Christine E. Cade

Works (2)

Updated: July 5th, 2023 15:41

2014 article

Modifying Caspase-3 Activity by Altering Allosteric Networks

Cade, C., Swartz, P., MacKenzie, S. H., & Clark, A. C. (2014, October 24). Biochemistry.

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
topics (OpenAlex): Cell death mechanisms and regulation; ATP Synthase and ATPases Research; Machine Learning in Bioinformatics
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)
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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

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