Results 31 to 40 of about 288,999 (305)

ErbB2 signaling in breast cancer : the role of ErbB, Akt and ShcA phosphorylation [PDF]

, 2004
Breast cancer is the most common malignancy in women and is estimated to account for more than 200,000 new cancer cases in the United States in the year 2002. It now represents the second leading cause of death (40,000) from cancer in women.
Cicenas, Jonas
core   +1 more source

Angiotensin II impairs endothelial function via tyrosine phosphorylation of the endothelial nitric oxide synthase [PDF]

, 2009
Proline-rich tyrosine kinase 2 (PYK2) can be activated by angiotensin II (Ang II) and reactive oxygen species. We report that in endothelial cells, Ang II enhances the tyrosine phosphorylation of endothelial NO synthase (eNOS) in an AT1-, H2O2-, and PYK2-
Loot, Annemarieke E., Ingrid Fleming, Annemarieke E. Loot, Fißlthaler, Beate, Fleming, Ingrid, Judith G. Schreiber, Beate Fisslthaler, Schreiber, Judith G.   +7 more
core   +1 more source

Marburg virus evades interferon responses by a mechanism distinct from ebola virus.

PLoS Pathogens, 2010
Previous studies have demonstrated that Marburg viruses (MARV) and Ebola viruses (EBOV) inhibit interferon (IFN)-alpha/beta signaling but utilize different mechanisms. EBOV inhibits IFN signaling via its VP24 protein which blocks the nuclear accumulation
Charalampos Valmas, Melanie N Grosch, Michael Schümann, Judith Olejnik, Osvaldo Martinez, Sonja M Best, Verena Krähling, Christopher F Basler, Elke Mühlberger   +8 more
doaj   +1 more source

Erythropoietin-induced serine 727 phosphorylation of STAT3 in erythroid cells is mediated by a MEK-, ERK-, and MSK1-dependent pathway [PDF]

, 2003
Objective. Erythropoietin (EPO) is a key regulator of erythropoiesis, playing a role in both the proliferation and differentiation of erythroid cells.
Eggen, BJL, Vellenga, E, Vellenga, Edo,, Vogelzang, Irma, Eggen, BJL; id_orcid, Vogelzang, Irma,, Wierenga, Albertus T.J., Wierenga, Albertus T.J.,, Eggen, Bart J.L.,   +8 more
core   +1 more source

Tyrosine phosphorylation of WW proteins [PDF]

Experimental Biology and Medicine, 2015
A number of key regulatory proteins contain one or two copies of the WW domain known to mediate protein–protein interaction via proline-rich motifs, such as PPxY. The Hippo pathway components take advantage of this module to transduce tumor suppressor signaling.
Nina, Reuven, Matan, Shanzer, Yosef, Shaul   +2 more
openaire   +2 more sources

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

PLoS 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, Yun Zhang, Zheng Mou, Shifeng Chu, Xiaoyu Chen, Wenbin He, Xiaofeng Guo, Yuhe Yuan, Masami Takahashi, Naihong Chen   +9 more
doaj   +1 more source

T cell development and T cell responses in mice with mutations affecting tyrosines 292 or 315 of the ZAP-70 protein tyrosine kinase [PDF]

, 2001
After stimulation of the T cell receptor (TCR), the tyrosine residues 292 and 315 in interdomain B of the protein tyrosine kinase ZAP-70 become phosphorylated and plausibly function as docking sites for Cbl and Vav1, respectively. The two latter proteins
Magnan, A, Anne Gillet, Arrieumerlou, C, Antoine Magnan, Boyer, C, Malissen, Bernard, Vincenzo Di Bartolo, Mireille Richelme, Marie Malissen, Lin, YL, Gillet, A., Roure, A, Mura, A. M., Boyer, C., Malissen, B, Arrieumerlou, C., Malissen, M., Malissen, M, Roure, A., Richelme, M, Acuto, O, Lin, Y. L., Bernard Malissen, Claude Boyer, Malissen, B., Di Bartolo, V, Cécile Arrieumerlou, Yea-Lih Lin, Agnès Roure, Oreste Acuto, Mura, AM, Acuto, O., Richelme, M., Acuto, Oreste, Di Bartolo, V., Anne-Marie Mura, Gillet, A, Boyer, Claudine, Magnan, A.   +38 more
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Quercetin inhibits collagen-stimulated platelet activation through inhibition of multiple components of the glycoprotein VI signaling pathway [PDF]

, 2003
Background: The regulation of platelet function by pharmacological agents that modulate platelet signaling haspharmacolo proven a successful approach to the prevention of thrombosis.
Cicmil, M, Jordan, P.A., Sage, T., C. M. Williams, G. P. Hubbard, T. Sage, Lovegrove, J.A., Stevens, J M; id_orcid, P. A. Jordan, J. M. Gibbins, Hubbard, G.P., M. Cicmil, Sage, T, Gibbins, J.M., Williams, C M, Williams, C.M., Gibbins, J M, Jordan, P A, Lovegrove, J A, Hubbard, G P, Stevens, J.M., J. A. Lovegrove, J. M. Stevens, Cicmil, M.   +23 more
core   +1 more source

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

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

On the Extent of Tyrosine Phosphorylation in Chloroplasts [PDF]

Plant Physiology, 2015
Reanalysis of published mass spectrometry data on Tyr-phosphorylated chloroplast proteins indicates that the majority of peptide spectrum matches reporting Tyr phosphorylation are ambiguous.
Qintao, Lu, Stefan, Helm, Anja, Rödiger, Sacha, Baginsky   +3 more
openaire   +2 more sources