856106-63-3Relevant academic research and scientific papers
A potent and selective small-molecule inhibitor for the lymphoid-specific tyrosine phosphatase (LYP), a target associated with autoimmune diseases
He, Yantao,Liu, Sijiu,Menon, Ambili,Stanford, Stephanie,Oppong, Emmanuel,Gunawan, Andrea M.,Wu, Li,Wu, Dennis J.,Barrios, Amy M.,Bottini, Nunzio,Cato, Andrew C. B.,Zhang, Zhong-Yin
, p. 4990 - 5008 (2013/07/26)
Lymphoid-specific tyrosine phosphatase (LYP), a member of the protein tyrosine phosphatase (PTP) family of signaling enzymes, is associated with a broad spectrum of autoimmune diseases. Herein we describe our structure-based lead optimization efforts with
Discovery and evaluation of novel inhibitors of mycobacterium protein tyrosine phosphatase B from the 6-hydroxy-benzofuran-5-carboxylic acid scaffold
He, Yantao,Xu, Jie,Yu, Zhi-Hong,Gunawan, Andrea M.,Wu, Li,Wang, Lina,Zhang, Zhong-Yin
, p. 832 - 842 (2013/03/28)
Mycobacterium tuberculosis (Mtb) protein tyrosine phosphatase B (mPTPB) is a virulence factor secreted by the pathogen and mediates mycobacterial survival in macrophages by targeting host cell immune responses. Consequently, mPTPB represents an exciting n
TYROSINE PHOSPHATASE INHIBITORS AND USES THEREOF TO MODULATE THE ACTIVITY OF LYP
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Page/Page column title page; 45; 58; 62; 63; 80, (2012/11/13)
A variety of benzofurans and indole derivatives some with an acetyl linker are disclosed herein. These compounds are not highly charged at physiological pH and have good bioavailability characteristics. These compounds exhibit selective or at least preferential affinity for the active sites of various sub-sets of protein tyrosine phosphatases. The lymphoid- specific tyrosine phosphatase (Lyp) has received enormous attention because of the finding that a single- nucleotide polymorphism (SNP) in the gene (PTPN22) encoding Lyp is associated with several autoimmune diseases, including type I diabetes. Many of these compounds and pharmaceutically acceptable salts thereof are novel therapeutic compounds useful for the treatment of various diseases including a number of autoimmune diseases.
Design, synthesis, and structure - Activity relationships for chimeric inhibitors of Hsp90
Shen, Gang,Wang, Mingwen,Welch, Timothy R.,Blagg, Brian S. J.
, p. 7618 - 7631 (2007/10/03)
(Chemical Equation Presented) Inhibition of the 90 kDa heat shock protein (Hsp90) family of molecular chaperones represents a promising new chemotherapeutic approach toward the treatment of several cancers. Previous studies have demonstrated that the natural products, radicicol and geldanamycin, are potent inhibitors of the Hsp90 N-terminal ATP binding site. The cocrystal structures of these molecules bound to Hsp90 have been determined, and through molecular modeling and superimposition of these ligands, hybrids of radicicol and geldanamycin have been designed. A series of macrocylic chimeras of radicicol and geldanamycin and the corresponding seco-agents have been prepared and evaluated for both antiproliferative activity and their ability to induce Hsp90-dependent client protein degradation.
