Results 11 to 20 of about 514,942 (384)

Activation of receptor protein-tyrosine kinases from the cytoplasmic compartment [PDF]

Journal of Biochemistry, 2012
It is widely accepted that receptor protein-tyrosine kinases (RTKs) are activated upon dimerization by binding to their extracellular ligands. However, EGF receptor (EGFR) dimerization per se does not require ligand binding. Instead, its cytoplasmic kinase domains have to form characteristic head-to-tail asymmetric dimers to become active, where one ...
Tohru Tezuka, Yuji Yamanashi, Kazumasa Yokoyama   +2 more
openaire   +4 more sources

Receptor Protein Tyrosine Kinases and Phosphatases

Cold Spring Harbor Symposia on Quantitative Biology, 1992
It is clear that the number of receptor PTKs and PTPs encoded by a typical vertebrate genome is rather large. Although the signal pathways activated by the receptor PTKs may in many cases be common, specificity is provided by the ligand-binding domain and the availability of ligand.
David S. Middlemas, P van der Geer, Richard A. Lindberg, Tony Hunter, S. Tracy   +4 more
openaire   +4 more sources

Characterization of B61, the Ligand for the Eck Receptor Protein-Tyrosine Kinase [PDF]

Journal of Biological Chemistry, 1995
B61 was originally described as a novel secreted tumor necrosis factor-alpha-inducible gene product in endothelial cells (Holzman, L. B., Marks, R. M., and Dixit, V. M. (1990) Mol. Cell. Biol. 10, 5830-5838). It was recently discovered that soluble recombinant B61 could serve as a ligand for the Eck receptor protein-tyrosine kinase, a member of the Eph/
Vishva M. Dixit, Akhilesh Pandey, Haining Shao, Michael F Seldin, K. S. O'shea   +4 more
openaire   +4 more sources

CD5 acts as a tyrosine kinase substrate within a receptor complex comprising T-cell receptor zeta chain/CD3 and protein-tyrosine kinases p56lck and p59fyn.

Proceedings of the National Academy of Sciences of the United States of America, 1992
Karl Burgess, Masahiro Yamamoto, Kartik Prasad, Christopher E. Rudd   +3 more
openalex   +2 more sources

Tyrosine phosphorylation controls brassinosteroid receptor activation by triggering membrane release of its kinase inhibitor [PDF]

, 2011
Receptor tyrosine kinases control many critical processes in metazoans, but these enzymes appear to be absent in plants. Recently, two Arabidopsis receptor kinases-BRASSINOSTEROID INSENSITIVE 1 (BRI1) and BRI1-ASSOCIATED KINASE1 (BAK1), the ...
Belkhadir, Youssef, Chory, Joanne, Dabi, Tsegaye, Hothorn, Michael, Jaillais, Yvon, Meyerowitz, Elliot M., Nimchuk, Zachary L.   +6 more
core   +4 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

Association of the erythropoietin receptor with protein tyrosine kinase activity. [PDF]

Proceedings of the National Academy of Sciences, 1992
We have examined the signal transduction mechanism of the hematopoietic growth factor erythropoietin (Epo). Epo stimulation of Ba/F3 cells transfected with the Epo receptor resulted in increases in tyrosine phosphorylation of proteins of 97, 75, and 55 kDa.
William L. Farrar, Gerald A. Evans, Alan D. D'Andrea, Diana Linnekin   +3 more
openaire   +2 more sources

Tyrosine phosphorylation of the BRI1 receptor kinase occurs via a posttranslational modification and is activated by the juxtamembrane domain

Frontiers in Plant Science, 2012
In metazoans, receptor kinases control many essential processes related to growth and development and response to the environment. The receptor kinases in plants and animals are structurally similar but evolutionarily distinct and thus while most animal ...
Man-Ho eOh, Steven D. Clouse, Steven C. Huber, Steven C. Huber   +3 more
doaj   +1 more source

Grb2 binding induces phosphorylation-independent activation of Shp2

Communications Biology, 2021
Lin et al. investigate the interactions between adaptor protein, Grb2, and the ubiquitously expressed protein tyrosine phosphatase, Shp2. They find that monomeric Grb2 can activate Shp2 and its downstream signalling in the absence of up-regulation of ...
Chi-Chuan Lin, Lukasz Wieteska, Kin Man Suen, Arnout P. Kalverda, Zamal Ahmed, John E. Ladbury   +5 more
doaj   +1 more source

Inhibition of tyrosine kinase activity decreases expression of surfactant protein A in a human lung adenocarcinoma cell line independent of epidermal growth factor receptor [PDF]

, 1997
Epidermal growth factor (EGF) enhances fetal lung development in vivo and in vitro. Ligand binding to the EGF receptor stimulates an intrinsic receptor tyrosine kinase initiating a signal transduction cascade.
Klein, Jonathan M, McCarthy, Troy A
core   +1 more source