Chromaffin granule H+-ATPase has F1-like structure
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(91)81111-K/fullpdf
Reference30 articles.
1. Structure, molecular genetics, and evolution of vacuolar H+-ATPases
2. Characterization of detergent-solubilized adenosine triphosphatase of chromaffin granule membranes
3. Bioenergetics of secretory vesicles
4. Accumulation of biological amines into chromaffin granules: a model for hormone and neurotransmitter transport
5. The purified ATPase from chromaffin granule membranes is an anion-dependent proton pump.
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1. The V-type H+ ATPase: molecular structure and function,physiological roles and regulation;Journal of Experimental Biology;2006-02-15
2. Diverse Roles of Single Membrane Organelles: Factors Establishing the Acid Lumenal pH;Journal of Biochemistry;1998-08-01
3. The Physiology, Biochemistry and Molecular Biology of the Plant Vacuolar ATPase;Advances in Botanical Research;1997
4. The synaptic vesicle and its targets;Neuroscience;1995-01
5. Evidence for a Common Binding-Site for Omeprazole and N-Ethylmaleimide in Subunit A of Chromaffin Granule Vacuolar-Type H+-ATPase;Biochemical and Biophysical Research Communications;1993-10
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