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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:

Cryo-EM analysis of homodimeric full-length LRRK2 and LRRK1 protein complexes
Kushal Sejwal, Mohamed Chami, Hervé Remigy, et al.
Scientific Reports (2017) Vol. 7, Iss. 1
Open Access | Times Cited: 53

Showing 1-25 of 53 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
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
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
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
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
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
Deciphering the LRRK code: LRRK1 and LRRK2 phosphorylate distinct Rab proteins and are regulated by diverse mechanisms
Asad Malik, Athanasios Karapetsas, Raja Sekhar Nirujogi, et al.
Biochemical Journal (2021) Vol. 478, Iss. 3, pp. 553-578
Open Access | Times Cited: 41
Progress in LRRK2-Associated Parkinson’s Disease Animal Models
Steven P. Seegobin, George R. Heaton, Dongxiao Liang, et al.
Frontiers in Neuroscience (2020) Vol. 14
Open Access | Times Cited: 40
Roco Proteins: GTPases with a Baroque Structure and Mechanism
Lina Wauters, Wim Versées, Arjan Kortholt
International Journal of Molecular Sciences (2019) Vol. 20, Iss. 1, pp. 147-147
Open Access | Times Cited: 37
The Regulation of Rab GTPases by Phosphorylation
Lejia Xu, Yuki Nagai, Yotaro Kajihara, et al.
Biomolecules (2021) Vol. 11, Iss. 9, pp. 1340-1340
Open Access | Times Cited: 28
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
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
The E3 ligase TRIM1 ubiquitinates LRRK2 and controls its localization, degradation, and toxicity
Adrienne E.D. Stormo, Farbod Shavarebi, Molly FitzGibbon, et al.
The Journal of Cell Biology (2022) Vol. 221, Iss. 4
Open Access | Times Cited: 16
LRRK2: Genetic mechanisms vs genetic subtypes
Ignacio Mata, Philippe A. Salles, Mario Cornejo‐Olivas, et al.
Handbook of clinical neurology (2023), pp. 133-154
Closed Access | Times Cited: 9
Physiological and pathological roles of LRRK2 in the nuclear envelope integrity
Vered Shani, Hazem Safory, Raymonde Szargel, et al.
Human Molecular Genetics (2019) Vol. 28, Iss. 23, pp. 3982-3996
Open Access | Times Cited: 26
Physiological and pathological functions of LRRK2: implications from substrate proteins
Miho Araki, Genta Ito, Taisuke Tomita
Neuronal Signaling (2018) Vol. 2, Iss. 4
Open Access | Times Cited: 24
Kinase activity of mutant LRRK2 manifests differently in hetero-dimeric vs. homo-dimeric complexes
Emmanouela Leandrou, Eliana Markidi, Anna Memou, et al.
Biochemical Journal (2019) Vol. 476, Iss. 3, pp. 559-579
Closed Access | Times Cited: 24
Kinase Domain Is a Dynamic Hub for Driving LRRK2 Allostery
Susan S. Taylor, Pallavi Kaila Sharma, Jui-Hung Weng, et al.
Frontiers in Molecular Neuroscience (2020) Vol. 13
Open Access | Times Cited: 23
Parkinson’s Disease-linked LRRK2 structure and model for microtubule interaction
Colin Deniston, John Salogiannis, Sebastian Mathea, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 22
LRRK2 signaling in neurodegeneration: two decades of progress
Lucia Iannotta, Elisa Greggio
Essays in Biochemistry (2021) Vol. 65, Iss. 7, pp. 859-872
Closed Access | Times Cited: 18
Discovery and Optimization of Potent, Selective, and Brain-Penetrant 1-Heteroaryl-1H-Indazole LRRK2 Kinase Inhibitors for the Treatment of Parkinson’s Disease
David A. Candito, Vladimir Simov, Anmol Gulati, et al.
Journal of Medicinal Chemistry (2022) Vol. 65, Iss. 24, pp. 16801-16817
Closed Access | Times Cited: 13
The Roc‐COR tandem domain of leucine‐rich repeat kinase 2 forms dimers and exhibits conventional Ras‐like GTPase properties
Ryan D. Mills, Lung‐Yu Liang, Daisy Lio, et al.
Journal of Neurochemistry (2018) Vol. 147, Iss. 3, pp. 409-428
Open Access | Times Cited: 19
PAK6-mediated phosphorylation of PPP2R2C regulates LRRK2-PP2A complex formation
Lucia Iannotta, Marco Emanuele, Giulia Favetta, et al.
Frontiers in Molecular Neuroscience (2023) Vol. 16
Open Access | Times Cited: 5
Thein situstructure of Parkinson’s disease-linked LRRK2
Reika Watanabe, Robert Buschauer, Jan Böhning, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2019)
Open Access | Times Cited: 15
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