The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Voltage-Gated Proton Channels and Other Proton Transfer Pathways
Abstract
Proton channels exist in a wide variety of membrane proteins where they transport protons rapidly and efficiently. Usually the proton pathway is formed mainly by water molecules present in the protein, but its function is regulated by titratable groups on critical amino acid residues in the pathway. All proton channels conduct protons by a hydrogen-bonded chain mechanism in which the proton hops from one water or titratable group to the next. Voltage-gated proton channels represent a specific subset of proton channels that have voltage- and time-dependent gating like other ion channels. However, they differ from most ion channels in their extraordinarily high selectivity, tiny conductance, strong temperature and deuterium isotope effects on conductance and gating kinetics, and insensitivity to block by steric occlusion. Gating of H+channels is regulated tightly by pH and voltage, ensuring that they open only when the electrochemical gradient is outward. Thus they function to extrude acid from cells. H+channels are expressed in many cells. During the respiratory burst in phagocytes, H+current compensates for electron extrusion by NADPH oxidase. Most evidence indicates that the H+channel is not part of the NADPH oxidase complex, but rather is a distinct and as yet unidentified molecule.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Hydrogen Ion Buffers for Biological Research*
Good, N. E., Winget, G. D., Winter, W., Connolly, T. N., Izawa, S., & Singh, R. M. M. (1966) · Biochemistry · doi:10.1021/bi00866a011 · Cited by 2,762
Thermogenic mechanisms in brown fat.
Nicholls, D. G., & Locke, R. M. (1984) · Physiological Reviews · doi:10.1152/physrev.1984.64.1.1 · Cited by 1,602
Superoxide activates mitochondrial uncoupling proteins
Echtay, K. S., Roussel, D., St-Pierre, J., Jekabsons, M. B., Cadenas, S., Stuart, J. A., Harper, J. A., Roebuck, S. J., Morrison, A., Pickering, S., et al. (2002) · Nature · doi:10.1038/415096a · Cited by 1,382
Killing activity of neutrophils is mediated through activation of proteases by K+ flux
Reeves, E. P., Lu, H., Jacobs, H. L., Messina, C. G. M., Bolsover, S., Gabella, G., Potma, E. O., Warley, A., Roes, J., & Segal, A. W. (2002) · Nature · doi:10.1038/416291a · Cited by 1,153
Structure and mechanism of carbonic anhydrase
Lindskog, S. (1997) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(96)00198-2 · Cited by 1,022
PARSEGIAN, A. (1969) · Nature · doi:10.1038/221844a0 · Cited by 854
Energy metabolism in uncoupling protein 3 gene knockout mice
Vidal-Puig, A. J., Grujic, D., Zhang, C.-Y., Hagen, T., Boss, O., Ido, Y., Szczepanik, A., Wade, J., Mootha, V., Cortright, R., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910179199 · Cited by 677
A Ca2+-activated NADPH Oxidase in Testis, Spleen, and Lymph Nodes
Bánfi, B., Molnár, G., Maturana, A., Steger, K., Hegedûs, B., Demaurex, N., & Krause, K.-H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103034200 · Cited by 622
Paula, S., Volkov, A. G., Van Hoek, A. N., Haines, T. H., & Deamer, D. W. (1996) · Biophysical Journal · doi:10.1016/s0006-3495(96)79575-9 · Cited by 578
Cross, A. R., & Jones, O. T. G. (1986) · Biochemical Journal · doi:10.1042/bj2370111 · Cited by 551
Cited by
The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989
“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, 592, 639), and 2) NO…”
BackgroundMyeloperoxidase: friend and foe
Klebanoff, S. J. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.1204697 · Cited by 2,282
Proton-coupled electron transfer
Huynh, M. H. V., & Meyer, T. J. (2007) · Chemical Reviews · doi:10.1021/cr0500030 · Cited by 1,659
Proton Transfer 200 Years after von Grotthuss: Insights from Ab Initio Simulations
Marx, D. (2006) · ChemPhysChem · doi:10.1002/cphc.200600128 · Cited by 920
Anomalously Immobilized Water: A New Water Phase Induced by Confinement in Nanotubes
Mashl, R. J., Joseph, S., Aluru, N. R., & Jakobsson, E. (2003) · Nano Letters · doi:10.1021/nl0340226 · Cited by 447
Metadata
- Authors
- Decoursey, T. E.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2003-04-01
- Volume
- 83
- Issue
- 2
- Pages
- 475-579
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2103566186
- Cited by
- 737
- References
- 17
- FWCI
- 2.24
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Voltage-Gated Proton Channels and Other Proton Transfer Pathways. https://app.cochat.ai/papers/10.1152/physrev.00028.2002
- The paper
- Decoursey, T. E. (2003). Voltage-Gated Proton Channels and Other Proton Transfer Pathways. Physiological Reviews. https://doi.org/10.1152/physrev.00028.2002
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
