The Human Cytochrome c Domain-Swapped Dimer Facilitates Tight Regulation of Intrinsic Apoptosis
Author:
Affiliation:
1. Department of Chemistry & Biochemistry, University of Montana, Missoula, Montana 59812, United States
2. Center for Biomolecular Structure & Dynamics, University of Montana, Missoula, Montana 59812, United States
Funder
Division of Chemistry
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.0c00326
Reference120 articles.
1. Cytochromes c
2. Sealing the Mitochondrial Respirasome
3. Oxidation state-dependent conformational changes in cytochrome c
4. Heightened Dynamics of the Oxidized Y48H Variant of Human Cytochrome c Increases Its Peroxidatic Activity
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2. Phosphorylations and Acetylations of Cytochrome c Control Mitochondrial Respiration, Mitochondrial Membrane Potential, Energy, ROS, and Apoptosis;Cells;2024-03-12
3. Alkaline State of the Domain-Swapped Dimer of Human Cytochrome c: A Conformational Switch for Apoptotic Peroxidase Activity;Journal of the American Chemical Society;2022-11-08
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