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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 
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 
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
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 
ProteomicsIdentification of host PDZ-based interactions with SARS-CoV-2 E protein in human monocytes
PDZ (Post-synaptic density, PSD-95)/ Disc large, Dlg/ Zonula occludens, ZO-1) proteins are central in the assembly of multiprotein signalling complexes that are formed in distinctive, specialized cell regions. In these complexes different signals are orchestrated and traduced into quick and efficien...
ORGANISM(S): Homo sapiens (Human) 
2023-10-24 | PXD042620 | Pride
Viral targeting Sars-cov-2 Macrophage Innate immune response Syntenin Zo-2 Pdz Monocyte Il-16 Coronavirus Envelope e protein 
ProteomicsMultisite phosphorylation of intrinsically disordered region of Dishevelled
When WNT binds to its receptor Frizzled (FZD) to activate the signaling, Dishevelled (DVL), the central component of Wnt signaling, is phosphorylated by redundant Casein kinase 1 (CK1) isoforms ε or δ, to transduce the signal downstream. Although the basic principles of Wnt signal transduction are k...
ORGANISM(S): Homo sapiens (Human) Escherichia coli 
2026-04-07 | PXD063470 | Pride
Dishevelled Phosphorylation Hdx-ms 
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 
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
GenomicsLPS-induced systemic inflammation is suppressed by the PDZ motif peptide of ZO-1 via regulation of macrophage M1/M2 polarization
LPS-induced systemic inflammation is suppressed by the PDZ motif peptide of ZO-1 via regulation of macrophage M1/M2 polarization
PRJNA1152345 | ENA
TranscriptomicsLPS-induced systemic inflammation is suppressed by the PDZ motif peptide of ZO-1 via regulation of macrophage M1/M2 polarization
The gram-negative bacterium lipopolysaccharide (LPS) is frequently administered to generate models of systemic inflammation. In particular, both kidney and lung are more sensitive to acute injury caused by LPS-induced systemic inflammation. However, there are several side effects and no effective tr...
ORGANISM(S): Homo sapiens 
2024-09-15 | GSE275635 | GEO
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