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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:

Specific RNA interactions promote TDP‐43 multivalent phase separation and maintain liquid properties
Zachary R. Grese, Alliny C.S. Bastos, Lohany D. Mamede, et al.
EMBO Reports (2021) Vol. 22, Iss. 12
Open Access | Times Cited: 84

Showing 1-25 of 84 citing articles:

Liquid-Liquid Phase Separation of TDP-43 and FUS in Physiology and Pathology of Neurodegenerative Diseases
Jenny L. Carey, Lin Guo
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 103
Intra-condensate demixing of TDP-43 inside stress granules generates pathological aggregates
Xiao Yan, David Kuster, Priyesh Mohanty, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 23
Fundamental Aspects of Phase-Separated Biomolecular Condensates
Huan‐Xiang Zhou, Divya Kota, Sanbo Qin, et al.
Chemical Reviews (2024) Vol. 124, Iss. 13, pp. 8550-8595
Closed Access | Times Cited: 23
Structured protein domains enter the spotlight: modulators of biomolecular condensate form and function
Nathaniel Hess, Jerelle A. Joseph
Trends in Biochemical Sciences (2025)
Open Access | Times Cited: 3
Structural insights and milestones in TDP-43 research: A comprehensive review of its pathological and therapeutic advances
Mei Dang, Longjiang Wu, Xiaoying Zhang
International Journal of Biological Macromolecules (2025), pp. 141677-141677
Open Access | Times Cited: 2
Emerging Therapies and Novel Targets for TDP-43 Proteinopathy in ALS/FTD
Lindsey R. Hayes, Petr Kaláb
Neurotherapeutics (2022) Vol. 19, Iss. 4, pp. 1061-1084
Open Access | Times Cited: 43
TDP-43 Oligomerization and Phase Separation Properties Are Necessary for Autoregulation
Lydia C. Koehler, Zachary R. Grese, Alliny C.S. Bastos, et al.
Frontiers in Neuroscience (2022) Vol. 16
Open Access | Times Cited: 40
Role of aberrant phase separation in pathological protein aggregation
Pijush Chakraborty, Markus Zweckstetter
Current Opinion in Structural Biology (2023) Vol. 82, pp. 102678-102678
Closed Access | Times Cited: 38
Molecular mechanisms of phase separation and amyloidosis of ALS/FTD-linked FUS and TDP-43
Jianxing Song
Aging and Disease (2023) Vol. 15, Iss. 5, pp. 2084-2084
Open Access | Times Cited: 24
Nuclear-import receptors as gatekeepers of pathological phase transitions in ALS/FTD
Bilal Khalil, Miriam Linsenmeier, Courtney L. Smith, et al.
Molecular Neurodegeneration (2024) Vol. 19, Iss. 1
Open Access | Times Cited: 15
Stress-induced TDP-43 nuclear condensation causes splicing loss of function and STMN2 depletion
Wan-Ping Huang, Brittany C.S. Ellis, Rachel E. Hodgson, et al.
Cell Reports (2024) Vol. 43, Iss. 7, pp. 114421-114421
Open Access | Times Cited: 13
Specific protein-RNA interactions are mostly preserved in biomolecular condensates
Tebbe de Vries, Mihajlo Novakovic, Yinan Ni, et al.
Science Advances (2024) Vol. 10, Iss. 10
Open Access | Times Cited: 12
RNA-mediated ribonucleoprotein assembly controls TDP-43 nuclear retention
Patricia M. dos Passos, Erandika H. Hemamali, Lohany D. Mamede, et al.
PLoS Biology (2024) Vol. 22, Iss. 2, pp. e3002527-e3002527
Open Access | Times Cited: 10
RNA-binding properties orchestrate TDP-43 homeostasis through condensate formation in vivo
Natalie M. Scherer, Cindy Maurel, Matthew S. Graus, et al.
Nucleic Acids Research (2024) Vol. 52, Iss. 9, pp. 5301-5319
Open Access | Times Cited: 9
Disrupting pathologic phase transitions in neurodegeneration
Bryan Hurtle, Longxin Xie, Christopher J. Donnelly
Journal of Clinical Investigation (2023) Vol. 133, Iss. 13
Open Access | Times Cited: 23
Phase separation and pathologic transitions of RNP condensates in neurons: implications for amyotrophic lateral sclerosis, frontotemporal dementia and other neurodegenerative disorders
Aditi Naskar, Asima Nayak, Muthu Raj Salaikumaran, et al.
Frontiers in Molecular Neuroscience (2023) Vol. 16
Open Access | Times Cited: 23
The kinesin-3 KIF1C undergoes liquid-liquid phase separation for accumulation of specific transcripts at the cell periphery
Qi Geng, Jakia Jannat Keya, Takashi Hotta, et al.
The EMBO Journal (2024) Vol. 43, Iss. 15, pp. 3192-3213
Open Access | Times Cited: 7
Structural details of helix-mediated TDP-43 C-terminal domain multimerization
Azamat Rizuan, Jayakrishna Kanhangad Shenoy, Priyesh Mohanty, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 7
Dysregulation of Translation in TDP-43 Proteinopathies: Deficits in the RNA Supply Chain and Local Protein Production
Reed T. Bjork, Nicholas P. Mortimore, Suvithanandhini Loganathan, et al.
Frontiers in Neuroscience (2022) Vol. 16
Open Access | Times Cited: 28
Multivalent GU-rich oligonucleotides sequester TDP-43 in the nucleus by inducing high molecular weight RNP complexes
Xi Zhang, Tanuza Das, Tiffany F. Chao, et al.
iScience (2024) Vol. 27, Iss. 6, pp. 110109-110109
Open Access | Times Cited: 5
FUS fibrillation occurs through a nucleation-based process below the critical concentration required for liquid–liquid phase separation
E Bertrand, Clément Demongin, Ioana Dobra, et al.
Scientific Reports (2023) Vol. 13, Iss. 1
Open Access | Times Cited: 12
Aggregation of the amyloid-β peptide (Aβ40) within condensates generated through liquid–liquid phase separation
Owen M. Morris, Zenon Toprakcioglu, Alexander Röntgen, et al.
Scientific Reports (2024) Vol. 14, Iss. 1
Open Access | Times Cited: 4
RNA-binding deficient TDP-43 drives cognitive decline in a mouse model of TDP-43 proteinopathy
Julie Necarsulmer, Jeremy M. Simon, Baggio Evangelista, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 10
Long way up: rethink diseases in light of phase separation and phase transition
Mingrui Ding, Weifan Xu, Gaofeng Pei, et al.
Protein & Cell (2023) Vol. 15, Iss. 7, pp. 475-492
Open Access | Times Cited: 10
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