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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:

Energy landscapes of Aβ monomers are sculpted in accordance with Ostwald’s rule of stages
Debayan Chakraborty, John E. Straub, D. Thirumalai
Science Advances (2023) Vol. 9, Iss. 12
Open Access | Times Cited: 21

Showing 21 citing articles:

A brief history of amyloid aggregation simulations
Hebah Fatafta, Mohammed Khaled, Batuhan Kav, et al.
Wiley Interdisciplinary Reviews Computational Molecular Science (2024) Vol. 14, Iss. 1
Closed Access | Times Cited: 9
Amyloid Aggregation and Liquid–Liquid Phase Separation from the Perspective of Phase Transitions
Zhenzhen Zhang, Gangtong Huang, Zhiyuan Song, et al.
The Journal of Physical Chemistry B (2023) Vol. 127, Iss. 28, pp. 6241-6250
Open Access | Times Cited: 17
Machine Learning Subtle Conformational Change due to Phosphorylation in Intrinsically Disordered Proteins
Subinoy Adhikari, Jagannath Mondal
The Journal of Physical Chemistry B (2023) Vol. 127, Iss. 44, pp. 9433-9449
Closed Access | Times Cited: 15
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
Hairpin trimer transition state of amyloid fibril
Levent Sari, Sofia Bali, Łukasz A. Joachimiak, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 5
Odd–even disparity in the population of slipped hairpins in RNA repeat sequences with implications for phase separation
Hiranmay Maity, Hung T. Nguyen, Naoto Hori, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 24
Open Access | Times Cited: 11
The mechanism of amyloid fibril growth from Φ-value analysis
Jacob Aunstrup Larsen, Abigail Barclay, Nicola Vettore, et al.
Nature Chemistry (2025) Vol. 17, Iss. 3, pp. 403-411
Closed Access
Impacts of D-aspartate on the aggregation kinetics and structural polymorphism of amyloid β peptide 1-42
Li Li Hsiao, Chih‐Hsuan Lee, Karine Mazmanian, et al.
Journal of Molecular Biology (2025), pp. 169092-169092
Closed Access
Sizes, conformational fluctuations, and SAXS profiles for intrinsically disordered proteins
Mauro L. Mugnai, Debayan Chakraborty, Hung T. Nguyen, et al.
Protein Science (2025) Vol. 34, Iss. 4
Closed Access
Delving into the crucial role of the initial structure in the dynamic and self-assembly of amyloid beta
Maryam Ghorbaninia, Shirin Doroudgar, Mohamad Reza Ganjalikhany
Biochemical and Biophysical Research Communications (2025) Vol. 758, pp. 151652-151652
Closed Access
SOP-MULTI: A Self-Organized Polymer-Based Coarse-Grained Model for Multidomain and Intrinsically Disordered Proteins with Conformation Ensemble Consistent with Experimental Scattering Data
Krishnakanth Baratam, Anand Srivastava
Journal of Chemical Theory and Computation (2024) Vol. 20, Iss. 22, pp. 10179-10198
Open Access | Times Cited: 3
Transition Networks Unveil Disorder-to-Order Transformations in Aβ Caused by Glycosaminoglycans or Lipids
Moritz Schäffler, Suman Samantray, Birgit Strodel
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 14, pp. 11238-11238
Open Access | Times Cited: 5
Conformational fluctuations and phases in fused in sarcoma (FUS) low‐complexity domain
D. Thirumalai, Abhinaw Kumar, Debayan Chakraborty, et al.
Biopolymers (2023)
Open Access | Times Cited: 4
Confined liquid crystallization governed by electric field for API crystal polymorphism screening and massive preparation
Zhijie Yuan, Ling‐Feng Wang, Mengyuan Wu, et al.
Journal of Colloid and Interface Science (2024) Vol. 664, pp. 74-83
Closed Access | Times Cited: 1
Heterotypic Seeding Generates Mixed Amyloid Polymorphs
Siddhartha Banerjee, Divya Baghel, Harrison O. Edmonds, et al.
Small Science (2024)
Open Access | Times Cited: 1
Survey of the Aβ-peptide structural diversity: molecular dynamics approaches
Anna P. Tolstova, Alexei A. Adzhubei, Maria A. Strelkova, et al.
Biophysical Reviews (2024) Vol. 16, Iss. 6, pp. 701-722
Closed Access | Times Cited: 1
Energy Landscapes and Heat Capacity Signatures for Monomers and Dimers of Amyloid-Forming Hexapeptides
Nicy, David J. Wales
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 13, pp. 10613-10613
Open Access | Times Cited: 3
Helix-to-sheet transition of the Aβ42 peptide revealed using an enhanced sampling strategy and Markov state model
Huilin Wen, Hao Ouyang, Hao Shang, et al.
Computational and Structural Biotechnology Journal (2023) Vol. 23, pp. 688-699
Open Access | Times Cited: 2
SOP-MULTI: A self-organized polymer based coarse-grained model for multi-domain and intrinsically disordered proteins with conformation ensemble consistent with experimental scattering data
Krishnakanth Baratam, Anand Srivastava
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
The energy landscape of Aβ1-42: a funnel to disorder for the monomer becomes a folding funnel for self-assembly
Moritz Schäffler, David J. Wales, Birgit Strodel
Chemical Communications (2024)
Open Access
Tuning Phase Transition of Molecular Self-Assembly by Artificial Chaperones through Aromatic–Aromatic Interactions
Honglei Lu, Xuejiao Yang, Huaimin Wang
Biomacromolecules (2023)
Closed Access | Times Cited: 1
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