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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:

Pharmacological LRRK2 kinase inhibition induces LRRK2 protein destabilization and proteasomal degradation
Evy Lobbestael, Laura Civiero, Tina De Wit, et al.
Scientific Reports (2016) Vol. 6, Iss. 1
Open Access | Times Cited: 69

Showing 1-25 of 69 citing articles:

LRRK2 Inhibition by BIIB122 in Healthy Participants and Patients with Parkinson's Disease
Danna Jennings, Sarah Huntwork‐Rodriguez, Maurits F. J. M. Vissers, et al.
Movement Disorders (2023) Vol. 38, Iss. 3, pp. 386-398
Open Access | Times Cited: 45
Interrogating Parkinson's disease LRRK2 kinase pathway activity by assessing Rab10 phosphorylation in human neutrophils
Ying Fan, Andrew J.M. Howden, Adil R. Sarhan, et al.
Biochemical Journal (2017) Vol. 475, Iss. 1, pp. 23-44
Open Access | Times Cited: 158
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
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
Progress and Challenges in Targeted Protein Degradation for Neurodegenerative Disease Therapy
Yingxu Fang, Jiaxing Wang, Min Zhao, et al.
Journal of Medicinal Chemistry (2022) Vol. 65, Iss. 17, pp. 11454-11477
Closed Access | Times Cited: 49
LRRK2 G2019S-induced mitochondrial DNA damage is LRRK2 kinase dependent and inhibition restores mtDNA integrity in Parkinson’s disease
Evan H. Howlett, Nicholas O. Jensen, Frances Belmonte, et al.
Human Molecular Genetics (2017) Vol. 26, Iss. 22, pp. 4340-4351
Open Access | Times Cited: 85
Small-Molecule Kinase Downregulators
Lyn H. Jones
Cell chemical biology (2017) Vol. 25, Iss. 1, pp. 30-35
Open Access | Times Cited: 65
Vitamin B12 modulates Parkinson’s disease LRRK2 kinase activity through allosteric regulation and confers neuroprotection
Adam Schaffner, Xianting Li, Yacob Gómez-Llorente, et al.
Cell Research (2019) Vol. 29, Iss. 4, pp. 313-329
Open Access | Times Cited: 58
Monomeric Targeted Protein Degraders
Emily J. Hanan, Jun Liang, Xiaojing Wang, et al.
Journal of Medicinal Chemistry (2020) Vol. 63, Iss. 20, pp. 11330-11361
Closed Access | Times Cited: 57
Dopaminergic neurodegeneration induced by Parkinson's disease-linked G2019S LRRK2 is dependent on kinase and GTPase activity
An Phu Tran Nguyen, Elpida Tsika, Kaela Kelly, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 29, pp. 17296-17307
Open Access | Times Cited: 53
LRRK2 Phosphorylation, More Than an Epiphenomenon
Antoine Marchand, Matthieu Drouyer, Alessia Sarchione, et al.
Frontiers in Neuroscience (2020) Vol. 14
Open Access | Times Cited: 52
Preclinical modeling of chronic inhibition of the Parkinson’s disease associated kinase LRRK2 reveals altered function of the endolysosomal system in vivo
Jillian H. Kluss, Melissa Conti Mazza, Yan Li, et al.
Molecular Neurodegeneration (2021) Vol. 16, Iss. 1
Open Access | Times Cited: 45
LRRK2 Targeting Strategies as Potential Treatment of Parkinson’s Disease
Dominika Wojewska, Arjan Kortholt
Biomolecules (2021) Vol. 11, Iss. 8, pp. 1101-1101
Open Access | Times Cited: 44
The small GTPase Rit2 modulates LRRK2 kinase activity, is required for lysosomal function and protects against alpha-synuclein neuropathology
Julia Obergasteiger, Anne-Marie Castonguay, Sara Pizzi, et al.
npj Parkinson s Disease (2023) Vol. 9, Iss. 1
Open Access | Times Cited: 18
LRRK2 in Parkinson's disease: upstream regulation and therapeutic targeting
Yulan Xiong, Jianzhong Yu
Trends in Molecular Medicine (2024) Vol. 30, Iss. 10, pp. 982-996
Closed Access | Times Cited: 7
Structural interface between LRRK2 and 14-3-3 protein
Loes M. Stevers, R.M.J.M. de Vries, Richard G. Doveston, et al.
Biochemical Journal (2017) Vol. 474, Iss. 7, pp. 1273-1287
Open Access | Times Cited: 59
Clinically Precedented Protein Kinases: Rationale for Their Use in Neurodegenerative Disease
Caroline Benn, Lee A. Dawson
Frontiers in Aging Neuroscience (2020) Vol. 12
Open Access | Times Cited: 42
Pathways to Parkinson’s disease: a spotlight on 14-3-3 proteins
Elena Giusto, Talene A. Yacoubian, Elisa Greggio, et al.
npj Parkinson s Disease (2021) Vol. 7, Iss. 1
Open Access | Times Cited: 39
The Development and Design Strategy of Leucine-Rich Repeat Kinase 2 Inhibitors: Promising Therapeutic Agents for Parkinson’s Disease
Xu Tang, Shuaishuai Xing, Mingkang Ma, et al.
Journal of Medicinal Chemistry (2023) Vol. 66, Iss. 4, pp. 2282-2307
Closed Access | Times Cited: 14
Targeting LRRK2 in Parkinson’s disease: an update on recent developments
Sharon L. Chan, Eng‐King Tan
Expert Opinion on Therapeutic Targets (2017) Vol. 21, Iss. 6, pp. 601-610
Closed Access | Times Cited: 45
The G2019S mutation in LRRK2 imparts resiliency to kinase inhibition
Kaela Kelly, Shijie Wang, Ravindra Boddu, et al.
Experimental Neurology (2018) Vol. 309, pp. 1-13
Open Access | Times Cited: 44
Reduced LRRK2 in association with retromer dysfunction in post-mortem brain tissue from LRRK2 mutation carriers
Ye Zhao, Gayathri Perera, Junko Takahashi‐Fujigasaki, et al.
Brain (2017) Vol. 141, Iss. 2, pp. 486-495
Open Access | Times Cited: 43
G2019S-LRRK2 mutation enhances MPTP-linked Parkinsonism in mice
Nicolas Arbez, XiaoFei He, Yong Huang, et al.
Human Molecular Genetics (2019) Vol. 29, Iss. 4, pp. 580-590
Open Access | Times Cited: 36
Small-Molecule Approaches to Targeted Protein Degradation
T.B. Faust, Katherine A. Donovan, Hong Yue, et al.
Annual Review of Cancer Biology (2020) Vol. 5, Iss. 1, pp. 181-201
Open Access | Times Cited: 36
Mitochondrial DNA damage as a potential biomarker of LRRK2 kinase activity in LRRK2 Parkinson’s disease
Claudia P. González-Hunt, Elizabeth Thacker, C. M. Toste, et al.
Scientific Reports (2020) Vol. 10, Iss. 1
Open Access | Times Cited: 33
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