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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.

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Showing 26-50 of 62 citing articles:

Identification of a Region in the Common Amino-terminal Domain of Hendra Virus P, V, and W Proteins Responsible for Phase Transition and Amyloid Formation
Edoardo Salladini, Frank Gondelaud, Juliet F. Nilsson, et al.
Biomolecules (2021) Vol. 11, Iss. 9, pp. 1324-1324
Open Access | Times Cited: 24
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: 11
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: 4
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.
(2025)
Open 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), pp. 1-15
Closed Access
Intrinsic Disorder in Protein Interaction Networks Linking Cancer with Metabolic Diseases
Veda Naga Priya Vangala, Vladimir N. Uversky
Computational Biology and Chemistry (2025) Vol. 118, pp. 108493-108493
Closed Access
Intrinsic Disorder and Phase Separation Coordinate Exocytosis, Motility, and Chromatin Remodeling in the Human Acrosomal Proteome
Shivam Shukla, Sean S. Lastorka, Vladimir N. Uversky
Proteomes (2025) Vol. 13, Iss. 2, pp. 16-16
Open Access
Age‐related neurodegenerative diseases
Michael R. Duggan, Bahareh Torkzaban, Taha Mohseni Ahooyi, et al.
Journal of Cellular Physiology (2019) Vol. 235, Iss. 4, pp. 3131-3141
Open Access | Times Cited: 28
A liquid-to-solid phase transition of Cu/Zn superoxide dismutase 1 initiated by oxidation and disease mutation
Siyu Gu, Ming Xu, Long Chen, et al.
Journal of Biological Chemistry (2022) Vol. 299, Iss. 2, pp. 102857-102857
Open Access | Times Cited: 15
Functions of short lifetime biological structures at large: the case of intrinsically disordered proteins
Vladimir N. Uversky
Briefings in Functional Genomics (2018)
Closed Access | Times Cited: 26
MAPK- and glycogen synthase kinase 3–mediated phosphorylation regulates the DEAD-box protein modulator Gle1 for control of stress granule dynamics
Aditi Aditi, Aaron C. Mason, Manisha Sharma, et al.
Journal of Biological Chemistry (2018) Vol. 294, Iss. 2, pp. 559-575
Open Access | Times Cited: 24
Functional benefit of structural disorder for the replication of measles, Nipah and Hendra viruses
Frank Gondelaud, Giulia Pesce, Juliet F. Nilsson, et al.
Essays in Biochemistry (2022) Vol. 66, Iss. 7, pp. 915-934
Open Access | Times Cited: 14
Structural basis for RNA recognition by the N-terminal tandem RRM domains of human RBM45
Xiaolei Chen, Zhongmei Yang, Wenfeng Wang, et al.
Nucleic Acids Research (2021) Vol. 49, Iss. 5, pp. 2946-2958
Open Access | Times Cited: 18
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: 7
RBM45 associates with nuclear stress bodies and forms nuclear inclusions during chronic cellular stress and in neurodegenerative diseases
Mahlon A. Collins, Yang Li, Robert Bowser
Acta Neuropathologica Communications (2020) Vol. 8, Iss. 1
Open Access | Times Cited: 17
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
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.
eLife (2024)
Open Access | Times Cited: 1
Spinal cord phosphoproteome of a SCA2/ALS13 mouse model reveals alteration of ATXN2-N-term SH3-actin interactome and of autophagy via WNK1-MYO6-OPTN-SQSTM1
Luis E. Almaguer-Mederos, Arvind Reddy Kandi, Nesli-Ece Şen, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Perspectives on drug discovery strategies based on IDPs
Gustavo Fuertes, Laura Nevola, Santiago Esteban‐Martín
Elsevier eBooks (2019), pp. 275-327
Closed Access | Times Cited: 9
Analyzing aggregation propensities of clinically relevant PTEN mutants: a new culprit in pathogenesis of cancer and other PTENopathies
Emily Palumbo, Bi Zhao, Bin Xue, et al.
Journal of Biomolecular Structure and Dynamics (2019) Vol. 38, Iss. 8, pp. 2253-2266
Closed Access | Times Cited: 8
What's in the BAGs? Intrinsic disorder angle of the multifunctionality of the members of a family of chaperone regulators
Liberato Marzullo, Maria Caterina Turco, Vladimir N. Uversky
Journal of Cellular Biochemistry (2021) Vol. 123, Iss. 1, pp. 22-42
Closed Access | Times Cited: 7
SHARK enables homology assessment in unalignable and disordered sequences
Chi Fung Willis Chow, Soumyadeep Ghosh, Anna Hadarovich, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 2
POCT devices for neurodegenerative disorders: from lab to clinics
Arpana Parihar, Nishant Kumar Choudhary, Raju Khan
Elsevier eBooks (2023), pp. 279-310
Closed Access | Times Cited: 2
Strategies in the design and development of (TAR) DNA-binding protein 43 (TDP-43) binding ligands
Praveen P. N. Rao, Arash Shakeri, Yusheng Zhao, et al.
European Journal of Medicinal Chemistry (2021) Vol. 225, pp. 113753-113753
Closed Access | Times Cited: 5
Structure and disorder: protein functions depend on this new binary transforming lock-and-key into structure-function continuum
Munishwar N. Gupta, Vladimir N. Uversky
Elsevier eBooks (2022), pp. 127-148
Closed Access | Times Cited: 3

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