The polybasic lysine-rich domain of plasma membrane-resident STIM1 is essential for the modulation of store-operated divalent cation entry by extracellular calcium-Reference-Cited by-同舟云学术

The polybasic lysine-rich domain of plasma membrane-resident STIM1 is essential for the modulation of store-operated divalent cation entry by extracellular calcium

Published:2013-05 Issue:5 Volume:25 Page:1328-1337
ISSN:0898-6568
Container-title:Cellular Signalling
language:en
Short-container-title:Cellular Signalling

Author:

Jardin Isaac,Dionisio Natalia,Frischauf Irene,Berna-Erro Alejandro,Woodard Geoffrey E.,López José J.,Salido Ginés M.,Rosado Juan A.

Publisher

Elsevier BV

Subject

Cell Biology

Reference52 articles.

1. Exon structure and promoter identification of STIM1 (alias GOK), a human gene causing growth arrest of the human tumor cell lines G401 and RD

2. STIM1: a novel phosphoprotein located at the cell surface

3. Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation

4. A single EF-hand isolated from STIM1 forms dimer in the absence and presence of Ca2+

Cited by 16 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. STIM Proteins: The Gas and Brake of Calcium Entry in Neurons;Neuroscience Bulletin;2024-09-12

2. The Ca2+ Sensor STIM in Human Diseases;Biomolecules;2023-08-22

3. Activation mechanisms and structural dynamics of STIM proteins;The Journal of Physiology;2023-02-02

4. Paraquat is an agonist of STIM1 and increases intracellular calcium levels;Communications Biology;2022-10-30

5. Orai1α, but not Orai1β, co-localizes with TRPC1 and is required for its plasma membrane location and activation in HeLa cells;Cellular and Molecular Life Sciences;2022-01