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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 and its substrate Rab GTPases are sequentially targeted onto stressed lysosomes and maintain their homeostasis
Tomoya Eguchi, Tomoki Kuwahara, Maria Sakurai, et al.
Proceedings of the National Academy of Sciences (2018) Vol. 115, Iss. 39
Open Access | Times Cited: 277

Showing 1-25 of 277 citing articles:

Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)1
Daniel J. Klionsky, Amal Kamal Abdel‐Aziz, Sara Abdelfatah, et al.
Autophagy (2021) Vol. 17, Iss. 1, pp. 1-382
Open Access | Times Cited: 1988
Rab family of small GTPases: an updated view on their regulation and functions
Yuta Homma, Shu Hiragi, Mitsunori Fukuda
FEBS Journal (2020) Vol. 288, Iss. 1, pp. 36-55
Open Access | Times Cited: 338
Autophagy in Parkinson's Disease
Xu Hou, Jens O. Watzlawik, Fabienne C. Fiesel, et al.
Journal of Molecular Biology (2020) Vol. 432, Iss. 8, pp. 2651-2672
Open Access | Times Cited: 280
LRRK2 mediates tubulation and vesicle sorting from lysosomes
Luis Bonet‐Ponce, Alexandra Beilina, Chad D. Williamson, et al.
Science Advances (2020) Vol. 6, Iss. 46
Open Access | Times Cited: 208
The In Situ Structure of Parkinson’s Disease-Linked LRRK2
Reika Watanabe, Robert Buschauer, Jan Böhning, et al.
Cell (2020) Vol. 182, Iss. 6, pp. 1508-1518.e16
Open Access | Times Cited: 191
Parkinson's Disease Genetics and Pathophysiology
Gabriel E. Vázquez-Vélez, Huda Y. Zoghbi
Annual Review of Neuroscience (2021) Vol. 44, Iss. 1, pp. 87-108
Open Access | Times Cited: 156
LRRK2 kinase activity regulates lysosomal glucocerebrosidase in neurons derived from Parkinson’s disease patients
Daniel Ysselstein, Maria Nguyen, Tiffany Young, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 155
Increased LRRK2 kinase activity alters neuronal autophagy by disrupting the axonal transport of autophagosomes
C. Alexander Boecker, Juliet Goldsmith, Dan Dou, et al.
Current Biology (2021) Vol. 31, Iss. 10, pp. 2140-2154.e6
Open Access | Times Cited: 137
LRRK2 and idiopathic Parkinson’s disease
Emily M. Rocha, Matthew T. Keeney, Roberto Di Maio, et al.
Trends in Neurosciences (2022) Vol. 45, Iss. 3, pp. 224-236
Open Access | Times Cited: 106
Perspective on the current state of the LRRK2 field
Jean‐Marc Taymans, Matt Fell, Tim Greenamyre, et al.
npj Parkinson s Disease (2023) Vol. 9, Iss. 1
Open Access | Times Cited: 70
Lysosome damage triggers direct ATG8 conjugation and ATG2 engagement via non-canonical autophagy
Jake Cross, Joanne Durgan, David G. McEwan, et al.
The Journal of Cell Biology (2023) Vol. 222, Iss. 12
Open Access | Times Cited: 51
Cell biology of Parkinson's disease: Mechanisms of synaptic, lysosomal, and mitochondrial dysfunction
Sarah M. Brooker, G Naylor, Dimitri Krainc
Current Opinion in Neurobiology (2024) Vol. 85, pp. 102841-102841
Closed Access | Times Cited: 26
The V-ATPase–ATG16L1 axis recruits LRRK2 to facilitate the lysosomal stress response
Tomoya Eguchi, Maria Sakurai, Yingxue Wang, et al.
The Journal of Cell Biology (2024) Vol. 223, Iss. 3
Open Access | Times Cited: 22
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
Pathogenesis of Parkinson’s Disease
Bin Xiao, Zhidong Zhou, Yinxia Chao, et al.
Neurologic Clinics (2025)
Closed Access | Times Cited: 2
LRRK2 Biology from structure to dysfunction: research progresses, but the themes remain the same
Daniel C. Berwick, George R. Heaton, Sonia Azeggagh, et al.
Molecular Neurodegeneration (2019) Vol. 14, Iss. 1
Open Access | Times Cited: 144
LRRK2 impairs PINK1/Parkin-dependent mitophagy via its kinase activity: pathologic insights into Parkinson’s disease
Fiona Bonello, Sidi-Mohamed Hassoun, François Mouton‐Liger, et al.
Human Molecular Genetics (2019) Vol. 28, Iss. 10, pp. 1645-1660
Open Access | Times Cited: 135
LRRK2 regulation of immune-pathways and inflammatory disease
Rebecca L. Wallings, Malú G. Tansey
Biochemical Society Transactions (2019) Vol. 47, Iss. 6, pp. 1581-1595
Open Access | Times Cited: 126
Role of the endolysosomal system in Parkinson’s disease
D. J. Vidyadhara, John E. Lee, Sreeganga S. Chandra
Journal of Neurochemistry (2019) Vol. 150, Iss. 5, pp. 487-506
Open Access | Times Cited: 124
Lysosomal Dysfunction at the Centre of Parkinson’s Disease and Frontotemporal Dementia/Amyotrophic Lateral Sclerosis
Rebecca L. Wallings, Stewart W. Humble, Michael E. Ward, et al.
Trends in Neurosciences (2019) Vol. 42, Iss. 12, pp. 899-912
Open Access | Times Cited: 116
Advances in elucidating the function of leucine-rich repeat protein kinase-2 in normal cells and Parkinson's disease
Matthew Taylor, Dario R. Alessi
Current Opinion in Cell Biology (2020) Vol. 63, pp. 102-113
Open Access | Times Cited: 116
Autophagy lysosomal pathway dysfunction in Parkinson's disease; evidence from human genetics
Konstantin Senkevich, Ziv Gan‐Or
Parkinsonism & Related Disorders (2019) Vol. 73, pp. 60-71
Open Access | Times Cited: 109
“LRRK2: Autophagy and Lysosomal Activity”
Marta Madureira, Natalie Connor‐Robson, Richard Wade‐Martins
Frontiers in Neuroscience (2020) Vol. 14
Open Access | Times Cited: 109
Pharmacological rescue of impaired mitophagy in Parkinson’s disease-related LRRK2 G2019S knock-in mice
François Singh, Alan R. Prescott, Philippa Rosewell, et al.
eLife (2021) Vol. 10
Open Access | Times Cited: 100
Lysosome and Inflammatory Defects in GBA1‐Mutant Astrocytes Are Normalized by LRRK2 Inhibition
Anwesha Sanyal, Mark P. DeAndrade, Hailey S. Novis, et al.
Movement Disorders (2020) Vol. 35, Iss. 5, pp. 760-773
Open Access | Times Cited: 85
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