Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Michael Shokhen"'
Publikováno v:
Current Research in Structural Biology, Vol 8, Iss , Pp 100158- (2024)
Mutations in the IQSEC2 gene result in severe intellectual disability, epilepsy and autism. The primary function of IQSEC2 is to serve as a guanine exchange factor (GEF) controlling the activation of ARF6 which in turn mediates membrane trafficking a
Externí odkaz:
https://doaj.org/article/65ec50d393f348a8a9b739160e39b106
Autor:
Dhanoop Manikoth Ayyathan, Gal Levy-Cohen, Moran Shubely, Sandy Boutros-Suleiman, Veronica Lepechkin-Zilbermintz, Michael Shokhen, Amnon Albeck, Arie Gruzman, Michael Blank
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 36, Iss 1, Pp 401-409 (2021)
The C2-WW-HECT-domain E3 ubiquitin ligase SMURF2 emerges as an important regulator of diverse cellular processes. To date, SMURF2-specific modulators were not developed. Here, we generated and investigated a set of SMURF2-targeting synthetic peptides
Externí odkaz:
https://doaj.org/article/15135819ca6b42c9a244f5e97bd412c2
Autor:
Michael Shokhen, Randall Walikonis, Vladimir N. Uversky, Amnon Allbeck, Camryn Zezelic, Danielle Feldman, Nina S. Levy, Andrew P. Levy
Publikováno v:
Journal of Biomolecular Structure and Dynamics. :1-12
Autor:
Yoni Moskovits, Sharon Ruthstein, Pinchas Zer Aviv, Michael Shokhen, Didier Vertommen, Olga Viskind, Arie Gruzman, Moran Shubely, Amnon Albeck
Publikováno v:
ChemistrySelect. 1:4658-4667
Reduced Prostatic acid Phosphatase (PAcP) secretion is associated with inhibition of the proliferation rate of prostate cancer cells. Signal peptidase 1 (SPase 1) is the main protease that cleaves the signal peptide of secretory proteins and allows t
Publikováno v:
Angewandte Chemie. 128:1712-1716
General-base catalysis in serine proteases still poses mechanistic challenges despite decades of research. Whether proton transfer from the catalytic Ser to His and nucleophilic attack on the substrate are concerted or stepwise is still under debate,
Autor:
Michael Shokhen, Netaly Khazanov, Rachel Ozeri, Nurit Perlman, Tamar Traube, Michal Hirsch, Amnon Albeck, S. Vijayakumar
Publikováno v:
Israel Journal of Chemistry. 54:1137-1151
Mechanistic studies of catalysis and the inhibition of serine and cysteine proteases afford new and sometimes surprising insights, challenging conventional dogmas in enzymology. The intrinsic source of the difference in the catalytic mechanisms of se
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 79:975-985
Various mechanisms for the reversible formation of a covalent tetrahedral complex (TC) between papain and peptidyl aldehyde inhibitors were simulated by DFT calculations, applying the quantum mechanical/self consistent reaction field (virtual solvent
Publikováno v:
Journal of Chemical Information and Modeling. 50:2256-2265
We introduce an enzyme mechanism-based method, EMBM, aimed at rational design of chemical sites, CS, of reaction coordinate analog inhibitors. The energy of valence reorganization of CS, caused by the formation of the enzyme-inhibitor covalent comple
Publikováno v:
Proteins: Structure, Function, and Bioinformatics
A central mechanistic paradigm of cysteine proteases is that the His-Cys catalytic diad forms an ion-pair NH(+)/S(-) already in the catalytically active free enzyme. Most molecular modeling studies of cysteine proteases refer to this paradigm as thei
Publikováno v:
Bioorganic & Medicinal Chemistry. 16:9032-9039
Endo peptidyl epoxides, in which the central epoxidic moiety replaces the scissile amide bond of a P3–P3′ peptide, were designed as cysteine proteases inhibitors. The additional P′–S′ interactions, relative to those of an exo peptidyl epoxi