Works (2)

Updated: July 5th, 2023 15:41

2014 journal article

Modifying Caspase-3 Activity by Altering Allosteric Networks

BIOCHEMISTRY, 53(48), 7582–7595.

By: C. Cade n, P. Swartz n, S. MacKenzie n & A. Clark n

MeSH headings : Allosteric Site / genetics; Amino Acid Substitution; Caspase 3 / chemistry; Caspase 3 / genetics; Caspase 3 / metabolism; Crystallography, X-Ray; Humans; Kinetics; Models, Molecular; Molecular Dynamics Simulation; Mutagenesis, Site-Directed; Protein Conformation; Protein Multimerization; Protein Structure, Quaternary; Recombinant Proteins / chemistry; Recombinant Proteins / genetics; Recombinant Proteins / metabolism
TL;DR: The data show that the caspase-3 native ensemble includes the canonical active state as well as an inactive conformation characterized by an intact substrate-binding pocket, but with an altered helix 3, which reflects the relative population of each species in the native ensemble. (via Semantic Scholar)
Source: Web Of Science
Added: August 6, 2018

2010 journal article

Isioniazid-resistance conferring mutations in Mycobacterium tuberculosis KatG: Catalase, peroxidase, and INH-NADH adduct formation activities

Protein Science, 19(3), 458–474.

By: C. Cade, A. Dlouhy, K. Medzihradszky, S. Salas-Castillo & R. Ghiladi

Source: NC State University Libraries
Added: August 6, 2018

Citation Index includes data from a number of different sources. If you have questions about the sources of data in the Citation Index or need a set of data which is free to re-distribute, please contact us.

Certain data included herein are derived from the Web of Science© and InCites© (2024) of Clarivate Analytics. All rights reserved. You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.