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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:

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

Showing 1-25 of 84 citing articles:

Structure of LRRK2 in Parkinson’s disease and model for microtubule interaction
Colin K. Deniston, John Salogiannis, Sebastian Mathea, et al.
Nature (2020) Vol. 588, Iss. 7837, pp. 344-349
Open Access | Times Cited: 201
The In Situ Structure of Parkinson’s Disease-Linked LRRK2
Reika Watanabe, Robert Buschauer, Jan Böhning, et al.
Cell (2020) Vol. 182, Iss. 6, pp. 1508-1518.e16
Open Access | Times Cited: 191
LRRK2 links genetic and sporadic Parkinson's disease
Jillian H. Kluss, Adamantios Mamais, Mark Cookson
Biochemical Society Transactions (2019) Vol. 47, Iss. 2, pp. 651-661
Open Access | Times Cited: 187
Parkinson's disease in the Western Pacific Region
Shen‐Yang Lim, Ai Huey Tan, Azlina Ahmad‐Annuar, et al.
The Lancet Neurology (2019) Vol. 18, Iss. 9, pp. 865-879
Closed Access | Times Cited: 157
Structural analysis of the full-length human LRRK2
Alexander Myasnikov, Hanwen Zhu, Patricia Hixson, et al.
Cell (2021) Vol. 184, Iss. 13, pp. 3519-3527.e10
Open Access | Times Cited: 157
Impact of 100 LRRK2 variants linked to Parkinson's disease on kinase activity and microtubule binding
Alexia F. Kalogeropulou, Elena Purlyte, Francesca Tonelli, et al.
Biochemical Journal (2022) Vol. 479, Iss. 17, pp. 1759-1783
Open Access | Times Cited: 87
Leucine-Rich Repeat Kinases
Dario R. Alessi, Suzanne R. Pfeffer
Annual Review of Biochemistry (2024) Vol. 93, Iss. 1, pp. 261-287
Closed Access | Times Cited: 17
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
Advances in elucidating the function of leucine-rich repeat protein kinase-2 in normal cells and Parkinson's disease
Matthew Taylor, Dario R. Alessi
Current Opinion in Cell Biology (2020) Vol. 63, pp. 102-113
Open Access | Times Cited: 116
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
Nanobodies as allosteric modulators of Parkinson’s disease–associated LRRK2
Ranjan K. Singh, Ahmed Soliman, Giambattista Guaitoli, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 9
Open Access | Times Cited: 44
Structural basis for Parkinson’s disease-linked LRRK2’s binding to microtubules
David Snead, Mariusz Matyszewski, Andrea M. Dickey, et al.
Nature Structural & Molecular Biology (2022) Vol. 29, Iss. 12, pp. 1196-1207
Open Access | Times Cited: 38
Small-molecule LRRK2 inhibitors for PD therapy: Current achievements and future perspectives
Jiarui Hu, Dan Zhang, Keyue Tian, et al.
European Journal of Medicinal Chemistry (2023) Vol. 256, pp. 115475-115475
Closed Access | Times Cited: 27
Pharmacology of LRRK2 with type I and II kinase inhibitors revealed by cryo-EM
Hanwen Zhu, Patricia Hixson, Wen Ma, et al.
Cell Discovery (2024) Vol. 10, Iss. 1
Open Access | Times Cited: 15
In silico screening of LRRK2 WDR domain inhibitors using deep docking and free energy simulations
Evgeny Gutkin, Filipp Gusev, Francesco Gentile, et al.
Chemical Science (2024) Vol. 15, Iss. 23, pp. 8800-8812
Open Access | Times Cited: 9
Practical Three-Component Regioselective Synthesis of Drug-Like 3-Aryl(or heteroaryl)-5,6-dihydrobenzo[h]cinnolines as Potential Non-Covalent Multi-Targeting Inhibitors To Combat Neurodegenerative Diseases
Hossein Mousavi, Mehdi Rimaz, Behzad Zeynizadeh
ACS Chemical Neuroscience (2024) Vol. 15, Iss. 9, pp. 1828-1881
Closed Access | Times Cited: 8
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
CACHE Challenge #1: Targeting the WDR Domain of LRRK2, A Parkinson’s Disease Associated Protein
Fengling Li, Suzanne Ackloo, C.H. Arrowsmith, et al.
Journal of Chemical Information and Modeling (2024) Vol. 64, Iss. 22, pp. 8521-8536
Open Access | Times Cited: 7
The Cell Biology of LRRK2 in Parkinson's Disease
Ahsan Usmani, Farbod Shavarebi, Annie Hiniker
Molecular and Cellular Biology (2021) Vol. 41, Iss. 5
Open Access | Times Cited: 34
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
Capturing the domain crosstalk in full length LRRK2 and LRRK2RCKW
Eliza Störmer, Jui-Hung Weng, Jian Wu, et al.
Biochemical Journal (2023) Vol. 480, Iss. 11, pp. 815-833
Open Access | Times Cited: 13
Subpocket Similarity-Based Hit Identification for Challenging Targets: Application to the WDR Domain of LRRK2
Merveille Eguida, Guillaume Bret, François Sindt, et al.
Journal of Chemical Information and Modeling (2024) Vol. 64, Iss. 13, pp. 5344-5355
Open Access | Times Cited: 5
The Roc domain of LRRK2 as a hub for protein-protein interactions: a focus on PAK6 and its impact on RAB phosphorylation
Susanna Cogo, Franz Y. Ho, Elena Tosoni, et al.
Brain Research (2022) Vol. 1778, pp. 147781-147781
Open Access | Times Cited: 21
Distinct nuclear and cytoplasmic assemblies and interactomes of the mammalian CTLH E3 ligase complex
Gabriel Onea, Matthew E. R. Maitland, Xu Wang, et al.
Journal of Cell Science (2022) Vol. 135, Iss. 14
Open Access | Times Cited: 20
LRRK2 Structure-Based Activation Mechanism and Pathogenesis
Xiaojuan Zhang, Arjan Kortholt
Biomolecules (2023) Vol. 13, Iss. 4, pp. 612-612
Open Access | Times Cited: 11
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