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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:

The dead phosphatases society: a review of the emerging roles of pseudophosphatases
Veronika Reiterer, Krzysztof Pawłowski, Guillaume Desrochers, et al.
FEBS Journal (2020) Vol. 287, Iss. 19, pp. 4198-4220
Open Access | Times Cited: 40

Showing 1-25 of 40 citing articles:

Pseudophosphatases as Regulators of MAPK Signaling
Emma Marie Wilber Hepworth, Shantá D. Hinton
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 22, pp. 12595-12595
Open Access | Times Cited: 51
Protein tyrosine phosphatases in cell adhesion
Katherine A. Young, Laura Biggins, Hayley J. Sharpe
Biochemical Journal (2021) Vol. 478, Iss. 5, pp. 1061-1083
Open Access | Times Cited: 32
Emerging functions of pseudoenzymes
Timea Goldberg, Anju Sreelatha
Biochemical Journal (2023) Vol. 480, Iss. 10, pp. 715-728
Open Access | Times Cited: 9
A PPP-type pseudophosphatase is required for the maintenance of basal complex integrity in Plasmodium falciparum
Alexander A. Morano, Rachel M. Rudlaff, Jeffrey D. Dvorin
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 9
The Roles of Pseudophosphatases in Disease
Andrew M. Mattei, Jonathan D. Smailys, Emma Marie Wilber Hepworth, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 13, pp. 6924-6924
Open Access | Times Cited: 16
Dual-specificity phosphatases 13 and 27 as key switches in muscle stem cell transition from proliferation to differentiation
Takuto Hayashi, Shunya Sadaki, Ryosuke Tsuji, et al.
Stem Cells (2024) Vol. 42, Iss. 9, pp. 830-847
Open Access | Times Cited: 2
The expanding landscape of canonical and non-canonical protein phosphorylation
Thibault Houlès, Sang-Oh Yoon, Philippe P. Roux
Trends in Biochemical Sciences (2024) Vol. 49, Iss. 11, pp. 986-999
Closed Access | Times Cited: 2
Release of CHK-2 from PPM-1.D anchorage schedules meiotic entry
Antoine Baudrimont, Dimitra Paouneskou, Ariz Mohammad, et al.
Science Advances (2022) Vol. 8, Iss. 7
Open Access | Times Cited: 11
HPV18 E7 inhibits LATS1 kinase and activates YAP1 by degrading PTPN14
William J. Blakely, Joshua Hatterschide, Elizabeth White
mBio (2024)
Open Access | Times Cited: 1
Pseudoenzymes: dead enzymes with a lively role in biology
Colin Adrain
FEBS Journal (2020) Vol. 287, Iss. 19, pp. 4102-4105
Open Access | Times Cited: 9
Structural characterization of a pathogenic mutant of human protein tyrosine phosphatase PTPN2 ( Cys216Gly ) that causes very early onset autoimmune enteropathy
Qing Nian, Jérémy Berthelet, Marianna Parlato, et al.
Protein Science (2021) Vol. 31, Iss. 2, pp. 538-544
Open Access | Times Cited: 8
Conserved Structure Modules within the lncRNA SChLAP1 Mediate Protein Recognition Implicated in Aggressive Prostate Cancer
Emily J. McFadden, James P. Falese, Amanda E. Hargrove
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 5
The CHK-2 antagonizing phosphatase PPM-1.D regulates meiotic entry via catalytic and non-catalytic activities
Antoine Baudrimont, Dimitra Paouneskou, Ariz Mohammad, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 4
Evolutionary genomic relationships and coupling in MK-STYX and STYX pseudophosphatases
Qi Yi, Di “Silas” Kuang, Kylan Kelley, et al.
Scientific Reports (2022) Vol. 12, Iss. 1
Open Access | Times Cited: 3
Author Response: Styxl2 regulates de novo sarcomere assembly by binding to non-muscle myosin IIs and promoting their degradation
Xianwei Chen, Yanfeng Li, Jin Xu, et al.
(2024)
Open Access
eLife assessment: Styxl2 regulates de novo sarcomere assembly by binding to non-muscle myosin IIs and promoting their degradation
Noboru Mizushima
(2024)
Open Access
Styxl2 regulates de novo sarcomere assembly by binding to non-muscle myosin IIs and promoting their degradation
Xianwei Chen, Yanfeng Li, Jin Xu, et al.
(2024)
Open Access
Reviewer #2 (Public Review): Styxl2 regulates de novo sarcomere assembly by binding to non-muscle myosin IIs and promoting their degradation
Xianwei Chen, Yanfeng Li, Jin Xu, et al.
(2024)
Open Access
Reviewer #3 (Public Review): Styxl2 regulates de novo sarcomere assembly by binding to non-muscle myosin IIs and promoting their degradation
Xianwei Chen, Yanfeng Li, Jin Xu, et al.
(2024)
Open Access
Reviewer #1 (Public Review): Styxl2 regulates de novo sarcomere assembly by binding to non-muscle myosin IIs and promoting their degradation
Xianwei Chen, Yanfeng Li, Jin Xu, et al.
(2024)
Open Access
HPV18 E7 inhibits LATS1 kinase and activates YAP1 by degrading PTPN14
William J. Blakely, Joshua Hatterschide, Elizabeth White
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Styxl2 regulates de novo sarcomere assembly by binding to non-muscle myosin IIs and promoting their degradation
Xianwei Chen, Yanfeng Li, Jin Xu, et al.
eLife (2024) Vol. 12
Open Access
Inactive metallopeptidase homologs: the secret lives of pseudopeptidases
Peter J. Lyons
Frontiers in Molecular Biosciences (2024) Vol. 11
Open Access
Pseudophosphatase STYXL1 depletion enhances glucocerebrosidase trafficking to lysosomes via ER stress
Saloni Patel, Anshul Milap Bhatt, Priyanka Bhansali, et al.
Traffic (2023) Vol. 24, Iss. 7, pp. 254-269
Open Access | Times Cited: 1
The DUSP domain of pseudophosphatase MK-STYX interacts with G3BP1 to decrease stress granules
Jonathan Smailys, Fei Jiang, Tatiana Prioleau, et al.
Archives of Biochemistry and Biophysics (2023) Vol. 744, pp. 109702-109702
Open Access | Times Cited: 1
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