871721-44-7Relevant articles and documents
CALPAIN-2 INHIBITOR COMPOUNDS AND METHODS OF TREATMENT
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Page/Page column 93, (2021/08/20)
Compounds of Formula (I) or (X) are provided including for treatment of disorders such as a disorder or symptom associated with neuronal cell death. In one aspect, compounds which are selective inhibitors of calpain-2 are provided. Preferred compounds can
Targeting the von Hippel-Lindau E3 ubiquitin ligase using small molecules to disrupt the VHL/HIF-1α interaction
Buckley, Dennis L.,Van Molle, Inge,Gareiss, Peter C.,Tae, Hyun Seop,Michel, Julien,Noblin, Devin J.,Jorgensen, William L.,Ciulli, Alessio,Crews, Craig M.
supporting information; experimental part, p. 4465 - 4468 (2012/04/23)
E3 ubiquitin ligases, which bind protein targets, leading to their ubiquitination and subsequent degradation, are attractive drug targets due to their exquisite substrate specificity. However, the development of small-molecule inhibitors has proven extrao
Tripodal tris-tacn and tris-dpa platforms for assembling phosphate-templated trimetallic centers
Cao, Rui,Mueller, Peter,Lippard, Stephen J.
supporting information; experimental part, p. 17366 - 17369 (2011/02/23)
Multidentate tripodal ligands, N(CH2-m-C6H 4-CH2tacn)3 (L1) and N(CH2-o-C 6H4-CH2N(CH2py)2) 3 (L2), have been devised for assembling high-nuclearity metal clusters. By using the same tripodal platform with different ligand appendages, either triazacyclononanes or dipicolylamines, and functionalizing either the ortho or the meta positions on the tris(xylyl) linker arms, discrete trimetal phosphate units of relevance to phosphate-metabolizing trimetallic centers in biology were prepared. Four such compounds, [(CuIICl) 3(HPO4)L1](PF6) (1), [(CuIICl) 3(HAsO4)L1](PF6) (2), Na2[Mn III6MnII2(H2O) 2(HPO4)6(PO4)4(L1) 2] (3), and [CoII3(H2PO 4)Cl2(MeCN)L2](PF6)3 (4), all containing three metal centers bound to a central phosphate or arsenate unit bridging oxygen atoms, have been synthesized and structurally characterized. These results demonstrate the propensity of this novel tripodal ligand platform, in the presence of phosphate or arsenate, to assemble {M3(EO 4)} units and thus structurally mimic trimetallic active sites of proteins involved in phosphate metabolism. Reactivity studies reveal that the tricopper complex 1 is more efficient than monocopper analogues in catalyzing the hydrolysis of 4-nitrophenyl phosphate.
