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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 recruitment, activity, and function in organelles
Luis Bonet‐Ponce, Mark Cookson
FEBS Journal (2021) Vol. 289, Iss. 22, pp. 6871-6890
Open Access | Times Cited: 60

Showing 1-25 of 60 citing articles:

Preclinical and clinical evaluation of the LRRK2 inhibitor DNL201 for Parkinson’s disease
Danna Jennings, Sarah Huntwork‐Rodriguez, Anastasia G. Henry, et al.
Science Translational Medicine (2022) Vol. 14, Iss. 648
Closed Access | Times Cited: 162
Mitochondrial dysfunction in Parkinson’s disease – a key disease hallmark with therapeutic potential
Martin T. Henrich, Wolfgang H. Oertel, D. James Surmeier, et al.
Molecular Neurodegeneration (2023) Vol. 18, Iss. 1
Open Access | Times Cited: 92
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
LRRK2 Inhibition by BIIB122 in Healthy Participants and Patients with Parkinson's Disease
Danna Jennings, Sarah Huntwork‐Rodriguez, Maurits F. J. M. Vissers, et al.
Movement Disorders (2023) Vol. 38, Iss. 3, pp. 386-398
Open Access | Times Cited: 45
Lysosomal positioning regulates Rab10 phosphorylation at LRRK2 + lysosomes
Jillian H. Kluss, Alexandra Beilina, Chad D. Williamson, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 43
Open Access | Times Cited: 40
Different pieces of the same puzzle: a multifaceted perspective on the complex biological basis of Parkinson’s disease
Amica Corda Müller-Nedebock, Marieke C. J. Dekker, Matthew J. Farrer, et al.
npj Parkinson s Disease (2023) Vol. 9, Iss. 1
Open Access | Times Cited: 30
Pharmacology of LRRK2 with type I and II kinase inhibitors revealed by cryo-EM
Hanwen Zhu, Patricia Hixson, Wen Ma, et al.
Cell Discovery (2024) Vol. 10, Iss. 1
Open Access | Times Cited: 15
A potential patient stratification biomarker for Parkinson´s disease based on LRRK2 kinase-mediated centrosomal alterations in peripheral blood-derived cells
Yahaira Naaldijk, Belén Fernández, Rachel Fasiczka, et al.
npj Parkinson s Disease (2024) Vol. 10, Iss. 1
Open Access | Times Cited: 11
Blocking IL-6 signaling prevents astrocyte-induced neurodegeneration in an iPSC-based model of Parkinson’s disease
Meritxell Pons‐Espinal, Lucas Blasco-Agell, Irene Fernández‐Carasa, et al.
JCI Insight (2024) Vol. 9, Iss. 3
Open Access | Times Cited: 11
Revolutionizing our understanding of Parkinson’s disease: Dr. Heinz Reichmann’s pioneering research and future research direction
Masaru Tanaka, László Vécsei
Journal of Neural Transmission (2024) Vol. 131, Iss. 12, pp. 1367-1387
Open Access | Times Cited: 10
PRKAA2, MTOR, and TFEB in the regulation of lysosomal damage response and autophagy
Mohd Shariq, Mohammad Firoz Khan, Reshmi Raj, et al.
Journal of Molecular Medicine (2024) Vol. 102, Iss. 3, pp. 287-311
Closed Access | Times Cited: 9
Structural basis for Parkinson’s disease-linked LRRK2’s binding to microtubules
David Snead, Mariusz Matyszewski, Andrea M. Dickey, et al.
Nature Structural & Molecular Biology (2022) Vol. 29, Iss. 12, pp. 1196-1207
Open Access | Times Cited: 38
Early-Onset Parkinson’s Disease: Creating the Right Environment for a Genetic Disorder
Ana Kolicheski, Pierpaolo Turcano, Nicole Tamvaka, et al.
Journal of Parkinson s Disease (2022) Vol. 12, Iss. 8, pp. 2353-2367
Open Access | Times Cited: 27
LRRK2 kinase activity regulates GCase level and enzymatic activity differently depending on cell type in Parkinson’s disease
Maria Kedariti, Emanuele Frattini, Pascale Baden, et al.
npj Parkinson s Disease (2022) Vol. 8, Iss. 1
Open Access | Times Cited: 26
LRRK2 as a target for modulating immune system responses
Isabella Russo, Luigi Bubacco, Elisa Greggio
Neurobiology of Disease (2022) Vol. 169, pp. 105724-105724
Open Access | Times Cited: 24
Lapatinib ditosylate rescues motor deficits in rotenone-intoxicated rats: Potential repurposing of anti-cancer drug as a disease-modifying agent in Parkinson's disease
Heba M. Mansour, Ahmed F. Mohamed, Mahmoud M. Khattab, et al.
European Journal of Pharmacology (2023) Vol. 954, pp. 175875-175875
Closed Access | Times Cited: 14
Human iPSC-derived microglia carrying the LRRK2-G2019S mutation show a Parkinson’s disease related transcriptional profile and function
Sohvi Ohtonen, Luca Giudice, Henna Jäntti, et al.
Scientific Reports (2023) Vol. 13, Iss. 1
Open Access | Times Cited: 11
Lysosome quality control in health and neurodegenerative diseases
Veronica Ferrari, B. Tedesco, Marta Cozzi, et al.
Cellular & Molecular Biology Letters (2024) Vol. 29, Iss. 1
Open Access | Times Cited: 4
LRRK2 in Drosophila Melanogaster Model: Insights into Cellular Dysfunction and Neuroinflammation in Parkinson’s Disease
Cristina Ciampelli, Grazia Galleri, Manuela Galioto, et al.
International Journal of Molecular Sciences (2025) Vol. 26, Iss. 5, pp. 2093-2093
Open 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
The homozygous LRRK2.p.N1437D point mutation mouse is a novel model of parkinsonism
Linhua Gan, Yi‐Min Sun, Xinyue Zhou, et al.
npj Parkinson s Disease (2025) Vol. 11, Iss. 1
Open Access
The Role of LRRK2 in Intracellular Organelle Dynamics
C. Alexander Boecker
Journal of Molecular Biology (2023) Vol. 435, Iss. 12, pp. 167998-167998
Open Access | Times Cited: 10
Astrocytic uptake of posttranslationally modified amyloid‐β leads to endolysosomal system disruption and induction of pro‐inflammatory signaling
Sarah Wirth, A. Schlosser, Antonia Beiersdorfer, et al.
Glia (2024) Vol. 72, Iss. 8, pp. 1451-1468
Open Access | Times Cited: 3
Modeling Parkinson's disease in LRRK2 mice: focus on synaptic dysfunction and the autophagy-lysosomal pathway
Federica Albanese, Chiara Domenicale, Mattia Volta, et al.
Biochemical Society Transactions (2022) Vol. 50, Iss. 1, pp. 621-632
Closed Access | Times Cited: 15
LRRK2 signaling in neurodegeneration: two decades of progress
Lucia Iannotta, Elisa Greggio
Essays in Biochemistry (2021) Vol. 65, Iss. 7, pp. 859-872
Closed Access | Times Cited: 18
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