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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:

Rab12 is a regulator of LRRK2 and its activation by damaged lysosomes
Xiang Wang, Vitaliy V. Bondar, Oliver B. Davis, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 22

Showing 22 citing articles:

Key genes and convergent pathogenic mechanisms in Parkinson disease
Robert Coukos, Dimitri Krainc
Nature reviews. Neuroscience (2024) Vol. 25, Iss. 6, pp. 393-413
Closed Access | Times Cited: 27
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
LRRK2 in Parkinson's disease: upstream regulation and therapeutic targeting
Yulan Xiong, Jianzhong Yu
Trends in Molecular Medicine (2024) Vol. 30, Iss. 10, pp. 982-996
Closed Access | Times Cited: 7
Adult-onset deletion of ATP13A2 in mice induces progressive nigrostriatal pathway dopaminergic degeneration and lysosomal abnormalities
Madalynn Erb, Kayla Sipple, Nathan Levine, et al.
npj Parkinson s Disease (2024) Vol. 10, Iss. 1
Open Access | Times Cited: 5
LRRK2, lysosome damage, and Parkinson's disease
Amanda Bentley‐DeSousa, D.J. Clegg, Shawn M. Ferguson
Current Opinion in Cell Biology (2025) Vol. 93, pp. 102482-102482
Open Access
A STING-CASM-GABARAP Pathway Activates LRRK2 at Lysosomes
Amanda Bentley‐DeSousa, Agnes Roczniak-Ferguson, Shawn M. Ferguson
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 10
Opposing actions of JIP4 and RILPL1 provide antagonistic motor force to dynamically regulate membrane reformation during lysosomal tubulation/sorting driven by LRRK2
Luis Bonet‐Ponce, Tsion Tegicho, Alexandra Beilina, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 2
An Update on the Interplay between LRRK2, Rab GTPases and Parkinson’s Disease
Tadayuki Komori, Tomoki Kuwahara
Biomolecules (2023) Vol. 13, Iss. 11, pp. 1645-1645
Open Access | Times Cited: 4
RAB12-LRRK2 Complex Suppresses Primary Ciliogenesis and Regulates Centrosome Homeostasis in Astrocytes
Xingjian Li, Hanwen Zhu, Bik Tzu Huang, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Pathogenic LRRK2 causes age-dependent and region-specific deficits in ciliation, innervation and viability of cholinergic neurons
Besma Brahmia, Yahaira Naaldijk, Pallabi Sarkar, et al.
(2024)
Open Access | Times Cited: 1
RAB12-LRRK2 complex suppresses primary ciliogenesis and regulates centrosome homeostasis in astrocytes
Xingjian Li, Hanwen Zhu, Bik Tzu Huang, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 1
Adult-Onset Deletion of ATP13A2 in Mice Induces Progressive Nigrostriatal Pathway Dopaminergic Degeneration and Lysosomal Abnormalities
Madalynn Erb, Kayla Sipple, Nathan Levine, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
In-depth mass-spectrometry reveals phospho-RAB12 as a blood biomarker of G2019S LRRK2-driven Parkinson
Adriana Cortés, Toan K. Phung, Lorena de Mena, et al.
medRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
15-Lipoxygenase-Mediated Lipid Peroxidation Regulates LRRK2 Kinase Activity
Matthew T. Keeney, Eric K. Hoffman, Julie Weir, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Pathogenic LRRK2 causes age-dependent and region-specific deficits in ciliation, innervation and viability of cholinergic neurons
Besma Brahmia, Yahaira Naaldijk, Pallabi Sarkar, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Closed Access
Mechanisms of lysosomal tubulation and sorting driven by LRRK2
Luis Bonet‐Ponce, Jillian H. Kluss, Mark Cookson
Biochemical Society Transactions (2024) Vol. 52, Iss. 4, pp. 1909-1919
Closed Access
Targeting Specific Kinase Substrates Rescues Increased Colitis Severity Induced by the Crohn's Disease-Linked LRRK2-N2081D Variant
George Heaton, Xianting Li, Xiaoting Zhou, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Closed Access
Pathogenic LRRK2 causes age-dependent and region-specific deficits in ciliation, innervation and viability of cholinergic neurons
Besma Brahmia, Yahaira Naaldijk, Pallabi Sarkar, et al.
(2024)
Open Access
Proteostasis dysregulation in p.A53T-α-Synuclein iPSC-derived astrocytes exacerbates neurodegeneration in a Parkinson's disease model with Lewy-like pathology
Christina Paschou, Olympia Apokotou, Αναστάσιος Κόλλιας, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
CalDAG-GEFI acts as a guanine nucleotide exchange factor for LRRK2 to regulate LRRK2 function and neurodegeneration
Qinfang Liu, Bingxu Huang, Noah Guy Lewis Guiberson, et al.
Science Advances (2024) Vol. 10, Iss. 47
Open Access
14-3-3 binding maintains the Parkinson's associated kinase LRRK2 in an inactive state
Juliana A. Martinez Fiesco, Ning Li, Arthur Adelino de Freitas Cruz, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
In-depth mass-spectrometry reveals phospho-RAB12 as a blood biomarker of G2019S LRRK2-driven Parkinson’s disease
Adriana Cortés, Toan K. Phung, Lorena de Mena, et al.
Brain (2024)
Open Access
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