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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:

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

Showing 1-25 of 124 citing articles:

Genetic Analysis of Pathways to Parkinson Disease
John Hardy
Neuron (2010) Vol. 68, Iss. 2, pp. 201-206
Open Access | Times Cited: 268
Synaptic Dysfunction in Parkinson’s Disease
Barbara Picconi, Giovanni Piccoli, Paolo Calabresi
Advances in experimental medicine and biology (2012), pp. 553-572
Closed Access | Times Cited: 255
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: 207
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
Parkinson's disease-linked leucine-rich repeat kinase 2(R1441G) mutation increases proinflammatory cytokine release from activated primary microglial cells and resultant neurotoxicity
Frank Gillardon, Ralph A. Schmid, Henning J. Draheim
Neuroscience (2012) Vol. 208, pp. 41-48
Closed Access | Times Cited: 204
LRRK2 knockout mice have an intact dopaminergic system but display alterations in exploratory and motor co-ordination behaviors
Kelly M. Hinkle, Mei Yue, Bahareh Behrouz, et al.
Molecular Neurodegeneration (2012) Vol. 7, Iss. 1
Open Access | Times Cited: 183
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
Synaptic dysfunction in Parkinson's disease
Vincenza Bagetta, Veronica Ghiglieri, Carmelo Sgobio, et al.
Biochemical Society Transactions (2010) Vol. 38, Iss. 2, pp. 493-497
Closed Access | Times Cited: 153
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: 151
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 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: 129
Astrocytes, Microglia, and Parkinson’s Disease
Eun-hye Joe, Dong‐Joo Choi, Jiawei An, et al.
Experimental Neurobiology (2018) Vol. 27, Iss. 2, pp. 77-87
Open Access | Times Cited: 125
Altered Development of Synapse Structure and Function in Striatum Caused by Parkinson's Disease-Linked LRRK2-G2019S Mutation
Bridget A. Matikainen‐Ankney, Nebojsa Kezunovic, Roxana Mesias, et al.
Journal of Neuroscience (2016) Vol. 36, Iss. 27, pp. 7128-7141
Open Access | Times Cited: 122
LRRK2 Phosphorylates Tubulin-Associated Tau but Not the Free Molecule: LRRK2-Mediated Regulation of the Tau-Tubulin Association and Neurite Outgrowth
Fumitaka Kawakami, Yabata Takatoshi, Etsuro Ohta, et al.
PLoS ONE (2012) Vol. 7, Iss. 1, pp. e30834-e30834
Open Access | Times Cited: 117
Regulation of myeloid cell phagocytosis by LRRK2 via WAVE2 complex stabilization is altered in Parkinson’s disease
Kwang S. Kim, Paul C. Marcogliese, Jungwoo Yang, et al.
Proceedings of the National Academy of Sciences (2018) Vol. 115, Iss. 22
Open Access | Times Cited: 105
LRRK2 G2019S mutation attenuates microglial motility by inhibiting focal adhesion kinase
Insup Choi, Beomsue Kim, Ji-Won Byun, et al.
Nature Communications (2015) Vol. 6, Iss. 1
Open Access | Times Cited: 100
Leucine-Rich Repeat Kinase 2 Binds to Neuronal Vesicles through Protein Interactions Mediated by Its C-Terminal WD40 Domain
Giovanni Piccoli, Franco Onofri, Maria Daniela Cirnaru, et al.
Molecular and Cellular Biology (2014) Vol. 34, Iss. 12, pp. 2147-2161
Open Access | Times Cited: 98
Selective LRRK2 kinase inhibition reduces phosphorylation of endogenous Rab10 and Rab12 in human peripheral mononuclear blood cells
Kenneth Thirstrup, Justus C. Dächsel, Felix Oppermann, et al.
Scientific Reports (2017) Vol. 7, Iss. 1
Open Access | Times Cited: 94
NEAT1 is overexpressed in Parkinson's disease substantia nigra and confers drug‐inducible neuroprotection from oxidative stress
Alon Simchovitz, Mor Hanan, Naomi Niederhoffer, et al.
The FASEB Journal (2019) Vol. 33, Iss. 10, pp. 11223-11234
Open Access | Times Cited: 86
Proteomics-Based Methods for Discovery, Quantification, and Validation of Protein–Protein Interactions
Yana Miteva, Hanna G. Budayeva, Ileana M. Cristea
Analytical Chemistry (2012) Vol. 85, Iss. 2, pp. 749-768
Open Access | Times Cited: 103
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
The LRRK2 inhibitor GSK2578215A induces protective autophagy in SH-SY5Y cells: involvement of Drp-1-mediated mitochondrial fission and mitochondrial-derived ROS signaling
Sara Sáez-Atiénzar, Luis Bonet‐Ponce, Rafael Blesa, et al.
Cell Death and Disease (2014) Vol. 5, Iss. 8, pp. e1368-e1368
Open Access | Times Cited: 93
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: 93
LRRK2 kinase inhibition prevents pathological microglial phagocytosis in response to HIV-1 Tat protein
Daniel F. Marker, Jenna M. Puccini, Taryn E. Mockus, et al.
Journal of Neuroinflammation (2012) Vol. 9, Iss. 1
Open Access | Times Cited: 90
Expression Analysis of Lrrk1, Lrrk2 and Lrrk2 Splice Variants in Mice
Florian Giesert, Andreas Hofmann, Bürger Alexander, et al.
PLoS ONE (2013) Vol. 8, Iss. 5, pp. e63778-e63778
Open Access | Times Cited: 89
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