Results 21 to 30 of about 3,948,731 (294)

Regulation of Phosphoinositide Levels in the Retina by Protein Tyrosine Phosphatase 1B and Growth Factor Receptor-Bound Protein 14

open access: yesBiomolecules, 2021
Protein tyrosine kinases and protein phosphatases play a critical role in cellular regulation. The length of a cellular response depends on the interplay between activating protein kinases and deactivating protein phosphatases.
Raju V. S. Rajala   +4 more
doaj   +1 more source

A role for the protein tyrosine phosphatase CD45 in macrophage adhesion through the regulation of paxillin degradation. [PDF]

open access: yesPLoS ONE, 2013
CD45 is a protein tyrosine phosphatase expressed on all cells of hematopoietic origin that is known to regulate Src family kinases. In macrophages, the absence of CD45 has been linked to defects in adhesion, however the molecular mechanisms involved ...
Joëlle St-Pierre, Hanne L Ostergaard
doaj   +1 more source

Protein-tyrosine phosphorylation interaction network in Bacillus subtilis reveals new substrates, kinase activators and kinase cross-talk.

open access: yesFrontiers in Microbiology, 2014
Signal transduction in eukaryotes is generally transmitted through phosphorylation cascades that involve a complex interplay of transmembrane receptors, protein kinases, phosphatases and their targets.
Lei eShi   +9 more
doaj   +1 more source

The protein tyrosine kinases EpsB and PtkA differentially affect biofilm formation in Bacillus subtilis [PDF]

open access: yes, 2014
The Gram-positive soil bacterium Bacillus subtilis is able to choose between motile and sessile lifestyles. The sessile way of life, also referred to as biofilm, depends on the formation of an extracellular polysaccharide matrix and some extracellular ...
Stanley-Wall, Nicola   +6 more
core   +1 more source

High-throughput profiling of sequence recognition by tyrosine kinases and SH2 domains using bacterial peptide display

open access: yeseLife, 2023
Tyrosine kinases and SH2 (phosphotyrosine recognition) domains have binding specificities that depend on the amino acid sequence surrounding the target (phospho)tyrosine residue.
Allyson Li   +4 more
doaj   +1 more source

Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases [PDF]

open access: yes, 2009
Background: The c-Cbl-associated protein (CAP), also known as ponsin, localizes to focal adhesions and stress fibers and is involved in signaling events.
Tomasovic, Ana   +11 more
core   +1 more source

The Oncogenic Signaling Disruptor, NDRG1: Molecular and Cellular Mechanisms of Activity

open access: yesCells, 2021
NDRG1 is an oncogenic signaling disruptor that plays a key role in multiple cancers, including aggressive pancreatic tumors. Recent studies have indicated a role for NDRG1 in the inhibition of multiple tyrosine kinases, including EGFR, c-Met, HER2 and ...
Jason Chekmarev   +2 more
doaj   +1 more source

Role of protein phosphorylation in cell signaling, disease, and the intervention therapy

open access: yesMedComm, 2022
Protein phosphorylation is an important post‐transcriptional modification involving an extremely wide range of intracellular signaling transduction pathways, making it an important therapeutic target for disease intervention.
Kun Pang   +10 more
doaj   +1 more source

Tyrosine 402 phosphorylation of Pyk2 is involved in ionomycin-induced neurotransmitter release. [PDF]

open access: yesPLoS ONE, 2014
Protein tyrosine kinases, which are highly expressed in the central nervous system, are implicated in many neural processes. However, the relationship between protein tyrosine kinases and neurotransmitter release remains unknown.
Zhao Zhang   +9 more
doaj   +1 more source

Receptor-specific regulation of phosphatidylinositol 3'-kinase activation by the protein tyrosine phosphatase Shp2 [PDF]

open access: yes, 2002
Receptor tyrosine kinases (RTKs) play distinct roles in multiple biological systems. Many RTKs transmit similar signals, raising questions about how specificity is achieved.
Zhang, S.   +13 more
core   +1 more source

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