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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:

Refinement of α-Synuclein Ensembles Against SAXS Data: Comparison of Force Fields and Methods
Mustapha Carab Ahmed, Line K. Skaanning, Alexander Jussupow, et al.
Frontiers in Molecular Biosciences (2021) Vol. 8
Open Access | Times Cited: 78

Showing 1-25 of 78 citing articles:

Accurate model of liquid–liquid phase behavior of intrinsically disordered proteins from optimization of single-chain properties
Giulio Tesei, Thea K. Schulze, Ramón Crehuet, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 44
Open Access | Times Cited: 289
Improving Martini 3 for Disordered and Multidomain Proteins
F. Emil Thomasen, Francesco Pesce, Mette Ahrensback Roesgaard, et al.
Journal of Chemical Theory and Computation (2022) Vol. 18, Iss. 4, pp. 2033-2041
Open Access | Times Cited: 126
AlphaFold2: A Role for Disordered Protein/Region Prediction?
Carter J. Wilson, Wing‐Yiu Choy, Mikko Karttunen
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 9, pp. 4591-4591
Open Access | Times Cited: 121
Improved predictions of phase behaviour of intrinsically disordered proteins by tuning the interaction range
Giulio Tesei, Kresten Lindorff‐Larsen
Open Research Europe (2023) Vol. 2, pp. 94-94
Open Access | Times Cited: 83
Rescaling protein-protein interactions improves Martini 3 for flexible proteins in solution
F. Emil Thomasen, Tórur Skaalum, Ashutosh Kumar, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 19
Chemically Informed Coarse-Graining of Electrostatic Forces in Charge-Rich Biomolecular Condensates
Andrés R. Tejedor, Anne Aguirre Gonzalez, Maria Julia Maristany, et al.
ACS Central Science (2025) Vol. 11, Iss. 2, pp. 302-321
Open Access | Times Cited: 2
On the Potential of Machine Learning to Examine the Relationship Between Sequence, Structure, Dynamics and Function of Intrinsically Disordered Proteins
Kresten Lindorff‐Larsen, Birthe B. Kragelund
Journal of Molecular Biology (2021) Vol. 433, Iss. 20, pp. 167196-167196
Open Access | Times Cited: 77
Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2
T. Reid Alderson, Iva Pritišanac, Đesika Kolarić, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 41
IDPConformerGenerator: A Flexible Software Suite for Sampling the Conformational Space of Disordered Protein States
João M. C. Teixeira, Zi Hao Liu, Ashley Namini, et al.
The Journal of Physical Chemistry A (2022) Vol. 126, Iss. 35, pp. 5985-6003
Open Access | Times Cited: 41
Learning to evolve structural ensembles of unfolded and disordered proteins using experimental solution data
Oufan Zhang, Mojtaba Haghighatlari, Jie Li, et al.
The Journal of Chemical Physics (2023) Vol. 158, Iss. 17
Open Access | Times Cited: 24
A coarse-grained model for disordered and multi-domain proteins
Fan Cao, Sören von Bülow, Giulio Tesei, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 11
A conformational fingerprint for amyloidogenic light chains
Cristina Paissoni, Sarita Puri, Luca Broggini, et al.
(2025)
Open Access | Times Cited: 1
Improved predictions of phase behaviour of intrinsically disordered proteins by tuning the interaction range
Giulio Tesei, Kresten Lindorff‐Larsen
Open Research Europe (2022) Vol. 2, pp. 94-94
Open Access | Times Cited: 36
Intrinsically disordered proteins: Ensembles at the limits of Anfinsen's dogma
Prakash Kulkarni, Vitor B. P. Leite, Susmita Roy, et al.
Biophysics Reviews (2022) Vol. 3, Iss. 1
Closed Access | Times Cited: 34
Sequence-Dependent Backbone Dynamics of Intrinsically Disordered Proteins
Souvik Dey, Matthew MacAinsh, Huan‐Xiang Zhou
Journal of Chemical Theory and Computation (2022) Vol. 18, Iss. 10, pp. 6310-6323
Open Access | Times Cited: 31
Assessment of models for calculating the hydrodynamic radius of intrinsically disordered proteins
Francesco Pesce, Estella A. Newcombe, Pernille Seiffert, et al.
Biophysical Journal (2022) Vol. 122, Iss. 2, pp. 310-321
Open Access | Times Cited: 30
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
Integrating single-molecule spectroscopy and simulations for the study of intrinsically disordered proteins
Jhullian J. Alston, Andrea Soranno, Alex S. Holehouse
Methods (2021) Vol. 193, pp. 116-135
Open Access | Times Cited: 33
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: 23
Role of conformational dynamics in pathogenic protein aggregation
Xun Sun, H. Jane Dyson, Peter E. Wright
Current Opinion in Chemical Biology (2023) Vol. 73, pp. 102280-102280
Open Access | Times Cited: 16
Sizes, conformational fluctuations, and SAXS profiles for Intrinsically Disordered Proteins
Mauro L. Mugnai, Debayan Chakraborty, Abhinaw Kumar, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 14
Hierarchical Assembly of Single-Stranded RNA
Lisa M. Pietrek, Lukas S. Stelzl, Gerhard Hummer
Journal of Chemical Theory and Computation (2024) Vol. 20, Iss. 5, pp. 2246-2260
Open Access | Times Cited: 6
Chemically-informed coarse-graining of electrostatic forces in charge-rich biomolecular condensates
Andrés R. Tejedor, Anne Aguirre Gonzalez, Maria Julia Maristany, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 5
Refining conformational ensembles of flexible proteins against small-angle x-ray scattering data
Francesco Pesce, Kresten Lindorff‐Larsen
Biophysical Journal (2021) Vol. 120, Iss. 22, pp. 5124-5135
Open Access | Times Cited: 30
Predicting molecular properties of α‐synuclein using force fields for intrinsically disordered proteins
Kasper B. Pedersen, Jose C. Flores‐Canales, Birgit Schiøtt
Proteins Structure Function and Bioinformatics (2022) Vol. 91, Iss. 1, pp. 47-61
Open Access | Times Cited: 20
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