The Native Conformation of the Human VDAC1 N Terminus-Reference-Cited by-同舟云学术

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The Native Conformation of the Human VDAC1 N Terminus

Published:2010-03-01 Issue:10 Volume:49 Page:1882-1885
ISSN:1433-7851
Container-title:Angewandte Chemie International Edition
language:en
Short-container-title:Angew. Chem. Int. Ed.

Author:

Schneider Robert,Etzkorn Manuel,Giller Karin,Daebel Venita,Eisfeld Jörg,Zweckstetter Markus,Griesinger Christian,Becker Stefan,Lange Adam

Publisher

Wiley

Subject

General Chemistry,Catalysis

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/anie.200906241/fullpdf

Reference22 articles.

1. VDAC: The channel at the interface between mitochondria and the cytosol

2. The VDAC1 N-terminus is essential both for apoptosis and the protective effect of anti-apoptotic proteins

3. The crystal structure of mouse VDAC1 at 2.3 Å resolution reveals mechanistic insights into metabolite gating

4. Solution Structure of the Integral Human Membrane Protein VDAC-1 in Detergent Micelles

5. Structure of the human voltage-dependent anion channel

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1. Solute Transport through Mitochondrial Porins In Vitro and In Vivo;Biomolecules;2024-03-04

2. Mechanistic Studies of Membrane Proteins Using Integrated Solid-state NMR and Computational Approaches;Integrated Structural Biology;2023-12-08

3. Structure and Gating Behavior of the Human Integral Membrane Protein VDAC1 in a Lipid Bilayer;Journal of the American Chemical Society;2022-02-14

4. Structure, gating and interactions of the voltage-dependent anion channel;European Biophysics Journal;2021-03

5. The intrinsically disordered N-terminus of the voltage-dependent anion channel;PLOS Computational Biology;2021-02-12

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