The DOI matches its Crossref record; 94 of the 94 references it cites were found in a registry or an index.
Structure and gating mechanism of the α7 nicotinic acetylcholine receptor
Open accessAbstract
Summary The α7 nicotinic acetylcholine receptor plays critical roles in the central nervous system and in the cholinergic inflammatory pathway. This ligand-gated ion channel assembles as a homopentamer, is exceptionally permeable to Ca2+, and desensitizes faster than any other Cys-loop receptor. The α7 receptor has served as a prototype for the Cys-loop superfamily yet has proven refractory to structural analysis. We present cryo-EM structures of the human α7 nicotinic receptor in a lipidic environment in resting, activated, and desensitized states, illuminating the principal steps in the gating cycle. The structures also reveal elements that contribute to its function, including a C-terminal latch that is permissive for channel opening, and an anionic ring in the extracellular vestibule that contributes to its high conductance and calcium permeability. Comparisons among the α7 structures provide a foundation for mapping the gating cycle and reveal divergence in gating mechanisms in the Cys-loop receptor superfamily.
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
UCSF Chimera—A visualization system for exploratory research and analysis
Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 45,828
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 29,915
SWISS-MODEL: homology modelling of protein structures and complexes
Waterhouse, A., Bertoni, M., Bienert, S., Studer, G., Tauriello, G., Gumienny, R., Heer, F. T., de Beer, T. A. P., Rempfer, C., Bordoli, L., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky427 · Cited by 13,067
UCSF ChimeraX: Structure visualization for researchers, educators, and developers
Pettersen, E. F., Goddard, T. D., Huang, C. C., Meng, E. C., Couch, G. S., Croll, T. I., Morris, J. H., & Ferrin, T. E. (2021) · Protein Science · doi:10.1002/pro.3943 · Cited by 9,514
MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
Zheng, S. Q., Palovcak, E., Armache, J.-P., Verba, K. A., Cheng, Y., & Agard, D. A. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,777
Automated electron microscope tomography using robust prediction of specimen movements
Mastronarde, D. N. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.07.007 · Cited by 5,336
New tools for automated high-resolution cryo-EM structure determination in RELION-3
Zivanov, J., Nakane, T., Forsberg, B. O., Kimanius, D., Hagen, W. J., Lindahl, E., & Scheres, S. H. (2018) · eLife · doi:10.7554/elife.42166 · Cited by 4,621
Gctf: Real-time CTF determination and correction
Zhang, K. (2016) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.11.003 · Cited by 3,537
Real-space refinement in PHENIX for cryo-EM and crystallography
Afonine, P. V., Poon, B. K., Read, R. J., Sobolev, O. V., Terwilliger, T. C., Urzhumtsev, A., & Adams, P. D. (2018) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798318006551 · Cited by 3,281
Nicotinic acetylcholine receptor α7 subunit is an essential regulator of inflammation
Wang, H., Yu, M., Ochani, M., Amella, C. A., Tanovic, M., Susarla, S., Li, J. H., Wang, H., Yang, H., Ulloa, L., et al. (2003) · Nature · doi:10.1038/nature01339 · Cited by 3,228
Cited by
The role of astrocytic α7 nicotinic acetylcholine receptors in Alzheimer disease
Fontana, I. C., Kumar, A., & Nordberg, A. (2023) · Nature Reviews Neurology · doi:10.1038/s41582-023-00792-4 · Cited by 86
α7 nicotinic acetylcholine receptors in the hippocampal circuit: taming complexity
Letsinger, A. C., Gu, Z., & Yakel, J. L. (2022) · Trends in Neurosciences · doi:10.1016/j.tins.2021.11.006 · Cited by 74
Sanfilippo, P., Kim, A. J., Bhukel, A., Yoo, J., Mirshahidi, P. S., Pandey, V., Bevir, H., Yuen, A., Mirshahidi, P. S., Guo, P., et al. (2024) · Neuron · doi:10.1016/j.neuron.2023.12.014 · Cited by 36
Structure and dynamics of differential ligand binding in the human ρ-type GABAA receptor
Cowgill, J., Fan, C., Haloi, N., Tobiasson, V., Zhuang, Y., Howard, R. J., & Lindahl, E. (2023) · Neuron · doi:10.1016/j.neuron.2023.08.006 · Cited by 25
Hampsey, E., Perkins, A., & Young, A. H. (2023) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2023.2192922 · Cited by 9
“NAChRs more broadly are nonselective cation channels, with the α7 subtype particularly permeable to calcium [39], in addition to sodium [40].”
Background
Metadata
- Authors
- Noviello, C. M., Gharpure, A., Mukhtasimova, N., Cabuco, R., Baxter, L., Borek, D., Sine, S. M., & Hibbs, R. E.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2021-04
- Volume
- 184
- Issue
- 8
- Pages
- 2121-2134.e13
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W3139482760
- Cited by
- 299
- References
- 94
- FWCI
- 12.28
- 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: Structure and gating mechanism of the α7 nicotinic acetylcholine receptor. https://app.cochat.ai/papers/10.1016/j.cell.2021.02.049
- The paper
- Noviello, C. M., Gharpure, A., Mukhtasimova, N., Cabuco, R., Baxter, L., Borek, D., Sine, S. M., & Hibbs, R. E. (2021). Structure and gating mechanism of the α7 nicotinic acetylcholine receptor. Cell. https://doi.org/10.1016/j.cell.2021.02.049
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.
