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Cryo-EM structures of the TMEM16A calcium-activated chloride channel
Open accessAbstract
Calcium-activated chloride channels (CaCCs) encoded by TMEM16A control neuronal signalling, smooth muscle contraction, airway and exocrine gland secretion, and rhythmic movements of the gastrointestinal system. To understand how CaCCs mediate and control anion permeation to fulfil these physiological functions, knowledge of the mammalian TMEM16A structure and identification of its pore-lining residues are essential. TMEM16A forms a dimer with two pores. Previous CaCC structural analyses have relied on homology modelling of a homologue (nhTMEM16) from the fungus Nectria haematococca that functions primarily as a lipid scramblase, as well as subnanometre-resolution electron cryo-microscopy. Here we present de novo atomic structures of the transmembrane domains of mouse TMEM16A in nanodiscs and in lauryl maltose neopentyl glycol as determined by single-particle electron cryo-microscopy. These structures reveal the ion permeation pore and represent different functional states. The structure in lauryl maltose neopentyl glycol has one Ca 2+ ion resolved within each monomer with a constricted pore; this is likely to correspond to a closed state, because a CaCC with a single Ca 2+ occupancy requires membrane depolarization in order to open (C.J.P. et al., manuscript submitted). The structure in nanodiscs has two Ca 2+ ions per monomer and its pore is in a closed conformation; this probably reflects channel rundown, which is the gradual loss of channel activity that follows prolonged CaCC activation in 1 mM Ca 2+. Our mutagenesis and electrophysiological studies, prompted by analyses of the structures, identified ten residues distributed along the pore that interact with permeant anions and affect anion selectivity, as well as seven pore-lining residues that cluster near pore constrictions and regulate channel gating. Together, these results clarify the basis of CaCC anion conduction.
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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 45,882
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
PHENIX : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716
MolProbity : all-atom structure validation for macromolecular crystallography
Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115
MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
Zheng, S. Q., Palovcak, E. J., Armache, J., Verba, K. A., Cheng, Y., & Agard, D. A. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,496
Self-citationPHENIX: a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkòczi, G., Chen, V. B., Davis, I., Echols, N., Headd, J. J., Hung, L., Kapral, G. J., Grosse‐Kunstleve, R. W., et al. (2012) · International Tables for Crystallography · doi:10.1107/97809553602060000865 · Cited by 7,334
RELION: Implementation of a Bayesian approach to cryo-EM structure determination
Scheres, S. H. W. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.09.006 · Cited by 5,446
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 5,136
CTFFIND4: Fast and accurate defocus estimation from electron micrographs
Rohou, A. L., & Grigorieff, N. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.08.008 · Cited by 4,759
Gctf: Real-time CTF determination and correction
Zhang, K. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.11.003 · Cited by 3,417
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Jesus-Perez, J. J. D., López-Romero, A. E., Posadas, O., Segura-Covarrubias, G., Aréchiga-Figueroa, I. A., Gutiérrez–Medina, B., Pérez‐Cornejo, P., & Arreola, J. (2022) · The Journal of General Physiology · doi:10.1085/jgp.202113027 · Cited by 10
Li, S., Sun, W., Li, S., Zhu, L., Guo, S., He, J., Li, Y., Tian, C., Zhao, Z., Yu, T., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2407493121 · Cited by 9
Lin, W., Chung, W. Y., Park, S., Abtahi, A. M., Leblanc, B., Ahuja, M., & Muallem, S. (2025) · Nature Communications · doi:10.1038/s41467-025-58682-w · Cited by 9
Li, G., Cai, C., Zhang, N., Wang, Z., Zhang, M., Liu, Q., Chen, S., Shang, Y., Zhao, C., Ren, S., et al. (2025) · Materials Today Bio · doi:10.1016/j.mtbio.2025.102426 · Cited by 9
The Role of Lipids in CRAC Channel Function
Maltan, L., Andova, A.-M., & Derler, I. (2022) · Biomolecules · doi:10.3390/biom12030352 · Cited by 10
Jimenez, C., Hawn, M. B., Akin, E. J., & Leblanc, N. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115320 · Cited by 10
Talbi, K., Ousingsawat, J., Centeio, R., Schreiber, R., & Kunzelmann, K. (2023) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-023-02829-5 · Cited by 9
The physiological roles of anoctamin2/TMEM16B and anoctamin1/TMEM16A in chemical senses
Dibattista, M., Pifferi, S., Hernandez, A., & Menini, A. (2024) · Cell Calcium · doi:10.1016/j.ceca.2024.102889 · Cited by 10
Insights into the function and regulation of the calcium-activated chloride channel TMEM16A
Arreola, J., López-Romero, A. E., Huerta, M., Guzmán-Hernández, M. L., & Pérez‐Cornejo, P. (2024) · Cell Calcium · doi:10.1016/j.ceca.2024.102891 · Cited by 9
Brunner, J. D., & Schenck, S. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9136-5_14 · Cited by 9
Luo, Z., Campos-Acevedo, A. A., Lv, L., Wang, Q., & Ma, J. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2013756118 · Cited by 9
Molecular dynamics simulation of TMEM16A channel: Linking structure with gating
Shi, S., Pang, C., Ren, S., Sun, F., Ma, B., Guo, S., Li, J., Chen, Y., & An, H. (2021) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2021.183777 · Cited by 9
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Tonggu, L., & Wang, L. (2018) · SSRN Electronic Journal · doi:10.2139/ssrn.3310822 · Cited by 9
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Deng, S., Qiu, Q., Dang, S., & Yan, Z. (2025) · The Journal of Cell Biology · doi:10.1083/jcb.202507014 · Cited by 8
Self-citationZhang, L., Ren, C., Liu, J., Huang, S., Wu, C., & Zhang, J. (2024) · Drug Discovery Today · doi:10.1016/j.drudis.2024.103995 · Cited by 8
Nguyen, D. M., & Chen, T. (2022) · Handbook of experimental pharmacology · doi:10.1007/164_2022_595 · Cited by 8
Self-citationGrigoriev, V. V. (2021) · Biomeditsinskaya Khimiya · doi:10.18097/pbmc20216701017 · Cited by 8
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Koh, Y. H., Kim, S., & Roh, S. (2024) · FEBS Letters · doi:10.1002/1873-3468.15059 · Cited by 7
Kostritskii, A. Y., Kostritskaia, Y., Dmitrieva, N., Stauber, T., & Machtens, J. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2421900122 · Cited by 7
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Cao, X., Zhou, Z., Tian, Y., Liu, Z., Cheng, K. O., Chen, X., Hu, W., Wong, Y. M., Li, X., Zhang, H., et al. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100738 · Cited by 7
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Yuan, W., Cui, C.-C., Li, J., Xu, Y.-H., Fan, C., Chen, Y., Fan, H., Hu, B.-X., Shi, M., Sun, Z., et al. (2022) · iScience · doi:10.1016/j.isci.2022.105446 · Cited by 7
Zhang, B., Zhang, W., Pearce, R., Zhang, Y., & Shen, H. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c09903 · Cited by 7
Anada, C., Ikeda, K., Nakao, H., & Nakano, M. (2022) · Langmuir · doi:10.1021/acs.langmuir.2c00533 · Cited by 7
Arreola, J., López-Romero, A. E., Pérez‐Cornejo, P., & Rodríguez‐Menchaca, A. A. (2023) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-21547-6_10 · Cited by 7
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Mata‐Daboin, A., Garrud, T. A. C., & Jaggar, J. H. (2025) · The Journal of Physiology · doi:10.1113/jp287608 · Cited by 6
Yang, X., Ding, Z., Peng, L., Song, Q., Zhang, D., Cui, F., Xia, C., Li, K., Yin, H., Li, S., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34364-9 · Cited by 6
Roh, J. W., Hwang, G. E., Kim, W. K., & Nam, J. H. (2021) · Molecules and Cells · doi:10.14348/molcells.2021.2203 · Cited by 6
Tembo, M., Bainbridge, R. E., Lara‐Santos, C., Komondor, K. M., Daskivich, G. J., Durrant, J. D., Rosenbaum, J. C., & Carlson, A. E. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102264 · Cited by 7
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Henckels, K., Fong, D., & Phillips, J. E. (2020) · Assay and Drug Development Technologies · doi:10.1089/adt.2019.962 · Cited by 5
Guo, X., Geng, R., Li, C., Ma, Z., Chen, Y., Liu, Y., Li, S., Kang, X., & Guo, S. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.134057 · Cited by 5
Yu, Z., Chen, Y., Zheng, B., Cai, Z., Zou, Y., Ke, J., Lan, P., Gao, F., & Wu, X. (2021) · Cancer Cell International · doi:10.1186/s12935-021-01794-2 · Cited by 5
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Liu, X., Xiao-hong, J., Hong, Q., Wang, X., Wu, M., Xing, W., Xu, M., Hu, C., & Hao, F. (2022) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-022-01119-8 · Cited by 4
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Zhang, Y., Wu, K., Li, Y., Wu, S., Warshel, A., & Bai, C. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.3c11940 · Cited by 4
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Korte, N., Ilkan, Z., Pearson, C. L., Pfeiffer, T., Singhal, P., Rock, J. R., Sethi, H., Gill, D., Attwell, D., & Tammaro, P. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.02.03.479031 · Cited by 4
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Zhang, S., Luo, S., Zhang, H., & Xiao, Q. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.143598 · Cited by 3
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Hu, Y., & Tuo, B. (2025) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2025.5540 · Cited by 3
Kaye, R., Pearson, C. L., Babiker, T., Agostinelli, E., Al‐Hosni, R., & Tammaro, P. (2025) · British Journal of Pharmacology · doi:10.1111/bph.70077 · Cited by 3
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Li, S., & Yan, Z. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-981-16-4254-8_17 · Cited by 3
Morán, Ó., & Tammaro, P. (2024) · Biophysical Chemistry · doi:10.1016/j.bpc.2024.107194 · Cited by 3
Clark, S., Jeong, H., Posert, R., Goehring, A. S., & Gouaux, E. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.16.553618 · Cited by 3
Ebrahim, S., Ballesteros, Á., Zheng, W., Mukherjee, S., Hu, G., Weng, W.-H., Montgomery, J. S., Agyemang, Y., Cui, R., Sun, W. W., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.22.609173 · Cited by 3
Stephens, C. A., van Hilten, N., Zheng, L., & Grabe, M. (2025) · eLife · doi:10.7554/elife.105111.1 · Cited by 3
Stephens, C. A., van Hilten, N., Zheng, L., & Grabe, M. (2025) · eLife · doi:10.7554/elife.105111 · Cited by 3
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Petit, C., & Avan, P. (2025) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2025.103148 · Cited by 2
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Feng, Z., Alvarenga, O. E., Zanni, E. D., Lee, S., Khelashvili, G., & Accardi, A. (2026) · Nature Structural & Molecular Biology · doi:10.1038/s41594-026-01789-5 · Cited by 2
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Zheng, K., Hu, J., Hu, C., Liu, X., Wang, Y., Han, H., Xing, W., Yang, L., Zhang, J., Hong, Q., et al. (2024) · Molecules · doi:10.3390/molecules29051036 · Cited by 2
TMEM16 Proteins (Anoctamins) in Epithelia
Scudieri, P., & Galietta, L. J. V. (2020) · Physiology in health and disease · doi:10.1007/978-3-030-55454-5_17 · Cited by 2
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Billesbølle, C. B., Azumaya, C. M., Kretsch, R. C., Powers, A. S., Gonen, S., Schneider, S., Arvedson, T., Dror, R. O., Cheng, Y., & Manglik, A. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.16.993006 · Cited by 3
Self-citationIon Channels as Therapeutic Drug Targets
García, M. L., & Kaczorowski, G. J. (2021) · Wiley eBooks · doi:10.1002/0471266949.bmc255 · Cited by 2
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Kang, H., Jeong, H., Han, A. R., Koh, W., Lee, J. M., Jo, H., Lee, H., Bhalla, M., Roh, W. S., Jang, H. J., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.01.03.522543 · Cited by 2
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Zhou, C. X., Li, H., Wang, J., Chu, Z., Sun, S., Sun, K., Zhu, A., Wang, J., Jin, X., Yang, F., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.25.630309 · Cited by 2
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Townsend, C. Y. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820472-6.99998-5 · Cited by 1
Zhou, Y., Li, R., Wang, K., Lin, F., Chen, Y., Yang, J., Han, H., Tu, L., Jia, Y., Yuan, K., et al. (2024) · Journal of Stroke and Cerebrovascular Diseases · doi:10.1016/j.jstrokecerebrovasdis.2024.107579 · Cited by 1
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Li, X. Y., Wang, Y., Zhang, L., Yao, S., Liu, Q., Jin, H. D., & Tuo, B. (2024) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.18320 · Cited by 1
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Teulon, J., Planelles, G., Sepúlveda, F. V., Andrini, O., Lourdel, S., & Paulais, M. (2019) · Comprehensive physiology · doi:10.1002/j.2040-4603.2019.tb00065.x · Cited by 1
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Zhang, X., Lin, J., Xu, H., Zhou, Y., Mu, Z., Shi, R., & Lv, Y. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1599100 · Cited by 1
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Babar, Z., Wahid, J., Ji, X., Zhao, H., Yu, H., & Wang, D. (2025) · Chinese Physics B · doi:10.1088/1674-1056/ae172d · Cited by 1
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Self-citationKomariah, A. (2021) · Psychology and Education Journal · doi:10.17762/pae.v58i1.820 · Cited by 1
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Gao, Y. (2022) · Springer eBooks · doi:10.1007/978-981-19-7122-8_4 · Cited by 1
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Takayama, Y., Shibasaki, K., Furue, H., Uta, D., & Tominaga, M. (2018) · PAIN RESEARCH · doi:10.11154/pain.33.1 · Cited by 1
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Sierra-Valdez, F. J., Stein, R. A., Velisetty, P., Vásquez, V., & Cordero-Morales, J. F. (2018) · Journal of Visualized Experiments · doi:10.3791/57796 · Cited by 1
Fain, G. (2019) · Oxford University Press eBooks · doi:10.1093/oso/9780198835028.003.0001 · Cited by 1
Fain, G. (2019) · Oxford University Press eBooks · doi:10.1093/oso/9780198835028.003.0008 · Cited by 1
Akabas, M. H. (2020) · Encyclopedia of Life Sciences · doi:10.1002/9780470015902.a0000039.pub3 · Cited by 1
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Vasodilators activate TMEM16A channels in endothelial cells to reduce blood pressurePreprint
Mata‐Daboin, A., Garrud, T. A. C., Fernández‐Peña, C., Peixoto‐Neves, D., Leo, M. D., Bernardelli, A. K., Singh, P., Malik, K. U., & Jaggar, J. H. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.02.543450 · Cited by 1
Unraveling membrane protein localization and stabilization in nanodiscsPreprint
Kim, S.-J., Koh, Y. H., & Roh, S. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.07.20.549795 · Cited by 1
Stephens, C. A., van Hilten, N., Zheng, L., & Grabe, M. (2025) · eLife · doi:10.7554/elife.105111.2 · Cited by 1
TMEM16 Proteins (Anoctamins) in Epithelia
Scudieri, P., & Galietta, L. J. V. (2015) · Springer eBooks · doi:10.1007/978-1-4939-3366-2_17
A Phosphoinositide Binding Module Controls TMEM16A Desensitization
Le, S. C., Jia, Z., Chen, J., & Yang, H. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2018.11.2151
Improving the resolution of Cryo-EM single particle analysisPreprint
Luo, Z. (2019) · arXiv (Cornell University) · doi:10.48550/arxiv.1905.13408
Channels and electrical signals
Fain, G. (2019) · Oxford University Press eBooks · doi:10.1093/oso/9780198835028.003.0003
Fain, G. (2019) · Oxford University Press eBooks · doi:10.1093/oso/9780198835028.003.0005
Chemoreception and the sense of smell
Fain, G. (2019) · Oxford University Press eBooks · doi:10.1093/oso/9780198835028.003.0007
Metadata
- Authors
- Dang, S., Feng, S., Tien, J., Peters, C. J., Bulkley, D., Lolicato, M., Zhao, J., Zuberbühler, K., Ye, W., Qi, L., Chen, T., Craik, C. S., Jan, Y. N., Minor, D. L., Cheng, Y., & Jan, L. Y.
- Affiliations
- University of California, San Francisco (US)
- Howard Hughes Medical Institute (US)
- Lawrence Berkeley National Laboratory (US)
- Corresponding author
- Cheng, Yifan
- Jan, Lily Yeh
- ORCID
- Venue
- Nature
- Published
- 2017-12
- Volume
- 552
- Issue
- 7685
- Pages
- 426-429
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC5750132
- OpenAlex
- W2774013165
- Cited by
- 333
- References
- 54
- Citations by year
- 2026: 16 · 2025: 29 · 2024: 32 · 2023: 28 · 2022: 38 · 2021: 54 · 2020: 40 · 2019: 64 · 2018: 29
- FWCI
- 15.18
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Rare & Special e-Zone (The Hong Kong University of Science and Technology) (submittedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institutes of Health (1s10od020054-01)
- National Heart, Lung, and Blood Institute (R01HL080050)
- National Institute on Drug Abuse (K99DA041500)
- National Cancer Institute (P41CA196276)
- National Institute on Deafness and Other Communication Disorders (R01DC007664)
- National Institute of General Medical Sciences (P50GM082250, P01GM111126, R01GM098672)
- National Institute of Neurological Disorders and Stroke (R01NS069229, R35NS097227)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Keywords
- TMEM16A, calcium-activated chloride channels, TMEM16, channel gating, calcium binding, channel rundown, nanodiscs, detergent solubilization, pore-lining residues, lipid scramblase, channel structure-function relationship
- MeSH terms
- Anoctamin-1, Animals, Anions, Calcium, Glucosides, Humans, Models, Molecular, Protein Conformation, Ion Channel Gating, Ion Transport, Cryoelectron Microscopy, Nanostructures, Mice, HEK293 Cells
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