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:

Biological soft matter: intrinsically disordered proteins in liquid–liquid phase separation and biomolecular condensates
Alexander V. Fonin, Iuliia A. Antifeeva, Irina М. Kuznetsova, et al.
Essays in Biochemistry (2022) Vol. 66, Iss. 7, pp. 831-847
Closed Access | Times Cited: 39

Showing 1-25 of 39 citing articles:

Biological importance of arginine: A comprehensive review of the roles in structure, disorder, and functionality of peptides and proteins
Munishwar N. Gupta, Vladimir N. Uversky
International Journal of Biological Macromolecules (2023) Vol. 257, pp. 128646-128646
Open Access | Times Cited: 22

The Protein Scaffolding Functions of Polyphosphate
Jian Guan, Ursula Jakob
Journal of Molecular Biology (2024) Vol. 436, Iss. 14, pp. 168504-168504
Closed Access | Times Cited: 10

Fragile X mental retardation protein modulates translation of proteins with predicted tendencies for liquid-liquid phase separation
Omar Jurado, Marco V. José, Eugenio Frixione
Biosystems (2025), pp. 105405-105405
Closed Access

Functional diversity of intrinsically disordered proteins and their structural heterogeneity: Protein structure-function continuum
Vladimir N. Uversky
Progress in molecular biology and translational science (2025)
Closed Access

Biomolecular condensates: insights into early and late steps of the HIV-1 replication cycle
Francesca Di Nunzio, Vladimir N. Uversky, Andrew J. Mouland
Retrovirology (2023) Vol. 20, Iss. 1
Open Access | Times Cited: 18

The Role of Liquid–Liquid Phase Separation in Actin Polymerization
Olga I. Povarova, Iuliia A. Antifeeva, Alexander V. Fonin, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 4, pp. 3281-3281
Open Access | Times Cited: 11

A sequence‐based model for identifying proteins undergoing liquid–liquid phase separation/forming fibril aggregates via machine learning
Shaofeng Liao, Yujun Zhang, Xinchen Han, et al.
Protein Science (2024) Vol. 33, Iss. 3
Closed Access | Times Cited: 3

Functional unfoldomics: Roles of intrinsic disorder in protein (multi)functionality
Vladimir N. Uversky
Advances in protein chemistry and structural biology (2023)
Closed Access | Times Cited: 10

Interfacial stabilization of aqueous two-phase systems: a review
Caitlyn Fick, Zara Khan, Samanvaya Srivastava
Materials Advances (2023) Vol. 4, Iss. 20, pp. 4665-4678
Open Access | Times Cited: 9

Intrinsic disorder in PRAME and its role in uveal melanoma
Michael Antonietti, David J. Taylor Gonzalez, Mak B. Djulbegovic, et al.
Cell Communication and Signaling (2023) Vol. 21, Iss. 1
Open Access | Times Cited: 8

Chaotic aging: intrinsically disordered proteins in aging-related processes
Vladimir D. Manyilov, Nikolay S. Ilyinsky, Semen V. Nesterov, et al.
Cellular and Molecular Life Sciences (2023) Vol. 80, Iss. 9
Open Access | Times Cited: 5

Reexamining the diverse functions of arginine in biochemistry
Munishwar N. Gupta, Vladimir N. Uversky
Biochemical and Biophysical Research Communications (2024) Vol. 705, pp. 149731-149731
Closed Access | Times Cited: 1

SERBP1 interacts with PARP1 and is present in PARylation-dependent protein complexes regulating splicing, cell division, and ribosome biogenesis
Kira Breunig, Xiufen Lei, Mauro Montalbano, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1

Osmolyte-IDP interactions during desiccation
Vincent Nicholson, Emma Meese, Thomas E. Boothby
Progress in molecular biology and translational science (2024)
Closed Access | Times Cited: 1

On the Roles of Protein Intrinsic Disorder in the Origin of Life and Evolution
Vladimir N. Uversky
Life (2024) Vol. 14, Iss. 10, pp. 1307-1307
Open Access | Times Cited: 1

Proteomic tools to study phosphorylation of intrinsically disordered proteins
Barbara Spolaore, Luca Secco, Giulia Rocca, et al.
Expert Review of Proteomics (2023) Vol. 20, Iss. 4-6, pp. 93-107
Closed Access | Times Cited: 2

Imaging-Based Quantitative Assessment of Biomolecular Condensates in vitro and in Cells
Tessa Bergsma, Anton Steen, Julia Kamenz, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

Metadynamics and Free-Energy Landscape Approaches for Structural Characterization of Galectin-3
Rik Ganguly, Vladimir N. Uversky, Prosperwell Ingty, et al.
Research Square (Research Square) (2024)
Closed Access

Implications of liquid-liquid phase separation and ferroptosis in Alzheimer's disease
Fu-Wei Wang, Zihao Chen, Qiong Zhou, et al.
Neuropharmacology (2024) Vol. 259, pp. 110083-110083
Closed Access

Conformations of a Low-Complexity Protein in Homogeneous and Phase-Separated Frozen Solutions
C. Blake Wilson, Myungwoon Lee, Wai‐Ming Yau, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

Translational Diffusion and Self-Association of an Intrinsically Disordered Protein κ-Casein Using NMR with Ultra-High Pulsed-Field Gradient and Time-Resolved FRET
Daria L. Melnikova, Venkatesh Ranjan, Yuri E. Nesmelov, et al.
The Journal of Physical Chemistry B (2024) Vol. 128, Iss. 32, pp. 7781-7791
Open Access

Atomistic Insights into Sequence-Mediated Spontaneous Association of Short RNA Chains
Manas Mondal, Yi Qin Gao
Biochemistry (2024) Vol. 63, Iss. 21, pp. 2916-2936
Closed Access

Conformations of a Low-Complexity Protein in Homogeneous and Phase-Separated Frozen Solutions
C. Blake Wilson, Myungwoon Lee, Wai‐Ming Yau, et al.
Biophysical Journal (2024)
Open Access

Page 1 - Next Page

Scroll to top