Transient Receptor Potential Canonical 6 (TRPC6) Channel in the Pathogenesis of Diseases: A Jack of Many Trades-Reference-Cited by-同舟云学术

Transient Receptor Potential Canonical 6 (TRPC6) Channel in the Pathogenesis of Diseases: A Jack of Many Trades

Published:2023-04-18 Issue:4 Volume:46 Page:1144-1160
ISSN:0360-3997
Container-title:Inflammation
language:en
Short-container-title:Inflammation

Author:

Saqib Uzma,Munjuluri Sreepadaarchana,Sarkar Sutripta,Biswas Subir,Mukherjee Oyshi,Satsangi Hargopal,Baig Mirza S.,Obukhov Alexander G.,Hajela Krishnan

Funder

University Grants Commission

Publisher

Springer Science and Business Media LLC

Subject

Immunology,Immunology and Allergy

Link

https://link.springer.com/content/pdf/10.1007/s10753-023-01808-3.pdf

Reference122 articles.

1. Chen, X., G. Sooch, I.S. Demaree, F.A. White, and A.G. Obukhov. 2020. Transient Receptor Potential Canonical (TRPC) channels: then and now, Cells. 9.

2. Wes, P.D., J. Chevesich, A. Jeromin, C. Rosenberg, G. Stetten, and C. Montell. 1995. TRPC1, a human homolog of a Drosophila store-operated channel. Proceedings of the National Academy of Sciences USA 92: 9652–9656.

3. Zhu, X., P.B. Chu, M. Peyton, and L. Birnbaumer. 1995. Molecular cloning of a widely expressed human homologue for the Drosophila trp gene. FEBS Letters 373: 193–198.

4. Fan, C., W. Choi, W. Sun, J. Du, and W. Lu. 2018. Structure of the human lipid-gated cation channel TRPC3. Elife. 7.

5. Sierra-Valdez, F., C.M. Azumaya, L.O. Romero, T. Nakagawa, and J.F. Cordero-Morales. 2018. Structure-function analyses of the ion channel TRPC3 reveal that its cytoplasmic domain allosterically modulates channel gating. Journal of Biological Chemistry 293: 16102–16114.

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