Results 71 to 80 of about 288,999 (305)

Peripherin Is Tyrosine‐Phosphorylated at Its Carboxyl‐Terminal Tyrosine [PDF]

Journal of Neurochemistry, 1998
Abstract: Peripherin is a type III intermediate filament present in peripheral and certain CNS neurons. We report here that peripherin contains a phosphotyrosine residue and, as such, is the only identified intermediate filament protein known to be modified in this manner.
J M, Angelastro, C L, Ho, T, Frappier, R K, Liem, L A, Greene   +4 more
openaire   +2 more sources

ABL kinase‐dependent phosphorylation of SH proteins promotes their direct interaction with CRK family SH2 domains

FEBS Letters, EarlyView.
CT10 regulator of kinase (CRK) and CRK‐Like (CRKL) are signaling adaptors driving cell adhesion, motility, differentiation, and proliferation. SH2‐domain containing (SH) proteins are enriched in YXXP motifs which when phosphorylated create preferred binding sites for CRK family SH2 domains.
Phoebe M. Cousens, Brendan W. Chandler, Anna M. Schmoker, Jaye L. Weinert, Charlotte A. Kearns, Warren T. Yacawych, Amila Šemić, Alicia M. Ebert, Bryan A. Ballif   +8 more
wiley   +1 more source

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

, 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, Stuelkel, Joerg, Gunka, Katrin, Stülke, Jörg, Stanley-Wall, Nicola; id_orcid, Gerwig, Jan, Kiley, Taryn B.   +6 more
core   +1 more source

Homodimerization and intermolecular tyrosine phosphorylation of the Tyk‐2 tyrosine kinase [PDF]

FEBS Letters, 1995
The Jak kinases and Stat transcription factors play a major role in signaling of various cytokines including IFNα. In this report we show a ligand‐independent interaction between Tyk‐2 and Jak‐1 kinases. We also demonstrate that the Tyk‐2 kinase forms a homodimer that has the ability to undergo intermolecular tyrosine phosphorylation.
Domanski, Paul, Yan, Hai, Witte, Michael M., Krolewski, John, Colamonici, Oscar R.   +4 more
openaire   +2 more sources

EDNRB‐dependent endothelin signaling reduces proliferation and promotes proneural‐to‐mesenchymal transition in gliomas

Molecular Oncology, EarlyView.
Glioma cells mainly express the endothelin receptor EDNRB, while EDNRA is restricted to a perivascular tumor subpopulation. Endothelin signaling reduces glioma cell proliferation while promoting migration and a proneural‐to‐mesenchymal transition associated with poor prognosis. This pathway activates Ca2+, K+, ERK, and STAT3 signalings and is regulated
Donovan Pineau, Leonor Garcia, Hugo Arnold, Antonija Hanžek, Maialen Arrieta, Laurent R Gauthier, Christine Granotier‐Beckers, François D Boussin, Amaury Herbet, Marie Hautière, Valentin Asei‐Ceschino, Clémentin Jacques, Laura Brard, Thomas Harnois, Valérie Coronas, Bruno Constantin, Aurélien Chatelier, Jean Chemin, Serge Urbach, Martial Seveno, Szimonetta Hideg, Chantal Ripoll, Kasandra Aguilar‐Cázarez, Min Zheng, Guo‐Hao Huang, Sheng‐Qing Lv, Lei Zhang, Philippe Rondard, Laurent Prezeau, Jean‐Philippe Pin, Hugues Duffau, Luc Bauchet, Valérie Rigau, Franck Denat, Charles Truillet, Didier Boquet, Jean‐Philippe Hugnot   +36 more
wiley   +1 more source

Disruption of fyn SH3 domain interaction with a proline-rich motif in liver kinase B1 results in activation of AMP-activated protein kinase [PDF]

, 2013
Fyn-deficient mice display increased AMP-activated Protein Kinase (AMPK) activity as a result of Fyn-dependent regulation of Liver Kinase B1 (LKB1) in skeletal muscle.
Bastie, Claire C., Yamada, Eijiro, Eijiro Yamada, Eijiro Yamada (187269), Claire C Bastie, Claire C. Bastie, Claire C. Bastie (187271)   +6 more
core   +1 more source

Heterozygous loss‐of‐function alleles associate the conserved 3′‐5′ exoribonuclease EXOSC10 with hypersensitivity to the anticancer drug 5‐fluorouracil

Molecular Oncology, EarlyView.
EXOSC10, an essential nuclear RNA exosome‐associated 3′‐5′ exoribonuclease, is inhibited by the anticancer drug 5‐fluorouracil (5‐FU), and EXOSC10 depletion increases 5‐FU sensitivity. The colon‐cancer variant EXOSC10S402T, located in a proteolysis motif, is stable and nuclear but nonfunctional in vivo.
Radhika Sain, Yann Le Page, Frédéric Percevault, Emmanuelle Becker, Luc Negroni, Almudena Fernandez, Marta Cantero, Diego Muñoz‐Santos, Lluís Montoliu, Cyrille Garnier, Michael Primig   +10 more
wiley   +1 more source

Genome-wide analysis to predict protein sequence variations that change phosphorylation sites or their corresponding kinases [PDF]

, 2008
We define phosphovariants as genetic variations that change phosphorylation sites or their interacting kinases. Considering the essential role of phosphorylation in protein functions, it is highly likely that phosphovariants change protein functions and ...
Pamela Song, Kyu-Won Kim, Jong Hun Kim, Kyung-Soo Oh, Gil-Mi Ryu   +4 more
core   +1 more source

Molecular networks in FGF signaling: Flotillin-1 and Cbl-associated protein compete for the binding to fibroblast growth factor receptor substrate 2 [PDF]

, 2012
Fibroblast growth factor receptor substrate 2 (FRS2α) is a signaling adaptor protein that regulates downstream signaling of many receptor tyrosine kinases.
Traub Stephanie, Tomasovic, Ana, Stephanie Traub, Ana Tomasovic, Ana Tomasovic (189773), Ritva Tikkanen (189783), Tikkanen Ritva, Tikkanen, Ritva, Traub, Stephanie, Tomasovic Ana, Ritva Tikkanen, Stephanie Traub (189777)   +11 more
core   +1 more source

Phosphorylation and identification of a major tyrosine phosphorylation site in protein tyrosine phosphatase 1C.

Journal of Biological Chemistry, 1994
Protein tyrosine phosphatase 1C (PTP1C) was the first member of the protein tyrosine phosphatase family demonstrated to contain the src homology 2 (SH2) domain. This enzyme is believed to play a role in regulating downstream signaling in hematopoietic cells since it was predominantly expressed in these cells.
E. H. Fischer, F. Dumas, Denis Banville, Zhizhuang Zhao, Patrice Bouchard, Shi-Hsiang Shen   +5 more
openaire   +4 more sources