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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:

Structural and Functional Insights into α-Synuclein Fibril Polymorphism
Surabhi Mehra, Laxmikant Gadhe, Riya Bera, et al.
Biomolecules (2021) Vol. 11, Iss. 10, pp. 1419-1419
Open Access | Times Cited: 66

Showing 1-25 of 66 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: 23
Propagation of tau and α-synuclein in the brain: therapeutic potential of the glymphatic system
Douglas M. Lopes, Sophie K. Llewellyn, Ian F. Harrison
Translational Neurodegeneration (2022) Vol. 11, Iss. 1
Open Access | Times Cited: 43
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
Thermodynamic characterization of amyloid polymorphism by microfluidic transient incomplete separation
Azad Farzadfard, Antonín Kunka, Thomas O. Mason, et al.
Chemical Science (2024) Vol. 15, Iss. 7, pp. 2528-2544
Open Access | Times Cited: 10
Positron emission tomography tracers for synucleinopathies
Jie Xiang, Zhentao Zhang, Shengxi Wu, et al.
Molecular Neurodegeneration (2025) Vol. 20, Iss. 1
Open Access | Times Cited: 1
Cryo-EM structure of amyloid fibril formed by α-synuclein hereditary A53E mutation reveals a distinct protofilament interface
Chuanqi Sun, Kang Zhou, Peter DePaola, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 4, pp. 104566-104566
Open Access | Times Cited: 17
Liquid–liquid phase separation of α‐synuclein is highly sensitive to sequence complexity
Anindita Mahapatra, Robert W. Newberry
Protein Science (2024) Vol. 33, Iss. 4
Open Access | Times Cited: 7
The impact of hUC MSC–derived exosome-nanoliposome hybrids on α-synuclein fibrillation and neurotoxicity
Farhang Aliakbari, Kimia Marzookian, Soha Parsafar, et al.
Science Advances (2024) Vol. 10, Iss. 14
Open Access | Times Cited: 6
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
The association of lipids with amyloid fibrils
John M. Sanderson
Journal of Biological Chemistry (2022) Vol. 298, Iss. 8, pp. 102108-102108
Open Access | Times Cited: 26
Recent advances in Lewy body dementia: A comprehensive review
Sakshi Prasad, Maanya Rajasree Katta, Shuchi Abhishek, et al.
Disease-a-Month (2022) Vol. 69, Iss. 5, pp. 101441-101441
Open Access | Times Cited: 26
Resolving the Nanoscale Structure of β-Sheet Peptide Self-Assemblies Using Single-Molecule Orientation–Localization Microscopy
Weiyan Zhou, Conor L. O’Neill, Tianben Ding, et al.
ACS Nano (2024) Vol. 18, Iss. 12, pp. 8798-8810
Closed Access | Times Cited: 5
Microstructural Organization in α-Synuclein Solutions
Shibananda Das, M. Muthukumar
Macromolecules (2022) Vol. 55, Iss. 11, pp. 4228-4236
Closed Access | Times Cited: 21
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
Anionic lipid catalyzes the generation of cytotoxic insulin oligomers
Jhinuk Saha, Audrey Wolszczak, Navneet Kaur, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access
Factors responsible for alpha-Synuclein aggregation
Khuraijam Surjalal Singh, Rahul Verma, N. Okendro Singh, et al.
Progress in molecular biology and translational science (2025)
Closed Access
Rationally designed peptides inhibit the formation of α-synuclein fibrils and oligomers
Tariq Tammam Ali, Madiha Mohieldin Merghani, Mohammed Al-Azzani, et al.
European Journal of Medicinal Chemistry (2025) Vol. 289, pp. 117452-117452
Open Access
Unveiling the Assembly Transition of Diphenylalanine and Its Analogs: from Oligomer Equilibrium to Nanocluster Formation
Chang Liu, Yoav Dan, Ji Sun Yun, et al.
ACS Nano (2025)
Closed Access
Multivalent interaction induces phase separation and formation of more toxic aggregates of α-syn in a yeast model of Parkinson’s disease
Rajeev Jain, S. K. Sharavanakkumar, Krishnananda Chattopadhyay
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access
Transition of amyloid/mutant p53 from tumor suppressor to an oncogene and therapeutic approaches to ameliorate metastasis and cancer stemness
Shinjinee Sengupta, Shaikh Maryam Ghufran, Aqsa Khan, et al.
Cancer Cell International (2022) Vol. 22, Iss. 1
Open Access | Times Cited: 16
Resistance exercise stress: theoretical mechanisms for growth hormone processing and release from the anterior pituitary somatotroph
Wesley C. Hymer, William J. Kraemer
European Journal of Applied Physiology (2023) Vol. 123, Iss. 9, pp. 1867-1878
Closed Access | Times Cited: 9
Alpha-synuclein in skin as a high-quality biomarker for Parkinson's disease
Haoran Peng, Siyuan Chen, Shaopu Wu, et al.
Journal of the Neurological Sciences (2023) Vol. 451, pp. 120730-120730
Open Access | Times Cited: 9
Structural Variations of Prions and Prion-like Proteins Associated with Neurodegeneration
Carter Sky Christensen, Sean K. Wang, Wenshu Li, et al.
Current Issues in Molecular Biology (2024) Vol. 46, Iss. 7, pp. 6423-6439
Open Access | Times Cited: 3
Rapid on-site amplification and visual detection of misfolded proteins via microfluidic quaking-induced conversion (Micro-QuIC)
Dong Jun Lee, Peter R. Christenson, Gage R. Rowden, et al.
Deleted Journal (2024) Vol. 1, Iss. 1
Open Access | Times Cited: 3
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