The N-terminus of VDAC: Structure, mutational analysis, and a potential role in regulating barrel shape-Reference-Cited by-同舟云学术

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The N-terminus of VDAC: Structure, mutational analysis, and a potential role in regulating barrel shape

Published:2016-06 Issue:6 Volume:1858 Page:1350-1361
ISSN:0005-2736
Container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes

Author:

Shuvo Sabbir R.,Ferens Fraser G.,Court Deborah A.

Funder

NSERC Discovery Grant

University of Manitoba Graduate Fellowship

Faculty of Science and the Graduate Enhancement of Tri-Council Stipends programme of the University of Manitoba

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference90 articles.

1. The mitochondrial voltage-dependent anion channel 1 in tumor cells;Shoshan-Barmatz;Biochim. Biophys. Acta,2015

2. Permeation of hydrophilic solutes through mitochondrial outer membranes: review on mitochondrial porins;Benz;Biochim. Biophys. Acta,1994

3. Plant VDAC: facts and speculations;Homble;Biochim. Biophys. Acta,2012

4. VDAC, a multi-functional mitochondrial protein regulating cell life and death;Shoshan-Barmatz;Mol. Asp. Med.,2010

5. Abnormal alpha-synuclein reduces nigral voltage-dependent anion channel 1 in sporadic and experimental Parkinson's disease;Chu;Neurobiol. Dis.,2014

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