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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:

Chaperone-Based Therapies for Disease Modification in Parkinson’s Disease
Erik Loewen Friesen, Mitchell L. De Snoo, Luckshi Rajendran, et al.
Parkinson s Disease (2017) Vol. 2017, pp. 1-11
Open Access | Times Cited: 42

Showing 1-25 of 42 citing articles:

Current understanding of the molecular mechanisms in Parkinson's disease: Targets for potential treatments
Panchanan Maiti, Jayeeta Manna, Gary Dunbar
Translational Neurodegeneration (2017) Vol. 6, Iss. 1
Open Access | Times Cited: 449
Plant Extracts and Phytochemicals Targeting α-Synuclein Aggregation in Parkinson's Disease Models
Hayate Javed, Mohamed Fizur Nagoor Meeran, Sheikh Azimullah, et al.
Frontiers in Pharmacology (2019) Vol. 9
Open Access | Times Cited: 101
LRRK2 and α-Synuclein: Distinct or Synergistic Players in Parkinson’s Disease?
Darren M. O’Hara, Grishma Pawar, Suneil K. Kalia, et al.
Frontiers in Neuroscience (2020) Vol. 14
Open Access | Times Cited: 62
Broken but not beaten: Challenge of reducing the amyloids pathogenicity by degradation
Maksim I. Sulatsky, Olga V. Stepanenko, Olesya V. Stepanenko, et al.
Journal of Advanced Research (2024)
Open Access | Times Cited: 7
The making of a Lewy body: the role of alpha-synuclein post-fibrillization modifications in regulating the formation and the maturation of pathological inclusions.
Anne‐Laure Mahul‐Mellier, Melek Firat Altay, Johannes Burtscher, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2018)
Open Access | Times Cited: 48
Bcl-2-associated athanogene 5 (BAG5) regulates Parkin-dependent mitophagy and cell death
Mitchell L. De Snoo, Erik Loewen Friesen, Yu Tong Zhang, et al.
Cell Death and Disease (2019) Vol. 10, Iss. 12
Open Access | Times Cited: 42
Chaperone-Mediated Autophagy and Its Implications for Neurodegeneration and Cancer
Masresha Ahmed Assaye, Solomon Tebeje Gizaw
International Journal of General Medicine (2022) Vol. Volume 15, pp. 5635-5649
Open Access | Times Cited: 19
The disturbance of protein synthesis/degradation homeostasis is a common trait of age-related neurodegenerative disorders
Fabio Di Domenico, Chiara Lanzillotta
Advances in protein chemistry and structural biology (2022), pp. 49-87
Closed Access | Times Cited: 19
Neuroprotective effects of increasing levels of HSP70 against neuroinflammation in Parkinson's disease model by inhibition of NF-κB and STAT3
Haining Li, Juan Yang, Yanbai Wang, et al.
Life Sciences (2019) Vol. 234, pp. 116747-116747
Closed Access | Times Cited: 35
UBA52 Is Crucial in HSP90 Ubiquitylation and Neurodegenerative Signaling during Early Phase of Parkinson’s Disease
Shubhangini Tiwari, Abhishek Singh, Parul Gupta, et al.
Cells (2022) Vol. 11, Iss. 23, pp. 3770-3770
Open Access | Times Cited: 14
On the nature of the optimal form of the holdase‐type chaperone stress response
Damien Hall
FEBS Letters (2019) Vol. 594, Iss. 1, pp. 43-66
Open Access | Times Cited: 23
J-domain proteins interaction with neurodegenerative disease-related proteins
Sara María Ayala Mariscal, Janine Kirstein
Experimental Cell Research (2021) Vol. 399, Iss. 2, pp. 112491-112491
Closed Access | Times Cited: 19
Chaperone Proteins and Chaperonopathies
Alberto J.L. Macario, Everly Conway de Macario
Elsevier eBooks (2019), pp. 135-152
Closed Access | Times Cited: 21
Proteinopathies: Deciphering Physiology and Mechanisms to Develop Effective Therapies for Neurodegenerative Diseases
Gouri Chopra, Shabnam Shabir, Sumaira Yousuf, et al.
Molecular Neurobiology (2022) Vol. 59, Iss. 12, pp. 7513-7540
Closed Access | Times Cited: 11
Chaperones and Proteostasis: Role in Parkinson’s Disease
Neha Joshi, Atchaya Raveendran, Shirisha Nagotu
Diseases (2020) Vol. 8, Iss. 2, pp. 24-24
Open Access | Times Cited: 16
Alpha-B-Crystallin Effect on Mature Amyloid Fibrils: Different Degradation Mechanisms and Changes in Cytotoxicity
Olga V. Stepanenko, Maksim I. Sulatsky, Е. В. Михайлова, et al.
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 20, pp. 7659-7659
Open Access | Times Cited: 16
Internalization of α-synuclein oligomers into SH-SY5Y cells
Lindsay J. Shearer, Nils O. Petersen, Michael T. Woodside
Biophysical Journal (2021) Vol. 120, Iss. 5, pp. 877-885
Open Access | Times Cited: 15
Potential application of heat shock proteins as therapeutic targets in Parkinson's disease
Haodong Guo, Jingsong Yi, Fan Wang, et al.
Neurochemistry International (2022) Vol. 162, pp. 105453-105453
Closed Access | Times Cited: 10
Societal Burden and Persisting Unmet Needs of Parkinson’s Disease
К. Ray Chaudhuri, Nataliya Titova
European Neurological Review (2019) Vol. 14, Iss. 1, pp. 28-28
Open Access | Times Cited: 17
Proteostasis and Mitochondrial Role on Psychiatric and Neurodegenerative Disorders: Current Perspectives
Pablo Olivero, Carlo Lozano, Ramón Sotomayor‐Zárate, et al.
Neural Plasticity (2018) Vol. 2018, pp. 1-10
Open Access | Times Cited: 16
Neurodegenerative Proteinopathies Induced by Environmental Pollutants: Heat Shock Proteins and Proteasome as Promising Therapeutic Tools
Paula Moyano, Emma Sola, María Victoria Naval, et al.
Pharmaceutics (2023) Vol. 15, Iss. 8, pp. 2048-2048
Open Access | Times Cited: 4
Degradation of pathogenic amyloids induced by matrix metalloproteinase-9
Olga V. Stepanenko, Maksim I. Sulatsky, Е. В. Михайлова, et al.
International Journal of Biological Macromolecules (2024) Vol. 281, pp. 136362-136362
Closed Access | Times Cited: 1
Identification of inhibitors of the E. coli chaperone SurA using in silico and in vitro techniques
Eric W. Bell, Erica J. Zheng, Lisa M. Ryno
Bioorganic & Medicinal Chemistry Letters (2018) Vol. 28, Iss. 22, pp. 3540-3548
Closed Access | Times Cited: 12
The proSAAS Chaperone Provides Neuroprotection and Attenuates Transsynaptic α-Synuclein Spread in Rodent Models of Parkinson’s Disease
Iris Lindberg, Zhan Shu, Hoa A. Lam, et al.
Journal of Parkinson s Disease (2022) Vol. 12, Iss. 5, pp. 1463-1478
Open Access | Times Cited: 7
Lanostane Triterpenoid Metabolites from a Penares sp. Marine Sponge Protect Neuro-2a Cells against Paraquat Neurotoxicity
Ekaterina A. Yurchenko, Sophia A. Kolesnikova, Ekaterina G. Lyakhova, et al.
Molecules (2020) Vol. 25, Iss. 22, pp. 5397-5397
Open Access | Times Cited: 9
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