OpenAlex Citation Counts

OpenAlex Citations Logo

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 biology of the LRRK2 GTPase and kinase domains: implications for regulation
Bernd K. Gilsbach, Arjan Kortholt
Frontiers in Molecular Neuroscience (2014) Vol. 7
Open Access | Times Cited: 78

Showing 1-25 of 78 citing articles:

A homologue of the Parkinson’s disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover
Egon Deyaert, Lina Wauters, Giambattista Guaitoli, et al.
Nature Communications (2017) Vol. 8, Iss. 1
Open Access | Times Cited: 465

The role of the LRRK2 gene in Parkinsonism
Jieqiong Li, Lan Tan, Jin‐Tai Yu
Molecular Neurodegeneration (2014) Vol. 9, Iss. 1
Open Access | Times Cited: 223

Genetics and genomics of Parkinson’s disease
Michelle K. Lin, Matthew J. Farrer
Genome Medicine (2014) Vol. 6, Iss. 6
Open Access | Times Cited: 170

Structural model of the dimeric Parkinson’s protein LRRK2 reveals a compact architecture involving distant interdomain contacts
Giambattista Guaitoli, Francesco Raimondi, Bernd K. Gilsbach, et al.
Proceedings of the National Academy of Sciences (2016) Vol. 113, Iss. 30
Open Access | Times Cited: 146

Inflammatory Bowel Diseases and Parkinson’s Disease
Tomasz Brudek
Journal of Parkinson s Disease (2019) Vol. 9, Iss. s2, pp. S331-S344
Open Access | Times Cited: 118

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

PPM1H phosphatase counteracts LRRK2 signaling by selectively dephosphorylating Rab proteins
Kerryn Berndsen, Paweł Lis, Wondwossen M Yeshaw, et al.
eLife (2019) Vol. 8
Open Access | Times Cited: 114

LRRK 2 regulates endoplasmic reticulum–mitochondrial tethering through the PERK ‐mediated ubiquitination pathway
Toshihiko Toyofuku, Yuki Okamoto, Takako Ishikawa, et al.
The EMBO Journal (2019) Vol. 39, Iss. 2
Open Access | Times Cited: 87

LRRK2 and Parkinson's disease: from genetics to targeted therapy
Yuri L. Sosero, Ziv Gan‐Or
Annals of Clinical and Translational Neurology (2023) Vol. 10, Iss. 6, pp. 850-864
Open Access | Times Cited: 30

Identification and validation of key genes associated with non‐small‐cell lung cancer
Qiang Ma, Yuan Xu, Hebin Liao, et al.
Journal of Cellular Physiology (2019) Vol. 234, Iss. 12, pp. 22742-22752
Closed Access | Times Cited: 66

Potential for therapeutic targeting of AKAP signaling complexes in nervous system disorders
Angela R. Wild, Mark L. Dell’Acqua
Pharmacology & Therapeutics (2017) Vol. 185, pp. 99-121
Open Access | Times Cited: 64

Leucine Rich Repeat Kinase 2 and Innate Immunity
Diba Ahmadi Rastegar, Nicolas Dzamko
Frontiers in Neuroscience (2020) Vol. 14
Open Access | Times Cited: 55

Protective LRRK2 R1398H Variant Enhances GTPase and Wnt Signaling Activity
Jonathon Nixon‐Abell, Daniel C. Berwick, Simone Grannò, et al.
Frontiers in Molecular Neuroscience (2016) Vol. 9
Open Access | Times Cited: 59

Understanding the GTPase Activity of LRRK2: Regulation, Function, and Neurotoxicity
An Phu Tran Nguyen, Darren J. Moore
Advances in neurobiology (2017), pp. 71-88
Open Access | Times Cited: 56

Leucine-Rich Repeat Kinase 2 (LRRK2) phosphorylates p53 and induces p21WAF1/CIP1 expression
Dong Hwan Ho, Hye Jung Kim, Jisun Kim, et al.
Molecular Brain (2015) Vol. 8, Iss. 1
Open Access | Times Cited: 55

LRRK2 inhibitors and their potential in the treatment of Parkinson’s disease: current perspectives
Farzaneh Atashrazm, Nicolas Dzamko
Clinical Pharmacology Advances and Applications (2016) Vol. Volume 8, pp. 177-189
Open Access | Times Cited: 53

LRRK2 and the Immune System
Nicolas Dzamko
Advances in neurobiology (2017), pp. 123-143
Closed Access | Times Cited: 49

Neuroprotective Effect of the LRRK2 Kinase Inhibitor PF-06447475 in Human Nerve-Like Differentiated Cells Exposed to Oxidative Stress Stimuli: Implications for Parkinson’s Disease
Miguel Mendivil‐Perez, Carlos Velez‐Pardo, Marlene Jiménez-Del-Río
Neurochemical Research (2016) Vol. 41, Iss. 10, pp. 2675-2692
Closed Access | Times Cited: 47

Design of Leucine-Rich Repeat Kinase 2 (LRRK2) Inhibitors Using a Crystallographic Surrogate Derived from Checkpoint Kinase 1 (CHK1)
D.S. Williamson, Garrick P. Smith, P. Acheson-Dossang, et al.
Journal of Medicinal Chemistry (2017) Vol. 60, Iss. 21, pp. 8945-8962
Open Access | Times Cited: 47

Molecular insights of the G2019S substitution in LRRK2 kinase domain associated with Parkinson's disease: A molecular dynamics simulation approach
Ashish Kumar Agrahari, C. George Priya Doss, Siva Ramamoorthy, et al.
Journal of Theoretical Biology (2019) Vol. 469, pp. 163-171
Closed Access | Times Cited: 38

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

Systematic review of genetic variants associated with cognitive impairment and depressive symptoms in Parkinson’s disease
Tyrra D’Souza, Anto P. Rajkumar
Acta Neuropsychiatrica (2019) Vol. 32, Iss. 1, pp. 10-22
Open Access | Times Cited: 36

Sequential screening nominates the Parkinson's disease associated kinase LRRK2 as a regulator of Clathrin-mediated endocytosis
George R. Heaton, Natalie Landeck, Adamantios Mamais, et al.
Neurobiology of Disease (2020) Vol. 141, pp. 104948-104948
Open Access | Times Cited: 34

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

Page 1 - Next Page

Scroll to top