Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

Protein folding problem: enigma, paradox, solution
Alexei V. Finkelstein, Natalya S. Bogatyreva, Dmitry N. Ivankov, et al.
Biophysical Reviews (2022) Vol. 14, Iss. 6, pp. 1255-1272
Open Access | Times Cited: 26

Showing 1-25 of 26 citing articles:

Mechanisms of SNARE proteins in membrane fusion
Reinhard Jahn, David C. Cafiso, Lukas K. Tamm
Nature Reviews Molecular Cell Biology (2023) Vol. 25, Iss. 2, pp. 101-118
Closed Access | Times Cited: 56
From covalent transition states in chemistry to noncovalent in biology: from β- to Φ-value analysis of protein folding
Alan R. Fersht
Quarterly Reviews of Biophysics (2024) Vol. 57
Open Access | Times Cited: 6
Life and death of Yfh1: how cool is cold denaturation
Piero Andrea Temussi, Stephen R. Martin, Annalisa Pastore
Quarterly Reviews of Biophysics (2025) Vol. 58
Closed Access
AlphaFold and what is next: bridging functional, systems and structural biology
Kacper Szczepski, Łukasz Jaremko
Expert Review of Proteomics (2025)
Closed Access
Origins of Life: The Protein Folding Problem all over again?
Charles D. Kocher, Ken A. Dill
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 34
Open Access | Times Cited: 3
Sugarcane polyphenol oxidase: Structural elucidation using molecular modeling and docking analyses
Shruti A. Patil, Ali Jawad Akki, Anjanapura V. Raghu, et al.
Process Biochemistry (2023) Vol. 134, pp. 243-249
Closed Access | Times Cited: 9
Molecular Peptide Grafting as a Tool to Create Novel Protein Therapeutics
Anton A. Komar
Molecules (2023) Vol. 28, Iss. 5, pp. 2383-2383
Open Access | Times Cited: 7
Protein folding rate evolution upon mutations
Jorge A. Vila
Biophysical Reviews (2023) Vol. 15, Iss. 4, pp. 661-669
Open Access | Times Cited: 5
Step Forward Cross Validation for Bioactivity Prediction: Out of Distribution Validation in Drug Discovery
Udit Surya Saha, Michele Vendruscolo, Anne E. Carpenter, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Biophysical Reviews: And the winner is …
Damien Hall
Biophysical Reviews (2023) Vol. 15, Iss. 2, pp. 145-149
Open Access | Times Cited: 4
Why Do Proteins Fold into Unique 3D Structures? And Other Questions...
К. В. Шайтан
Russian Journal of Physical Chemistry B (2023) Vol. 17, Iss. 3, pp. 550-570
Closed Access | Times Cited: 4
Clarification to “Protein folding problem: enigma, paradox, solution”
Alexei V. Finkelstein, Natalya S. Bogatyreva, Dmitry N. Ivankov, et al.
Biophysical Reviews (2023) Vol. 15, Iss. 2, pp. 161-161
Open Access | Times Cited: 3
Почему белок сворачивается в уникальную 3D-структуру? И не только это…
К. В. Шайтан
Химическая физика (2023) Vol. 42, Iss. 6, pp. 40-62
Closed Access | Times Cited: 3
Analysis of the Structural Dynamics of Proteins in the Ligand-Unbound and -Bound States by Diffracted X-ray Tracking
Masayuki Oda
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 18, pp. 13717-13717
Open Access | Times Cited: 2
Computational biophysics and structural biology of proteins—a Special Issue in honor of Prof. Haruki Nakamura’s 70th birthday
Damien Hall, Gautam Basu, Nobutoshi Ito
Biophysical Reviews (2022) Vol. 14, Iss. 6, pp. 1211-1222
Open Access | Times Cited: 4
The dynamic-process characterization and prediction of synthetic gene circuits by dynamic delay model
Yanhong Sun, Fengyu Zhang, Qi Ouyang, et al.
iScience (2024) Vol. 27, Iss. 3, pp. 109142-109142
Open Access
Computational approach based on freely accessible tools for antimicrobial drug designR2
Gisele Strieder Philippsen, Flávio Augusto Vicente Seixas
Bioorganic & Medicinal Chemistry Letters (2024) Vol. 115, pp. 130010-130010
Closed Access
In silico evolution of globular protein folds from random sequences
Harutyun Sahakyan, S. G. Babajanyan, Yuri I. Wolf, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Various levels of phase transitions in the protein universe and around
Alexei V. Finkelstein, Vladimir N. Uversky
Elsevier eBooks (2024), pp. 213-254
Closed Access
Frustration and fuzziness in the three functional states of proteins
Priyanka Dogra, Bappaditya Chandra
Elsevier eBooks (2024), pp. 315-332
Closed Access
How Proteins Manage to Fold and How Chaperones Manage to Assist the Folding
Sergiy O. Garbuzynskiy, Victor Marchenkov, Natalia Marchenko, et al.
Physics of Life Reviews (2024) Vol. 52, pp. 66-79
Closed Access
Biophysical Reviews: Turning the page from 2022 to 2023
Damien Hall
Biophysical Reviews (2023) Vol. 15, Iss. 1, pp. 1-11
Open Access | Times Cited: 1
How does a biopolymer (protein) fold into a unique 3D structure?
К. В. Шайтан
Vestnik Moskovskogo universiteta Seria 16 Biologia (2023) Vol. 78, Iss. №3s, 2023, pp. 9-12
Open Access | Times Cited: 1
How Does a Biopolymer (Protein) Fold into a Unique 3D Structure?
К. В. Шайтан
Moscow University Biological Sciences Bulletin (2023) Vol. 78, Iss. S1, pp. S5-S8
Open Access | Times Cited: 1
A Study of a Protein-Folding Machine: Transient Rotation of the Polypeptide Backbone Facilitates Rapid Folding of Protein Domains in All-Atom Molecular Dynamics Simulations
Harutyun Sahakyan, Karen Nazaryan, Arcady Mushegian, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 12, pp. 10049-10049
Open Access
Page 1 - Next Page

Scroll to top