Presentation is loading. Please wait.

Presentation is loading. Please wait.

Separation of colonospheres from differentiated tumor cells by cluster analysis. Separation of colonospheres from differentiated tumor cells by cluster.

Published byΗμέρα Μιαούλης Modified over 5 years ago

Similar presentations

Presentation on theme: "Separation of colonospheres from differentiated tumor cells by cluster analysis. Separation of colonospheres from differentiated tumor cells by cluster."— Presentation transcript:

1 Separation of colonospheres from differentiated tumor cells by cluster analysis.
Separation of colonospheres from differentiated tumor cells by cluster analysis.A, Heat map of unsupervised cluster analysis of all identified proteins. B, Heat map of supervised cluster analysis of all significantly up- and down-regulated proteins (p < 0.05 according to the Fisher exact test per pair.) The selected list of regulated proteins separates colonospheres from differentiated tumor cells. WJ Van Houdt et al. Mol Cell Proteomics 2011;10:M © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.

Download ppt "Separation of colonospheres from differentiated tumor cells by cluster analysis. Separation of colonospheres from differentiated tumor cells by cluster."

Similar presentations

Correlation of log-transformed signal intensity from two Affymetrix microarray hybridizations using platelet RNA. Plotted are those probesets with an average.

Correlation of log-transformed signal intensity from two Affymetrix microarray hybridizations using platelet RNA. Plotted are those probesets with an average.
Sequence alignment of C-terminal phosphorylated plant aquaporins

Sequence alignment of C-terminal phosphorylated plant aquaporins
Phosphorylation and sequence disorder in microtubule-associated protein Tau.A, schematic illustration of the domain profile of Tau with all known phosphorylation.

Phosphorylation and sequence disorder in microtubule-associated protein Tau.A, schematic illustration of the domain profile of Tau with all known phosphorylation.
Distribution of phosphorylation sites identified in the cytosolic phosphoproteome.A, numbers of approved phosphopeptides, previously phosphorylated peptides,

Distribution of phosphorylation sites identified in the cytosolic phosphoproteome.A, numbers of approved phosphopeptides, previously phosphorylated peptides,
Percentage of proteins identified in envelope membrane extracts according to the purification method and the number of transmembrane domains. Percentage.

Percentage of proteins identified in envelope membrane extracts according to the purification method and the number of transmembrane domains. Percentage.
Illustration of matched (FL-IFN-γR2/GFP and IFN-γR1/EBFP) and mismatched (IFN-γR1/EBFP and FL-IL-10R2/GFP) pairs of receptors. Illustration of matched.

Illustration of matched (FL-IFN-γR2/GFP and IFN-γR1/EBFP) and mismatched (IFN-γR1/EBFP and FL-IL-10R2/GFP) pairs of receptors. Illustration of matched.
Frequency distribution of the GRAVY of the theoretical proteins (open bars) and of 110 genes encoding proteins identified on a 2-D electrophoresis gel,

Frequency distribution of the GRAVY of the theoretical proteins (open bars) and of 110 genes encoding proteins identified on a 2-D electrophoresis gel,
Time course of phosphorylation changes at Ser-293, Ser-300, and Ser-232 in PDHE1α following kinase inhibition with DCA. A, relative quantitation over three.

Time course of phosphorylation changes at Ser-293, Ser-300, and Ser-232 in PDHE1α following kinase inhibition with DCA. A, relative quantitation over three.
Two-dimensional electrophoresis results and validation with Western blotting. Two-dimensional electrophoresis results and validation with Western blotting.

Two-dimensional electrophoresis results and validation with Western blotting. Two-dimensional electrophoresis results and validation with Western blotting.
Distributions of the ELDP values and Mascot scores for all protein identifications.a, frequency of ELDP value returned by correct (gray bars) and incorrect.

Distributions of the ELDP values and Mascot scores for all protein identifications.a, frequency of ELDP value returned by correct (gray bars) and incorrect.
Significantly enriched phosphorylation motifs from up-regulated phosphopeptides by Motif-X analysis. Significantly enriched phosphorylation motifs from.

Significantly enriched phosphorylation motifs from up-regulated phosphopeptides by Motif-X analysis. Significantly enriched phosphorylation motifs from.
Visual validation of the computational outputs.

Visual validation of the computational outputs.
Frequency distribution of the effect size measure (ESM) of sperm protein spots of type-1 diabetic (A), type-2 diabetic (B) and non-diabetic obese (C) patients.

Frequency distribution of the effect size measure (ESM) of sperm protein spots of type-1 diabetic (A), type-2 diabetic (B) and non-diabetic obese (C) patients.
Schematic representation of proteogenomic annotation strategy.

Schematic representation of proteogenomic annotation strategy.
Novel p53 target genes identified by RNA-Seq, pSILAC and ChIP-Seq.

Novel p53 target genes identified by RNA-Seq, pSILAC and ChIP-Seq.
Assay of NOS activity. Assay of NOS activity. Box show total NOS activity, the calcium-dependent activity of the constitutive isoforms of NOS (eNOS and.

Assay of NOS activity. Assay of NOS activity. Box show total NOS activity, the calcium-dependent activity of the constitutive isoforms of NOS (eNOS and.
Relative abundance of proteins identified in MALDI IMS

Relative abundance of proteins identified in MALDI IMS
Bottom-up proteomic characterization of MALDI IMS samples.

Bottom-up proteomic characterization of MALDI IMS samples.
Representative example of LAXIC performance for complex plant phosphoproteome. Representative example of LAXIC performance for complex plant phosphoproteome.A.

Representative example of LAXIC performance for complex plant phosphoproteome. Representative example of LAXIC performance for complex plant phosphoproteome.A.
Success rates in validation of antibodies from external providers

Success rates in validation of antibodies from external providers

Similar presentations

Ads by Google