Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

Lysosomal positioning regulates Rab10 phosphorylation at LRRK2 + lysosomes
Jillian H. Kluss, Alexandra Beilina, Chad D. Williamson, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 43
Open Access | Times Cited: 40

Showing 1-25 of 40 citing articles:

Autophagy in Parkinson’s Disease
Lior Nechushtai, Dan Frenkel, Ronit Pinkas‐Kramarski
Biomolecules (2023) Vol. 13, Iss. 10, pp. 1435-1435
Open Access | Times Cited: 34
Axonal transport of autophagosomes is regulated by dynein activators JIP3/JIP4 and ARF/RAB GTPases
Sydney E. Cason, Erika L.F. Holzbaur
The Journal of Cell Biology (2023) Vol. 222, Iss. 12
Open Access | Times Cited: 27
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
VPS13C regulates phospho-Rab10-mediated lysosomal function in human dopaminergic neurons
Leonie F. Schrӧder, Wesley Peng, Ge Gao, et al.
The Journal of Cell Biology (2024) Vol. 223, Iss. 5
Open Access | Times Cited: 10
Current trends in basic research on Parkinson’s disease: from mitochondria, lysosome to α-synuclein
Hideaki Matsui, Ryōsuke Takahashi
Journal of Neural Transmission (2024) Vol. 131, Iss. 6, pp. 663-674
Open Access | Times Cited: 9
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
Membrane remodeling properties of the Parkinson’s disease protein LRRK2
Xinbo Wang, Javier Espadas, Yumei Wu, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 43
Open Access | Times Cited: 17
Rab10 regulates the sorting of internalised TrkB for retrograde axonal transport
Oscar M. Lazo, Giampietro Schiavo
eLife (2023) Vol. 12
Open Access | Times Cited: 15
A fluorogenic chemically induced dimerization technology for controlling, imaging and sensing protein proximity
Sara Bottone, Octave Joliot, Zeyneb Vildan Cakil, et al.
Nature Methods (2023) Vol. 20, Iss. 10, pp. 1553-1562
Open Access | Times Cited: 14
Novel autophagy inducers by accelerating lysosomal clustering against Parkinson’s disease
Yuki Date, Yukiko Sasazawa, Mitsuhiro Kitagawa, et al.
eLife (2024) Vol. 13
Open Access | Times Cited: 5
RpH-ILV: Probe for lysosomal pH and acute LLOMe-induced membrane permeabilization in cell lines and Drosophila
Izaak J. Cheetham‐Wilkinson, Bhavya Sivalingam, Chloe Flitton, et al.
Science Advances (2025) Vol. 11, Iss. 1
Open Access
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
Salmonella exploits LRRK2-dependent plasma membrane dynamics to invade host cells
Hongxian Zhu, Andrew M. Sydor, Bing-Ru Yan, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Retromer promotes the lysosomal turnover of mtDNA
Parisa Kakanj, Mari Bonse, Arya Kshirsagar, et al.
Science Advances (2025) Vol. 11, Iss. 14
Open Access
Is Glial Dysfunction the Key Pathogenesis of LRRK2-Linked Parkinson’s Disease?
Tatou Iseki, Yuzuru Imai, Nobutaka Hattori
Biomolecules (2023) Vol. 13, Iss. 1, pp. 178-178
Open Access | Times Cited: 10
Endogenous Rab38 regulates LRRK2’s membrane recruitment and substrate Rab phosphorylation in melanocytes
Alexandra Unapanta, Farbod Shavarebi, Jacob Porath, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 10, pp. 105192-105192
Open Access | Times Cited: 8
The endoplasmic reticulum contributes to lysosomal tubulation/sorting driven by LRRK2
Luis Bonet‐Ponce, Mark Cookson
Molecular Biology of the Cell (2022) Vol. 33, Iss. 13
Open Access | Times Cited: 14
Axonal transport of autophagosomes is regulated by dynein activators JIP3/JIP4 and ARF/RAB GTPases
Sydney E. Cason, Erika L.F. Holzbaur
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 7
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
Rab12 regulates LRRK2 activity by promoting its localization to lysosomes
Vitaliy V. Bondar, Xiang Wang, Oliver B. Davis, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 6
Insights into the cellular consequences of LRRK2-mediated Rab protein phosphorylation
Rachel Fasiczka, Yahaira Naaldijk, Besma Brahmia, et al.
Biochemical Society Transactions (2023) Vol. 51, Iss. 2, pp. 587-595
Open Access | Times Cited: 4
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
The LRRK2-G2019S mutation attenuates repair of brain injury partially by reducing the release of osteopontin-containing monocytic exosome-like vesicles
Jiawei An, Hai‐Jie Yang, Sang Myun Park, et al.
Neurobiology of Disease (2024) Vol. 197, pp. 106528-106528
Open Access | Times Cited: 1
How Parkinson’s Disease-Linked LRRK2 Mutations Affect Different CNS Cell Types
Hannah M. Bailey, Mark Cookson
Journal of Parkinson s Disease (2024) Vol. 14, Iss. 7, pp. 1331-1352
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.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Page 1 - Next Page

Scroll to top