The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.
Principles of conduction and hydrophobic gating in K + channels
Open accessAbstract
We present the first atomic-resolution observations of permeation and gating in a K + channel, based on molecular dynamics simulations of the Kv1.2 pore domain. Analysis of hundreds of simulated permeation events revealed a detailed conduction mechanism, resembling the Hodgkin–Keynes “knock-on” model, in which translocation of two selectivity filter–bound ions is driven by a third ion; formation of this knock-on intermediate is rate determining. In addition, at reverse or zero voltages, we observed pore closure by a novel “hydrophobic gating” mechanism: A dewetting transition of the hydrophobic pore cavity—fastest when K + was not bound in selectivity filter sites nearest the cavity—caused the open, conducting pore to collapse into a closed, nonconducting conformation. Such pore closure corroborates the idea that voltage sensors can act to prevent pore collapse into the intrinsically more stable, closed conformation, and it further suggests that molecular-scale dewetting facilitates a specific biological function: K + channel gating. Existing experimental data support our hypothesis that hydrophobic gating may be a fundamental principle underlying the gating of voltage-sensitive K + channels. We suggest that hydrophobic gating explains, in part, why diverse ion channels conserve hydrophobic pore cavities, and we speculate that modulation of cavity hydration could enable structural determination of both open and closed channels.
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
Hodgkin, A. L., & Huxley, A. F. (1952) · The Journal of Physiology · doi:10.1113/jphysiol.1952.sp004764 · Cited by 23,191
All-Atom Empirical Potential for Molecular Modeling and Dynamics Studies of Proteins
MacKerell, A. D., Bashford, D., Bellott, M., Dunbrack, R. L., Evanseck, J. D., Field, M. J., Fischer, S., Gao, J., Guo, H., Ha, S., et al. (1998) · The Journal of Physical Chemistry B · doi:10.1021/jp973084f · Cited by 14,311
The Structure of the Potassium Channel: Molecular Basis of K + Conduction and Selectivity
Doyle, D. A., Cabral, J. M., Pfuetzner, R. A., Kuo, A., Gulbis, J. M., Cohen, S. L., Chait, B. T., & MacKinnon, R. (1998) · Science · doi:10.1126/science.280.5360.69 · Cited by 6,807
Ion Channels/Excitable Membranes
(2011) · SpringerReference · doi:10.1007/springerreference_33998 · Cited by 4,034
Water conduction through the hydrophobic channel of a carbon nanotube
Hummer, G., Rasaiah, J. C., & Noworyta, J. P. (2001) · Nature · doi:10.1038/35102535 · Cited by 3,557
Mackerell, A. D., Feig, M., & Brooks, C. L. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20065 · Cited by 3,319
Molecular dynamics---Scalable algorithms for molecular dynamics simulations on commodity clusters
Bowers, K. J., Sacerdoti, F. D., Salmon, J. K., Shan, Y., Shaw, D. E., Chow, E., Xu, H., Dror, R. O., Eastwood, M. P., Gregersen, B. A., et al. (2006) · Proceedings of the 2006 ACM/IEEE conference on Supercomputing - SC '06 · doi:10.1145/1188455.1188544 · Cited by 2,580
Self-citationCrystal Structure of a Mammalian Voltage-Dependent Shaker Family K + Channel
Long, S. B., Campbell, E. B., & MacKinnon, R. (2005) · Science · doi:10.1126/science.1116269 · Cited by 2,124
Chemistry of ion coordination and hydration revealed by a K+ channel–Fab complex at 2.0 Å resolution
Zhou, Y., Morais-Cabral, J. H., Kaufman, A., & MacKinnon, R. (2001) · Nature · doi:10.1038/35102009 · Cited by 2,097
Ion Channels/Excitable Membranes
Terlau, H., & Kirchhoff, F. (2006) · Encyclopedic Reference of Genomics and Proteomics in Molecular Medicine · doi:10.1007/3-540-29623-9_5640 · Cited by 1,789
Cited by
Allostery and the Monod-Wyman-Changeux Model After 50 Years
Changeux, J.-P. (2012) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-050511-102222 · Cited by 391
The future of molecular dynamics simulations in drug discovery
Borhani, D. W., & Shaw, D. E. (2012) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-011-9517-y · Cited by 313
“Their mechanistic results likely apply to the entire ‘‘Cys-loop’’ superfamily of ligand-gated ion channels, of which the nicotinic receptor is a much-studied prototype; these results also heralded hydrophobic gating in the structurally distinct voltage-gated ion channel superfamily [32].”
BackgroundSelf-citationStructure of potassium channels
Kuang, Q., Purhonen, P., & Hebert, H. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1948-5 · Cited by 291
Revealing Atomic-Level Mechanisms of Protein Allostery with Molecular Dynamics Simulations
Hertig, S., Latorraca, N. R., & Dror, R. O. (2016) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1004746 · Cited by 118
Self-citation
Metadata
- Authors
- Jensen, M. Ø., Borhani, D. W., Lindorff-Larsen, K., Maragakis, P., Jogini, V., Eastwood, M. P., Dror, R. O., & Shaw, D. E.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2010-03-15
- Volume
- 107
- Issue
- 13
- Pages
- 5833-5838
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1963480981
- Cited by
- 311
- References
- 53
- FWCI
- 11.70
- Type
- journal article
- Language
- en
- Open access
- bronze
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: Principles of conduction and hydrophobic gating in K + channels. https://app.cochat.ai/papers/10.1073/pnas.0911691107
- The paper
- Jensen, M. Ø., Borhani, D. W., Lindorff-Larsen, K., Maragakis, P., Jogini, V., Eastwood, M. P., Dror, R. O., & Shaw, D. E. (2010). Principles of conduction and hydrophobic gating in K + channels. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0911691107
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.
