期刊
JOURNAL OF BIOENERGETICS AND BIOMEMBRANES
卷 40, 期 3, 页码 149-155出版社
SPRINGER/PLENUM PUBLISHERS
DOI: 10.1007/s10863-008-9143-0
关键词
VDAC; mitochondrial porin; patch clamp; planar bilayer; channel; mitochondria
资金
- NIH [GM57249]
- NSF
There is excellent agreement between the electrophysiological properties and the structure of the mitochondrial outer membrane protein, VDAC, ex vivo. However, the inference that the well-defined canonical open state of the VDAC pore is the normal physiological state of the channel in vivo is being challenged by several lines of evidence. Knowing the atomic structure of the detergent solubilized protein, a long sought after goal, will not be sufficient to understand the functioning of this channel protein. In addition, detailed information about VDAC's topology in the outer membrane of intact mitochondria, and the structural changes that it undergoes in response to different stimuli in the cell will be needed to define its physiological functions and regulation.
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