864132-41-2Relevant academic research and scientific papers
Structure-based optimization of protein tyrosine phosphatase 1B inhibitors: From the active site to the second phosphotyrosine binding site
Wilson, Douglas P.,Wan, Zhao-Kui,Xu, Wei-Xin,Kirincich, Steven J.,Follows, Bruce C.,Joseph-McCarthy, Diane,Foreman, Kenneth,Moretto, Alessandro,Wu, Junjun,Zhu, Min,Binnun, Eva,Zhang, Yan-Ling,Tam, May,Erbe, David V.,Tobin, James,Xu, Xin,Leung, Louis,Shilling, Adam,Tam, Steve Y.,Mansour, Tarek S.,Lee, Jinbo
, p. 4681 - 4698 (2007)
Protein tyrosine phosphatase 1B (PTP1B) is a negative regulator of the insulin and leptin receptor pathways and thus an attractive therapeutic target for diabetes and obesity. Starting with a high micromolar lead compound, structure-based optimization of
Inhibitors of protein tyrosine phosphatase 1B
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Page/Page column 114, (2008/06/13)
Protein tyrosine phosphatases (PTPases) such as PTP1B can play a role in regulating a wide variety of cellular responses such as insulin signaling. Substituted thiophene compounds such as, for example, 2-carboxyl, 3-carboxymethoxy, 5-aryl substituted thiophenes, can inhibit PTP1B and thereby induce greater insulin sensitivity. Accordingly, PTP1B inhibition can provide an alternate treatment for PTPase-mediated disorders such as diabetes.
