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:

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

Showing 1-25 of 95 citing articles:

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 phosphorylates membrane-bound Rabs and is activated by GTP-bound Rab7L1 to promote recruitment to the trans-Golgi network
Zhiyong Liu, Nicole Bryant, Ravindran Kumaran, et al.
Human Molecular Genetics (2017) Vol. 27, Iss. 2, pp. 385-395
Open Access | Times Cited: 252

Pathogenic Impact of α-Synuclein Phosphorylation and Its Kinases in α-Synucleinopathies
K. Kawahata, David I. Finkelstein, Kohji Fukunaga
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 11, pp. 6216-6216
Open Access | Times Cited: 69

Leucine-Rich Repeat Kinases
Dario R. Alessi, Suzanne R. Pfeffer
Annual Review of Biochemistry (2024) Vol. 93, Iss. 1, pp. 261-287
Closed Access | Times Cited: 17

Phos-tag analysis of Rab10 phosphorylation by LRRK2: a powerful assay for assessing kinase function and inhibitors
Genta Ito, Kristina Katsemonova, Francesca Tonelli, et al.
Biochemical Journal (2016) Vol. 473, Iss. 17, pp. 2671-2685
Open Access | Times Cited: 158

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 Biology from structure to dysfunction: research progresses, but the themes remain the same
Daniel C. Berwick, George R. Heaton, Sonia Azeggagh, et al.
Molecular Neurodegeneration (2019) Vol. 14, Iss. 1
Open Access | Times Cited: 144

LRRK2 promotes the activation of NLRC4 inflammasome during Salmonella Typhimurium infection
Weiwei Liu, Xianan Liu, Yu Li, et al.
The Journal of Experimental Medicine (2017) Vol. 214, Iss. 10, pp. 3051-3066
Open Access | Times Cited: 138

LRRK2 Pathways Leading to Neurodegeneration
Mark Cookson
Current Neurology and Neuroscience Reports (2015) Vol. 15, Iss. 7
Open Access | Times Cited: 133

Expanding functions of GIT Arf GTPase-activating proteins, PIX Rho guanine nucleotide exchange factors and GIT–PIX complexes
Wu Zhou, Xiaobo Li, Richard T. Premont
Journal of Cell Science (2016) Vol. 129, Iss. 10, pp. 1963-1974
Open Access | Times Cited: 102

LRRK2‐mediated Rab10 phosphorylation in immune cells from Parkinson's disease patients
Farzaneh Atashrazm, Deborah Hammond, Gayathri Perera, et al.
Movement Disorders (2018) Vol. 34, Iss. 3, pp. 406-415
Closed Access | Times Cited: 94

Casein kinase 1α: biological mechanisms and theranostic potential
Shaojie Jiang, Miaofeng Zhang, Jihong Sun, et al.
Cell Communication and Signaling (2018) Vol. 16, Iss. 1
Open Access | Times Cited: 93

Age-dependent dopamine transporter dysfunction and Serine129 phospho-α-synuclein overload in G2019S LRRK2 mice
Francesco Longo, Daniela Mercatelli, Salvatore Novello, et al.
Acta Neuropathologica Communications (2017) Vol. 5, Iss. 1
Open Access | Times Cited: 87

Parkinson's: A Disease of Aberrant Vesicle Trafficking
Pawan Singh, Miratul M. K. Muqit
Annual Review of Cell and Developmental Biology (2020) Vol. 36, Iss. 1, pp. 237-264
Open Access | Times Cited: 72

Genome-wide screen reveals Rab12 GTPase as a critical activator of Parkinson’s disease-linked LRRK2 kinase
Herschel S. Dhekne, Francesca Tonelli, Wondwossen M Yeshaw, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 34

LRRK2 G2019S-induced mitochondrial DNA damage is LRRK2 kinase dependent and inhibition restores mtDNA integrity in Parkinson’s disease
Evan H. Howlett, Nicholas O. Jensen, Frances Belmonte, et al.
Human Molecular Genetics (2017) Vol. 26, Iss. 22, pp. 4340-4351
Open Access | Times Cited: 85

Parkinson's disease-associated mutant LRRK2 phosphorylates Rab7L1 and modifies trans-Golgi morphology
Tetta Fujimoto, Tomoki Kuwahara, Tomoya Eguchi, et al.
Biochemical and Biophysical Research Communications (2017) Vol. 495, Iss. 2, pp. 1708-1715
Closed Access | Times Cited: 82

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: 73

mTOR independent regulation of macroautophagy by Leucine Rich Repeat Kinase 2 via Beclin-1
Claudia Manzoni, Adamantios Mamais, Dorien A. Roosen, et al.
Scientific Reports (2016) Vol. 6, Iss. 1
Open Access | Times Cited: 73

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

Pharmacological LRRK2 kinase inhibition induces LRRK2 protein destabilization and proteasomal degradation
Evy Lobbestael, Laura Civiero, Tina De Wit, et al.
Scientific Reports (2016) Vol. 6, Iss. 1
Open Access | Times Cited: 69

LRRK2 dephosphorylation increases its ubiquitination
Jing Zhao, Tyler P. Molitor, J. William Langston, et al.
Biochemical Journal (2015) Vol. 469, Iss. 1, pp. 107-120
Open Access | Times Cited: 66

Detection of endogenous S1292 LRRK2 autophosphorylation in mouse tissue as a readout for kinase activity
Jillian H. Kluss, Melissa M. Conti, Alice Kaganovich, et al.
npj Parkinson s Disease (2018) Vol. 4, Iss. 1
Open Access | Times Cited: 66

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: 62

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