Presentation is loading. Please wait.

Presentation is loading. Please wait.

Schematic illustration of the assembly and interactions of sperm-bound eppin protein complex (EPC) components. Schematic illustration of the assembly and.

Published byLester Miller Modified over 5 years ago

Similar presentations

Presentation on theme: "Schematic illustration of the assembly and interactions of sperm-bound eppin protein complex (EPC) components. Schematic illustration of the assembly and."— Presentation transcript:

1 Schematic illustration of the assembly and interactions of sperm-bound eppin protein complex (EPC) components. Schematic illustration of the assembly and interactions of sperm-bound eppin protein complex (EPC) components. EPN, eppin; CLU, clusterin; LTF, lactotransferrin; SEMG1, semenogelin-1. Because of limited data availability, stoichiometric aspects of EPC subunit composition and assembly have not been considered. Disulfide bonds that appear to be critical for EPC structure and function are indicated (CysX, cysteine residue of the eppin75–133 C-terminal fragment (39); CysA, CysB, cysteine residues of clusterin α and β subunits, respectively). Uwe Paasch et al. Mol Cell Proteomics 2011;10:M © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.

Download ppt "Schematic illustration of the assembly and interactions of sperm-bound eppin protein complex (EPC) components. Schematic illustration of the assembly and."

Similar presentations

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.
Novel phosphorylation sites on H+-ATPase proteins

Novel phosphorylation sites on H+-ATPase proteins
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.
Comparison of protein synthesis patterns of L

Comparison of protein synthesis patterns of L
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,
Complementary identification and novel protein discovery

Complementary identification and novel protein discovery
Top-down protein identification.

Top-down protein identification.
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.
Two-dimensional gel silver staining and two-dimensional immunoblotting using antibody to 3-nitrotyrosine. Two-dimensional gel silver staining and two-dimensional.

Two-dimensional gel silver staining and two-dimensional immunoblotting using antibody to 3-nitrotyrosine. Two-dimensional gel silver staining and two-dimensional.
Relative abundance of proteins identified in MALDI IMS

Relative abundance of proteins identified in MALDI IMS
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.

Similar presentations

Ads by Google