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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:

Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation establishes a connection to ciliogenesis
Martin Steger, Federico Diez, Herschel S. Dhekne, et al.
eLife (2017) Vol. 6
Open Access | Times Cited: 444

Showing 1-25 of 444 citing articles:

Inflammation and immune dysfunction in Parkinson disease
Malú G. Tansey, Rebecca L. Wallings, Madelyn C. Houser, et al.
Nature reviews. Immunology (2022) Vol. 22, Iss. 11, pp. 657-673
Open Access | Times Cited: 789
The lysosome as a cellular centre for signalling, metabolism and quality control
Rosalie Lawrence, Roberto Zoncu
Nature Cell Biology (2018) Vol. 21, Iss. 2, pp. 133-142
Closed Access | Times Cited: 779
LRRK2 in Parkinson disease: challenges of clinical trials
Eduardo Tolosa, Miquel Vila, Christine Klein, et al.
Nature Reviews Neurology (2020) Vol. 16, Iss. 2, pp. 97-107
Closed Access | Times Cited: 373
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
Rab29 activation of the Parkinson's disease‐associated LRRK2 kinase
Elena Purlyte, Herschel S. Dhekne, Adil R. Sarhan, et al.
The EMBO Journal (2017) Vol. 37, Iss. 1, pp. 1-18
Open Access | Times Cited: 326
Illuminating the dark phosphoproteome
Elise J. Needham, Benjamin L. Parker, Timur Burykin, et al.
Science Signaling (2019) Vol. 12, Iss. 565
Open Access | Times Cited: 300
LRRK2 kinase in Parkinson's disease
Dario R. Alessi, Esther Sammler
Science (2018) Vol. 360, Iss. 6384, pp. 36-37
Open Access | Times Cited: 298
Real-time volumetric microscopy of in vivo dynamics and large-scale samples with SCAPE 2.0
Venkatakaushik Voleti, Kripa Patel, Wenze Li, et al.
Nature Methods (2019) Vol. 16, Iss. 10, pp. 1054-1062
Open Access | Times Cited: 297
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
A pathway for Parkinson’s Disease LRRK2 kinase to block primary cilia and Sonic hedgehog signaling in the brain
Herschel S. Dhekne, Izumi Yanatori, Rachel C. Gomez, et al.
eLife (2018) Vol. 7
Open Access | Times Cited: 226
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
Rab GTPases and Membrane Trafficking in Neurodegeneration
Ferdi Rıdvan Kiral, Friederike E. Kohrs, Eugene Jennifer Jin, et al.
Current Biology (2018) Vol. 28, Iss. 8, pp. R471-R486
Open Access | Times Cited: 201
Structure of LRRK2 in Parkinson’s disease and model for microtubule interaction
Colin K. Deniston, John Salogiannis, Sebastian Mathea, et al.
Nature (2020) Vol. 588, Iss. 7837, pp. 344-349
Open Access | Times Cited: 201
The Parkinson's disease VPS35[D620N] mutation enhances LRRK2-mediated Rab protein phosphorylation in mouse and human
Rafeeq Mir, Francesca Tonelli, Paweł Lis, et al.
Biochemical Journal (2018) Vol. 475, Iss. 11, pp. 1861-1883
Open Access | Times Cited: 193
LRRK2 links genetic and sporadic Parkinson's disease
Jillian H. Kluss, Adamantios Mamais, Mark Cookson
Biochemical Society Transactions (2019) Vol. 47, Iss. 2, pp. 651-661
Open Access | Times Cited: 188
Cellular and Molecular Basis of Neurodegeneration in Parkinson Disease
Xiansi Zeng, Wen-Shuo Geng, Jing Jia, et al.
Frontiers in Aging Neuroscience (2018) Vol. 10
Open Access | Times Cited: 178
LRRK2 mutations impair depolarization-induced mitophagy through inhibition of mitochondrial accumulation of RAB10
Fieke Wauters, Tom Cornelissen, Dorien Imberechts, et al.
Autophagy (2019) Vol. 16, Iss. 2, pp. 203-222
Open Access | Times Cited: 165
LRRK2 modifies α-syn pathology and spread in mouse models and human neurons
Gregor Bieri, Michel Brahic, Luc Bousset, et al.
Acta Neuropathologica (2019) Vol. 137, Iss. 6, pp. 961-980
Open Access | Times Cited: 164
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: 163
Structural analysis of the full-length human LRRK2
Alexander Myasnikov, Hanwen Zhu, Patricia Hixson, et al.
Cell (2021) Vol. 184, Iss. 13, pp. 3519-3527.e10
Open Access | Times Cited: 157
In‐depth and 3‐dimensional exploration of the budding yeast phosphoproteome
Michael C. Lanz, Kumar Yugandhar, Shagun Gupta, et al.
EMBO Reports (2021) Vol. 22, Iss. 2
Open Access | Times Cited: 140
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
Urinary proteome profiling for stratifying patients with familial Parkinson’s disease
Sebastian Virreira Winter, Özge Karayel, Maximilian T. Strauss, et al.
EMBO Molecular Medicine (2021) Vol. 13, Iss. 3
Open Access | Times Cited: 119
Proteome profiling of cerebrospinal fluid reveals biomarker candidates for Parkinson’s disease
Özge Karayel, Sebastian Virreira Winter, Shalini Padmanabhan, et al.
Cell Reports Medicine (2022) Vol. 3, Iss. 6, pp. 100661-100661
Open Access | Times Cited: 111
Discovery of XL01126: A Potent, Fast, Cooperative, Selective, Orally Bioavailable, and Blood–Brain Barrier Penetrant PROTAC Degrader of Leucine-Rich Repeat Kinase 2
Xingui Liu, Alexia F. Kalogeropulou, Sofia Domingos, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 37, pp. 16930-16952
Open Access | Times Cited: 110
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