Results 271 to 280 of about 894,703 (310)

Anp32e (Cpd1) and related protein phosphatase 2 inhibitors

The Cerebellum, 2003
Mouse Anp32e (Acidic leucine-rich nuclear phosphoprotein 32 family, member e: NM_023210, P97822, formerly Cpd1), a protein identified in postnatal cerebellum by differential display, belongs to the superfamily of leucine rich repeat (LRR) proteins and to the Acidic Nuclear Phosphoprotein 32 (ANP32) family of protein phosphatase 2 (PPP2, formerly PP2A ...
openaire   +2 more sources

Inhibitor Binding Sites in the Protein Tyrosine Phosphatase SHP-2

Mini-Reviews in Medicinal Chemistry, 2020
Protein tyrosine phosphatase 2 (SHP-2) has long been proposed as a cancer drug target. Several small-molecule compounds with different mechanisms of SHP-2 inhibition have been reported, but none are commercially available. Pool selectivity over protein tyrosine phosphatase 1 (SHP-1) and a lack of cellular activity have hindered the development of ...
Haonan Zhang   +4 more
openaire   +2 more sources

SHP-2, SH2-containing protein tyrosine phosphatase-2.

The international journal of biochemistry & cell biology, 1998
SHP-2 is an ubiquitously expressed cytosolic protein tyrosine phosphatase composed of two amino-terminal SH2 domains, a central phosphatase domain and a carboxy-terminal tail. Upon activation of cells with different stimuli, SHP-2 is recruited to the plasma membrane where it can associate with a number of tyrosine phosphorylated molecules, including ...
M, Stein-Gerlach   +2 more
openaire   +1 more source

Specific dephosphorylation of Janus Kinase 2 by protein tyrosine phosphatases

PROTEOMICS, 2014
Many protein kinases are activated through phosphorylation of an activation loop thereby turning on downstream signaling pathways. Activation of JAK2, a nonreceptor tyrosine kinase with an important role in growth factor and cytokine signaling, requires phosphorylation of the 1007 and 1008 tyrosyl residues.
Jianzhuo, Li   +9 more
openaire   +2 more sources

Protein tyrosine phosphatase-1B and T-cell protein tyrosine phosphatase regulate IGF-2-induced MCF-7 cell migration

Biochemical and Biophysical Research Communications, 2010
The protein tyrosine phosphatase-1B (PTP1B) and the T-cell protein tyrosine phosphatase (TC-PTP) have been implicated in down-regulation of tyrosine kinase receptors, conferring anti-oncogenic functions to these PTPases. However, recent work has shown that PTP1B is positively implicated in oncogenic properties of breast cancer cells by regulating the ...
Christophe, Blanquart   +2 more
openaire   +2 more sources

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