These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: Mini review on the structure and supramolecular assembly of VDAC.
    Author: Gonçalves RP, Buzhysnskyy N, Scheuring S.
    Journal: J Bioenerg Biomembr; 2008 Jun; 40(3):133-8. PubMed ID: 18683037.
    Abstract:
    The Voltage Dependent Anion Channel (VDAC) is the most abundant protein in the outer membrane of mitochondria. This strategic localization puts it at the heart of a great number of phenomena. Its recent implication in apoptosis is an example of the major importance of this protein and has created a surge of interest in VDAC. There is no atomic-resolution structure allowing a better understanding of the function of VDAC, so alternative techniques to X-ray diffraction have been used to study VDAC. Here we discuss structural models from folding predictions and review data acquired by Atomic Force Microscopy (AFM) imaging that allowed to observe VDAC's structure and supramolecular organization in the mitochondrial outer membrane.
    [Abstract] [Full Text] [Related] [New Search]