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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:

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: 444

Showing 51-75 of 444 citing articles:

The Original Social Network: White Matter and Social Cognition
Yin Wang, Ingrid R. Olson
Trends in Cognitive Sciences (2018) Vol. 22, Iss. 6, pp. 504-516
Open Access | Times Cited: 98
Neurotheranostics as personalized medicines
Bhavesh D. Kevadiya, Brendan M. Ottemann, Midhun Ben Thomas, et al.
Advanced Drug Delivery Reviews (2018) Vol. 148, pp. 252-289
Open Access | Times Cited: 97
In vivo identification of GTPase interactors by mitochondrial relocalization and proximity biotinylation
Alison K. Gillingham, Jessie Bertram, Farida Begum, et al.
eLife (2019) Vol. 8
Open Access | Times Cited: 92
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
Mechanisms of PINK1, ubiquitin and Parkin interactions in mitochondrial quality control and beyond
Andrew N. Bayne, Jean‐François Trempe
Cellular and Molecular Life Sciences (2019) Vol. 76, Iss. 23, pp. 4589-4611
Closed Access | Times Cited: 89
RAB8, RAB10 and RILPL1 contribute to both LRRK2 kinase–mediated centrosomal cohesion and ciliogenesis deficits
Antonio Jesús Lara Ordóñez, Belén Fernández, Elena Fdez, et al.
Human Molecular Genetics (2019) Vol. 28, Iss. 21, pp. 3552-3568
Open Access | Times Cited: 88
LRRK2 inhibition prevents endolysosomal deficits seen in human Parkinson's disease
Emily M. Rocha, Briana R. De Miranda, Sandra L. Castro, et al.
Neurobiology of Disease (2019) Vol. 134, pp. 104626-104626
Open Access | Times Cited: 85
Crystal structure of the WD40 domain dimer of LRRK2
Pengfei Zhang, Ying Fan, Heng Ru, et al.
Proceedings of the National Academy of Sciences (2019) Vol. 116, Iss. 5, pp. 1579-1584
Open Access | Times Cited: 84
A multidimensional perspective on microbial interactions
Alan R. Pacheco, Daniel Segrè
FEMS Microbiology Letters (2019) Vol. 366, Iss. 11
Open Access | Times Cited: 82
LRRK2 and Rab10 coordinate macropinocytosis to mediate immunological responses in phagocytes
Zhiyong Liu, Enquan Xu, Hien Zhao, et al.
The EMBO Journal (2020) Vol. 39, Iss. 20
Open Access | Times Cited: 82
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
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
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: 77
Pathogenic LRRK2 regulates ciliation probability upstream of tau tubulin kinase 2 via Rab10 and RILPL1 proteins
Yuriko Sobu, Paulina S. Wawro, Herschel S. Dhekne, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 10
Open Access | Times Cited: 77
The Ras Superfamily of Small GTPases in Non-neoplastic Cerebral Diseases
Liang Qu, Chao Pan, Shiming He, et al.
Frontiers in Molecular Neuroscience (2019) Vol. 12
Open Access | Times Cited: 76
Primary cilia and ciliary signaling pathways in aging and age-related brain disorders
Rong Ma, Naseer A. Kutchy, Liang Chen, et al.
Neurobiology of Disease (2021) Vol. 163, pp. 105607-105607
Open Access | Times Cited: 75
Pathogenic LRRK2 control of primary cilia and Hedgehog signaling in neurons and astrocytes of mouse brain
Shahzad S. Khan, Yuriko Sobu, Herschel S. Dhekne, et al.
eLife (2021) Vol. 10
Open Access | Times Cited: 74
Parkinson's: A Disease of Aberrant Vesicle Trafficking
Pawan Singh, Miratul M. K. Muqit
Annual Review of Cell and Developmental Biology (2020) Vol. 36, Iss. 1, pp. 237-264
Open Access | Times Cited: 72
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
Structural Basis for Rab8a Recruitment of RILPL2 via LRRK2 Phosphorylation of Switch 2
Dieter Waschbüsch, Elena Purlyte, Prosenjit Pal, et al.
Structure (2020) Vol. 28, Iss. 4, pp. 406-417.e6
Open Access | Times Cited: 71
Role of protein phosphorylation in cell signaling, disease, and the intervention therapy
Kun Pang, Wei Wang, Jiaxin Qin, et al.
MedComm (2022) Vol. 3, Iss. 4
Open Access | Times Cited: 67
Energy and Dynamics of Caveolae Trafficking
Claudia Matthaeus, Justin W. Taraska
Frontiers in Cell and Developmental Biology (2021) Vol. 8
Open Access | Times Cited: 62
LRRK2 recruitment, activity, and function in organelles
Luis Bonet‐Ponce, Mark Cookson
FEBS Journal (2021) Vol. 289, Iss. 22, pp. 6871-6890
Open Access | Times Cited: 60
A feed-forward pathway drives LRRK2 kinase membrane recruitment and activation
Edmundo G. Vides, Ayan Adhikari, Claire Y Chiang, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 46
LRRK2 phosphorylation of Rab GTPases in Parkinson's disease
Suzanne R. Pfeffer
FEBS Letters (2022) Vol. 597, Iss. 6, pp. 811-818
Open Access | Times Cited: 42

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