Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Sarah K. I. Watt"'
Autor:
Lavleen Mader, Sarah K. I. Watt, Harish R. Iyer, Linh Nguyen, Harpreet Kaur, Jeffrey W. Keillor
Publikováno v:
RSC Medicinal Chemistry. 14:277-298
This systematic structure–activity relationship study provides key insights into warhead design and application for optimizing efficiency, selectivity, and pharmacokinetic stability of hTG2 inhibitors.
Publikováno v:
Organic & Biomolecular Chemistry. 21:2204-2212
A kinetic study of the reaction mechanism of the thiol addition reaction of the acryloyl piperidine ‘warhead’ reveals its intrinsic reactivity and thiol sensitivity, which are relevant to inhibitor design.
Publikováno v:
Organic & Biomolecular Chemistry.
Experimental evidence is provided for an SN2 mechanism of thiol addition to the N-phenylchloroacetamide warhead, and a detailed comparison of intrinsic reactivity is performed against conventional acrylamide derivatives.
Publikováno v:
Organic & Biomolecular Chemistry. 20:8898-8906
Experimental data from a Brønsted-type plot, a solvent kinetic isotope effect, a pH-rate plot and temperature studies are all consistent with rate-limiting nucleophilic attack of thiolate followed by rapid protonation of the enolate adduct.
Autor:
Alana M. M. Rangaswamy, Pauline Navals, Eric W. J. Gates, Sammir Shad, Sarah K. I. Watt, Jeffrey W. Keillor
Publikováno v:
RSC Med Chem
Tissue transglutaminase (TG2) is a multifunctional protein that plays biological roles based on its ability to catalyse protein cross-linking and to function as a non-canonical G-protein known as Ghα. The non-regulated activity of TG2 has been impli
Publikováno v:
Organicbiomolecular chemistry. 20(45)
Cysteine (Cys) residues contain a redox-sensitive thiol and are commonly found in enzyme active sites. In recent years, the presence of a reactive thiolate group on a protein has been exploited in the development of irreversible enzyme inhibitors as