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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 1-25 of 62 citing articles:

Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis
A. Aditya Prasad, Vidhya Bharathi, Vishwanath Sivalingam, et al.
Frontiers in Molecular Neuroscience (2019) Vol. 12
Open Access | Times Cited: 640
The Pathobiology of TDP-43 C-Terminal Fragments in ALS and FTLD
Britt A. Berning, Adam K. Walker
Frontiers in Neuroscience (2019) Vol. 13
Open Access | Times Cited: 171
Liquid–Liquid Phase Separation by Intrinsically Disordered Protein Regions of Viruses: Roles in Viral Life Cycle and Control of Virus–Host Interactions
Stefania Brocca, Rita Grandori, Sonia Longhi, et al.
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 23, pp. 9045-9045
Open Access | Times Cited: 157
SOD1, more than just an antioxidant
Elis C. A. Eleuthério, Rayne Stfhany Silva Magalhães, Aline de Araújo Brasil, et al.
Archives of Biochemistry and Biophysics (2020) Vol. 697, pp. 108701-108701
Open Access | Times Cited: 152
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: 74
Stochasticity of Biological Soft Matter: Emerging Concepts in Intrinsically Disordered Proteins and Biological Phase Separation
Konstantin К. Turoverov, Irina М. Kuznetsova, Alexander V. Fonin, et al.
Trends in Biochemical Sciences (2019) Vol. 44, Iss. 8, pp. 716-728
Closed Access | Times Cited: 122
Protein intrinsic disorder and structure-function continuum
Vladimir N. Uversky
Progress in molecular biology and translational science (2019), pp. 1-17
Closed Access | Times Cited: 121
Molecular and Cellular Mechanisms Affected in ALS
Laura Le Gall, Ekene Anakor, Owen Connolly, et al.
Journal of Personalized Medicine (2020) Vol. 10, Iss. 3, pp. 101-101
Open Access | Times Cited: 112
Pan-retroviral Nucleocapsid-Mediated Phase Separation Regulates Genomic RNA Positioning and Trafficking
Anne Monette, Meijuan Niu, Lois Chen, et al.
Cell Reports (2020) Vol. 31, Iss. 3, pp. 107520-107520
Open Access | Times Cited: 103
LLPSDB v2.0: an updated database of proteins undergoing liquid–liquid phase separation in vitro
Xi Wang, Xiang Zhou, Qinglin Yan, et al.
Bioinformatics (2022) Vol. 38, Iss. 7, pp. 2010-2014
Open Access | Times Cited: 44
SERBP1 interacts with PARP1 and is present in PARylation-dependent protein complexes regulating splicing, cell division, and ribosome biogenesis
Kira Breunig, X. Lei, Mauro Montalbano, et al.
eLife (2025) Vol. 13
Open Access | Times Cited: 1
Intrinsically Disordered Proteins: The Dark Horse of the Dark Proteome
Prakash Kulkarni, Vladimir N. Uversky
PROTEOMICS (2018) Vol. 18, Iss. 21-22
Open Access | Times Cited: 82
Intrinsic Disorder-Based Emergence in Cellular Biology: Physiological and Pathological Liquid-Liquid Phase Transitions in Cells
April L. Darling, Boris Y. Zaslavsky, Vladimir N. Uversky
Polymers (2019) Vol. 11, Iss. 6, pp. 990-990
Open Access | Times Cited: 74
In Aqua Veritas: The Indispensable yet Mostly Ignored Role of Water in Phase Separation and Membrane-less Organelles
Boris Y. Zaslavsky, Vladimir N. Uversky
Biochemistry (2018) Vol. 57, Iss. 17, pp. 2437-2451
Closed Access | Times Cited: 73
A Systematic Review of Suggested Molecular Strata, Biomarkers and Their Tissue Sources in ALS
Udaya Geetha Vijayakumar, Vanessa Milla, M. Stafford, et al.
Frontiers in Neurology (2019) Vol. 10
Open Access | Times Cited: 65
Amyotrophic Lateral Sclerosis and Autophagy: Dysfunction and Therapeutic Targeting
Azin Amin, Nirma D. Perera, Philip M. Beart, et al.
Cells (2020) Vol. 9, Iss. 11, pp. 2413-2413
Open Access | Times Cited: 61
Solid-State NMR Reveals the Structural Transformation of the TDP-43 Amyloidogenic Region upon Fibrillation
Xiao-Feng Zhuo, Jian Wang, Jing Zhang, et al.
Journal of the American Chemical Society (2020) Vol. 142, Iss. 7, pp. 3412-3421
Closed Access | Times Cited: 60
Aberrant liquid-liquid phase separation and amyloid aggregation of proteins related to neurodegenerative diseases
Azeem Ahmad, Vladimir N. Uversky, Rizwan Hasan Khan
International Journal of Biological Macromolecules (2022) Vol. 220, pp. 703-720
Closed Access | Times Cited: 36
Background-deflection Brillouin microscopy reveals altered biomechanics of intracellular stress granules by ALS protein FUS
Giuseppe Antonacci, Valeria de Turris, Alessandro Rosa, et al.
Communications Biology (2018) Vol. 1, Iss. 1
Open Access | Times Cited: 58
Relation Between Stress Granules and Cytoplasmic Protein Aggregates Linked to Neurodegenerative Diseases
Ioana Dobra, Serhii Pankivskyi, Anastasiia Samsonova, et al.
Current Neurology and Neuroscience Reports (2018) Vol. 18, Iss. 12
Closed Access | Times Cited: 48
Connecting the “dots”: RNP granule network in health and disease
Haiyan An, Camille Rabesahala de Meritens, Tatyana A. Shelkovnikova
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (2021) Vol. 1868, Iss. 8, pp. 119058-119058
Open Access | Times Cited: 38
SHARK enables sensitive detection of evolutionary homologs and functional analogs in unalignable and disordered sequences
Chi Fung Willis Chow, Soumyadeep Ghosh, Anna Hadarovich, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 42
Open Access | Times Cited: 6
Granulins modulate liquid–liquid phase separation and aggregation of the prion-like C-terminal domain of the neurodegeneration-associated protein TDP-43
Anukool A. Bhopatkar, Vladimir N. Uversky, Vijayaraghavan Rangachari
Journal of Biological Chemistry (2020) Vol. 295, Iss. 8, pp. 2506-2519
Open Access | Times Cited: 36
Computational insights into mechanism of AIM4-mediated inhibition of aggregation of TDP-43 protein implicated in ALS and evidence for in vitro inhibition of liquid-liquid phase separation (LLPS) of TDP-432C-A315T by AIM4
Amandeep Girdhar, Vidhya Bharathi, Vikas Tiwari, et al.
International Journal of Biological Macromolecules (2020) Vol. 147, pp. 117-130
Open Access | Times Cited: 34
The dark side of Alzheimer’s disease: unstructured biology of proteins from the amyloid cascade signaling pathway
Kundlik Gadhave, Bhuvaneshwari R. Gehi, Prateek Kumar, et al.
Cellular and Molecular Life Sciences (2020) Vol. 77, Iss. 20, pp. 4163-4208
Closed Access | Times Cited: 33
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