Voltage‐activated complexation of α‐synuclein with three diverse β‐barrel channels: VDAC, MspA, and α‐hemolysin

Author:

Hoogerheide David P.1ORCID,Gurnev Philip A.2,Rostovtseva Tatiana K.2,Bezrukov Sergey M.2

Affiliation:

1. Center for Neutron Research National Institute of Standards and Technology Gaithersburg Maryland USA

2. Section on Molecular Transport Eunice Kennedy Shriver National Institute of Child Health and Human Development National Institutes of Health Bethesda Maryland USA

Funder

Eunice Kennedy Shriver National Institute of Child Health and Human Development

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference65 articles.

1. Regulation of mitochondrial respiration by VDAC is enhanced by membrane‐bound inhibitors with disordered polyanionic C‐terminal domains;Rostovtseva T. K.;International Journal of Molecular Sciences,2021

2. Exploring lipid‐dependent conformations of membrane‐bound α‐synuclein with the VDAC nanopore;Hoogerheide D. P.;Biochimica Et Biophysica Acta‐Biomembranes,2021

3. Reconstitution in planar lipid bilayers of a voltage‐dependent anion‐selective channel obtained from paramecium mitochondria;Schein S. J.;Journal of Membrane Biology,1976

4. Conductance hysteresis in the voltage‐dependent anion channel;Rappaport S. M.;European Biophysics Journal with Biophysics Letters,2015

5. Tubulin binding blocks mitochondrial voltage‐dependent anion channel and regulates respiration;Rostovtseva T. K.;Proceedings of the National Academy of Sciences of the United States of America,2008

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