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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:

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: 100

Showing 1-25 of 100 citing articles:

Rab family of small GTPases: an updated view on their regulation and functions
Yuta Homma, Shu Hiragi, Mitsunori Fukuda
FEBS Journal (2020) Vol. 288, Iss. 1, pp. 36-55
Open Access | Times Cited: 337
LRRK2 and its substrate Rab GTPases are sequentially targeted onto stressed lysosomes and maintain their homeostasis
Tomoya Eguchi, Tomoki Kuwahara, Maria Sakurai, et al.
Proceedings of the National Academy of Sciences (2018) Vol. 115, Iss. 39
Open Access | Times Cited: 274
A pathway for Parkinson’s Disease LRRK2 kinase to block primary cilia and Sonic hedgehog signaling in the brain
Herschel S. Dhekne, Izumi Yanatori, Rachel C. Gomez, et al.
eLife (2018) Vol. 7
Open Access | Times Cited: 225
Perspective on the current state of the LRRK2 field
Jean‐Marc Taymans, Matt Fell, Tim Greenamyre, et al.
npj Parkinson s Disease (2023) Vol. 9, Iss. 1
Open Access | Times Cited: 66
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
Membrane association but not identity is required for LRRK2 activation and phosphorylation of Rab GTPases
Rachel C. Gomez, Paulina S. Wawro, Paweł Lis, et al.
The Journal of Cell Biology (2019) Vol. 218, Iss. 12, pp. 4157-4170
Open Access | Times Cited: 101
The Emerging Role of the Lysosome in Parkinson’s Disease
Alba Navarro-Romero, Marta Montpeyó, Marta Martínez‐Vicente
Cells (2020) Vol. 9, Iss. 11, pp. 2399-2399
Open Access | Times Cited: 101
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
LRRK2 and the Endolysosomal System in Parkinson’s Disease
Madalynn L. Erb, Darren J. Moore
Journal of Parkinson s Disease (2020) Vol. 10, Iss. 4, pp. 1271-1291
Open Access | Times Cited: 81
Rab GTPases: Switching to Human Diseases
Noemi Antonella Guadagno, Cinzia Progida
Cells (2019) Vol. 8, Iss. 8, pp. 909-909
Open Access | Times Cited: 77
The Ras Superfamily of Small GTPases in Non-neoplastic Cerebral Diseases
Liang Qu, Chao Pan, Shiming He, et al.
Frontiers in Molecular Neuroscience (2019) Vol. 12
Open Access | Times Cited: 76
LRRK2 Is Recruited to Phagosomes and Co-recruits RAB8 and RAB10 in Human Pluripotent Stem Cell-Derived Macrophages
Heyne Lee, Rowan Flynn, Ishta Sharma, et al.
Stem Cell Reports (2020) Vol. 14, Iss. 5, pp. 940-955
Open Access | Times Cited: 76
Stem-cell-derived human microglia transplanted into mouse brain to study human disease
Nicola Fattorelli, Anna Martínez‐Muriana, Leen Wolfs, et al.
Nature Protocols (2021) Vol. 16, Iss. 2, pp. 1013-1033
Closed Access | Times Cited: 76
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
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
Pathological Functions of LRRK2 in Parkinson’s Disease
Ga Ram Jeong, Byoung Dae Lee
Cells (2020) Vol. 9, Iss. 12, pp. 2565-2565
Open Access | Times Cited: 70
Mutations in LRRK2 linked to Parkinson disease sequester Rab8a to damaged lysosomes and regulate transferrin-mediated iron uptake in microglia
Adamantios Mamais, Jillian H. Kluss, Luis Bonet‐Ponce, et al.
PLoS Biology (2021) Vol. 19, Iss. 12, pp. e3001480-e3001480
Open Access | Times Cited: 64
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
Loss of primary cilia and dopaminergic neuroprotection in pathogenic LRRK2-driven and idiopathic Parkinson’s disease
Shahzad S. Khan, Ebsy Jaimon, Yu‐En Lin, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 14
A potential patient stratification biomarker for Parkinson´s disease based on LRRK2 kinase-mediated centrosomal alterations in peripheral blood-derived cells
Yahaira Naaldijk, Belén Fernández, Rachel Fasiczka, et al.
npj Parkinson s Disease (2024) Vol. 10, Iss. 1
Open Access | Times Cited: 11
Loss of primary cilia and dopaminergic neuroprotection in pathogenic LRRK2-driven and idiopathic Parkinson’s disease
Shahzad S. Khan, Ebsy Jaimon, Yu‐En Lin, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 32
Open Access | Times Cited: 10
The G2019S variant of leucine-rich repeat kinase 2 (LRRK2) alters endolysosomal trafficking by impairing the function of the GTPase RAB8A
Pilar Rivero-Ríos, María Romo-Lozano, Jesús Madero‐Pérez, et al.
Journal of Biological Chemistry (2019) Vol. 294, Iss. 13, pp. 4738-4758
Open Access | Times Cited: 68
Identification and validation of key genes associated with non‐small‐cell lung cancer
Qiang Ma, Yuan Xu, Hebin Liao, et al.
Journal of Cellular Physiology (2019) Vol. 234, Iss. 12, pp. 22742-22752
Closed Access | Times Cited: 66
The Emerging Functions of LRRK2 and Rab GTPases in the Endolysosomal System
Tomoki Kuwahara, Takeshi Iwatsubo
Frontiers in Neuroscience (2020) Vol. 14
Open Access | Times Cited: 56
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