Voltage-gated proton channels and other proton transfer pathways.
By T. DeCoursey. Physiological Reviews, 2003
675 citations recorded by the source corpus.
Subfields: Cellular and Molecular Neuroscience, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/f63b689b21aac667465cb07b3689757bdebe425a
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In Cellular and Molecular Neuroscience
In Molecular Biology
Citations in the corpus
- The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. (2007, background): “Thus there is no doubt that there is a close relationship between NOX enzymes and proton channels; however, there are two different molecular interpretations: 1) NOX enzymes possess a proton channel domain, suggested to reside within the histidine-rich third transmembrane domain (55, 57, 365, 368, 5”
- Myeloperoxidase: friend and foe (2005, background): “However, other studies have suggested that the H channel is separate from the NADPH oxidase [335–337].”
- Expression cloning of TMEM16A as a calcium-activated chloride channel subunit (2008, background): “2 to close voltagegated proton channels, which only open when the electrochemical gradient is outward (Decoursey, 2003), yielded very small currents in the absence of external calcium (Figure 3G) but large”
- The ABCs of solute carriers: physiological, pathological and therapeutic implications of human membrane transport proteins (2004, background): “Similar to transporters, channels allow movement of solutes down their electrochemical gradients [1, 4, 6 , 9, 10, 14, 20].”