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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:

Alpha-synuclein at the intracellular and the extracellular side: functional and dysfunctional implications
Denis Ottolini, Tito Calì, Ildikò Szabó, et al.
Biological Chemistry (2016) Vol. 398, Iss. 1, pp. 77-100
Closed Access | Times Cited: 61

Showing 1-25 of 61 citing articles:

Neurodegenerative Diseases: Regenerative Mechanisms and Novel Therapeutic Approaches
Rashad Hussain, Hira Zubair, Sarah Pursell, et al.
Brain Sciences (2018) Vol. 8, Iss. 9, pp. 177-177
Open Access | Times Cited: 190
Small-molecule PET Tracers for Imaging Proteinopathies
Chester A. Mathis, Brian J. Lopresti, Miloš D. Ikonomović, et al.
Seminars in Nuclear Medicine (2017) Vol. 47, Iss. 5, pp. 553-575
Open Access | Times Cited: 106
Mitochondrial Dysfunction in Neural Injury
Xiu‐Yun Zhao, Mei‐Hong Lu, De‐Juan Yuan, et al.
Frontiers in Neuroscience (2019) Vol. 13
Open Access | Times Cited: 100
Are We Ready for Detecting α-Synuclein Prone to Aggregation in Patients? The Case of “Protein-Misfolding Cyclic Amplification” and “Real-Time Quaking-Induced Conversion” as Diagnostic Tools
Silvia Paciotti, G. Bellomo, Leonardo Gatticchi, et al.
Frontiers in Neurology (2018) Vol. 9
Open Access | Times Cited: 75
Can Interactions Between α-Synuclein, Dopamine and Calcium Explain Selective Neurodegeneration in Parkinson's Disease?
Michael R. Post, Ori J. Lieberman, Eugene V. Mosharov
Frontiers in Neuroscience (2018) Vol. 12
Open Access | Times Cited: 70
Activation of Atg7-dependent autophagy by a novel inhibitor of the Keap1–Nrf2 protein–protein interaction from Penthorum chinense Pursh. attenuates 6-hydroxydopamine-induced ferroptosis in zebrafish and dopaminergic neurons
Yiran Sun, Libo He, Wang Wang, et al.
Food & Function (2022) Vol. 13, Iss. 14, pp. 7885-7900
Closed Access | Times Cited: 35
Looking at the recent advances in understanding α-synuclein and its aggregation through the proteoform prism
Vladimir N. Uversky
F1000Research (2017) Vol. 6, pp. 525-525
Open Access | Times Cited: 52
Mitochondria focused neurotherapeutics for spinal cord injury
Alexander G. Rabchevsky, Felicia M. Michael, Samir P. Patel
Experimental Neurology (2020) Vol. 330, pp. 113332-113332
Open Access | Times Cited: 48
Parkinson's and Lewy body dementia CSF biomarkers
Lucilla Parnetti, Silvia Paciotti, Lucia Farotti, et al.
Clinica Chimica Acta (2019) Vol. 495, pp. 318-325
Closed Access | Times Cited: 47
Impaired Phasic Discharge of Locus Coeruleus Neurons Based on Persistent High Tonic Discharge—A New Hypothesis With Potential Implications for Neurodegenerative Diseases
Kathrin Janitzky
Frontiers in Neurology (2020) Vol. 11
Open Access | Times Cited: 44
Alpha-synuclein is involved in manganese-induced spatial memory and synaptic plasticity impairments via TrkB/Akt/Fyn-mediated phosphorylation of NMDA receptors
Zhuo Ma, Kuan Liu, Xinru Li, et al.
Cell Death and Disease (2020) Vol. 11, Iss. 10
Open Access | Times Cited: 43
The involvement of oxidative stress, neuronal lesions, neurotransmission impairment, and neuroinflammation in acrylamide-induced neurotoxicity in C57/BL6 mice
Mengyao Zhao, Linlin Deng, Xiaoxuan Lu, et al.
Environmental Science and Pollution Research (2022) Vol. 29, Iss. 27, pp. 41151-41167
Closed Access | Times Cited: 24
ER-Mitochondria Calcium Transfer, Organelle Contacts and Neurodegenerative Diseases
Francesca Vallese, Lucia Barazzuol, Lorenzo Maso, et al.
Advances in experimental medicine and biology (2019), pp. 719-746
Closed Access | Times Cited: 39
Self- and Cross-Seeding on α-Synuclein Fibril Growth Kinetics and Structure Observed by High-Speed Atomic Force Microscopy
Takahiro Watanabe‐Nakayama, Maika Nawa, Hiroki Konno, et al.
ACS Nano (2020) Vol. 14, Iss. 8, pp. 9979-9989
Closed Access | Times Cited: 34
Alpha-Synuclein Toxicity on Protein Quality Control, Mitochondria and Endoplasmic Reticulum
Thaiany Quevedo Melo, Sjef J. C. V. M. Copray, M Ferrari
Neurochemical Research (2018) Vol. 43, Iss. 12, pp. 2212-2223
Closed Access | Times Cited: 37
Alternative Splicing of Alpha- and Beta-Synuclein Genes Plays Differential Roles in Synucleinopathies
Ana Gámez‐Valero, Katrin Beyer
Genes (2018) Vol. 9, Iss. 2, pp. 63-63
Open Access | Times Cited: 36
Asiatic Acid Prevents Oxidative Stress and Apoptosis by Inhibiting the Translocation of α-Synuclein Into Mitochondria
Hongqun Ding, Yuyun Xiong, Jing Sun, et al.
Frontiers in Neuroscience (2018) Vol. 12
Open Access | Times Cited: 35
Synergy between plasminogen activator inhibitor-1, α-synuclein, and neuroinflammation in Parkinson’s disease
Carolyn Reuland, Frank Church
Medical Hypotheses (2020) Vol. 138, pp. 109602-109602
Open Access | Times Cited: 30
X1INH, an improved next-generation affinity-optimized hydrazonic ligand, attenuates abnormal copper(i)/copper(ii)-α-Syn interactions and affects protein aggregation in a cellular model of synucleinopathy
Daphne S. Cukierman, Diana F. Lázaro, Pamela Sacco, et al.
Dalton Transactions (2020) Vol. 49, Iss. 45, pp. 16252-16267
Closed Access | Times Cited: 28
Photobiomodulation provides neuroprotection through regulating mitochondrial fission imbalance in the subacute phase of spinal cord injury
Zhe Wang, Xueyu Hu, Xin Li, et al.
Neural Regeneration Research (2023)
Open Access | Times Cited: 10
Glycation of α-synuclein amplifies the binding with glyceraldehyde-3-phosphate dehydrogenase
Pavel I. Semenyuk, Kseniya Barinova, Vladimir I. Muronetz
International Journal of Biological Macromolecules (2019) Vol. 127, pp. 278-285
Closed Access | Times Cited: 26
Quantitative Binding Behavior of Intrinsically Disordered Proteins to Nanoparticle Surfaces at Individual Residue Level
Mouzhe Xie, Dawei Li, Jiaqi Yuan, et al.
Chemistry - A European Journal (2018) Vol. 24, Iss. 64, pp. 16997-17001
Closed Access | Times Cited: 27
Dimerization of Tyr136Cys alpha-synuclein prevents amyloid transformation of wild type alpha-synuclein
K.V. Barinova, Mikhail Kuravsky, Alexander M. Arutyunyan, et al.
International Journal of Biological Macromolecules (2016) Vol. 96, pp. 35-43
Closed Access | Times Cited: 24
Navigating the dynamic landscape of alpha-synuclein morphology: a review of the physiologically relevant tetrameric conformation
Heather R. Lucas, Ricardo D. Fernández
Neural Regeneration Research (2019) Vol. 15, Iss. 3, pp. 407-407
Open Access | Times Cited: 24
Cellular Prion Protein Mediates α‐Synuclein Uptake, Localization, and Toxicity In Vitro and In Vivo
Tobias Thom, Matthias Schmitz, Anna‐Lisa Fischer, et al.
Movement Disorders (2021) Vol. 37, Iss. 1, pp. 39-51
Open Access | Times Cited: 18
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