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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:

Gel‐like inclusions of C‐terminal fragments of TDP‐43 sequester stalled proteasomes in neurons
Henrick Riemenschneider, Qiang Guo, Jakob M. Bader, et al.
EMBO Reports (2022) Vol. 23, Iss. 6
Open Access | Times Cited: 44

Showing 1-25 of 44 citing articles:

Mechanisms and pathology of protein misfolding and aggregation
Nikolaos Louros, Joost Schymkowitz, Frédéric Rousseau
Nature Reviews Molecular Cell Biology (2023) Vol. 24, Iss. 12, pp. 912-933
Closed Access | Times Cited: 105
The Multiple Roles of Autophagy in Neural Function and Diseases
Yanyan Li, Zheng‐Hong Qin, Rui Sheng
Neuroscience Bulletin (2023) Vol. 40, Iss. 3, pp. 363-382
Open Access | Times Cited: 43
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: 22
Interplay of Proteostasis Capacity and Protein Aggregation: Implications for Cellular Function and Disease
Mark S. Hipp, F. Ulrich Hartl
Journal of Molecular Biology (2024) Vol. 436, Iss. 14, pp. 168615-168615
Open Access | Times Cited: 18
CryoET reveals organelle phenotypes in huntington disease patient iPSC-derived and mouse primary neurons
Gong‐Her Wu, Charlene Smith-Geater, Jesús G. Galaz-Montoya, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 40
Proteotoxic stress and the ubiquitin proteasome system
Rachel Kandel, Jasmine Jung, Sonya E. Neal
Seminars in Cell and Developmental Biology (2023) Vol. 156, pp. 107-120
Open Access | Times Cited: 36
Advanced Techniques for Detecting Protein Misfolding and Aggregation in Cellular Environments
Yulong Bai, Shengnan Zhang, Hui Dong, et al.
Chemical Reviews (2023) Vol. 123, Iss. 21, pp. 12254-12311
Closed Access | Times Cited: 26
Highly Charged Proteins and Their Repulsive Interactions Antagonize Biomolecular Condensation
Cheng Tan, Ai Niitsu, Yuji Sugita
JACS Au (2023) Vol. 3, Iss. 3, pp. 834-848
Open Access | Times Cited: 24
Integration of O-GlcNAc into Stress Response Pathways
Kamau Fahie, Kyriakos N. Papanicolaou, Natasha E. Zachara
Cells (2022) Vol. 11, Iss. 21, pp. 3509-3509
Open Access | Times Cited: 35
Metamorphism in TDP-43 prion-like domain determines chaperone recognition
Jaime Carrasco, Rosa Antón, Alejandro Valbuena, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 22
Targeting the glycine-rich domain of TDP-43 with antibodies prevents its aggregation in vitro and reduces neurofilament levels in vivo
Henrick Riemenschneider, Francesca Simonetti, Udit Sheth, et al.
Acta Neuropathologica Communications (2023) Vol. 11, Iss. 1
Open Access | Times Cited: 21
Molecular Chaperones’ Potential against Defective Proteostasis of Amyotrophic Lateral Sclerosis
Sumit Kinger, Ankur Rakesh Dubey, Prashant Kumar, et al.
Cells (2023) Vol. 12, Iss. 9, pp. 1302-1302
Open Access | Times Cited: 13
The Spectrum of Cognitive Dysfunction in Amyotrophic Lateral Sclerosis: An Update
K. A. Jellinger
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 19, pp. 14647-14647
Open Access | Times Cited: 12
TDP-43 seeding induces cytoplasmic aggregation heterogeneity and nuclear loss of function of TDP-43
JL Rummens, Bilal Khalil, Günseli Yıldırım, et al.
Neuron (2025)
Open Access
The Molecular Intersection of NEK1, C21ORF2, Cyclin F, and VCP in ALS Pathogenesis
Yasuaki Watanabe, Tadashi Nakagawa, Makiko Nakagawa, et al.
Genes (2025) Vol. 16, Iss. 4, pp. 407-407
Open Access
Hypothermia Shifts Neurodegeneration Phenotype in Neonatal Human Hypoxic–Ischemic Encephalopathy but Not in Related Piglet Models: Possible Relationship to Toxic Conformer and Intrinsically Disordered Prion-like Protein Accumulation
Lee J. Martin, Jennifer K. Lee, Mark V. Niedzwiecki, et al.
Cells (2025) Vol. 14, Iss. 8, pp. 586-586
Open Access
Molecular Investigations of Protein Aggregation in the Pathogenesis of Amyotrophic Lateral Sclerosis
Elisa Duranti, Chiara Villa
International Journal of Molecular Sciences (2022) Vol. 24, Iss. 1, pp. 704-704
Open Access | Times Cited: 18
Modulation of assembly of TDP-43 low-complexity domain by heparin: From droplets to amyloid fibrils
Dushyant Kumar Garg, Rajiv Bhat
Biophysical Journal (2022) Vol. 121, Iss. 13, pp. 2568-2582
Open Access | Times Cited: 17
Functional implication of ubiquitinating and deubiquitinating mechanisms in TDP-43 proteinopathies
Non-Nuoc Tran, Byung‐Hoon Lee
Frontiers in Cell and Developmental Biology (2022) Vol. 10
Open Access | Times Cited: 16
Structural polymorphism of the low-complexity C-terminal domain of TDP-43 amyloid aggregates revealed by solid-state NMR
Jayakrishna Shenoy, Alons Lends, Mélanie Berbon, et al.
Frontiers in Molecular Biosciences (2023) Vol. 10
Open Access | Times Cited: 10
Pathological Involvement of Protein Phase Separation and Aggregation in Neurodegenerative Diseases
Y. Wu, Biao Ma, Chang Yu Liu, et al.
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 18, pp. 10187-10187
Open Access | Times Cited: 3
New insights into the molecular architecture of neurons by cryo-electron tomography
Arsen Petrovic, Thanh Thao, Rubén Fernández‐Busnadiego
Current Opinion in Neurobiology (2024) Vol. 90, pp. 102939-102939
Open Access | Times Cited: 3
Looking for answers far away from the soma—the (un)known axonal functions of TDP-43, and their contribution to early NMJ disruption in ALS
Ariel Ionescu, Topaz Altman, Eran Perlson
Molecular Neurodegeneration (2023) Vol. 18, Iss. 1
Open Access | Times Cited: 9
Cellular liquid–liquid phase separation: Concept, functions, regulations, and detections
Xuanlin Che, Jiajun Wu, Hua Liu, et al.
Journal of Cellular Physiology (2023) Vol. 238, Iss. 5, pp. 847-865
Closed Access | Times Cited: 8
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