Results 271 to 280 of about 887,918 (307)
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Anp32e (Cpd1) and related protein phosphatase 2 inhibitors
The Cerebellum, 2003Mouse 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 ...
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Inhibitor Binding Sites in the Protein Tyrosine Phosphatase SHP-2
Mini-Reviews in Medicinal Chemistry, 2020Protein 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
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SHP-2, SH2-containing protein tyrosine phosphatase-2.
The international journal of biochemistry & cell biology, 1998SHP-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
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Specific dephosphorylation of Janus Kinase 2 by protein tyrosine phosphatases
PROTEOMICS, 2014Many 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
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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
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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
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Alkaline Phosphatase ALPPL-2 Is a Novel Pancreatic Carcinoma-Associated Protein
Cancer Research, 2013Abstract Pancreatic ductal adenocarcinoma (PDAC) is a highly aggressive malignancy with a very low median survival rate. The lack of early sensitive diagnostic markers is one of the main causes of PDAC-associated lethality. Therefore, to identify novel pancreatic cancer biomarkers that can facilitate early diagnosis and also help in ...
Pooja, Dua +5 more
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How phosphorylation activates the protein phosphatase-1 • inhibitor-2 complex
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2013Phosphorylation regulates activity of many proteins; however, atomic level details are known for very few examples. Inhibitor-2 (I2) squelches the ubiquitous protein phosphatase-1 (PP1) enzyme activity by blocking access to the metal-containing active site.
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[Research progress of protein tyrosine phosphatase SHP-2].
Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences, 2013The Src homology-2 domain-containing phosphatase SHP-2 encoded by PTPN11 is an essential component in several signaling pathways.Different types of mutation in SHP-2 have been confirmed in several types of leukemia and solid tumors. Elucidation of the events underlying Shp2-evoked transformation may provide new insights into the novel targets ...
Hong-ke, Cai, Yong-chuan, Deng
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