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ProteomicsComparison of culture supernatants from wild-type Vibrio cholerae and a mutant lacking the PDZ domain of the type II secretion system
The culture supernatant of wild-type (WT) Vibrio cholerae N16961 and mutant epsC∆PDZ strains were compared to determine which, if any, type II secretion system substrates were affected by the deletion of the PDZ domain of EpsC
ORGANISM(S): Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) 
2025-08-25 | PXD062995 | Pride
Vibrio cholerae T2ss Pdz Protein secretion Gspc 
GenomicsAllosteric and energetic remodeling of a PDZ domain by protein domain extensions
Allosteric and energetic remodeling of a PDZ domain by protein domain extensions
PRJNA1276451 | ENA
ProteomicsMS analysis of photocrosslink adducts for the mapping of interaction sites of selective engineered PSD-95 PDZ domain ligands
Designing highly specific modulators of protein-protein interactions (PPIs) is especially challenging in the context of multiple paralogs and conserved interaction surfaces. In this case, direct generation of selective and competitive inhibitors is hindered by high similarity within the evolutionary...
ORGANISM(S): Rattus norvegicus (Rat) 
2019-11-12 | PXD015366 | Pride
Engineered ligand/pdz domains/photocrosslinking/p-azidophenylalanine 
ProteomicsMS analysis of cellular targets of an engineered selective PSD-95 PDZ domain ligand
Designing highly specific modulators of protein-protein interactions (PPIs) is especially challenging in the context of multiple paralogs and conserved interaction surfaces. In this case, direct generation of selective and competitive inhibitors is hindered by high similarity within the evolutionary...
ORGANISM(S): Rattus norvegicus (Rat) 
2019-11-12 | PXD015313 | Pride
Engineered ligand/pdz domains/pull-down 
TranscriptomicsThe PDZ-binding motif of SARS-CoV envelope protein is a determinant of viral pathogenesis
A recombinant SARS-CoV lacking the envelope (E) protein is attenuated in vivo. Here we report that E protein PDZ-binding motif (PBM), a domain involved in protein-protein interactions, is a major virulence determinant in vivo. Elimination of SARS-CoV E protein PBM by using reverse genetics led to at...
ORGANISM(S): Mus musculus 
2014-10-31 | E-GEOD-52920 | biostudies-arrayexpress
TranscriptomicsGene expression profile associated with the PDZ ligand-motif of HPV16-E6 oncoprotin in the skin of transgenic mice models
The K14E6 transgenic mice developskin hyperplasia,benign tumors and skin cancer. The tumor formation capacity diminishes when E6 lacks its PDZ ligand-motif. This study aims to compare the transciptional profiles of transgenic K14E6 mice with K14E6 Δ146-151 (lacking the PDZ domain) in order to explor...
ORGANISM(S): Mus musculus 
2010-07-27 | E-GEOD-22417 | biostudies-arrayexpress
OtherAllosteric and energetic remodeling of a PDZ domain by protein domain extensions
Many functions of proteins are performed by independently folding structural units called domains. These domains are structurally conserved but not identical in different proteins. Here, to understand the consequences for regulation and evolvability of domain extensions, we quantify the energetic ef...
ORGANISM(S): Saccharomyces cerevisiae 
2025-07-25 | GSE299757 | GEO
ProteomicsQuantitative fragmentomics to map affinities of interactomes
~500,000 protein interactions have been identified in human but most binding affinities remain unknown, limiting quantitative investigation of interactome-function relationships. This gap can be filled by systematically measuring the affinities of minimal interacting protein fragments, the building ...
ORGANISM(S): Homo sapiens (Human) 
2022-10-14 | PXD027743 | Pride
Complexome Pdz Domain-motif interaction Interactome 
TranscriptomicsThe HPV16-E6 oncoprotein induces the expression of Keratin-6b and 2 delays wound healing by means of its PDZ-ligand domain in vivo
The K14E6 transgenic mice develop skin hyperplasia, benign tumors, and cancer in the dorsal skin spontaneously. The E6 oncoprotein own its tumorigenic potential to a region located near the C-Terminal domain, better known as the PDZ ligand-domain. The aim of this work was to describe early cellular ...
ORGANISM(S): Mus musculus 
2017-11-30 | GSE99868 | GEO
UnknownA molecular-properties-based approach to understanding PDZ domain proteins and PDZ ligands.
Not available
S-EPMC1524865 | biostudies-literature
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