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:

Frustration in Fuzzy Protein Complexes Leads to Interaction Versatility
María I. Freiberger, Peter G. Wolynes, Diego U. Ferreiro, et al.
The Journal of Physical Chemistry B (2021) Vol. 125, Iss. 10, pp. 2513-2520
Open Access | Times Cited: 72

Showing 1-25 of 72 citing articles:

Fuzziness and Frustration in the Energy Landscape of Protein Folding, Function, and Assembly
Stefano Gianni, María I. Freiberger, Per Jemth, et al.
Accounts of Chemical Research (2021) Vol. 54, Iss. 5, pp. 1251-1259
Open Access | Times Cited: 129

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

FuzDrop on AlphaFold: visualizing the sequence-dependent propensity of liquid–liquid phase separation and aggregation of proteins
András Hatos, Silvio C. E. Tosatto, Michele Vendruscolo, et al.
Nucleic Acids Research (2022) Vol. 50, Iss. W1, pp. W337-W344
Open Access | Times Cited: 94

Intermolecular interactions underlie protein/peptide phase separation irrespective of sequence and structure at crowded milieu
Manisha Poudyal, Komal Patel, Laxmikant Gadhe, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 78

Intrinsically Disordered Proteins: Critical Components of the Wetware
Prakash Kulkarni, S. Bhattacharya, Srisairam Achuthan, et al.
Chemical Reviews (2022) Vol. 122, Iss. 6, pp. 6614-6633
Open Access | Times Cited: 73

Protein misfolding and amyloid nucleation through liquid–liquid phase separation
S. Mukherjee, Manisha Poudyal, K. Dave, et al.
Chemical Society Reviews (2024) Vol. 53, Iss. 10, pp. 4976-5013
Closed Access | Times Cited: 25

Intrinsically disordered proteins/regions and insight into their biomolecular interactions
Pinak Chakrabarti, Devlina Chakravarty
Biophysical Chemistry (2022) Vol. 283, pp. 106769-106769
Closed Access | Times Cited: 55

Allostery: Allosteric Cancer Drivers and Innovative Allosteric Drugs
Ruth Nussinov, Mingzhen Zhang, Ryan Maloney, et al.
Journal of Molecular Biology (2022) Vol. 434, Iss. 17, pp. 167569-167569
Open Access | Times Cited: 47

Direct Observation of “Elongated” Conformational States in α‐Synuclein upon Liquid‐Liquid Phase Separation
Daniele Ubbiali, Marta Fratini, Lolita Piersimoni, et al.
Angewandte Chemie International Edition (2022) Vol. 61, Iss. 46
Open Access | Times Cited: 45

Protein conformational ensembles in function: roles and mechanisms
Ruth Nussinov, Yonglan Liu, Wengang Zhang, et al.
RSC Chemical Biology (2023) Vol. 4, Iss. 11, pp. 850-864
Open Access | Times Cited: 36

Surface frustration re-patterning underlies the structural landscape and evolvability of fungal orphan candidate effectors
Mark C. Derbyshire, Sylvain Raffaele
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 32

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: 10

Molecular switching in transcription through splicing and proline-isomerization regulates stress responses in plants
Frederik Friis Theisen, Andreas Prestel, Steffie Elkjær, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 9

Classifying the Binding Modes of Disordered Proteins
Mónika Fuxreiter
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 22, pp. 8615-8615
Open Access | Times Cited: 59

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

Local energetic frustration conservation in protein families and superfamilies
María I. Freiberger, Victoria Ruiz‐Serra, Camila Pontes, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 19

Conformational entropy in molecular recognition of intrinsically disordered proteins
Karen Skriver, Frederik Friis Theisen, Birthe B. Kragelund
Current Opinion in Structural Biology (2023) Vol. 83, pp. 102697-102697
Open Access | Times Cited: 18

Protein structure–function continuum model: Emerging nexuses between specificity, evolution, and structure
Munishwar N. Gupta, Vladimir N. Uversky
Protein Science (2024) Vol. 33, Iss. 4
Closed Access | Times Cited: 7

Context-dependent, fuzzy protein interactions: Towards sequence-based insights
Mónika Fuxreiter
Current Opinion in Structural Biology (2024) Vol. 87, pp. 102834-102834
Open Access | Times Cited: 7

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: 15

Unveiling induced folding of intrinsically disordered proteins – Protein engineering, frustration and emerging themes
Francesca Malagrinò, Awa Diop, Livia Pagano, et al.
Current Opinion in Structural Biology (2021) Vol. 72, pp. 153-160
Open Access | Times Cited: 25

The importance of the compact disordered state in the fuzzy interactions between intrinsically disordered proteins
Dan Wang, Shaowen Wu, Dongdong Wang, et al.
Chemical Science (2022) Vol. 13, Iss. 8, pp. 2363-2377
Open Access | Times Cited: 18

Conformational dynamics and multi-modal interaction of Paxillin with the Focal Adhesion Targeting Domain
S. Bhattacharya, Yanan He, Yihong Chen, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access

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