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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:

Rab GTPases and Membrane Trafficking in Neurodegeneration
Ferdi Rıdvan Kiral, Friederike E. Kohrs, Eugene Jennifer Jin, et al.
Current Biology (2018) Vol. 28, Iss. 8, pp. R471-R486
Open Access | Times Cited: 201

Showing 1-25 of 201 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: 338
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
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: 137
The cell biology of Parkinson’s disease
Nikhil Panicker, Preston Ge, Valina L. Dawson, et al.
The Journal of Cell Biology (2021) Vol. 220, Iss. 4
Open Access | Times Cited: 111
A review on evolution, structural characteristics, interactions, and regulation of the membrane transport protein: The family of Rab proteins
Zahoor Ahmad Parray
International Journal of Biological Macromolecules (2025) Vol. 296, pp. 139828-139828
Closed Access | Times Cited: 2
Association and shared biological bases between birth weight and cortical structure
Lu Zhang, Qiaoyue Ge, Zeyuan Sun, et al.
Translational Psychiatry (2025) Vol. 15, Iss. 1
Open Access | Times Cited: 2
LRRK2 regulation of immune-pathways and inflammatory disease
Rebecca L. Wallings, Malú G. Tansey
Biochemical Society Transactions (2019) Vol. 47, Iss. 6, pp. 1581-1595
Open Access | Times Cited: 126
Lysosomal Dysfunction at the Centre of Parkinson’s Disease and Frontotemporal Dementia/Amyotrophic Lateral Sclerosis
Rebecca L. Wallings, Stewart W. Humble, Michael E. Ward, et al.
Trends in Neurosciences (2019) Vol. 42, Iss. 12, pp. 899-912
Open Access | Times Cited: 116
Dynamic control of the dopamine transporter in neurotransmission and homeostasis
Mengfei Bu, Matthew J. Farrer, Habibeh Khoshbouei
npj Parkinson s Disease (2021) Vol. 7, Iss. 1
Open Access | Times Cited: 92
The Endolysosomal System and Proteostasis: From Development to Degeneration
Bettina Winckler, Victor Faúndez, Sandra Maday, et al.
Journal of Neuroscience (2018) Vol. 38, Iss. 44, pp. 9364-9374
Open Access | Times Cited: 91
Microglia roles in synaptic plasticity and myelination in homeostatic conditions and neurodevelopmental disorders
Ela Bar, Boaz Barak
Glia (2019) Vol. 67, Iss. 11, pp. 2125-2141
Closed Access | Times Cited: 90
Lipid and immune abnormalities causing age-dependent neurodegeneration and Parkinson’s disease
Penelope J. Hallett, Simone Engelender, Ole Isacson
Journal of Neuroinflammation (2019) Vol. 16, Iss. 1
Open Access | Times Cited: 90
Endosomal Dysfunction Induced by Directly Overactivating Rab5 Recapitulates Prodromal and Neurodegenerative Features of Alzheimer’s Disease
Anna Pensalfini, Seonil Kim, Shivakumar Subbanna, et al.
Cell Reports (2020) Vol. 33, Iss. 8, pp. 108420-108420
Open Access | Times Cited: 85
Proteomics Study of Peripheral Blood Mononuclear Cells in Down Syndrome Children
Chiara Lanzillotta, Viviana Greco, Diletta Valentini, et al.
Antioxidants (2020) Vol. 9, Iss. 11, pp. 1112-1112
Open Access | Times Cited: 83
Structural basis for VPS34 kinase activation by Rab1 and Rab5 on membranes
Shirley Tremel, Yohei Ohashi, Dustin R. Morado, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 82
Rab GTPases: Switching to Human Diseases
Noemi Antonella Guadagno, Cinzia Progida
Cells (2019) Vol. 8, Iss. 8, pp. 909-909
Open Access | Times Cited: 78
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: 72
Endocytosis in the axon initial segment maintains neuronal polarity
Kelsie Eichel, Takeshi Uenaka, Vivek Belapurkar, et al.
Nature (2022) Vol. 609, Iss. 7925, pp. 128-135
Open Access | Times Cited: 46
Alternative polyadenylation transcriptome-wide association study identifies APA-linked susceptibility genes in brain disorders
Ya Cui, Frederick J. Arnold, Fanglue Peng, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 33
Targeting small GTPases: emerging grasps on previously untamable targets, pioneered by KRAS
Guowei Yin, Jing Huang, Johnny Petela, et al.
Signal Transduction and Targeted Therapy (2023) Vol. 8, Iss. 1
Open Access | Times Cited: 31
Rab GTPases are evolutionarily conserved signals mediating selective autophagy
Pengwei Zhao, Rui Tian, Dandan Song, et al.
The Journal of Cell Biology (2025) Vol. 224, Iss. 5
Closed Access | Times Cited: 1
Endocytosis at the Drosophila blood–brain barrier as a function for sleep
Gregory Artiushin, Shirley Zhang, Hervé Tricoire, et al.
eLife (2018) Vol. 7
Open Access | Times Cited: 83
Vesicular transport mediates the uptake of cytoplasmic proteins into mitochondria in Drosophila melanogaster
Po‐Lin Chen, Kai‐Ting Huang, Chu-Ya Cheng, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 70
An integrated transcriptomics and proteomics analysis reveals functional endocytic dysregulation caused by mutations in LRRK2
Natalie Connor‐Robson, Heather Booth, Jeffrey G. Martin, et al.
Neurobiology of Disease (2019) Vol. 127, pp. 512-526
Open Access | Times Cited: 66
The multifaceted functions of ATG16L1 in autophagy and related processes
Noor Gammoh
Journal of Cell Science (2020) Vol. 133, Iss. 20
Open Access | Times Cited: 63
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