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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:

A feed-forward pathway drives LRRK2 kinase membrane recruitment and activation
Edmundo G. Vides, Ayan Adhikari, Claire Y Chiang, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 46

Showing 1-25 of 46 citing articles:

Impact of 100 LRRK2 variants linked to Parkinson's disease on kinase activity and microtubule binding
Alexia F. Kalogeropulou, Elena Purlyte, Francesca Tonelli, et al.
Biochemical Journal (2022) Vol. 479, Iss. 17, pp. 1759-1783
Open Access | Times Cited: 87
Key genes and convergent pathogenic mechanisms in Parkinson disease
Robert Coukos, Dimitri Krainc
Nature reviews. Neuroscience (2024) Vol. 25, Iss. 6, pp. 393-413
Closed Access | Times Cited: 27
Leucine-Rich Repeat Kinases
Dario R. Alessi, Suzanne R. Pfeffer
Annual Review of Biochemistry (2024) Vol. 93, Iss. 1, pp. 261-287
Closed Access | Times Cited: 17
A STING–CASM–GABARAP pathway activates LRRK2 at lysosomes
Amanda Bentley‐DeSousa, Agnes Roczniak-Ferguson, Shawn M. Ferguson
The Journal of Cell Biology (2025) Vol. 224, Iss. 2
Open Access | Times Cited: 3
Rab29-dependent asymmetrical activation of leucine-rich repeat kinase 2
Hanwen Zhu, Francesca Tonelli, Martin Turk, et al.
Science (2023) Vol. 382, Iss. 6677, pp. 1404-1411
Open Access | Times Cited: 39
Genome-wide screen reveals Rab12 GTPase as a critical activator of Parkinson’s disease-linked LRRK2 kinase
Herschel S. Dhekne, Francesca Tonelli, Wondwossen M Yeshaw, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 35
Rab12 is a regulator of LRRK2 and its activation by damaged lysosomes
Xiang Wang, Vitaliy V. Bondar, Oliver B. Davis, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 22
Membrane remodeling properties of the Parkinson’s disease protein LRRK2
Xinbo Wang, Javier Espadas, Yumei Wu, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 43
Open Access | Times Cited: 17
Lysosomal stress drives the release of pathogenic α-synuclein from macrophage lineage cells via the LRRK2-Rab10 pathway
Tetsuro Abe, Tomoki Kuwahara, Shoichi Suenaga, et al.
iScience (2024) Vol. 27, Iss. 2, pp. 108893-108893
Open Access | Times Cited: 7
LRRK2 in Parkinson's disease: upstream regulation and therapeutic targeting
Yulan Xiong, Jianzhong Yu
Trends in Molecular Medicine (2024) Vol. 30, Iss. 10, pp. 982-996
Closed Access | Times Cited: 7
Parkinson’s VPS35[D620N] mutation induces LRRK2-mediated lysosomal association of RILPL1 and TMEM55B
Prosenjit Pal, Matthew Taylor, Yuko P. Y. Lam, et al.
Science Advances (2023) Vol. 9, Iss. 50
Open Access | Times Cited: 16
Localization of PPM1H phosphatase tunes Parkinson’s disease-linked LRRK2 kinase-mediated Rab GTPase phosphorylation and ciliogenesis
Wondwossen M Yeshaw, Ayan Adhikari, Claire Y Chiang, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 44
Open Access | Times Cited: 13
A Pathogenic Variant in Rab32 Causes Autosomal Dominant Parkinson's Disease and Activates LRRK2 Kinase
Emil K. Gustavsson, Jordan Follett, Joanne Trinh, et al.
(2024)
Open Access | Times Cited: 5
Lysosomal TBK1 responds to amino acid availability to relieve Rab7-dependent mTORC1 inhibition
Gabriel Talaia, Amanda Bentley‐DeSousa, Shawn M. Ferguson
The EMBO Journal (2024) Vol. 43, Iss. 18, pp. 3948-3967
Open Access | Times Cited: 5
Genome-wide screen reveals Rab12 GTPase as a critical activator of pathogenic LRRK2 kinase
Herschel S. Dhekne, Francesca Tonelli, Wondwossen M Yeshaw, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 11
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
Endogenous LRRK2 and PINK1 function in a convergent neuroprotective ciliogenesis pathway in the brain
Enrico Bagnoli, Yu‐En Lin, Sophie Burel, et al.
Proceedings of the National Academy of Sciences (2025) Vol. 122, Iss. 5
Open Access
LRRK2, lysosome damage, and Parkinson's disease
Amanda Bentley‐DeSousa, D.J. Clegg, Shawn M. Ferguson
Current Opinion in Cell Biology (2025) Vol. 93, pp. 102482-102482
Open Access
Effect of LRRK2 Inhibition on the Activity of Glucocerebrosidase in Patient-Specific Cells from Patients with Gaucher Disease
Tatiana Usenko, Katerina Basharova, Anastasia Bezrukova, et al.
Biochemistry (Moscow) (2025) Vol. 90, Iss. 1, pp. 99-106
Closed Access
Salmonella exploits LRRK2-dependent plasma membrane dynamics to invade host cells
Hongxian Zhu, Andrew M. Sydor, Bing-Ru Yan, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Is Glial Dysfunction the Key Pathogenesis of LRRK2-Linked Parkinson’s Disease?
Tatou Iseki, Yuzuru Imai, Nobutaka Hattori
Biomolecules (2023) Vol. 13, Iss. 1, pp. 178-178
Open Access | Times Cited: 10
A STING-CASM-GABARAP Pathway Activates LRRK2 at Lysosomes
Amanda Bentley‐DeSousa, Agnes Roczniak-Ferguson, Shawn M. Ferguson
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 10
A pathogenic variant in RAB32 causes autosomal dominant Parkinson’s disease andactivates LRRK2 kinase
Emil K. Gustavsson, Jordan Follett, Joanne Trinh, et al.
medRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 3
Phosphorylation of Rab29 at Ser185 regulates its localization and role in the lysosomal stress response in concert with LRRK2
Tadayuki Komori, Tomoki Kuwahara, Tetta Fujimoto, et al.
Journal of Cell Science (2023) Vol. 136, Iss. 14
Open Access | Times Cited: 9
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