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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:

An early endosome regulator, Rab5b, is an LRRK2 kinase substrate
Hye Jin Yun, Hye Jung Kim, Inhwa Ga, et al.
The Journal of Biochemistry (2015) Vol. 157, Iss. 6, pp. 485-495
Closed Access | Times Cited: 74

Showing 1-25 of 74 citing articles:

Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPases
Martin Steger, Francesca Tonelli, Genta Ito, et al.
eLife (2016) Vol. 5
Open Access | Times Cited: 931
Excitotoxicity, calcium and mitochondria: a triad in synaptic neurodegeneration
Manish Verma, Britney N. Lizama, Charleen T. Chu
Translational Neurodegeneration (2022) Vol. 11, Iss. 1
Open Access | Times Cited: 259
Commensal bacteria direct selective cargo sorting to promote symbiosis
Qin Zhang, Ying Pan, Ruiqing Yan, et al.
Nature Immunology (2015) Vol. 16, Iss. 9, pp. 918-926
Closed Access | Times Cited: 192
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
APC-activated long noncoding RNA inhibits colorectal carcinoma pathogenesis through reduction of exosome production
Feng-Wei Wang, Chenhui Cao, Kai Han, et al.
Journal of Clinical Investigation (2018) Vol. 129, Iss. 2, pp. 727-743
Open Access | Times Cited: 147
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
Endocytic membrane trafficking and neurodegenerative disease
Andrea M. A. Schreij, Edward A. Fon, Peter S. McPherson
Cellular and Molecular Life Sciences (2015) Vol. 73, Iss. 8, pp. 1529-1545
Open Access | Times Cited: 142
α-Synuclein – Regulator of Exocytosis, Endocytosis, or Both?
Janin Lautenschläger, Clemens F. Kaminski, Gabriele S. Kaminski Schierle
Trends in Cell Biology (2017) Vol. 27, Iss. 7, pp. 468-479
Open Access | Times Cited: 120
Vps35 in cooperation with LRRK2 regulates synaptic vesicle endocytosis through the endosomal pathway in Drosophila
Tsuyoshi Inoshita, Taku Arano, Yuka Hosaka, et al.
Human Molecular Genetics (2017) Vol. 26, Iss. 15, pp. 2933-2948
Open Access | Times Cited: 112
“LRRK2: Autophagy and Lysosomal Activity”
Marta Madureira, Natalie Connor‐Robson, Richard Wade‐Martins
Frontiers in Neuroscience (2020) Vol. 14
Open Access | Times Cited: 107
Regulation of myeloid cell phagocytosis by LRRK2 via WAVE2 complex stabilization is altered in Parkinson’s disease
Kwang S. Kim, Paul C. Marcogliese, Jungwoo Yang, et al.
Proceedings of the National Academy of Sciences (2018) Vol. 115, Iss. 22
Open Access | Times Cited: 105
Parkinson's disease: convergence on synaptic homeostasis
Sandra‐Fausia Soukup, Roeland Vanhauwaert, Patrik Verstreken
The EMBO Journal (2018) Vol. 37, Iss. 18
Open Access | Times Cited: 105
Dysregulated phosphorylation of Rab GTPases by LRRK2 induces neurodegeneration
Ga Ram Jeong, Eun-Hae Jang, Jae Ryul Bae, et al.
Molecular Neurodegeneration (2018) Vol. 13, Iss. 1
Open Access | Times Cited: 101
Selective LRRK2 kinase inhibition reduces phosphorylation of endogenous Rab10 and Rab12 in human peripheral mononuclear blood cells
Kenneth Thirstrup, Justus C. Dächsel, Felix Oppermann, et al.
Scientific Reports (2017) Vol. 7, Iss. 1
Open Access | Times Cited: 94
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
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
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
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
Genes associated with Parkinson's disease: regulation of autophagy and beyond
Alexandra Beilina, Mark Cookson
Journal of Neurochemistry (2015) Vol. 139, Iss. S1, pp. 91-107
Open Access | Times Cited: 88
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
The dynamic switch mechanism that leads to activation of LRRK2 is embedded in the DFGψ motif in the kinase domain
Sven H. Schmidt, Matthias J. Knape, Daniela Boassa, et al.
Proceedings of the National Academy of Sciences (2019) Vol. 116, Iss. 30, pp. 14979-14988
Open Access | Times Cited: 73
The neurotrophin receptor signaling endosome: Where trafficking meets signaling
Kelly Barford, Christopher D. Deppmann, Bettina Winckler
Developmental Neurobiology (2016) Vol. 77, Iss. 4, pp. 405-418
Open Access | Times Cited: 71
Role of LRRK2 in the regulation of dopamine receptor trafficking
Mauro Rassu, Maria Grazia Del Giudice, Simona Sanna, et al.
PLoS ONE (2017) Vol. 12, Iss. 6, pp. e0179082-e0179082
Open Access | Times Cited: 64
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
Consequences of Rab GTPase dysfunction in genetic or acquired human diseases
Marcellus J. Banworth, Guangpu Li
Small GTPases (2017) Vol. 9, Iss. 1-2, pp. 158-181
Open Access | Times Cited: 57
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