Backbone resonance assignments of complexes of apo human calmodulin bound to IQ motif peptides of voltage-dependent sodium channels NaV1.1, NaV1.4 and NaV1.7-Reference-Cited by-同舟云学术

Backbone resonance assignments of complexes of apo human calmodulin bound to IQ motif peptides of voltage-dependent sodium channels NaV1.1, NaV1.4 and NaV1.7

Published:2018-05-04 Issue:2 Volume:12 Page:283-289
ISSN:1874-2718
Container-title:Biomolecular NMR Assignments
language:en
Short-container-title:Biomol NMR Assign

Author:

Isbell Holly M.^ORCID,Kilpatrick Adina M.^ORCID,Lin Zesen^ORCID,Mahling Ryan^ORCID,Shea Madeline A.^ORCID

Funder

Carver College of Medicine University of Iowa

National Institutes of Health

Office of the Vice President for Research and Economic Development, University of Iowa

University of Iowa

Publisher

Springer Science and Business Media LLC

Subject

Biochemistry,Structural Biology

Link

http://link.springer.com/article/10.1007/s12104-018-9824-5/fulltext.html

Reference29 articles.

1. Ben-Johny M, Yue DN, Yue DT (2016) Detecting stoichiometry of macromolecular complexes in live cells using FRET. Nat Commun 7:13709

2. Branco T, Tozer A, Magnus CJ, Sugino K, Tanaka S, Lee AK, Wood JN, Sternson SM (2016) Near-perfect synaptic integration by NaV1.7 in hypothalamic neurons regulates body weight. Cell 165:1749–1761

3. Chagot B, Chazin WJ (2011) Solution NMR structure of apo-calmodulin in complex with the IQ Motif of human cardiac sodium channel NaV1.5. J Mol Biol 406:106–119

4. Damo SM, Feldkamp MD, Chagot B, Chazin WJ (2013) NMR studies of the interaction of calmodulin with IQ motif peptides. Methods Mol Biol 963:173–186

5. Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293

Cited by 7 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Feedback contributions to excitation–contraction coupling in native functioning striated muscle;Philosophical Transactions of the Royal Society B: Biological Sciences;2023-05

2. NaV1.2 EFL domain allosterically enhances Ca2+ binding to sites I and II of WT and pathogenic calmodulin mutants bound to the channel CTD;Structure;2021-12

3. Focus on the role of Na(v)1.7 channel as molecular target of methocarbamol and its analgesic effects;Muscle & Nerve;2021-10-15

4. Calmodulin Interactions with Voltage-Gated Sodium Channels;International Journal of Molecular Sciences;2021-09-10

5. Properties of Calmodulin Binding to NaV1.2 IQ Motif and Its Autism-Associated Mutation R1902C;Neurochemical Research;2021-01-04