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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 Kinase Activity Is Dependent on LRRK2 GTP Binding Capacity but Independent of LRRK2 GTP Binding
Jean‐Marc Taymans, Renée Vancraenenbroeck, Petri Ollikainen, et al.
PLoS ONE (2011) Vol. 6, Iss. 8, pp. e23207-e23207
Open Access | Times Cited: 101

Showing 1-25 of 101 citing articles:

Ser 1292 Autophosphorylation Is an Indicator of LRRK2 Kinase Activity and Contributes to the Cellular Effects of PD Mutations
Zejuan Sheng, Shuo Zhang, Daisy Bustos, et al.
Science Translational Medicine (2012) Vol. 4, Iss. 164
Closed Access | Times Cited: 356
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
LRRK2 and neuroinflammation: partners in crime in Parkinson’s disease?
Isabella Russo, Luigi Bubacco, Elisa Greggio
Journal of Neuroinflammation (2014) Vol. 11, Iss. 1, pp. 52-52
Open Access | Times Cited: 165
Cellular processes associated with LRRK2 function and dysfunction
Rebecca L. Wallings, Claudia Manzoni, Rina Bandopadhyay
FEBS Journal (2015) Vol. 282, Iss. 15, pp. 2806-2826
Open Access | Times Cited: 153
LRRK2 pathobiology in Parkinson's disease
Ian Martin, Jungwoo Wren Kim, Valina L. Dawson, et al.
Journal of Neurochemistry (2014) Vol. 131, Iss. 5, pp. 554-565
Open Access | Times Cited: 153
Inhibition of LRRK2 kinase activity stimulates macroautophagy
Claudia Manzoni, Adamantios Mamais, Sybille Dihanich, et al.
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (2013) Vol. 1833, Iss. 12, pp. 2900-2910
Open Access | Times Cited: 141
LRRK2: Cause, Risk, and Mechanism
Coro Paisán‐Ruíz, Patrick A. Lewis, Andrew Singleton
Journal of Parkinson s Disease (2013) Vol. 3, Iss. 2, pp. 85-103
Open Access | Times Cited: 140
GTPase activity regulates kinase activity and cellular phenotypes of Parkinson's disease-associated LRRK2
Alice Biosa, Alžbeta Trančíková, Laura Civiero, et al.
Human Molecular Genetics (2012) Vol. 22, Iss. 6, pp. 1140-1156
Open Access | Times Cited: 135
LRRK2 Pathways Leading to Neurodegeneration
Mark Cookson
Current Neurology and Neuroscience Reports (2015) Vol. 15, Iss. 7
Open Access | Times Cited: 133
GTPase Activity and Neuronal Toxicity of Parkinson's Disease–Associated LRRK2 Is Regulated by ArfGAP1
Klodjan Stafa, Alžbeta Trančíková, Philip J. Webber, et al.
PLoS Genetics (2012) Vol. 8, Iss. 2, pp. e1002526-e1002526
Open Access | Times Cited: 130
Parkinson disease-associated mutations in LRRK2 cause centrosomal defects via Rab8a phosphorylation
Jesús Madero‐Pérez, Elena Fdez, Belén Fernández, et al.
Molecular Neurodegeneration (2018) Vol. 13, Iss. 1
Open Access | Times Cited: 101
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: 40
Structural basis of human LRRK2 membrane recruitment and activation
Hanwen Zhu, Francesca Tonelli, Dario R. Alessi, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 39
Unlocking the therapeutic potential of protein kinase inhibitors in neurodegenerative and psychiatric disorders
A. V., Polina Buzaeva, Izhak Michaelevski
(2025) Vol. 2, Iss. 6
Open Access | Times Cited: 1
Biochemical Characterization of Highly Purified Leucine-Rich Repeat Kinases 1 and 2 Demonstrates Formation of Homodimers
Laura Civiero, Renée Vancraenenbroeck, Elisa Belluzzi, et al.
PLoS ONE (2012) Vol. 7, Iss. 8, pp. e43472-e43472
Open Access | Times Cited: 99
Phosphorylation of LRRK2 by casein kinase 1α regulates trans-Golgi clustering via differential interaction with ARHGEF7
Ruth Chia, Sara Haddock, Alexandra Beilina, et al.
Nature Communications (2014) Vol. 5, Iss. 1
Open Access | Times Cited: 95
LRRK2, a puzzling protein: Insights into Parkinson's disease pathogenesis
A. Raquel Esteves, Russell H. Swerdlow, Sandra M. Cardoso
Experimental Neurology (2014) Vol. 261, pp. 206-216
Open Access | Times Cited: 94
Identification of protein phosphatase 1 as a regulator of the LRRK2 phosphorylation cycle
Evy Lobbestael, Jing Zhao, Iakov N. Rudenko, et al.
Biochemical Journal (2013) Vol. 456, Iss. 1, pp. 119-128
Open Access | Times Cited: 89
Phosphorylation of LRRK2 serines 955 and 973 is disrupted by Parkinson’s disease mutations and LRRK2 pharmacological inhibition
Elizabeth A. Doggett, Jing Zhao, Christina N. Mork, et al.
Journal of Neurochemistry (2011) Vol. 120, Iss. 1, pp. 37-45
Closed Access | Times Cited: 88
Parkinson’s disease-implicated kinases in the brain; insights into disease pathogenesis
Nicolas Dzamko, Jinxia Zhou, Yue Huang, et al.
Frontiers in Molecular Neuroscience (2014) Vol. 7
Open Access | Times Cited: 80
LRRK2 Kinase Inhibition as a Therapeutic Strategy for Parkinson's Disease, Where Do We Stand?
Jean‐Marc Taymans, Elisa Greggio
Current Neuropharmacology (2016) Vol. 14, Iss. 3, pp. 214-225
Open Access | Times Cited: 76
GTP binding regulates cellular localization of Parkinson's disease-associated LRRK2
Marian Blanca Ramírez, Antonio Jesús Lara Ordóñez, Elena Fdez, et al.
Human Molecular Genetics (2017) Vol. 26, Iss. 14, pp. 2747-2767
Open Access | Times Cited: 73
The Neurobiology of LRRK2 and its Role in the Pathogenesis of Parkinson’s Disease
Hardy J. Rideout, Leonidas Stefanis
Neurochemical Research (2013) Vol. 39, Iss. 3, pp. 576-592
Closed Access | Times Cited: 72
LRRK2 kinase activity and biology are not uniformly predicted by its autophosphorylation and cellular phosphorylation site status
April Reynolds, Elizabeth A. Doggett, Steve Riddle, et al.
Frontiers in Molecular Neuroscience (2014) Vol. 7
Open Access | Times Cited: 68
The Parkinson’s Disease Protein LRRK2 Interacts with the GARP Complex to Promote Retrograde Transport to the trans-Golgi Network
Alexandra Beilina, Luis Bonet‐Ponce, Ravindran Kumaran, et al.
Cell Reports (2020) Vol. 31, Iss. 5, pp. 107614-107614
Open Access | Times Cited: 63
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