๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Inhibition of protein tyrosine phosphatases causes phosphorylation of tyrosine-331 in the p60 TNF receptor and inactivates the receptor-associated kinase

โœ Scribed by Bryant G Darnay; Bharat B Aggarwal

Book ID
117107773
Publisher
Elsevier Science
Year
1997
Tongue
English
Weight
766 KB
Volume
410
Category
Article
ISSN
0014-5793

No coin nor oath required. For personal study only.

๐Ÿ“œ SIMILAR VOLUMES

On the cross-regulation of protein tyros
On the cross-regulation of protein tyrosine phosphatases and receptor tyrosine kinases in intracellular signaling
โœ Jason M. Haugh; Ian C. Schneider; Jodee M. Lewis ๐Ÿ“‚ Article ๐Ÿ“… 2004 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 587 KB

Intracellular signaling proteins are very often regulated by site-specific phosphorylation. For example, growth factor receptors in eukaryotic cells contain intrinsic tyrosine kinase activity and use inter- and intra-molecular interactions to recruit and orient potential protein substrates for phosp

Effect of tumor necrosis factor-ฮฑ on the
Effect of tumor necrosis factor-ฮฑ on the phosphorylation of tyrosine kinase receptors is associated with dynamic alterations in specific protein-tyrosine phosphatases
โœ Faiyaz Ahmad; Barry J. Goldstein ๐Ÿ“‚ Article ๐Ÿ“… 1997 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 161 KB ๐Ÿ‘ 1 views

Tumor necrosis factor-a (TNF-a) can modulate the signalling capacity of tyrosine kinase receptors; in particular, TNF-a has been shown to mediate the insulin resistance associated with animal models of obesity and noninsulin-dependent diabetes mellitus. In order to determine whether the effects of T