Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

Distinct Orai-coupling domains in STIM1 and STIM2 define the Orai-activating site
Xizhuo Wang, Youjun Wang, Yandong Zhou, et al.
Nature Communications (2014) Vol. 5, Iss. 1
Open Access | Times Cited: 149

Showing 1-25 of 149 citing articles:

Store-Operated Calcium Channels
Murali Prakriya, Richard S. Lewis
Physiological Reviews (2015) Vol. 95, Iss. 4, pp. 1383-1436
Open Access | Times Cited: 1082
Calcium signalling in T cells
Mohamed Trebak, Jean-Pierre Kinet
Nature reviews. Immunology (2019) Vol. 19, Iss. 3, pp. 154-169
Open Access | Times Cited: 404
Near-infrared photoactivatable control of Ca2+ signaling and optogenetic immunomodulation
Lian He, Yuanwei Zhang, Guolin Ma, et al.
eLife (2015) Vol. 4
Open Access | Times Cited: 209
Store-operated calcium entry: Mechanisms and modulation
Patrick G. Hogan, Anjana Rao
Biochemical and Biophysical Research Communications (2015) Vol. 460, Iss. 1, pp. 40-49
Open Access | Times Cited: 200
Proteomic mapping of ER–PM junctions identifies STIMATE as a regulator of Ca2+ influx
Jing Ji, Lian He, Aomin Sun, et al.
Nature Cell Biology (2015) Vol. 17, Iss. 10, pp. 1339-1347
Open Access | Times Cited: 197
Crosstalk between calcium and reactive oxygen species signaling in cancer
Nadine Hempel, Mohamed Trebak
Cell Calcium (2017) Vol. 63, pp. 70-96
Open Access | Times Cited: 195
Inside-out Ca2+ signalling prompted by STIM1 conformational switch
Guolin Ma, Ming Wei, Lian He, et al.
Nature Communications (2015) Vol. 6, Iss. 1
Open Access | Times Cited: 163
Elevated Orai1 expression mediates tumor-promoting intracellular Ca2+ oscillations in human esophageal squamous cell carcinoma
Hua Zhu, Hui Zhang, Feng Jin, et al.
Oncotarget (2014) Vol. 5, Iss. 11, pp. 3455-3471
Open Access | Times Cited: 136
Molecular mechanisms of STIM/Orai communication
Isabella Derler, Isaac Jardín, Christoph Romanin
AJP Cell Physiology (2016) Vol. 310, Iss. 8, pp. C643-C662
Open Access | Times Cited: 124
A Coiled-coil Clamp Controls Both Conformation and Clustering of Stromal Interaction Molecule 1 (STIM1)
Marc Fahrner, Martin Muik, Rainer Schindl, et al.
Journal of Biological Chemistry (2014) Vol. 289, Iss. 48, pp. 33231-33244
Open Access | Times Cited: 119
Quantitative Lipid Imaging Reveals a New Signaling Function of Phosphatidylinositol-3,4-Bisphophate: Isoform- and Site-Specific Activation of Akt
Shu‐Lin Liu, Zhigang Wang, Yusi Hu, et al.
Molecular Cell (2018) Vol. 71, Iss. 6, pp. 1092-1104.e5
Open Access | Times Cited: 118
A STIM2 splice variant negatively regulates store-operated calcium entry
Anna-Maria Miederer, Dalia Alansary, Gertrud Schwär, et al.
Nature Communications (2015) Vol. 6, Iss. 1
Open Access | Times Cited: 114
STIM and ORAI proteins in the nervous system
Robert Kraft
Channels (2015) Vol. 9, Iss. 5, pp. 245-252
Open Access | Times Cited: 111
The Orai1 Store-operated Calcium Channel Functions as a Hexamer
Xiangyu Cai, Yandong Zhou, Robert M. Nwokonko, et al.
Journal of Biological Chemistry (2016) Vol. 291, Iss. 50, pp. 25764-25775
Open Access | Times Cited: 103
Alternative splicing converts STIM2 from an activator to an inhibitor of store-operated calcium channels
Anshul Rana, Michelle Yen, Amir Masoud Sadaghiani, et al.
The Journal of Cell Biology (2015) Vol. 209, Iss. 5, pp. 653-670
Open Access | Times Cited: 101
Mitochondria control store‐operated Ca 2+ entry through Na + and redox signals
Tsipi Ben-Kasus Nissim, Xuexin Zhang, Assaf Elazar, et al.
The EMBO Journal (2017) Vol. 36, Iss. 6, pp. 797-815
Open Access | Times Cited: 95
Store-Operated Crac Channel Inhibitors: Opportunities and Challenges
Chengsen Tian, Lüpei Du, Yubin Zhou, et al.
Future Medicinal Chemistry (2016) Vol. 8, Iss. 7, pp. 817-832
Open Access | Times Cited: 90
STIM1 activation of Orai1
Victoria Lunz, Christoph Romanin, Irene Frischauf
Cell Calcium (2018) Vol. 77, pp. 29-38
Open Access | Times Cited: 88
Role of TRPC Channels in Store-Operated Calcium Entry
Hwei Ling Ong, Lorena Brito de Souza, Indu S. Ambudkar
Advances in experimental medicine and biology (2016), pp. 87-109
Closed Access | Times Cited: 86
The STIM1-binding site nexus remotely controls Orai1 channel gating
Yandong Zhou, Xiangyu Cai, Natalia A. Loktionova, et al.
Nature Communications (2016) Vol. 7, Iss. 1
Open Access | Times Cited: 86
Omnitemporal choreographies of all five STIM/Orai and IP3Rs underlie the complexity of mammalian Ca2+ signaling
Scott M. Emrich, Ryan E. Yoast, Ping Xin, et al.
Cell Reports (2021) Vol. 34, Iss. 9, pp. 108760-108760
Open Access | Times Cited: 75
Orai1 Inhibitors as Potential Treatments for Pulmonary Arterial Hypertension
Bastien Masson, Hélène Le Ribeuz, Jessica Sabourin, et al.
Circulation Research (2022) Vol. 131, Iss. 9
Open Access | Times Cited: 44
Ca2+ dynamics in interstitial cells: foundational mechanisms for the motor patterns in the gastrointestinal tract
Kenton M. Sanders, Bernard T. Drumm, Caroline A. Cobine, et al.
Physiological Reviews (2023) Vol. 104, Iss. 1, pp. 329-398
Closed Access | Times Cited: 26
Cellular calcium homeostasis and regulation of its dynamic perturbation
Colin Brownlee, Glen L. Wheeler
Quantitative Plant Biology (2025) Vol. 6
Open Access | Times Cited: 1
STIM2 enhances receptor-stimulated Ca 2+ signaling by promoting recruitment of STIM1 to the endoplasmic reticulum–plasma membrane junctions
Hwei Ling Ong, Lorena Brito de Souza, Changyu Zheng, et al.
Science Signaling (2015) Vol. 8, Iss. 359
Open Access | Times Cited: 90
Page 1 - Next Page

Scroll to top