Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

TDP-43 enhances translation of specific mRNAs linked to neurodegenerative disease
Nagammal Neelagandan, Giorgio Gonnella, Stefan Dang, et al.
Nucleic Acids Research (2018) Vol. 47, Iss. 1, pp. 341-361
Open Access | Times Cited: 53

Showing 1-25 of 53 citing articles:

ALS Genetics: Gains, Losses, and Implications for Future Therapies
Garam Kım, Olivia Gautier, Eduardo Tassoni-Tsuchida, et al.
Neuron (2020) Vol. 108, Iss. 5, pp. 822-842
Open Access | Times Cited: 292
Cytoplasmic functions of TDP-43 and FUS and their role in ALS
Nicol Birsa, Matthew P. Bentham, Pietro Fratta
Seminars in Cell and Developmental Biology (2019) Vol. 99, pp. 193-201
Open Access | Times Cited: 104
RNA-binding proteins in neurological development and disease
Shavanie Prashad, Pallavi P. Gopal
RNA Biology (2020) Vol. 18, Iss. 7, pp. 972-987
Open Access | Times Cited: 93
RNA-binding proteins balance brain function in health and disease
Rico Schieweck, Jovica Ninkovic, Michael Kiebler
Physiological Reviews (2020) Vol. 101, Iss. 3, pp. 1309-1370
Open Access | Times Cited: 78
Emerging Evidence of Translational Control by AU-Rich Element-Binding Proteins
Hiroshi Otsuka, Akira Fukao, Yoshinori Funakami, et al.
Frontiers in Genetics (2019) Vol. 10
Open Access | Times Cited: 77
Dysregulation of RNA-Binding Proteins in Amyotrophic Lateral Sclerosis
Yuan Chao Xue, Chen Seng Ng, Pinhao Xiang, et al.
Frontiers in Molecular Neuroscience (2020) Vol. 13
Open Access | Times Cited: 72
Molecular Mechanisms Underlying TDP-43 Pathology in Cellular and Animal Models of ALS and FTLD
Alistair Wood, Yuval Gurfinkel, Nicole Polain, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 9, pp. 4705-4705
Open Access | Times Cited: 69
Lost in local translation: TDP-43 and FUS in axonal/neuromuscular junction maintenance and dysregulation in amyotrophic lateral sclerosis
Diana Piol, Tessa Robberechts, Sandrine Da Cruz
Neuron (2023) Vol. 111, Iss. 9, pp. 1355-1380
Open Access | Times Cited: 26
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: 1
Loss of TDP-43 in astrocytes leads to motor deficits by triggering A1-like reactive phenotype and triglial dysfunction
Audrey Yi Tyan Peng, Ira Agrawal, Wan Yun Ho, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 46, pp. 29101-29112
Open Access | Times Cited: 58
The Role of VCP Mutations in the Spectrum of Amyotrophic Lateral Sclerosis—Frontotemporal Dementia
Eveljn Scarian, Giuseppe Fiamingo, Luca Diamanti, et al.
Frontiers in Neurology (2022) Vol. 13
Open Access | Times Cited: 32
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
TDP-43 dysfunction restricts dendritic complexity by inhibiting CREB activation and altering gene expression
Josiah J. Herzog, Weijin Xu, Mugdha Deshpande, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 21, pp. 11760-11769
Open Access | Times Cited: 41
Loss of TDP-43 function underlies hippocampal and cortical synaptic deficits in TDP-43 proteinopathies
Jiangxia Ni, Yongfei Ren, Tonghui Su, et al.
Molecular Psychiatry (2021) Vol. 28, Iss. 2, pp. 931-945
Closed Access | Times Cited: 36
Integrated Omic Analysis Delineates Pathways Modulating Toxic TDP-43 Protein Aggregates in Amyotrophic Lateral Sclerosis
R. Saiswaroop, Akhil P. Soman, Sai Phalguna Kanikaram, et al.
Cells (2023) Vol. 12, Iss. 9, pp. 1228-1228
Open Access | Times Cited: 13
Translation dysregulation in neurodegenerative diseases: a focus on ALS
ShaoPeng Wang, Shuying Sun
Molecular Neurodegeneration (2023) Vol. 18, Iss. 1
Open Access | Times Cited: 13
Global cataloguing of variations in untranslated regions of viral genome and prediction of key host RNA binding protein-microRNA interactions modulating genome stability in SARS-CoV-2
Moumita Mukherjee, Srikanta Goswami
PLoS ONE (2020) Vol. 15, Iss. 8, pp. e0237559-e0237559
Open Access | Times Cited: 37
Expanding the TDP-43 Proteinopathy Pathway From Neurons to Muscle: Physiological and Pathophysiological Functions
Lauren Versluys, Pedro Ervilha Pereira, Nika Schuermans, et al.
Frontiers in Neuroscience (2022) Vol. 16
Open Access | Times Cited: 19
Current insights in the molecular genetic pathogenesis of amyotrophic lateral sclerosis
Zhou Wan, Renshi Xu
Frontiers in Neuroscience (2023) Vol. 17
Open Access | Times Cited: 11
Integrated multi-omic data analysis and validation with yeast model show oxidative phosphorylation modulates protein aggregation in amyotrophic lateral sclerosis
R. Sai Swaroop, P. S. Akhil, Sai Sanwid Pradhan, et al.
Journal of Biomolecular Structure and Dynamics (2022) Vol. 41, Iss. 12, pp. 5548-5567
Closed Access | Times Cited: 16
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
Protein Translation in the Pathogenesis of Parkinson’s Disease
Daniyal Ashraf, Mohammed Repon Khan, Ted M. Dawson, et al.
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 4, pp. 2393-2393
Open Access | Times Cited: 3
Cytoplasmic TDP-43 is involved in cell fate during stress recovery
Youn‐Bok Lee, Emma L. Scotter, Do-Young Lee, et al.
Human Molecular Genetics (2021) Vol. 31, Iss. 2, pp. 166-175
Open Access | Times Cited: 20
The tweety Gene Family: From Embryo to Disease
Rithvik Nalamalapu, Michelle Yue, Aaron R. Stone, et al.
Frontiers in Molecular Neuroscience (2021) Vol. 14
Open Access | Times Cited: 19
TDP-43 proteinopathy alters the ribosome association of multiple mRNAs including the glypican Dally-like protein (Dlp)/GPC6
Erik M. Lehmkuhl, Suvithanandhini Loganathan, Eric Alsop, et al.
Acta Neuropathologica Communications (2021) Vol. 9, Iss. 1
Open Access | Times Cited: 15
Page 1 - Next Page

Scroll to top