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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:

Back to the tubule: microtubule dynamics in Parkinson’s disease
Laura Pellegrini, Andrea Wetzel, Simone Grannò, et al.
Cellular and Molecular Life Sciences (2016) Vol. 74, Iss. 3, pp. 409-434
Open Access | Times Cited: 123

Showing 1-25 of 123 citing articles:

The Unfolded Protein Response: Detecting and Responding to Fluctuations in the Protein-Folding Capacity of the Endoplasmic Reticulum
G Elif Karagöz, Diego Acosta‐Alvear, Peter Walter
Cold Spring Harbor Perspectives in Biology (2019) Vol. 11, Iss. 9, pp. a033886-a033886
Open Access | Times Cited: 264
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
Excessive tubulin polyglutamylation causes neurodegeneration and perturbs neuronal transport
Maria M. Magiera, Satish Bodakuntla, Jakub Žiak, et al.
The EMBO Journal (2018) Vol. 37, Iss. 23
Open Access | Times Cited: 135
Molecular understanding of label-free second harmonic imaging of microtubules
Valérie Van Steenbergen, Werend Boesmans, Z. Li, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 119
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 maintains mitochondrial homeostasis and regulates innate immune responses to Mycobacterium tuberculosis
Chi G. Weindel, Samantha L. Bell, Krystal J. Vail, et al.
eLife (2020) Vol. 9
Open Access | Times Cited: 101
Parkinson disease-associated mutations in LRRK2 cause centrosomal defects via Rab8a phosphorylation
Jesús Madero‐Pérez, Elena Fdez, Belén Fernández, et al.
Molecular Neurodegeneration (2018) Vol. 13, Iss. 1
Open Access | Times Cited: 100
Microtubule Dysfunction: A Common Feature of Neurodegenerative Diseases
Antonella Sferra, Francesco Nicita, Enrico Bertini
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 19, pp. 7354-7354
Open Access | Times Cited: 98
Metallothionein-3 as a multifunctional player in the control of cellular processes and diseases
Jae‐Young Koh, Sook-Jeong Lee
Molecular Brain (2020) Vol. 13, Iss. 1
Open Access | Times Cited: 82
Oxidative stress and synaptic dysfunction in rodent models of Parkinson's disease
Paola Imbriani, Giuseppina Martella, Paola Bonsi, et al.
Neurobiology of Disease (2022) Vol. 173, pp. 105851-105851
Open Access | Times Cited: 39
Large-scale rare variant burden testing in Parkinson's disease
Mary B. Makarious, Julie Lake, Vanessa Pitz, et al.
Brain (2023) Vol. 146, Iss. 11, pp. 4622-4632
Open Access | Times Cited: 31
Microtubule acetylation dyshomeostasis in Parkinson’s disease
Padmashri Naren, Khan Sabiya Samim, Kamatham Pushpa Tryphena, et al.
Translational Neurodegeneration (2023) Vol. 12, Iss. 1
Open Access | Times Cited: 29
Linking acetylated α-Tubulin redistribution to α-Synuclein pathology in brain of Parkinson’s disease patients
Samanta Mazzetti, Federica Giampietro, Alessandra Maria Calogero, et al.
npj Parkinson s Disease (2024) Vol. 10, Iss. 1
Open Access | Times Cited: 11
Sirtuin dysregulation in Parkinson's disease: Implications of acetylation and deacetylation processes
Sonia Dhiman, Ashi Mannan, Ayushi Taneja, et al.
Life Sciences (2024) Vol. 342, pp. 122537-122537
Closed Access | Times Cited: 8
Microtubules: Evolving roles and critical cellular interactions
Caitlin M. Logan, A. Sue Menko
Experimental Biology and Medicine (2019) Vol. 244, Iss. 15, pp. 1240-1254
Open Access | Times Cited: 70
In vitro Characterization of Gut Microbiota-Derived Bacterial Strains With Neuroprotective Properties
Suaad Ahmed, Alessandro Busetti, Parthena Fotiadou, et al.
Frontiers in Cellular Neuroscience (2019) Vol. 13
Open Access | Times Cited: 70
Emerging Role of Sirtuin 2 in Parkinson’s Disease
Yumei Liu, Yingying Zhang, Konghua Zhu, et al.
Frontiers in Aging Neuroscience (2020) Vol. 11
Open Access | Times Cited: 63
Parkinson's Disease Skin Fibroblasts Display Signature Alterations in Growth, Redox Homeostasis, Mitochondrial Function, and Autophagy
Joji Marie Teves, Vedanshi Bhargava, Konner R. Kirwan, et al.
Frontiers in Neuroscience (2018) Vol. 11
Open Access | Times Cited: 62
Differentially Expressed Circular RNAs in Peripheral Blood Mononuclear Cells of Patients with Parkinson's Disease
Stylianos Ravanidis, Anastasia Bougea, Dimitra Karampatsi, et al.
Movement Disorders (2021) Vol. 36, Iss. 5, pp. 1170-1179
Open Access | Times Cited: 55
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
The detyrosination/re-tyrosination cycle of tubulin and its role and dysfunction in neurons and cardiomyocytes
Chadni Sanyal, Niels Pietsch, Sacnicte Ramírez Ríos, et al.
Seminars in Cell and Developmental Biology (2021) Vol. 137, pp. 46-62
Open Access | Times Cited: 41
Computational Approaches to the Rational Design of Tubulin-Targeting Agents
Helena Pérez‐Peña, Anne‐Catherine Abel, M. D. Shevelev, et al.
Biomolecules (2023) Vol. 13, Iss. 2, pp. 285-285
Open Access | Times Cited: 14
The role of LRRK2 in cell signalling
Kirsten Harvey, Tiago F. Outeiro
Biochemical Society Transactions (2018) Vol. 47, Iss. 1, pp. 197-207
Open Access | Times Cited: 45
Reversible and Irreversible Modulation of Tubulin Self‐Assembly by Intense Nanosecond Pulsed Electric Fields
Djamel Eddine Chafai, Vadym Sulimenko, Daniel Havelka, et al.
Advanced Materials (2019) Vol. 31, Iss. 39
Open Access | Times Cited: 38
Prionoid Proteins in the Pathogenesis of Neurodegenerative Diseases
Cameron I. Wells, Samuel Brennan, Matt Keon, et al.
Frontiers in Molecular Neuroscience (2019) Vol. 12
Open Access | Times Cited: 36
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