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ProteomicsChasing protein arginine phosphorylation: development of a selective enrichment method using a trapping mutant phosphatase
Proof-of-principle pull-down experiments using a YwlE trapping mutant phosphatase to selective capture arginine phosphorylated proteins. Phosphoarginine is an acid labile protein modification that was demonstrated to exist in bacteria and probably also in higher eukaryotes. Due to the high abundance...
ORGANISM(S): Bacteria Bacillus subtilis subsp. subtilis str. 168 
2014-05-19 | PXD000560 | Pride
Arginie phosphorylation Trapping mutant phosphatase 
ProteomicsSystematic Identification of SHP2 Phosphatase Substrates
Phosphatases play essential roles in normal cell physiology and diseases like cancer. The challenges of studying phosphatases have limited our understanding of their substrates, molecular mechanisms, and unique functions within highly complicate networks. Here we introduce a novel strategy using sub...
ORGANISM(S): Homo sapiens (Human) 
2022-09-20 | PXD028404 | Pride
Phosphoproteomics Tyrosine phosphatase substrates Lc-ms Shp2 
ProteomicsVascular endothelial protein tyrosine phosphatase: Identification of novel cell junction-related substrates and a ternary receptor complex with EPHB4 and TIE2
Vascular endothelial protein tyrosine phosphatase (VE-PTP, PTPRB) is a receptor type phosphatase that is crucial for the regulation of endothelial junctions and blood vessel development. VE-PTP regulates vascular integrity by dephosphorylating substrates which are key players in endothelial junction...
ORGANISM(S): Mus musculus (Mouse) 
2019-08-20 | PXD011940 | Pride
Lc-msms Mouse Tyrosine phosphatase Endothelial cells Substrate trapping 
UnknownCharacterization of PTPRG in knockdown and phosphatase-inactive mutant mice and substrate trapping analysis of PTPRG in mammalian cells.
Not available
S-EPMC3447766 | biostudies-literature
UnknownA substrate-trapping strategy for protein phosphatase PP1 holoenzymes using hypoactive subunit fusions.
Not available
S-EPMC6166715 | biostudies-literature
ProteomicsPPM1H phosphatase counteracts LRRK2 signaling by selectively dephosphorylating Rab proteins
Mutations that activate LRRK2 protein kinase cause Parkinson’s disease. LRRK2 phosphorylates a subset of Rab GTPases within their Switch-II motif controlling interaction with effectors. An siRNA screen of all protein phosphatases revealed that a poorly studied protein phosphatase, PPM1H, counteracts...
ORGANISM(S): Homo sapiens (Human) 
2019-11-06 | PXD014794 | Pride
Lrrk2 Phosphatase Parkinson's disease Rab10 
ProteomicsQuantitative Proteomics Identifies Protein Tyrosine Phosphatase 1B as Modulator of B Cell Antigen Receptor Signaling
B cell antigen receptor (BCR) signaling is initiated by protein kinases and limited by counteracting phosphatases that currently are less well studied in their regulation of BCR signaling. We here used the B cell line Ramos to identify and quantify human B cell signaling components. Specifically, a ...
ORGANISM(S): Homo sapiens (Human) 
2022-02-16 | PXD024086 | Pride
Ramos b cells Ptp1b Bcr signaling Co-ip Silac Substrate trapping 
UnknownChasing Phosphoarginine Proteins: Development of a Selective Enrichment Method Using a Phosphatase Trap.
Not available
S-EPMC4125729 | biostudies-literature
UnknownTrapping the tetrahedral intermediate in the alkaline phosphatase reaction by substitution of the active site serine with threonine.
Not available
S-EPMC2242381 | biostudies-literature
ProteomicsMutant KRAS-associated proteome is mainly controled by exogenous factors
KRAS signaling has been extensively studied, yet the clarification between KRAS-autonomous and non-autonomous mechanisms are still less explored. Understanding how KRAS signaling and effects are affected by exogenous stimuli can provide valuable insights not only to understand resistance mechanisms ...
ORGANISM(S): Homo sapiens (Human) 
2022-04-06 | PXD030551 | Pride
Mutant kras  colorectal cancer  cancer associated-fibroblasts  proteomic analysis 
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