From ATP synthase dimers to C-ring conformational changes: unified model of the mitochondrial permeability transition pore

Cell Death Dis. 2017 Dec 4;8(12):1. doi: 10.1038/s41419-017-0042-3.

Authors

Giuseppe Federico Amodeo¹, Maria E Solesio¹, Evgeny V Pavlov²

Affiliations

¹ Department of Basic Sciences, New York University, College of Dentistry, 345 East 24th Street, New York, NY, 10010, USA.
² Department of Basic Sciences, New York University, College of Dentistry, 345 East 24th Street, New York, NY, 10010, USA. ep37@nyu.edu.

No abstract available

Publication types

Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

MeSH terms

Humans
Mitochondrial Membrane Transport Proteins / metabolism*
Mitochondrial Permeability Transition Pore
Mitochondrial Proton-Translocating ATPases / metabolism*

Substances

Mitochondrial Membrane Transport Proteins
Mitochondrial Permeability Transition Pore
Mitochondrial Proton-Translocating ATPases

Grants and funding

R01 GM115570/GM/NIGMS NIH HHS/United States