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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:

Screening of small molecules using the inhibition of oligomer formation in α-synuclein aggregation as a selection parameter
Roxine Staats, Thomas C. T. Michaels, Patrick Flagmeier, et al.
Communications Chemistry (2020) Vol. 3, Iss. 1
Open Access | Times Cited: 36

Showing 1-25 of 36 citing articles:

Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases
Dillon J. Rinauro, Fabrizio Chiti, Michele Vendruscolo, et al.
Molecular Neurodegeneration (2024) Vol. 19, Iss. 1
Open Access | Times Cited: 43
Alpha-Synuclein Targeting Therapeutics for Parkinson's Disease and Related Synucleinopathies
Sindhu Menon, Sabrina E.M. Armstrong, Amir Mohammad Hamzeh, et al.
Frontiers in Neurology (2022) Vol. 13
Open Access | Times Cited: 47
Sequence-based prediction of pH-dependent protein solubility using CamSol
Marc Oeller, Ryan Kang, Rosie Bell, et al.
Briefings in Bioinformatics (2023) Vol. 24, Iss. 2
Open Access | Times Cited: 30
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
Discovery of potent inhibitors of α-synuclein aggregation using structure-based iterative learning
Robert I. Horne, Ewa A. Andrzejewska, Parvez Alam, et al.
Nature Chemical Biology (2024) Vol. 20, Iss. 5, pp. 634-645
Open Access | Times Cited: 14
Pharmacological inhibition of α-synuclein aggregation within liquid condensates
Samuel Dada, Zenon Toprakcioglu, Mariana P. Cali, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 11
Using Generative Modeling to Endow with Potency Initially Inert Compounds with Good Bioavailability and Low Toxicity
Robert I. Horne, Jared Wilson-Godber, Alicia González Díaz, et al.
Journal of Chemical Information and Modeling (2024) Vol. 64, Iss. 3, pp. 590-596
Open Access | Times Cited: 9
N-Terminal Acetylation of α-Synuclein Slows down Its Aggregation Process and Alters the Morphology of the Resulting Aggregates
Rosie Bell, Rebecca J. Thrush, Marta Castellana-Cruz, et al.
Biochemistry (2022) Vol. 61, Iss. 17, pp. 1743-1756
Open Access | Times Cited: 32
Modulation of the Interactions Between α-Synuclein and Lipid Membranes by Post-translational Modifications
Rosie Bell, Michele Vendruscolo
Frontiers in Neurology (2021) Vol. 12
Open Access | Times Cited: 34
Molecular Mechanisms of Inhibition of Protein Amyloid Fibril Formation: Evidence and Perspectives Based on Kinetic Models
Igor A. Sedov, Diliara Khaibrakhmanova
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 21, pp. 13428-13428
Open Access | Times Cited: 27
Structure-Based Discovery of Small-Molecule Inhibitors of the Autocatalytic Proliferation of α-Synuclein Aggregates
Sean Chia, Z. Faidon Brotzakis, Robert I. Horne, et al.
Molecular Pharmaceutics (2022) Vol. 20, Iss. 1, pp. 183-193
Open Access | Times Cited: 25
Effects of N-terminal Acetylation on the Aggregation of Disease-related α-synuclein Variants
Rosie Bell, Marta Castellana-Cruz, Aishwarya Nene, et al.
Journal of Molecular Biology (2022) Vol. 435, Iss. 1, pp. 167825-167825
Open Access | Times Cited: 24
Exploration and Exploitation Approaches Based on Generative Machine Learning to Identify Potent Small Molecule Inhibitors of α-Synuclein Secondary Nucleation
Robert I. Horne, Mhd Hussein Murtada, Donghui Huo, et al.
Journal of Chemical Theory and Computation (2023) Vol. 19, Iss. 14, pp. 4701-4710
Open Access | Times Cited: 14
Detection of protein oligomers with nanopores
Robert I. Horne, Sarah E. Sandler, Michele Vendruscolo, et al.
Nature Reviews Chemistry (2025)
Closed Access
S100B chaperone multimers suppress the formation of oligomers during Aβ42 aggregation
António J. Figueira, Joana Saavedra, Isabel Cardoso, et al.
Frontiers in Neuroscience (2023) Vol. 17
Open Access | Times Cited: 8
Multiplexed Digital Characterization of Misfolded Protein Oligomers via Solid-State Nanopores
Sarah E. Sandler, Robert I. Horne, Sara Rocchetti, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 47, pp. 25776-25788
Open Access | Times Cited: 8
An antibody scanning method for the detection of α-synuclein oligomers in the serum of Parkinson's disease patients
Klara Kulenkampff, Derya Emin, Roxine Staats, et al.
Chemical Science (2022) Vol. 13, Iss. 46, pp. 13815-13828
Open Access | Times Cited: 11
Single-molecule digital sizing of proteins in solution
Georg Krainer, Raphaël P. B. Jacquat, Matthias M. Schneider, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 2
Spontaneous nucleation and fast aggregate-dependent proliferation of α-synuclein aggregates within liquid condensates at physiological pH
Samuel Dada, Maarten C. Hardenberg, Lena K. Mrugalla, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 13
Thermodynamic and kinetic approaches for drug discovery to target protein misfolding and aggregation
Michele Vendruscolo
Expert Opinion on Drug Discovery (2023) Vol. 18, Iss. 8, pp. 881-891
Open Access | Times Cited: 5
Optimization of a small molecule inhibitor of secondary nucleation in α-synuclein aggregation
Roxine Staats, Z. Faidon Brotzakis, Sean Chia, et al.
Frontiers in Molecular Biosciences (2023) Vol. 10
Open Access | Times Cited: 4
Inhibition of cytotoxic self-assembly of HEWL through promoting fibrillation by new synthesized α-hydroxycarbamoylphosphinic acids
Mohsen Mahdavimehr, Babak Kaboudin, Saied Alaie, et al.
RSC Advances (2024) Vol. 14, Iss. 42, pp. 31227-31242
Open Access | Times Cited: 1
Liquid–liquid phase separation and conformational strains of α-Synuclein: implications for Parkinson’s disease pathogenesis
Eva D. Ruiz-Ortega, Anna Wilkaniec, Agata Adamczyk
Frontiers in Molecular Neuroscience (2024) Vol. 17
Open Access | Times Cited: 1
Discovery of Potent Inhibitors of α-Synuclein Aggregation Using Structure-Based Iterative Learning
Robert I. Horne, Ewa Andrzejewska, Parvez Alam, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 8
Controlling amyloid formation of intrinsically disordered proteins and peptides: slowing down or speeding up?
Yong Xu, Roberto Maya‐Martinez, Sheena E. Radford
Essays in Biochemistry (2022) Vol. 66, Iss. 7, pp. 959-975
Open Access | Times Cited: 5
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