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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:

The Roc domain of leucine‐rich repeat kinase 2 is sufficient for interaction with microtubules
Payal N. Gandhi, Xinglong Wang, Xiongwei Zhu, et al.
Journal of Neuroscience Research (2008) Vol. 86, Iss. 8, pp. 1711-1720
Open Access | Times Cited: 169

Showing 1-25 of 169 citing articles:

The role of leucine-rich repeat kinase 2 (LRRK2) in Parkinson's disease
Mark Cookson
Nature reviews. Neuroscience (2010) Vol. 11, Iss. 12, pp. 791-797
Open Access | Times Cited: 522
Leucine-Rich Repeat Kinase 2 Regulates the Progression of Neuropathology Induced by Parkinson's-Disease-Related Mutant α-synuclein
Xian Lin, Loukia Parisiadou, Xinglong Gu, et al.
Neuron (2009) Vol. 64, Iss. 6, pp. 807-827
Open Access | Times Cited: 503
Parkinson's disease mutations in PINK1 result in decreased Complex I activity and deficient synaptic function
Vanessa A. Morais, Patrik Verstreken, Anne Roethig, et al.
EMBO Molecular Medicine (2009) Vol. 1, Iss. 2, pp. 99-111
Open Access | Times Cited: 402
Leucine-Rich Repeat Kinase 2 Mutations and Parkinson's Disease: Three Questions
Elisa Greggio, Mark Cookson
ASN NEURO (2009) Vol. 1, Iss. 1, pp. AN20090007-AN20090007
Open Access | Times Cited: 268
Impaired dopaminergic neurotransmission and microtubule-associated protein tau alterations in human LRRK2 transgenic mice
Heather L. Melrose, Justus C. Dächsel, Bahareh Behrouz, et al.
Neurobiology of Disease (2010) Vol. 40, Iss. 3, pp. 503-517
Open Access | Times Cited: 265
Pathogenic LRRK2 mutations, through increased kinase activity, produce enlarged lysosomes with reduced degradative capacity and increase ATP13A2 expression
Anastasia G. Henry, Soheil Aghamohammadzadeh, Harry Samaroo, et al.
Human Molecular Genetics (2015) Vol. 24, Iss. 21, pp. 6013-6028
Open Access | Times Cited: 206
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
Leucine‐rich repeat kinase 2 phosphorylates brain tubulin‐beta isoforms and modulates microtubule stability – a point of convergence in Parkinsonian neurodegeneration?
Frank Gillardon
Journal of Neurochemistry (2009) Vol. 110, Iss. 5, pp. 1514-1522
Open Access | Times Cited: 214
Roles of the Drosophila LRRK2 homolog in Rab7-dependent lysosomal positioning
Mark W. Dodson, Tao Zhang, Jiang Chu, et al.
Human Molecular Genetics (2011) Vol. 21, Iss. 6, pp. 1350-1363
Open Access | Times Cited: 200
LRRK2 Parkinson disease mutations enhance its microtubule association
Lauren R. Kett, Daniela Boassa, Cherry Cheng‐Ying Ho, et al.
Human Molecular Genetics (2011) Vol. 21, Iss. 4, pp. 890-899
Open Access | Times Cited: 193
LRRK2 regulates synaptogenesis and dopamine receptor activation through modulation of PKA activity
Loukia Parisiadou, Jia Yu, Carmelo Sgobio, et al.
Nature Neuroscience (2014) Vol. 17, Iss. 3, pp. 367-376
Open Access | Times Cited: 182
Neurodegeneration and microtubule dynamics: death by a thousand cuts
Jyoti Dubey, Neena Ratnakaran, Sandhya P. Koushika
Frontiers in Cellular Neuroscience (2015) Vol. 9
Open Access | Times Cited: 166
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: 164
LRRK2G2019S Mutation Induces Dendrite Degeneration through Mislocalization and Phosphorylation of Tau by Recruiting Autoactivated GSK3β
Chin‐Hsien Lin, Pei-I Tsai, Ruey‐Meei Wu, et al.
Journal of Neuroscience (2010) Vol. 30, Iss. 39, pp. 13138-13149
Open Access | Times Cited: 163
The LRRK2 G2019S mutant exacerbates basal autophagy through activation of the MEK/ERK pathway
José Manuel Bravo‐San Pedro, Mireia Niso‐Santano, Rubén Gómez‐Sánchez, et al.
Cellular and Molecular Life Sciences (2012) Vol. 70, Iss. 1, pp. 121-136
Open Access | Times Cited: 158
LRRK2 and Parkinson Disease
Justus C. Dächsel, Matthew J. Farrer
Archives of Neurology (2010) Vol. 67, Iss. 5
Closed Access | Times Cited: 152
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
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: 133
Deletion of the WD40 Domain of LRRK2 in Zebrafish Causes Parkinsonism-Like Loss of Neurons and Locomotive Defect
Donglai Sheng, Dianbo Qu, Ken Hon Hung Kwok, et al.
PLoS Genetics (2010) Vol. 6, Iss. 4, pp. e1000914-e1000914
Open Access | Times Cited: 127
A Direct Interaction between Leucine-rich Repeat Kinase 2 and Specific β-Tubulin Isoforms Regulates Tubulin Acetylation
Bernard M. H. Law, Victoria A. Spain, Veronica H.L. Leinster, et al.
Journal of Biological Chemistry (2013) Vol. 289, Iss. 2, pp. 895-908
Open Access | Times Cited: 124
LRRK2 and mitochondria: Recent advances and current views
Alpana Singh, Lianteng Zhi, Hui Zhang
Brain Research (2018) Vol. 1702, pp. 96-104
Open Access | Times Cited: 110
Microtubule Dysfunction: A Common Feature of Neurodegenerative Diseases
Antonella Sferra, Francesco Nicita, Enrico Bertini
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 19, pp. 7354-7354
Open Access | Times Cited: 97
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
Rare variants with large effects provide functional insights into the pathology of migraine subtypes, with and without aura
Gyða Björnsdóttir, Mona Ameri Chalmer, Lilja Stefánsdóttir, et al.
Nature Genetics (2023) Vol. 55, Iss. 11, pp. 1843-1853
Open Access | Times Cited: 23
A QUICK Screen for Lrrk2 Interaction Partners – Leucine-rich Repeat Kinase 2 is Involved in Actin Cytoskeleton Dynamics
Andrea Meixner, Karsten Boldt, Marleen Van Troys, et al.
Molecular & Cellular Proteomics (2010) Vol. 10, Iss. 1, pp. M110.001172-M110.001172
Open Access | Times Cited: 124
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