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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:

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

Showing 1-25 of 931 citing articles:

Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)1
Daniel J. Klionsky, Amal Kamal Abdel‐Aziz, Sara Abdelfatah, et al.
Autophagy (2021) Vol. 17, Iss. 1, pp. 1-382
Open Access | Times Cited: 1976
Mass-spectrometric exploration of proteome structure and function
Ruedi Aebersold, Matthias Mann
Nature (2016) Vol. 537, Iss. 7620, pp. 347-355
Closed Access | Times Cited: 1888
Ubiquitin modifications
Kirby N. Swatek, David Komander
Cell Research (2016) Vol. 26, Iss. 4, pp. 399-422
Open Access | Times Cited: 1661
LRRK2 activation in idiopathic Parkinson’s disease
Roberto Di Maio, Eric K. Hoffman, Emily M. Rocha, et al.
Science Translational Medicine (2018) Vol. 10, Iss. 451
Open Access | Times Cited: 528
Protein transmission in neurodegenerative disease
Chao Peng, John Q. Trojanowski, Virginia M.‐Y. Lee
Nature Reviews Neurology (2020) Vol. 16, Iss. 4, pp. 199-212
Open Access | Times Cited: 472
A homologue of the Parkinson’s disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover
Egon Deyaert, Lina Wauters, Giambattista Guaitoli, et al.
Nature Communications (2017) Vol. 8, Iss. 1
Open Access | Times Cited: 465
Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation establishes a connection to ciliogenesis
Martin Steger, Federico Diez, Herschel S. Dhekne, et al.
eLife (2017) Vol. 6
Open Access | Times Cited: 442
Defects in trafficking bridge Parkinson's disease pathology and genetics
Asa Abeliovich, Aaron D. Gitler
Nature (2016) Vol. 539, Iss. 7628, pp. 207-216
Closed Access | Times Cited: 424
LRRK2 in Parkinson disease: challenges of clinical trials
Eduardo Tolosa, Miquel Vila, Christine Klein, et al.
Nature Reviews Neurology (2020) Vol. 16, Iss. 2, pp. 97-107
Closed Access | Times Cited: 371
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
Functional variants in the LRRK2 gene confer shared effects on risk for Crohn’s disease and Parkinson’s disease
Ken Hui, Heriberto Fernandez-Hernandez, Jianzhong Hu, et al.
Science Translational Medicine (2018) Vol. 10, Iss. 423
Open Access | Times Cited: 330
Rab29 activation of the Parkinson's disease‐associated LRRK2 kinase
Elena Purlyte, Herschel S. Dhekne, Adil R. Sarhan, et al.
The EMBO Journal (2017) Vol. 37, Iss. 1, pp. 1-18
Open Access | Times Cited: 326
Genetics of Parkinson's disease
Christina M. Lill
Molecular and Cellular Probes (2016) Vol. 30, Iss. 6, pp. 386-396
Closed Access | Times Cited: 321
High-throughput and high-sensitivity phosphoproteomics with the EasyPhos platform
Sean J. Humphrey, Özge Karayel, David E. James, et al.
Nature Protocols (2018) Vol. 13, Iss. 9, pp. 1897-1916
Closed Access | Times Cited: 306
The interplay of aging, genetics and environmental factors in the pathogenesis of Parkinson’s disease
Shirley Yin-Yu Pang, Philip Wing‐Lok Ho, Huifang Liu, et al.
Translational Neurodegeneration (2019) Vol. 8, Iss. 1
Open Access | Times Cited: 306
Illuminating the dark phosphoproteome
Elise J. Needham, Benjamin L. Parker, Timur Burykin, et al.
Science Signaling (2019) Vol. 12, Iss. 565
Open Access | Times Cited: 299
Rab GTPases: master regulators that establish the secretory and endocytic pathways
Suzanne R. Pfeffer
Molecular Biology of the Cell (2017) Vol. 28, Iss. 6, pp. 712-715
Open Access | Times Cited: 295
LRRK2 kinase in Parkinson's disease
Dario R. Alessi, Esther Sammler
Science (2018) Vol. 360, Iss. 6384, pp. 36-37
Open Access | Times Cited: 295
Autophagy in Parkinson's Disease
Xu Hou, Jens O. Watzlawik, Fabienne C. Fiesel, et al.
Journal of Molecular Biology (2020) Vol. 432, Iss. 8, pp. 2651-2672
Open Access | Times Cited: 280
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
Synaptic, Mitochondrial, and Lysosomal Dysfunction in Parkinson’s Disease
Maria Nguyen, Yvette C. Wong, Daniel Ysselstein, et al.
Trends in Neurosciences (2018) Vol. 42, Iss. 2, pp. 140-149
Open Access | Times Cited: 270
LRRK2 phosphorylates membrane-bound Rabs and is activated by GTP-bound Rab7L1 to promote recruitment to the trans-Golgi network
Zhiyong Liu, Nicole Bryant, Ravindran Kumaran, et al.
Human Molecular Genetics (2017) Vol. 27, Iss. 2, pp. 385-395
Open Access | Times Cited: 252
Mitochondrial ROS promotes susceptibility to infection via gasdermin D-mediated necroptosis
Chi G. Weindel, E. Martínez, Xiao Zhao, et al.
Cell (2022) Vol. 185, Iss. 17, pp. 3214-3231.e23
Open Access | Times Cited: 233
The emerging role of mass spectrometry-based proteomics in drug discovery
Felix Meissner, Jennifer Geddes‐McAlister, Matthias Mann, et al.
Nature Reviews Drug Discovery (2022) Vol. 21, Iss. 9, pp. 637-654
Closed Access | Times Cited: 227
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
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