity of each protein by comparing polyps to non-neoplastic tissues (left panel), carcinomas to non-neoplastic tissues (middle panel), and carcinomas to polyps (right panel). The AUC values are indicated in each graph.

    Article Snippet: The processed sections were incubated with primary antibody overnight at 4°C at the following dilutions: Aurora A: 1:250, SKA3: 1:800, DSN1: 1:3000 (Abcam, Cambridge, MA, USA).

    Techniques:

    Correlations between protein levels and genomic alteration Each circle represents the proportion of tumor samples in each category. Fold change of protein levels in tumor samples were normalized to paired non-neoplastic tissues, and overexpression is defined as fold change ≥ 1.5. A. Overexpression of Aurora A, SKA3, and DSN1 protein is positively correlated with higher CIN (0 corresponds to CIN-stable, 1 to low degree of CIN, 2 to medium degree of CIN, 3 to high degree of CIN, and 4 to ultra-high degree of CIN). B. Overexpression of SKA3 and DSN1 proteins are correlated with the presence of LOH.

    Journal: Oncotarget

    Article Title: Over-expression of AURKA, SKA3 and DSN1 contributes to colorectal adenoma to carcinoma progression

    doi: 10.18632/oncotarget.9960

    Figure Lengend Snippet: Correlations between protein levels and genomic alteration Each circle represents the proportion of tumor samples in each category. Fold change of protein levels in tumor samples were normalized to paired non-neoplastic tissues, and overexpression is defined as fold change ≥ 1.5. A. Overexpression of Aurora A, SKA3, and DSN1 protein is positively correlated with higher CIN (0 corresponds to CIN-stable, 1 to low degree of CIN, 2 to medium degree of CIN, 3 to high degree of CIN, and 4 to ultra-high degree of CIN). B. Overexpression of SKA3 and DSN1 proteins are correlated with the presence of LOH.

    Article Snippet: The processed sections were incubated with primary antibody overnight at 4°C at the following dilutions: Aurora A: 1:250, SKA3: 1:800, DSN1: 1:3000 (Abcam, Cambridge, MA, USA).

    Techniques: Over Expression

    Knockdown of SKA3 or DSN1 inhibits cell cycle progression HT29 and HCT116 cells were transfected with control siRNA or target siRNA. A typical result of cell cycle distribution analysis is presented, with control siRNA in the left column and target RNA in the middle column. Quantification of the results of three independent experiments is presented in the right column. The percentages of cells at each cell cycle phase are shown as mean ± SD. A. SKA3 knockdown decreased the G1 phase population, increased the G2/M population, and increased the sub-G1 population in HT29 cells. B. SKA3 knockdown decreased the S phase population, increased the G2/M population, and increased the sub-G1 population in HCT116 cells. Knockdown of DSN1 increased G2/M arrest in C. HT29 cells and D. HCT116 cells. (* p

    Journal: Oncotarget

    Article Title: Over-expression of AURKA, SKA3 and DSN1 contributes to colorectal adenoma to carcinoma progression

    doi: 10.18632/oncotarget.9960

    Figure Lengend Snippet: Knockdown of SKA3 or DSN1 inhibits cell cycle progression HT29 and HCT116 cells were transfected with control siRNA or target siRNA. A typical result of cell cycle distribution analysis is presented, with control siRNA in the left column and target RNA in the middle column. Quantification of the results of three independent experiments is presented in the right column. The percentages of cells at each cell cycle phase are shown as mean ± SD. A. SKA3 knockdown decreased the G1 phase population, increased the G2/M population, and increased the sub-G1 population in HT29 cells. B. SKA3 knockdown decreased the S phase population, increased the G2/M population, and increased the sub-G1 population in HCT116 cells. Knockdown of DSN1 increased G2/M arrest in C. HT29 cells and D. HCT116 cells. (* p

    Article Snippet: The processed sections were incubated with primary antibody overnight at 4°C at the following dilutions: Aurora A: 1:250, SKA3: 1:800, DSN1: 1:3000 (Abcam, Cambridge, MA, USA).

    Techniques: Transfection

    Proper Chromosome Alignment and Ndc80 Phosphorylation Require Centromeric CPC ( A ) Upper panel: Representative images of spindles formed in WT and ΔCPC extracts with indicated CPC conditions. Chromatin was stained with Hoechst (blue), and rhodamine-labeled tubulin was added (red). Lower panel: Representative IF images of metaphase spindles stained for Dsn1 (green). ( B ) Mean of inter-kinetochore distances observed in ΔCPC extracts with indicated CPC conditions +/− nocodazole. n = 100 kinetochores. ( C ) Mean percent of bipolar spindles observed in (B) which contained multiple misaligned kinetochores. n = 75 total spindle structures per condition. ( D ) Mean integrated fluorescence intensities of Ndc80S40ph in metaphase spindles in WT and activated CPC ΔCEN .

    Journal: Developmental cell

    Article Title: Distinct Roles of the Chromosomal Passenger Complex in the Detection of and Response to Errors in Kinetochore-Microtubule Attachment

    doi: 10.1016/j.devcel.2017.08.022

    Figure Lengend Snippet: Proper Chromosome Alignment and Ndc80 Phosphorylation Require Centromeric CPC ( A ) Upper panel: Representative images of spindles formed in WT and ΔCPC extracts with indicated CPC conditions. Chromatin was stained with Hoechst (blue), and rhodamine-labeled tubulin was added (red). Lower panel: Representative IF images of metaphase spindles stained for Dsn1 (green). ( B ) Mean of inter-kinetochore distances observed in ΔCPC extracts with indicated CPC conditions +/− nocodazole. n = 100 kinetochores. ( C ) Mean percent of bipolar spindles observed in (B) which contained multiple misaligned kinetochores. n = 75 total spindle structures per condition. ( D ) Mean integrated fluorescence intensities of Ndc80S40ph in metaphase spindles in WT and activated CPC ΔCEN .

    Article Snippet: The following antibodies were used at the indicated dilutions: Dsn1 ( ) 1:500, p-Aurora (Cell Signaling 2914S) 1:500, Knl1 ( ) 1:200, Ndc80 ( ) 1:200, Mad2 ( ) 1:200, BubR1 ( ) 1:100, Borealin (Dasra A) 1:250 , 3F3/2 ( ) 1:2500, Cenp-K ( ) 1:250, Cenp-C 1:500, MBP (New England Biolabs E8032S) 1:1000, INCENP (39259, Active Motif) 1:500, Ndc80S44ph ( ) 1:2000 and Mps1 ( ) 1:100.

    Techniques: Staining, Labeling, Fluorescence