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:

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

Showing 1-25 of 94 citing articles:

Inflammation and immune dysfunction in Parkinson disease
Malú G. Tansey, Rebecca L. Wallings, Madelyn C. Houser, et al.
Nature reviews. Immunology (2022) Vol. 22, Iss. 11, pp. 657-673
Open Access | Times Cited: 781

LRRK2 activation in idiopathic Parkinson’s disease
Roberto Di Maio, Eric K. Hoffman, Emily M. Rocha, et al.
Science Translational Medicine (2018) Vol. 10, Iss. 451
Open Access | Times Cited: 528

Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation establishes a connection to ciliogenesis
Martin Steger, Federico Diez, Herschel S. Dhekne, et al.
eLife (2017) Vol. 6
Open Access | Times Cited: 442

LRRK2 phosphorylates membrane-bound Rabs and is activated by GTP-bound Rab7L1 to promote recruitment to the trans-Golgi network
Zhiyong Liu, Nicole Bryant, Ravindran Kumaran, et al.
Human Molecular Genetics (2017) Vol. 27, Iss. 2, pp. 385-395
Open Access | Times Cited: 252

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

Development of phospho-specific Rab protein antibodies to monitor in vivo activity of the LRRK2 Parkinson's disease kinase
Paweł Lis, Sophie Burel, Martin Steger, et al.
Biochemical Journal (2017) Vol. 475, Iss. 1, pp. 1-22
Open Access | Times Cited: 143

LRRK2 regulation of immune-pathways and inflammatory disease
Rebecca L. Wallings, Malú G. Tansey
Biochemical Society Transactions (2019) Vol. 47, Iss. 6, pp. 1581-1595
Open Access | Times Cited: 125

LRRK2‐mediated Rab10 phosphorylation in immune cells from Parkinson's disease patients
Farzaneh Atashrazm, Deborah Hammond, Gayathri Perera, et al.
Movement Disorders (2018) Vol. 34, Iss. 3, pp. 406-415
Closed 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

Mutations in LRRK2 linked to Parkinson disease sequester Rab8a to damaged lysosomes and regulate transferrin-mediated iron uptake in microglia
Adamantios Mamais, Jillian H. Kluss, Luis Bonet‐Ponce, et al.
PLoS Biology (2021) Vol. 19, Iss. 12, pp. e3001480-e3001480
Open Access | Times Cited: 64

LRRK2 phosphorylation of Rab GTPases in Parkinson's disease
Suzanne R. Pfeffer
FEBS Letters (2022) Vol. 597, Iss. 6, pp. 811-818
Open Access | Times Cited: 42

Blocking IL-6 signaling prevents astrocyte-induced neurodegeneration in an iPSC-based model of Parkinson’s disease
Meritxell Pons‐Espinal, Lucas Blasco-Agell, Irene Fernández‐Carasa, et al.
JCI Insight (2024) Vol. 9, Iss. 3
Open Access | Times Cited: 11

Detection of endogenous S1292 LRRK2 autophosphorylation in mouse tissue as a readout for kinase activity
Jillian H. Kluss, Melissa M. Conti, Alice Kaganovich, et al.
npj Parkinson s Disease (2018) Vol. 4, Iss. 1
Open Access | Times Cited: 66

LRRK2 at the Interface Between Peripheral and Central Immune Function in Parkinson’s
Rebecca L. Wallings, Mary K. Herrick, Malú G. Tansey
Frontiers in Neuroscience (2020) Vol. 14
Open Access | Times Cited: 66

The Parkinson’s Disease Protein LRRK2 Interacts with the GARP Complex to Promote Retrograde Transport to the trans-Golgi Network
Alexandra Beilina, Luis Bonet‐Ponce, Ravindran Kumaran, et al.
Cell Reports (2020) Vol. 31, Iss. 5, pp. 107614-107614
Open Access | Times Cited: 62

Accurate MS-based Rab10 Phosphorylation Stoichiometry Determination as Readout for LRRK2 Activity in Parkinson's Disease
Özge Karayel, Francesca Tonelli, Sebastian Virreira Winter, et al.
Molecular & Cellular Proteomics (2020) Vol. 19, Iss. 9, pp. 1546-1560
Open Access | Times Cited: 57

The Emerging Functions of LRRK2 and Rab GTPases in the Endolysosomal System
Tomoki Kuwahara, Takeshi Iwatsubo
Frontiers in Neuroscience (2020) Vol. 14
Open Access | Times Cited: 56

Antibody validation for Western blot: By the user, for the user
Lakshmi Pillai‐Kastoori, Sam Heaton, Steve Shiflett, et al.
Journal of Biological Chemistry (2019) Vol. 295, Iss. 4, pp. 926-939
Open Access | Times Cited: 55

Parkinson's disease and mitophagy: an emerging role for LRRK2
François Singh, Ian G. Ganley
Biochemical Society Transactions (2021) Vol. 49, Iss. 2, pp. 551-562
Open Access | Times Cited: 53

Understanding LRRK2 kinase activity in preclinical models and human subjects through quantitative analysis of LRRK2 and pT73 Rab10
Xiang Wang, Elvira Negrou, Michael T. Maloney, et al.
Scientific Reports (2021) Vol. 11, Iss. 1
Open Access | Times Cited: 47

P62/SQSTM1 is a novel leucine-rich repeat kinase 2 (LRRK2) substrate that enhances neuronal toxicity
Alexia F. Kalogeropulou, Jing Zhao, Marc Bolliger, et al.
Biochemical Journal (2018) Vol. 475, Iss. 7, pp. 1271-1293
Open Access | Times Cited: 50

Recent Developments in LRRK2-Targeted Therapy for Parkinson’s Disease
Ye Zhao, Nicolas Dzamko
Drugs (2019) Vol. 79, Iss. 10, pp. 1037-1051
Closed Access | Times Cited: 50

Divergent Effects of G2019S and R1441C LRRK2 Mutations on LRRK2 and Rab10 Phosphorylations in Mouse Tissues
Lucia Iannotta, Alice Biosa, Jillian H. Kluss, et al.
Cells (2020) Vol. 9, Iss. 11, pp. 2344-2344
Open Access | Times Cited: 45

Antibody validation for Western blot: By the user, for the user
Lakshmi Pillai‐Kastoori, Sam Heaton, Steve Shiflett, et al.
Journal of Biological Chemistry (2020) Vol. 295, Iss. 4, pp. 926-939
Open Access | Times Cited: 42

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