H, C and N chemical shift assignments for the N-terminal domain of the voltage-gated potassium channel-hERG
Biomolecular NMR Assignments, ISSN: 1874-2718, Vol: 4, Issue: 2, Page: 211-213
2010
- 15Citations
- 3Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations15
- Citation Indexes15
- 15
- CrossRef12
- Captures3
- Readers3
Article Description
The human ether à go-go related gene (hERG) voltage-gated potassium controls the rapid delayed rectifier potassium current (I) in heart. The N-terminal 135 amino acids (NTD) form a Per-Arnt-Sim (PAS) domain which involves in signal transduction and protein-protein interactions. NTD was shown to be necessary for the regulation of the channel activity through its interaction with the channel pore region of hERG. Mutations in NTD were related to serious heart diseases. We report the H, C and N chemical shift assignments for NTD using 2D and 3D heteronuclear NMR experiments. More than 95% backbone resonance assignments were obtained. © 2010 Springer Science+Business Media B.V.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=77957970678&origin=inward; http://dx.doi.org/10.1007/s12104-010-9248-3; http://www.ncbi.nlm.nih.gov/pubmed/20607461; http://link.springer.com/10.1007/s12104-010-9248-3; https://dx.doi.org/10.1007/s12104-010-9248-3; https://link.springer.com/article/10.1007/s12104-010-9248-3; http://www.springerlink.com/index/10.1007/s12104-010-9248-3; http://www.springerlink.com/index/pdf/10.1007/s12104-010-9248-3
Springer Science and Business Media LLC
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