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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:

The Molten Globule State of a Globular Protein in a Cell Is More or Less Frequent Case Rather than an Exception
Valentina E. Bychkova, Д. А. Долгих, Vitalii Balobanov, et al.
Molecules (2022) Vol. 27, Iss. 14, pp. 4361-4361
Open Access | Times Cited: 13

Showing 13 citing articles:

Pre-Molten, Wet, and Dry Molten Globules en Route to the Functional State of Proteins
Munishwar N. Gupta, Vladimir N. Uversky
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 3, pp. 2424-2424
Open Access | Times Cited: 20
Comparative Study of Polymer Globules and Liquid Droplets in Poor Solvents: Effects of Cosolvents and Solvent Quality
Tushar Mahendrakar, Kaustubh Rane
The Journal of Physical Chemistry B (2025)
Closed Access
Strategies for inhibiting amyloid fibrillation: Current status and future prospects
Md Nadir Hassan, Murtaza Shabbir Hussain, Rizwan Hasan Khan
Progress in molecular biology and translational science (2025)
Closed Access
A structural and biochemical approach to effect of temperature and pH on the Molten Globule phenomenon in a thermophilic protease: Molecular dynamics simulation, fluorescence spectroscopy and circular dichroism
Ghadir A. Jamal, Ehsan Jahangirian, Michael R. Hamblin, et al.
Journal of Molecular Structure (2024) Vol. 1318, pp. 139204-139204
Closed Access | Times Cited: 2
Formation of Supplementary Metal-Binding Centers in Proteins under Stress Conditions
O. V. Kosmachevskaya, Н. Н. Новикова, S. N. Yakunin, et al.
Biochemistry (Moscow) (2024) Vol. 89, Iss. S1, pp. S180-S204
Closed Access | Times Cited: 1
A molten globule ensemble primes Arf1–GDP for the nucleotide switch
Tejaswi Koduru, Noam Hantman, Edgar V. Peters, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 39
Open Access | Times Cited: 1
Conformational stability of peroxidase from the latex of Artocarpus lakoocha: influence of pH, chaotropes, and temperature
Kirti Shila Sonkar, Manendra Pachauri, Amit Kumar, et al.
Frontiers in Plant Science (2024) Vol. 15
Open Access
Probing Aromatic Side Chains Reveals the Site-Specific Melting in the SUMO1 Molten Globule
S. L. Arora, Sri Rama Koti Ainavarapu
Biochemistry (2024)
Closed 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
Adaptation of Erythrocytes: The Role of Hemoglobin, Nitric Oxide, and Methylglyoxal
O. V. Kosmachevskaya, A. F. Topunov
Applied Biochemistry and Microbiology (2024) Vol. 60, Iss. 6, pp. 977-992
Closed Access
Molecular intricacies of intrinsically disordered proteins and drought stress in plants
Vaishali Gupta, Priya Kumari, Kaberi Sonowal, et al.
International Journal of Biological Macromolecules (2024), pp. 139314-139314
Closed Access
Conformational Stability of Peroxidase from latex ofArtocarpus lakoocha: Influence of pH, Chaotropes, and Temperature
Kirti Shila Sonkar, Manendra Pachauri, Amit Kumar, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
Proteins turn “Proteans” – The over 40-year delayed paradigm shift in structural biology: From “native proteins in uniquely defined configurations” to “intrinsically disordered proteins”
Eugenio Frixione, Lourdes Ruiz-Zamarripa
BioMolecular Concepts (2023) Vol. 14, Iss. 1
Open Access
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