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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:

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

Showing 1-25 of 157 citing articles:

Discovery of XL01126: A Potent, Fast, Cooperative, Selective, Orally Bioavailable, and Blood–Brain Barrier Penetrant PROTAC Degrader of Leucine-Rich Repeat Kinase 2
Xingui Liu, Alexia F. Kalogeropulou, Sofia Domingos, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 37, pp. 16930-16952
Open Access | Times Cited: 107
LRRK2 and idiopathic Parkinson’s disease
Emily M. Rocha, Matthew T. Keeney, Roberto Di Maio, et al.
Trends in Neurosciences (2022) Vol. 45, Iss. 3, pp. 224-236
Open Access | Times Cited: 105
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
Perspective on the current state of the LRRK2 field
Jean‐Marc Taymans, Matt Fell, Tim Greenamyre, et al.
npj Parkinson s Disease (2023) Vol. 9, Iss. 1
Open Access | Times Cited: 66
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
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
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 of human LRRK2 membrane recruitment and activation
Hanwen Zhu, Francesca Tonelli, Dario R. Alessi, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 39
Rab29-dependent asymmetrical activation of leucine-rich repeat kinase 2
Hanwen Zhu, Francesca Tonelli, Martin Turk, et al.
Science (2023) Vol. 382, Iss. 6677, pp. 1404-1411
Open Access | Times Cited: 39
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
Genome-wide screen reveals Rab12 GTPase as a critical activator of Parkinson’s disease-linked LRRK2 kinase
Herschel S. Dhekne, Francesca Tonelli, Wondwossen M Yeshaw, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 34
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
Neuroinflammation in Parkinson’s Disease: From Gene to Clinic: A Systematic Review
Carlos Castillo-Rangel, Gonzalo Núñez Marín, Karla Aketzalli Hernández-Contreras, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 6, pp. 5792-5792
Open Access | Times Cited: 26
Novel LRR-ROC Motif That Links the N- and C-terminal Domains in LRRK2 Undergoes an Order–Disorder Transition Upon Activation
Jui-Hung Weng, Chiara R. Trilling, Pallavi Kaila Sharma, et al.
Journal of Molecular Biology (2023) Vol. 435, Iss. 12, pp. 167999-167999
Open Access | Times Cited: 22
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
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
Impact of Type II LRRK2 inhibitors on signaling and mitophagy
Anna Tasegian, François Singh, Ian G. Ganley, et al.
Biochemical Journal (2021) Vol. 478, Iss. 19, pp. 3555-3573
Open Access | Times Cited: 51
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
Inhibition of Parkinson’s disease–related LRRK2 by type I and type II kinase inhibitors: Activity and structures
Marta Sanz Murillo, Amalia Villagran Suarez, Verena Dederer, et al.
Science Advances (2023) Vol. 9, Iss. 48
Open Access | Times Cited: 19
Identification of LRRK2 Inhibitors through Computational Drug Repurposing
Shuoyan Tan, Ruiqiang Lu, Dahong Yao, et al.
ACS Chemical Neuroscience (2023) Vol. 14, Iss. 3, pp. 481-493
Closed Access | Times Cited: 17
Doubly Constrained C-terminal of Roc (COR) Domain-Derived Peptides Inhibit Leucine-Rich Repeat Kinase 2 (LRRK2) Dimerization
Pragya Pathak, Krista K. Alexander, Leah G. Helton, et al.
ACS Chemical Neuroscience (2023) Vol. 14, Iss. 11, pp. 1971-1980
Open Access | Times Cited: 17
Membrane remodeling properties of the Parkinson’s disease protein LRRK2
Xinbo Wang, Javier Espadas, Yumei Wu, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 43
Open Access | Times Cited: 17
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
Phosphorylation of AQP4 by LRRK2 R1441G impairs glymphatic clearance of IFNγ and aggravates dopaminergic neurodegeneration
Heng Huang, Lishan Lin, Tengteng Wu, et al.
npj Parkinson s Disease (2024) Vol. 10, Iss. 1
Open Access | Times Cited: 6
Structural insights into the GTP-driven monomerization and activation of a bacterial LRRK2 homolog using allosteric nanobodies
Christian Galicia, Giambattista Guaitoli, Marcus Fislage, et al.
eLife (2024) Vol. 13
Open Access | Times Cited: 6
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