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ProteomicsWW domain activated extracellular vesicles (WAEV) proteome
Extracellular vesicles (EVs), spherical nano-sized lipid-bilayer vesicular structure, is produced from host cells, and widely studied in microbiology, neurobiology, and bioengineering as drug delivery. Here, we report the new vaccine platform using a novel type of EVs, WW domain activated extracellu...
ORGANISM(S): Homo sapiens (Human) 
2023-01-30 | PXD033178 | Pride
Vaccine Ww domain Extracellular vesicles 
ProteomicsHuman WW-domain containing proteins TAP-LC-MSMS
To systematically investigate the regulations and functions of human WW-domain containing proteins, we conducted a proteomic analysis of 26 full-length WW-domain containing proteins and 17 WW-domains only, and identified their associated protein complexes in human HEK293T cells using tandem affinity...
ORGANISM(S): Homo sapiens (Human) 
2019-12-02 | PXD004649 | Pride
Human Lc-msms Ww-domain containing proteins Tap 
ProteomicsBAG3 regulates cilia homeostasis of glioblastoma via its WW domain
The multidomain protein BAG3 exerts pleiotropic oncogenic functions in many tumor entities including glioblastoma (GBM). Here we compared BAG3 protein-protein interactions in either adherently cultured or stem-like cultured U251 GBM cells. In line with BAG3´s putative role in stemness, identified in...
ORGANISM(S): Homo sapiens (Human) 
2024-04-09 | PXD050279 | Pride
Cilia homeostasis Stemness Yap1 Ww domain Glioblastoma Bag3 Yap1 signaling Primary cilia 
GenomicsRegulation of Microprocessor assembly and localization via Pasha’s WW domain in C. elegans
Regulation of Microprocessor assembly and localization via Pasha’s WW domain in C. elegans
PRJNA1099906 | ENA
GenomicsRegulation of Microprocessor assembly and localization via Pasha’s WW domain in C. elegans
Primary microRNA (pri-miRNA) transcripts are processed by a protein complex called the Microprocessor comprised of the ribonuclease Drosha and its RNA binding partner DGCR8/Pasha. We sequenced small RNAs from animals containing a mutation in the WW domain of C. elegans pash-1. We found that these mu...
ORGANISM(S): Caenorhabditis elegans 
2024-04-16 | GSE263914 | GEO
ProteomicsStructural Insights into Mycobacterial Protein-Mannosyltransferase: Evidence of a WW-Domain-Like Substrate Recognition Mechanism.
We have previously demonstrated that protein-O-mannosylation (POM), a widespread post-translational glycosyl modification of proteins, is a key virulence factor of Mycobacterium tuberculosis (Mt), the world’s deadliest infectious agent. Here, we report a detailed analysis of the structure-function r...
ORGANISM(S): Escherichia coli 
2025-07-22 | PXD065654 | Pride
Glycosylation Entire protein analysis Protein-o-mannosylation Glycoprotein 
UnknownDocking analysis of verteporfin with YAP WW domain.
Not available
S-EPMC5602291 | biostudies-literature
UnknownStructure-function-folding relationship in a WW domain.
Not available
S-EPMC1502286 | biostudies-literature
UnknownStructural basis for polyproline recognition by the FE65 WW domain.
Not available
S-EPMC2693091 | biostudies-literature
UnknownEnzyme-linked enzyme-binding assay for Pin1 WW domain ligands.
Not available
S-EPMC2876714 | biostudies-literature
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