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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:

Molecular Basis of Small-Molecule Binding to α-Synuclein
Paul Robustelli, Alain Ibanez-de-Opakua, Cecily K. Campbell-Bezat, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 6, pp. 2501-2510
Open Access | Times Cited: 90

Showing 1-25 of 90 citing articles:

Intrinsically disordered proteins and biomolecular condensates as drug targets
Mateusz Biesaga, Marta Frigolé‐Vivas, Xavier Salvatella
Current Opinion in Chemical Biology (2021) Vol. 62, pp. 90-100
Open Access | Times Cited: 83
Enhanced-Sampling Simulations for the Estimation of Ligand Binding Kinetics: Current Status and Perspective
Katya Ahmad, Andrea Rizzi, Riccardo Capelli, et al.
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 52
Small molecules targeting the disordered transactivation domain of the androgen receptor induce the formation of collapsed helical states
Jiaqi Zhu, Xavier Salvatella, Paul Robustelli
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 50
Tuning the rate of aggregation of hIAPP into amyloid using small-molecule modulators of assembly
Yong Xu, Roberto Maya‐Martinez, Nicolas Guthertz, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 46
A Small Molecule Stabilizes the Disordered Native State of the Alzheimer’s Aβ Peptide
Thomas Löhr, Kai Kohlhoff, Gabriella T. Heller, et al.
ACS Chemical Neuroscience (2022) Vol. 13, Iss. 12, pp. 1738-1745
Open Access | Times Cited: 41
Chiral inorganic nanomaterials for bioapplications
Gaoyang Wang, Hongyu Zhang, Hua Kuang, et al.
Matter (2023) Vol. 6, Iss. 6, pp. 1752-1781
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
Differentiable simulation to develop molecular dynamics force fields for disordered proteins
Joe G. Greener
Chemical Science (2024) Vol. 15, Iss. 13, pp. 4897-4909
Open Access | Times Cited: 13
Picosecond Dynamics of a Small Molecule in Its Bound State with an Intrinsically Disordered Protein
Gabriella T. Heller, Vaibhav Kumar Shukla, Angelo Miguel Figueiredo, et al.
Journal of the American Chemical Society (2024) Vol. 146, Iss. 4, pp. 2319-2324
Open Access | Times Cited: 12
Folding-upon-binding pathways of an intrinsically disordered protein from a deep Markov state model
Thomas R. Sisk, Paul Robustelli
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 6
Open Access | Times Cited: 8
Functional and Pathological Effects of α-Synuclein on Synaptic SNARE Complexes
Virginia Gao, Juan Antonio Briano, Lauren E. Komer, et al.
Journal of Molecular Biology (2022) Vol. 435, Iss. 1, pp. 167714-167714
Open Access | Times Cited: 35
AlphaFold Prediction of Structural Ensembles of Disordered Proteins
Z. Faidon Brotzakis, Shengyu Zhang, Michele Vendruscolo
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 19
Clustering Heterogeneous Conformational Ensembles of Intrinsically Disordered Proteins with t-Distributed Stochastic Neighbor Embedding
Rajeswari Appadurai, Jaya Krishna Koneru, Massimiliano Bonomi, et al.
Journal of Chemical Theory and Computation (2023) Vol. 19, Iss. 14, pp. 4711-4727
Open Access | Times Cited: 19
Conformational Plasticity in α-Synuclein and How Crowded Environment Modulates It
Sneha Menon, Jagannath Mondal
The Journal of Physical Chemistry B (2023) Vol. 127, Iss. 18, pp. 4032-4049
Closed Access | Times Cited: 17
Biomolecular NMR spectroscopy in the era of artificial intelligence
Vaibhav Kumar Shukla, Gabriella T. Heller, D. Flemming Hansen
Structure (2023) Vol. 31, Iss. 11, pp. 1360-1374
Open Access | Times Cited: 17
Structural ensembles of disordered proteins from hierarchical chain growth and simulation
Lisa M. Pietrek, Lukas S. Stelzl, Gerhard Hummer
Current Opinion in Structural Biology (2022) Vol. 78, pp. 102501-102501
Open Access | Times Cited: 22
Exploring the Curvature-Dependence of Boron Nitride Nanoparticles on the Inhibition of hIAPP Aggregation
Rituparna Roy, Sandip Paul
The Journal of Physical Chemistry B (2023) Vol. 127, Iss. 35, pp. 7558-7570
Closed Access | Times Cited: 13
Predicting Conformational Ensembles of Intrinsically Disordered Proteins: From Molecular Dynamics to Machine Learning
Jana Aupič, Pavlína Pokorná, Sharon Ruthstein, et al.
The Journal of Physical Chemistry Letters (2024) Vol. 15, Iss. 32, pp. 8177-8186
Closed Access | Times Cited: 5
Fasudil inhibits α-synuclein aggregation through ROCK-inhibition-mediated mechanisms
Lucia Lage, Ana I. Rodríguez‐Pérez, José L. Labandeira‐García, et al.
Neurotherapeutics (2025), pp. e00544-e00544
Open Access
AlphaFold prediction of structural ensembles of disordered proteins
Z. Faidon Brotzakis, Shengyu Zhang, Mhd Hussein Murtada, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Atomistic molecular dynamics simulations of intrinsically disordered proteins
Fidha Nazreen Kunnath Muhammedkutty, Matthew MacAinsh, Huan‐Xiang Zhou
Current Opinion in Structural Biology (2025) Vol. 92, pp. 103029-103029
Open Access
Martini3-IDP: improved Martini 3 force field for disordered proteins
Liguo Wang, Christopher Brasnett, Luís Borges-Araújo, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Energetics of a protein disorder–order transition in small molecule recognition
César Mendoza-Martínez, Michail Papadourakis, Salomé Llabrés, et al.
Chemical Science (2022) Vol. 13, Iss. 18, pp. 5220-5229
Open Access | Times Cited: 21
Baicalein exhibits differential effects and mechanisms towards disruption of α-synuclein fibrils with different polymorphs
Yifei Yao, Yiming Tang, Yun Zhou, et al.
International Journal of Biological Macromolecules (2022) Vol. 220, pp. 316-325
Closed Access | Times Cited: 21
Rational drug design targeting intrinsically disordered proteins
H. Wang, Ruoyao Xiong, Luhua Lai
Wiley Interdisciplinary Reviews Computational Molecular Science (2023) Vol. 13, Iss. 6
Closed Access | Times Cited: 12
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