ORAI1 channel gating and selectivity is differentially altered by natural mutations in the first or third transmembrane domain-Reference-Cited by-同舟云学术

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ORAI1 channel gating and selectivity is differentially altered by natural mutations in the first or third transmembrane domain

Published:2018-11-28 Issue:2 Volume:597 Page:561-582
ISSN:0022-3751
Container-title:The Journal of Physiology
language:en
Short-container-title:J Physiol

Author:

Bulla M.¹^ORCID,Gyimesi G.²,Kim J.H.³⁴,Bhardwaj R.²,Hediger M.A.²^ORCID,Frieden M.¹,Demaurex N.¹^ORCID

Affiliation:

1. Department of Cell Physiology and MetabolismUniversity of Geneva Geneva Switzerland

2. Institute of Biochemistry and Molecular MedicineUniversity of Bern Bern Switzerland

3. Departments of Physiology and Global Medical ScienceYonsei University Wonju College of Medicine Wonju Republic of Korea

4. Mitohormesis Research CenterYonsei University Wonju College of Medicine Wonju Republic of Korea

Publisher

Wiley

Subject

Physiology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1113/JP277079

Reference101 articles.

1. GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers

2. Thiol dependent intramolecular locking of Orai1 channels

3. Molecular Biophysics of Orai Store-Operated Ca2+ Channels

4. Toward high-resolution prediction and design of transmembrane helical protein structures

5. Regulation of endogenous and heterologous Ca2+ release-activated Ca2+ currents by pH

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