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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:

Patient-derived frontotemporal lobar degeneration brain extracts induce formation and spreading of TDP-43 pathology in vivo
Sílvia Porta, Yan Xu, Clark R. Restrepo, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 205

Showing 1-25 of 205 citing articles:

Limbic-predominant age-related TDP-43 encephalopathy (LATE): consensus working group report
Peter T. Nelson, Dennis W. Dickson, John Q. Trojanowski, et al.
Brain (2019) Vol. 142, Iss. 6, pp. 1503-1527
Open Access | Times Cited: 1171
Protein transmission in neurodegenerative disease
Chao Peng, John Q. Trojanowski, Virginia M.‐Y. Lee
Nature Reviews Neurology (2020) Vol. 16, Iss. 4, pp. 199-212
Open Access | Times Cited: 481
Phase Separation and Neurodegenerative Diseases: A Disturbance in the Force
Aurélie Zbinden, Manuela Pérez‐Berlanga, Pierre De Rossi, et al.
Developmental Cell (2020) Vol. 55, Iss. 1, pp. 45-68
Open Access | Times Cited: 384
Propagation and spread of pathogenic protein assemblies in neurodegenerative diseases
Mathias Jucker, Lary C. Walker
Nature Neuroscience (2018) Vol. 21, Iss. 10, pp. 1341-1349
Open Access | Times Cited: 365
The role of TDP-43 mislocalization in amyotrophic lateral sclerosis
Terry R. Suk, Maxime W.C. Rousseaux
Molecular Neurodegeneration (2020) Vol. 15, Iss. 1
Open Access | Times Cited: 304
TDP-43 proteinopathies: a new wave of neurodegenerative diseases
Eva Maria Johanna de Boer, Viyanti K Orie, Timothy L. Williams, et al.
Journal of Neurology Neurosurgery & Psychiatry (2020) Vol. 92, Iss. 1, pp. 86-95
Open Access | Times Cited: 277
The role of TDP-43 propagation in neurodegenerative diseases: integrating insights from clinical and experimental studies
Myungjin Jo, Shinrye Lee, Yu‐Mi Jeon, et al.
Experimental & Molecular Medicine (2020) Vol. 52, Iss. 10, pp. 1652-1662
Open Access | Times Cited: 262
FUS and TDP-43 Phases in Health and Disease
Bede Portz, Bo Lim Lee, James Shorter
Trends in Biochemical Sciences (2021) Vol. 46, Iss. 7, pp. 550-563
Open Access | Times Cited: 230
Cryo-EM structures of four polymorphic TDP-43 amyloid cores
Qin Cao, David R. Boyer, M.R. Sawaya, et al.
Nature Structural & Molecular Biology (2019) Vol. 26, Iss. 7, pp. 619-627
Open Access | Times Cited: 228
Structure of pathological TDP-43 filaments from ALS with FTLD
Diana Arseni, Masato Hasegawa, Alexey G. Murzin, et al.
Nature (2021) Vol. 601, Iss. 7891, pp. 139-143
Open Access | Times Cited: 212
Motor Neuron Susceptibility in ALS/FTD
Audrey Ragagnin, Sina Shadfar, Marta Vidal, et al.
Frontiers in Neuroscience (2019) Vol. 13
Open Access | Times Cited: 173
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
Molecular pathology of neurodegenerative diseases by cryo-EM of amyloids
Sjors H. W. Scheres, Benjamin Falcon, Michel Goedert
Nature (2023) Vol. 621, Iss. 7980, pp. 701-710
Closed Access | Times Cited: 116
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
Genetics of amyotrophic lateral sclerosis: seeking therapeutic targets in the era of gene therapy
Naoki Suzuki, Ayumi Nishiyama, Hitoshi Warita, et al.
Journal of Human Genetics (2022) Vol. 68, Iss. 3, pp. 131-152
Open Access | Times Cited: 93
TDP-43 forms amyloid filaments with a distinct fold in type A FTLD-TDP
Diana Arseni, Renren Chen, Alexey G. Murzin, et al.
Nature (2023) Vol. 620, Iss. 7975, pp. 898-903
Open Access | Times Cited: 72
Frontotemporal lobar degeneration
Murray Grossman, William W. Seeley, Adam L. Boxer, et al.
Nature Reviews Disease Primers (2023) Vol. 9, Iss. 1
Closed Access | Times Cited: 69
Seeding the aggregation of TDP-43 requires post-fibrillization proteolytic cleavage
Senthil T. Kumar, Sergey Nazarov, Sílvia Porta, et al.
Nature Neuroscience (2023) Vol. 26, Iss. 6, pp. 983-996
Open Access | Times Cited: 44
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
Prion-Like Propagation of Protein Misfolding and Aggregation in Amyotrophic Lateral Sclerosis
Luke McAlary, Steven S. Plotkin, Justin J. Yerbury, et al.
Frontiers in Molecular Neuroscience (2019) Vol. 12
Open Access | Times Cited: 137
Genetic Convergence Brings Clarity to the Enigmatic Red Line in ALS
Casey Cook, Leonard Petrucelli
Neuron (2019) Vol. 101, Iss. 6, pp. 1057-1069
Open Access | Times Cited: 125
Patient-Tailored, Connectivity-Based Forecasts of Spreading Brain Atrophy
Jesse A. Brown, Jersey Deng, John Neuhaus, et al.
Neuron (2019) Vol. 104, Iss. 5, pp. 856-868.e5
Open Access | Times Cited: 109
Invited Review: The role of prion‐like mechanisms in neurodegenerative diseases
Zane Jaunmuktane, Sebastian Brandner
Neuropathology and Applied Neurobiology (2019) Vol. 46, Iss. 6, pp. 522-545
Open Access | Times Cited: 109
The basis of clinicopathological heterogeneity in TDP-43 proteinopathy
Ito Kawakami, Tetsuaki Arai, Masato Hasegawa
Acta Neuropathologica (2019) Vol. 138, Iss. 5, pp. 751-770
Open Access | Times Cited: 106
Detection of TAR DNA-binding protein 43 (TDP-43) oligomers as initial intermediate species during aggregate formation
Rachel L. French, Zachary R. Grese, Himani Aligireddy, et al.
Journal of Biological Chemistry (2019) Vol. 294, Iss. 17, pp. 6696-6709
Open Access | Times Cited: 105
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