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OpenAlex Citation Counts

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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:

Human XPR1 structures reveal phosphate export mechanism
Rui Yan, Huiwen Chen, Chuanyu Liu, et al.
Nature (2024) Vol. 633, Iss. 8031, pp. 960-967
Closed Access | Times Cited: 13

Showing 13 citing articles:

Structural insights into the mechanism of phosphate recognition and transport by XPR1
Wenhui Zhang, Y.J. Chen, Zeyuan Guan, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 2
Structural basis of phosphate export by human XPR1
Qixian He, Ran Zhang, Sandrine Tury, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 1
Structural mechanism underlying PHO1;H1-mediated phosphate transport in Arabidopsis
Sunzhenhe Fang, Yang Yang, Xue Zhang, et al.
Nature Plants (2025)
Closed Access
Astrocytes in Primary Familial Brain Calcification (PFBC): Emphasis on the Importance of Induced Pluripotent Stem Cell-Derived Human Astrocyte Models
Ebru Kavakli, Nazish Gul, Onur Can Begentas, et al.
Advances in experimental medicine and biology (2025)
Closed Access
Structural basis of phosphate export by human XPR1
Yifei Wang, Yingrong Wang, Hui Yang, et al.
Cell Research (2025)
Open Access
Transport and InsP8 gating mechanisms of the human inorganic phosphate exporter XPR1
Qinyu Zhu, Madeleine F. Yaggi, Nikolaus Jork, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Synergistic activation of the human phosphate exporter XPR1 by KIDINS220 and inositol pyrophosphate
Peng Zuo, Weize Wang, Zonglin Dai, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Structure and function of human XPR1 in phosphate export
Long Chen, Jin He, Mingxing Wang, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Transport and InsP8activation mechanisms of the human inorganic phosphate exporter XPR1
Qinyu Zhu, Madeleine F. Yaggi, Nikolaus Jork, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 2
The Solute Carrier (SLC) Transporter Superfamily as Therapeutic Targets for the Treatment of Head and Neck Squamous Cell Carcinoma
Sang Yeon Cho, Nam Sook Kang
Cancers (2024) Vol. 16, Iss. 18, pp. 3226-3226
Open Access | Times Cited: 1
NUDIX Hydrolases Target Specific Inositol Pyrophosphates and Regulate Phosphate and Iron Homeostasis, and the Expression of Defense Genes in Arabidopsis
Robin Schneider, Klea Lami, Isabel Prucker, et al.
(2024)
Open Access | Times Cited: 1
The putative polyamine transporter Shp2 facilitates phosphate export in an Xpr1-independent manner and contributes to high phosphate tolerance
Tochi Komamura, Tomoki Nishimura, Naoki Ohta, et al.
Journal of Biological Chemistry (2024), pp. 108056-108056
Closed Access
Insights into phosphate homeostasis regulation by XPR1
Daniel P. Bondeson
Nature Structural & Molecular Biology (2024)
Closed Access
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