Open Access Helper

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:

Intermediates of α-synuclein aggregation: Implications in Parkinson's disease pathogenesis
Laxmikant Gadhe, Arunima Sakunthala, Semanti Mukherjee, et al.
Biophysical Chemistry (2021) Vol. 281, pp. 106736-106736
Closed Access | Times Cited: 39

Showing 1-25 of 39 citing articles:

Liquid-liquid Phase Separation of α-Synuclein: A New Mechanistic Insight for α-Synuclein Aggregation Associated with Parkinson's Disease Pathogenesis
Semanti Mukherjee, Arunima Sakunthala, Laxmikant Gadhe, et al.
Journal of Molecular Biology (2022) Vol. 435, Iss. 1, pp. 167713-167713
Open Access | Times Cited: 82
Protein misfolding and amyloid nucleation through liquid–liquid phase separation
S. Mukherjee, Manisha Poudyal, K. Dave, et al.
Chemical Society Reviews (2024) Vol. 53, Iss. 10, pp. 4976-5013
Closed Access | Times Cited: 25
Pathology in Parkinson’s Disease
Glenda M. Halliday, Yuhong Fu
Cambridge University Press eBooks (2025), pp. 194-201
Closed Access | Times Cited: 9
Pathogenic Impact of α-Synuclein Phosphorylation and Its Kinases in α-Synucleinopathies
K. Kawahata, David I. Finkelstein, Kohji Fukunaga
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 11, pp. 6216-6216
Open Access | Times Cited: 69
Epigallocatechin-3-gallate: A phytochemical as a promising drug candidate for the treatment of Parkinson’s disease
Yumin Wang, Shuang Wu, Qiang Li, et al.
Frontiers in Pharmacology (2022) Vol. 13
Open Access | Times Cited: 45
Development of Small Molecules Targeting α-Synuclein Aggregation: A Promising Strategy to Treat Parkinson’s Disease
Samuel Peña‐Díaz, Javier García‐Pardo, Salvador Ventura
Pharmaceutics (2023) Vol. 15, Iss. 3, pp. 839-839
Open Access | Times Cited: 27
Multifaceted interactions mediated by intrinsically disordered regions play key roles in alpha synuclein aggregation
Sagar D. Khare, Priscilla Chinchilla, Jean Baum
Current Opinion in Structural Biology (2023) Vol. 80, pp. 102579-102579
Open Access | Times Cited: 23
Probiotics as functional foods: How probiotics can alleviate the symptoms of neurological disabilities
Shadi Aghamohammad, Asal Hafezi, Mahdi Rohani
Biomedicine & Pharmacotherapy (2023) Vol. 163, pp. 114816-114816
Open Access | Times Cited: 20
Aggregation and phase separation of α-synuclein in Parkinson’s disease
W. Han, Mengrui Wei, Fei Xu, et al.
Chemical Communications (2024) Vol. 60, Iss. 52, pp. 6581-6590
Closed Access | Times Cited: 5
Deciphering the Seed Size-Dependent Cellular Internalization Mechanism for α-Synuclein Fibrils
Arunima Sakunthala, Samir K. Maji
Biochemistry (2025) Vol. 64, Iss. 2, pp. 377-400
Closed Access
Slightly viscous oxidized alginate dispersions as vehicles for intranasal administration of the α-synuclein aggregation inhibitor Anle 138b in free form or encapsulated in solid lipid nanoparticles
Rosanna Mallamaci, Stefano Castellani, Limosani Francesca, et al.
International Journal of Pharmaceutics (2025) Vol. 673, pp. 125399-125399
Closed Access
Modulation of α-Synuclein Fibrillation and Toxicity by 4-Phenylbutyric Acid
Kristos Baffour, Neelima Koti, Tony Nyabayo, et al.
ACS Chemical Neuroscience (2025)
Open Access
Factors affecting the physical stability of peptide self-assembly in neurodegenerative disorders
Jahnu Saikia, Mouli Sarkar, Vibin Ramakrishnan
Neuropeptides (2025) Vol. 111, pp. 102517-102517
Closed Access
Modulation of gut microbiota with probiotics as a strategy to counteract endogenous and exogenous neurotoxicity
Anatoly V. Skalny, Michael Aschner, В. А. Гриценко, et al.
Advances in neurotoxicology (2024), pp. 133-176
Open Access | Times Cited: 3
Thioflavin T─a Reporter of Microviscosity in Protein Aggregation Process: The Study Case of α-Synuclein
Konstantin Rusakov, Aadil El-Turabi, Lasse Reimer, et al.
The Journal of Physical Chemistry Letters (2024) Vol. 15, Iss. 25, pp. 6685-6690
Open Access | Times Cited: 3
Insights into the Interactions that Trigger the Primary Nucleation of Polymorphic α-Synuclein Dimers
Sapir Lan-Mark, Yifat Miller
ACS Chemical Neuroscience (2022) Vol. 13, Iss. 3, pp. 370-378
Closed Access | Times Cited: 16
Mitochondria-Directing Fluorogenic Probe: An Efficient Amyloid Marker for Imaging Lipid Metabolite-Induced Protein Aggregation in Live Cells and Caenorhabditis elegans
Shrishti P. Pandey, P. Kavyashree, Tanoy Dutta, et al.
Analytical Chemistry (2023) Vol. 95, Iss. 15, pp. 6341-6350
Closed Access | Times Cited: 9
Liquid-Liquid Phase Separation Promotes Protein Aggregation and Its Implications in Ferroptosis in Parkinson’s Disease Dementia
Mengzhu Li, Yaohua Fan, Qinglian Li, et al.
Oxidative Medicine and Cellular Longevity (2022) Vol. 2022, pp. 1-13
Open Access | Times Cited: 12
Amyloid Protein Cross-Seeding Provides a New Perspective on Multiple Diseases In Vivo
Wan‐Yi Ge, Xudong Deng, Wen‐Pu Shi, et al.
Biomacromolecules (2022) Vol. 24, Iss. 1, pp. 1-18
Closed Access | Times Cited: 12
Affinity of aromatic amino acid side chains in amino acid solvents
Akira Nomoto, Suguru Nishinami, Kentaro Shiraki
Biophysical Chemistry (2022) Vol. 287, pp. 106831-106831
Open Access | Times Cited: 11
Coffee and Parkinson's disease
Abraham Olufemi Asuku, Maryam Tayo Ayinla, Tobiloba Samuel Olajide, et al.
Progress in brain research (2024), pp. 1-19
Closed Access | Times Cited: 2
Parkinson’s Disease: A Tale of Many Players
Ernest K. J. Pauwels, Gerard J. Boer
Medical Principles and Practice (2023) Vol. 32, Iss. 3, pp. 155-165
Open Access | Times Cited: 6
Synuclein Proteins in MPTP-Induced Death of Substantia Nigra Pars Compacta Dopaminergic Neurons
Valeria Goloborshcheva, V. G. Kucheryanu, Н. А. Воронина, et al.
Biomedicines (2022) Vol. 10, Iss. 9, pp. 2278-2278
Open Access | Times Cited: 9
Influence of TiO2 and ZnO Nanoparticles on α-Synuclein and β-Amyloid Aggregation and Formation of Protein Fibrils
Nora Slekiene, Valentinas Snitka, Ingrida Bružaitė, et al.
Materials (2022) Vol. 15, Iss. 21, pp. 7664-7664
Open Access | Times Cited: 9
Liquid-liquid phase separation regulates alpha-synuclein aggregate and mitophagy in Parkinson’s disease
Kaiying Hou, Tingting Liu, Jing Li, et al.
Frontiers in Neuroscience (2023) Vol. 17
Open Access | Times Cited: 5
Page 1 - Next Page

Scroll to top