Open Access Helper

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 26-50 of 40 citing articles:

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.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 1
Conditional ablation of protein tyrosine phosphatase receptor U in midbrain dopaminergic neurons results in reduced neuronal size
Jiwei Liu, Yang Li, Han Li, et al.
Journal of Chemical Neuroanatomy (2022) Vol. 124, pp. 102135-102135
Closed Access | Times Cited: 1
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.
(2023)
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 (2023) Vol. 12
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.
(2023)
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.
(2023)
Open Access
eLife assessment: Styxl2 regulates de novo sarcomere assembly by binding to non-muscle myosin IIs and promoting their degradation
Noboru Mizushima
(2023)
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.
(2023)
Open Access
Protein tyrosine phosphatase non-receptor type 2 as the therapeutic target of atherosclerotic diseases: past, present and future
Xiao-Er Tang, Ya-Qiong Cheng, Chao‐Ke Tang
Frontiers in Pharmacology (2023) Vol. 14
Open Access
Understanding Pseudophosphatase Function Through Biochemical Interactions
Shantá D. Hinton
Methods in molecular biology (2023), pp. 21-41
Closed Access
Posttranslational Modifications: Key Players in Health and Disease
J. Fontiñan-Rubio, Juan R. Peinado, �. Lindberg, et al.
Elsevier eBooks (2022), pp. 385-395
Closed Access
The progress of research into pseudophosphatases
Deqiang Liu, Yiming Zhang, Hui Fang, et al.
Frontiers in Public Health (2022) Vol. 10
Open Access
Applications of nuclear magnetic resonance spectroscopy: from drug discovery to protein structure and dynamics.
Mark Vincent dela Cerna
(2022)
Open Access
Styxl2 regulatesde novosarcomere assembly by binding to non-muscle myosin IIs and promoting their degradation
Xianwei Chen, Yanfeng Li, Jin Xu, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access
The FEBS Journal in 2021: a sharp reminder that science really matters
Séamus J. Martin
FEBS Journal (2021) Vol. 288, Iss. 1, pp. 4-9
Open Access
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