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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:

Development of phospho-specific Rab protein antibodies to monitor in vivo activity of the LRRK2 Parkinson's disease kinase
Paweł Lis, Sophie Burel, Martin Steger, et al.
Biochemical Journal (2017) Vol. 475, Iss. 1, pp. 1-22
Open Access | Times Cited: 143

Showing 1-25 of 143 citing articles:

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: 442
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
The interplay of aging, genetics and environmental factors in the pathogenesis of Parkinson’s disease
Shirley Yin-Yu Pang, Philip Wing‐Lok Ho, Huifang Liu, et al.
Translational Neurodegeneration (2019) Vol. 8, Iss. 1
Open Access | Times Cited: 306
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 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: 162
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: 161
LRRK 2 activation controls the repair of damaged endomembranes in macrophages
Susanne Herbst, Philip Campbell, J. Harvey, et al.
The EMBO Journal (2020) Vol. 39, Iss. 18
Open Access | Times Cited: 152
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: 135
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: 107
LRRK2 and idiopathic Parkinson’s disease
Emily M. Rocha, Matthew T. Keeney, Roberto Di Maio, et al.
Trends in Neurosciences (2022) Vol. 45, Iss. 3, pp. 224-236
Open Access | Times Cited: 105
Impact of 100 LRRK2 variants linked to Parkinson's disease on kinase activity and microtubule binding
Alexia F. Kalogeropulou, Elena Purlyte, Francesca Tonelli, et al.
Biochemical Journal (2022) Vol. 479, Iss. 17, pp. 1759-1783
Open Access | Times Cited: 87
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
A STING–CASM–GABARAP pathway activates LRRK2 at lysosomes
Amanda Bentley‐DeSousa, Agnes Roczniak-Ferguson, Shawn M. Ferguson
The Journal of Cell Biology (2025) Vol. 224, Iss. 2
Open Access | Times Cited: 3
Interrogating Parkinson's disease LRRK2 kinase pathway activity by assessing Rab10 phosphorylation in human neutrophils
Ying Fan, Andrew J.M. Howden, Adil R. Sarhan, et al.
Biochemical Journal (2017) Vol. 475, Iss. 1, pp. 23-44
Open Access | Times Cited: 158
Advances in elucidating the function of leucine-rich repeat protein kinase-2 in normal cells and Parkinson's disease
Matthew Taylor, Dario R. Alessi
Current Opinion in Cell Biology (2020) Vol. 63, pp. 102-113
Open Access | Times Cited: 116
PPM1H phosphatase counteracts LRRK2 signaling by selectively dephosphorylating Rab proteins
Kerryn Berndsen, Paweł Lis, Wondwossen M Yeshaw, et al.
eLife (2019) Vol. 8
Open Access | Times Cited: 114
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
RAB8, RAB10 and RILPL1 contribute to both LRRK2 kinase–mediated centrosomal cohesion and ciliogenesis deficits
Antonio Jesús Lara Ordóñez, Belén Fernández, Elena Fdez, et al.
Human Molecular Genetics (2019) Vol. 28, Iss. 21, pp. 3552-3568
Open Access | Times Cited: 88
A new hypothesis for Parkinson’s disease pathogenesis: GTPase-p38 MAPK signaling and autophagy as convergence points of etiology and genomics
Julia Obergasteiger, Giulia Frapporti, Peter P. Pramstaller, et al.
Molecular Neurodegeneration (2018) Vol. 13, Iss. 1
Open Access | Times Cited: 85
LRRK2 inhibition prevents endolysosomal deficits seen in human Parkinson's disease
Emily M. Rocha, Briana R. De Miranda, Sandra L. Castro, et al.
Neurobiology of Disease (2019) Vol. 134, pp. 104626-104626
Open Access | Times Cited: 85
Crystal structure of the WD40 domain dimer of LRRK2
Pengfei Zhang, Ying Fan, Heng Ru, et al.
Proceedings of the National Academy of Sciences (2019) Vol. 116, Iss. 5, pp. 1579-1584
Open Access | Times Cited: 84
Pathogenic LRRK2 control of primary cilia and Hedgehog signaling in neurons and astrocytes of mouse brain
Shahzad S. Khan, Yuriko Sobu, Herschel S. Dhekne, et al.
eLife (2021) Vol. 10
Open Access | Times Cited: 74
LRRK2 recruitment, activity, and function in organelles
Luis Bonet‐Ponce, Mark Cookson
FEBS Journal (2021) Vol. 289, Iss. 22, pp. 6871-6890
Open Access | Times Cited: 60
Trafficking of the glutamate transporter is impaired in LRRK2-related Parkinson’s disease
Ludovica Iovino, Veronica Giusti, Francesca Pischedda, et al.
Acta Neuropathologica (2022) Vol. 144, Iss. 1, pp. 81-106
Open Access | Times Cited: 39
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