Mic10 Oligomerizes to Bend Mitochondrial Inner Membranes at Cristae Junctions
Open Access
- 1 May 2015
- journal article
- research article
- Published by Elsevier BV in Cell Metabolism
- Vol. 21 (5), 756-763
- https://doi.org/10.1016/j.cmet.2015.04.006
Abstract
No abstract availableThis publication has 32 references indexed in Scilit:
- Structure of the yeast F 1 F o -ATP synthase dimer and its role in shaping the mitochondrial cristaeProceedings of the National Academy of Sciences of the United States of America, 2012
- MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organizationMolecular Biology of the Cell, 2012
- Functional Reconstitution of a Voltage-Gated Potassium Channel in Giant Unilamellar VesiclesPLOS ONE, 2011
- Mechanism of endophilin N-BAR domain-mediated membrane curvatureThe EMBO Journal, 2006
- Generation of high curvature membranes mediated by direct endophilin bilayer interactionsThe Journal of cell biology, 2001
- The effect of point mutations on the free energy of transmembrane α-helix dimerizationJournal of Molecular Biology, 1997
- Entropy-driven tension and bending elasticity in condensed-fluid membranesPhysical Review Letters, 1990
- Isolation of peroxisome-deficient mutants of Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences of the United States of America, 1989
- Liposome electroformationFaraday Discussions of the Chemical Society, 1986
- The minimum energy of bending as a possible explanation of the biconcave shape of the human red blood cellJournal of Theoretical Biology, 1970