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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:

LRRK2 dephosphorylation increases its ubiquitination
Jing Zhao, Tyler P. Molitor, J. William Langston, et al.
Biochemical Journal (2015) Vol. 469, Iss. 1, pp. 107-120
Open Access | Times Cited: 66

Showing 1-25 of 66 citing articles:

Inhibitor treatment of peripheral mononuclear cells from Parkinson’s disease patients further validates LRRK2 dephosphorylation as a pharmacodynamic biomarker
G. Perera, Madelaine Ranola, Dominic B. Rowe, et al.
Scientific Reports (2016) Vol. 6, Iss. 1
Open Access | Times Cited: 258
Interrogating Parkinson's disease LRRK2 kinase pathway activity by assessing Rab10 phosphorylation in human neutrophils
Ying Fan, Andrew J.M. Howden, Adil R. Sarhan, et al.
Biochemical Journal (2017) Vol. 475, Iss. 1, pp. 23-44
Open Access | Times Cited: 158
Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR
Loes M. Stevers, Chan Vinh Lam, S. Leysen, et al.
Proceedings of the National Academy of Sciences (2016) Vol. 113, Iss. 9
Open Access | Times Cited: 133
Selective LRRK2 kinase inhibition reduces phosphorylation of endogenous Rab10 and Rab12 in human peripheral mononuclear blood cells
Kenneth Thirstrup, Justus C. Dächsel, Felix Oppermann, et al.
Scientific Reports (2017) Vol. 7, Iss. 1
Open Access | Times Cited: 94
The associations between Parkinson’s disease and cancer: the plot thickens
Danielle Feng, Waijiao Cai, Xiqun Chen
Translational Neurodegeneration (2015) Vol. 4, Iss. 1
Open Access | Times Cited: 91
Progress and Challenges in Targeted Protein Degradation for Neurodegenerative Disease Therapy
Yingxu Fang, Jiaxing Wang, Min Zhao, et al.
Journal of Medicinal Chemistry (2022) Vol. 65, Iss. 17, pp. 11454-11477
Closed Access | Times Cited: 49
Pharmacological LRRK2 kinase inhibition induces LRRK2 protein destabilization and proteasomal degradation
Evy Lobbestael, Laura Civiero, Tina De Wit, et al.
Scientific Reports (2016) Vol. 6, Iss. 1
Open Access | Times Cited: 69
Small-Molecule Kinase Downregulators
Lyn H. Jones
Cell chemical biology (2017) Vol. 25, Iss. 1, pp. 30-35
Open Access | Times Cited: 65
Vitamin B12 modulates Parkinson’s disease LRRK2 kinase activity through allosteric regulation and confers neuroprotection
Adam Schaffner, Xianting Li, Yacob Gómez-Llorente, et al.
Cell Research (2019) Vol. 29, Iss. 4, pp. 313-329
Open Access | Times Cited: 58
Monomeric Targeted Protein Degraders
Emily J. Hanan, Jun Liang, Xiaojing Wang, et al.
Journal of Medicinal Chemistry (2020) Vol. 63, Iss. 20, pp. 11330-11361
Closed Access | Times Cited: 57
Binding of the Human 14-3-3 Isoforms to Distinct Sites in the Leucine-Rich Repeat Kinase 2
Jascha T. Manschwetus, Maximilian Wallbott, Alexandra Fachinger, et al.
Frontiers in Neuroscience (2020) Vol. 14
Open Access | Times Cited: 54
LRRK2 Phosphorylation, More Than an Epiphenomenon
Antoine Marchand, Matthieu Drouyer, Alessia Sarchione, et al.
Frontiers in Neuroscience (2020) Vol. 14
Open Access | Times Cited: 52
Understanding LRRK2 kinase activity in preclinical models and human subjects through quantitative analysis of LRRK2 and pT73 Rab10
Xiang Wang, Elvira Negrou, Michael T. Maloney, et al.
Scientific Reports (2021) Vol. 11, Iss. 1
Open Access | Times Cited: 47
Structural interface between LRRK2 and 14-3-3 protein
Loes M. Stevers, R.M.J.M. de Vries, Richard G. Doveston, et al.
Biochemical Journal (2017) Vol. 474, Iss. 7, pp. 1273-1287
Open Access | Times Cited: 59
Interrogating the Roles of Post-Translational Modifications of Non-Histone Proteins
Zakey Yusuf Buuh, Zhigang Lyu, Rongsheng E. Wang
Journal of Medicinal Chemistry (2017) Vol. 61, Iss. 8, pp. 3239-3252
Closed Access | Times Cited: 56
LRRK2 inhibitors and their potential in the treatment of Parkinson’s disease: current perspectives
Farzaneh Atashrazm, Nicolas Dzamko
Clinical Pharmacology Advances and Applications (2016) Vol. Volume 8, pp. 177-189
Open Access | Times Cited: 53
Clinically Precedented Protein Kinases: Rationale for Their Use in Neurodegenerative Disease
Caroline Benn, Lee A. Dawson
Frontiers in Aging Neuroscience (2020) Vol. 12
Open Access | Times Cited: 42
Pathways to Parkinson’s disease: a spotlight on 14-3-3 proteins
Elena Giusto, Talene A. Yacoubian, Elisa Greggio, et al.
npj Parkinson s Disease (2021) Vol. 7, Iss. 1
Open Access | Times Cited: 39
The Cell Biology of LRRK2 in Parkinson's Disease
Ahsan Usmani, Farbod Shavarebi, Annie Hiniker
Molecular and Cellular Biology (2021) Vol. 41, Iss. 5
Open Access | Times Cited: 34
The G2019S mutation in LRRK2 imparts resiliency to kinase inhibition
Kaela Kelly, Shijie Wang, Ravindra Boddu, et al.
Experimental Neurology (2018) Vol. 309, pp. 1-13
Open Access | Times Cited: 44
LRRK2 levels and phosphorylation in Parkinson's disease brain and cases with restricted Lewy bodies
Nicolas Dzamko, Amanda M. Gysbers, Rina Bandopadhyay, et al.
Movement Disorders (2016) Vol. 32, Iss. 3, pp. 423-432
Closed Access | Times Cited: 42
Post-translational modifications of Parkinson's disease-related proteins: Phosphorylation, SUMOylation and Ubiquitination
Stella C. Junqueira, Eduarda Gervini Zampieri Centeno, Kevin A. Wilkinson, et al.
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (2018) Vol. 1865, Iss. 8, pp. 2001-2007
Open Access | Times Cited: 39
LRRK2 Structure-Based Activation Mechanism and Pathogenesis
Xiaojuan Zhang, Arjan Kortholt
Biomolecules (2023) Vol. 13, Iss. 4, pp. 612-612
Open Access | Times Cited: 11
A personalized 14-3-3 disease-targeting workflow yields repositioning drug candidates
Yonika Arum Larasati, Gonzalo P. Solis, Alexey Koval, et al.
Research Square (Research Square) (2025)
Open Access
A Personalized 14-3-3 Disease-Targeting Workflow Yields Repositioning Drug Candidates
Yonika Arum Larasati, Gonzalo P. Solis, Alexey Koval, et al.
Cells (2025) Vol. 14, Iss. 8, pp. 559-559
Open Access
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