Results 81 to 90 of about 1,485,018 (348)

The structural features of Trask that mediate its anti-adhesive functions.

PLoS ONE, 2011
Trask/CDCP1 is a transmembrane protein with a large extracellular and small intracellular domains. The intracellular domain (ICD) undergoes tyrosine phosphorylation by Src kinases during anchorage loss and, when phosphorylated, Trask functions to inhibit
Danislav S Spassov, Deepika Ahuja, Ching Hang Wong, Mark M Moasser   +3 more
doaj   +1 more source

Tyrosine Phosphorylation Regulates Maturation of Receptor Tyrosine Kinases [PDF]

Molecular and Cellular Biology, 2005
Constitutive activation of receptor tyrosine kinases (RTKs) is a frequent event in human cancer cells. Activating mutations in Fms-like tyrosine kinase 3 (FLT-3), notably, internal tandem duplications in the juxtamembrane domain (FLT-3 ITD), have been causally linked to acute myeloid leukemia.
Dirk-E, Schmidt-Arras, Annette, Böhmer, Boyka, Markova, Chunaram, Choudhary, Hubert, Serve, Frank-D, Böhmer   +5 more
openaire   +2 more sources

In vitro and in silico modelling of ROS1‐positive non‐small cell lung cancer reveals fusion‐dependent tyrosine kinase inhibitor responses

Molecular Oncology, EarlyView.
Drug resistance limits treatment success in a subset of lung cancers driven by ROS1 gene alterations. Using patient‐derived cells and computer simulations, we studied three key mutations and how they affect five targeted drugs. The mutations reduced drug effectiveness in different ways by altering protein structure and behavior.
Farhan Ul Haq, Marc Terrones, Felicia Rodrigues Fortes, Anne Schepers, Alessia Denis, Christophe Deben, Ken Op de Beeck, Guy Van Camp, Geert Vandeweyer   +8 more
wiley   +1 more source

Tyrosine phosphorylation of mitochondrial pyruvate dehydrogenase kinase 1 is important for cancer metabolism

Molecules and Cells, 2011
SUMMARY Many tumor cells rely on aerobic glycolysis instead of oxidative phosphorylation for their continued proliferation and survival. Myc and HIF-1 are believed to promote such a metabolic switch by, in part, upregulating gene expression of pyruvate ...
T. Hitosugi, Jun Fan, Tae-Wook Chung, Katherine Lythgoe, Xu Wang, Jianxin Xie, Q. Ge, T. Gu, R. Polakiewicz, J. Roesel, Z. Chen, T. Boggon, S. Lonial, H. Fu, F. Khuri, Su-Min Kang, Jing Chen   +16 more
semanticscholar   +1 more source

Receptor for activated C kinase-1 facilitates protein kinase C-dependent phosphorylation and functional modulation of GABA(A) receptors with the activation of G-protein-coupled receptors [PDF]

, 2002
GABA(A) receptors are the principal sites of fast synaptic inhibition in the brain. These receptors are hetero-pentamers that can be assembled from a number of subunit classes: alpha(1-6), beta(1-3), gamma(1-3), delta(1), epsilon, theta, and pi, but the ...
Trevor G Smart, Brandon, NJ, Jovanovic, JN, Moss, SJ, Stephen J Moss, Smart, TG, Nicholas J Brandon, Jasmina N Jovanovic   +7 more
core  

Somatostatin receptor 4 (SSTR4) is a tumor suppressor in cutaneous and head & neck squamous cell carcinomas

Molecular Oncology, EarlyView.
This study identifies somatostatin receptor 4 (Sstr4) as a critical tumor suppressor against skin and head/neck cancers (HNSCC, cSCC, and BCC). The loss of Sstr4 removes a check on cell growth, causing hyperactivation of the MAPK‐ERK signaling pathway (↑).
Ali Taqvi, Tuan Khang Huynh, Adway Kadam, Zahra Kardan, Yue Yan, Amina Jamal Laham, Sampath Kumar Loganathan   +6 more
wiley   +1 more source

Tyrosine phosphorylation: thirty years and counting

Current Opinion in Cell Biology, 2009
In the 30 years since its discovery, tyrosine phosphorylation has emerged as a fundamentally important mechanism of signal transduction and regulation in all eukaryotic cells, governing many processes, including cell proliferation, cell cycle progression,
T. Hunter
semanticscholar   +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

Protein kinase A (PKA) phosphorylation of Shp2 inhibits its phosphatase activity and modulates ligand specificity. [PDF]

, 2015
Pathological cardiac hypertrophy (an increase in cardiac mass resulting from stress-induced cardiac myocyte growth) is a major factor underlying heart failure.
O'Bryan, JP, Burmeister, BT, Wang, L, Gold, MG, Carnegie, GK, Skidgel, RA   +5 more
core  

Partial FAK suppression promotes tumor growth, an effect reversed by macrophage p110δ PI3K inactivation

Molecular Oncology, EarlyView.
Partial inhibition of focal adhesion kinase (FAK) can paradoxically promote tumor growth, rather than simply producing a weaker antitumor effect than that observed with strong FAK suppression. In breast cancer and melanoma models, targeting p110δ PI3K, particularly in macrophages, counteracted these tumor‐promoting effects, highlighting the importance ...
Lydia Xenou, Niki Tzenaki, Anna Tsapara, Maria Tzardi, Evangelia A. Papakonstanti   +4 more
wiley   +1 more source