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:

Pathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disorders
Jonathan Janssens, Christine Van Broeckhoven
Human Molecular Genetics (2013) Vol. 22, Iss. R1, pp. R77-R87
Open Access | Times Cited: 133

Showing 1-25 of 133 citing articles:

Alternative splicing as a regulator of development and tissue identity
Francisco E. Baralle, Jimena Giudice
Nature Reviews Molecular Cell Biology (2017) Vol. 18, Iss. 7, pp. 437-451
Open Access | Times Cited: 1116

TDP-43 repression of nonconserved cryptic exons is compromised in ALS-FTD
Jonathan P. Ling, Olga Pletniková, Juan C. Troncoso, et al.
Science (2015) Vol. 349, Iss. 6248, pp. 650-655
Open Access | Times Cited: 524

RNA Binding Antagonizes Neurotoxic Phase Transitions of TDP-43
Jacob R. Mann, Amanda M. Gleixner, Jocelyn C. Mauna, et al.
Neuron (2019) Vol. 102, Iss. 2, pp. 321-338.e8
Open Access | Times Cited: 481

An acetylation switch controls TDP-43 function and aggregation propensity
Todd J. Cohen, Andrew Hwang, Clark R. Restrepo, et al.
Nature Communications (2015) Vol. 6, Iss. 1
Open Access | Times Cited: 294

Human C9ORF72 Hexanucleotide Expansion Reproduces RNA Foci and Dipeptide Repeat Proteins but Not Neurodegeneration in BAC Transgenic Mice
Owen M. Peters, Gabriela Toro Cabrera, Hélène Tran, et al.
Neuron (2015) Vol. 88, Iss. 5, pp. 902-909
Open Access | Times Cited: 244

Genetics of Amyotrophic Lateral Sclerosis
Mehdi Ghasemi, Robert H. Brown
Cold Spring Harbor Perspectives in Medicine (2017) Vol. 8, Iss. 5, pp. a024125-a024125
Open Access | Times Cited: 225

Defective control of pre–messenger RNA splicing in human disease
Benoı̂t Chabot, Lulzim Shkreta
The Journal of Cell Biology (2016) Vol. 212, Iss. 1, pp. 13-27
Open Access | Times Cited: 203

Common pathobiochemical hallmarks of progranulin-associated frontotemporal lobar degeneration and neuronal ceroid lipofuscinosis
Julia K Götzl, Kohji Mori, Markus Daμμe, et al.
Acta Neuropathologica (2014)
Closed Access | Times Cited: 188

Retrotransposon activation contributes to neurodegeneration in a Drosophila TDP-43 model of ALS
Lisa Krug, Nabanita Chatterjee, Rebeca Borges-Monroy, et al.
PLoS Genetics (2017) Vol. 13, Iss. 3, pp. e1006635-e1006635
Open Access | Times Cited: 185

Futsch/MAP1B mRNA Is a Translational Target of TDP-43 and Is Neuroprotective in aDrosophilaModel of Amyotrophic Lateral Sclerosis
Alyssa N. Coyne, Bhavani B. Siddegowda, Patricia S. Estes, et al.
Journal of Neuroscience (2014) Vol. 34, Iss. 48, pp. 15962-15974
Open Access | Times Cited: 143

Ubiquitin pathways in neurodegenerative disease
Graham Atkin, Henry L. Paulson
Frontiers in Molecular Neuroscience (2014) Vol. 7
Open Access | Times Cited: 136

Functional roles of alternative splicing factors in human disease
Benjamin Cieply, Russ P. Carstens
Wiley Interdisciplinary Reviews - RNA (2015) Vol. 6, Iss. 3, pp. 311-326
Open Access | Times Cited: 130

TDP-43-mediated neurodegeneration: towards a loss-of-function hypothesis?
Lies Vanden Broeck, Patrick Callaerts, Bart Dermaut
Trends in Molecular Medicine (2013) Vol. 20, Iss. 2, pp. 66-71
Open Access | Times Cited: 125

In vitro prion-like behaviour of TDP-43 in ALS
Phillip Smethurst, Jia Newcombe, Claire Troakes, et al.
Neurobiology of Disease (2016) Vol. 96, pp. 236-247
Open Access | Times Cited: 124

Structural Insights Into TDP-43 and Effects of Post-translational Modifications
Liberty François‐Moutal, Samantha Perez‐Miller, David D. Scott, et al.
Frontiers in Molecular Neuroscience (2019) Vol. 12
Open Access | Times Cited: 123

Two familial ALS proteins function in prevention/repair of transcription-associated DNA damage
Sarah J. Hill, Daniel A. Mordes, Lisa Cameron, et al.
Proceedings of the National Academy of Sciences (2016) Vol. 113, Iss. 48
Open Access | Times Cited: 122

Role of mitochondria in mutant SOD1 linked amyotrophic lateral sclerosis
Wenzhi Tan, Piera Pasinelli, Davide Trotti
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (2014) Vol. 1842, Iss. 8, pp. 1295-1301
Open Access | Times Cited: 104

The cleavage pattern of TDP-43 determines its rate of clearance and cytotoxicity
Quan Li, Moe Yokoshi, Hitomi Okada, et al.
Nature Communications (2015) Vol. 6, Iss. 1
Open Access | Times Cited: 103

NF-κB and IRF1 Induce Endogenous Retrovirus K Expression via Interferon-Stimulated Response Elements in Its 5′ Long Terminal Repeat
Mamneet Manghera, Jennifer Ferguson-Parry, Rongtuan Lin, et al.
Journal of Virology (2016) Vol. 90, Iss. 20, pp. 9338-9349
Open Access | Times Cited: 103

Loss of function CHCHD10 mutations in cytoplasmic TDP-43 accumulation and synaptic integrity
Jung A. Woo, Tian Liu, Courtney Trotter, et al.
Nature Communications (2017) Vol. 8, Iss. 1
Open Access | Times Cited: 101

Development of disease-modifying drugs for frontotemporal dementia spectrum disorders
Francesco Panza, Madia Lozupone, Davide Seripa, et al.
Nature Reviews Neurology (2020) Vol. 16, Iss. 4, pp. 213-228
Closed Access | Times Cited: 97

Prion-like Mechanism in Amyotrophic Lateral Sclerosis: are Protein Aggregates the Key?
Shynrye Lee, Hyung‐Jun Kim
Experimental Neurobiology (2015) Vol. 24, Iss. 1, pp. 1-7
Open Access | Times Cited: 95

Frontotemporal Lobar Degeneration: A Clinical Approach
Elissaios Karageorgiou, Bruce Miller
Seminars in Neurology (2014) Vol. 34, Iss. 02, pp. 189-201
Open Access | Times Cited: 95

Fragile X protein mitigates TDP-43 toxicity by remodeling RNA granules and restoring translation
Alyssa N. Coyne, Shizuka Yamada, Bhavani B. Siddegowda, et al.
Human Molecular Genetics (2015), pp. ddv389-ddv389
Open Access | Times Cited: 91

Review: Prion‐like mechanisms of transactive response DNA binding protein of 43 kDa (TDP‐43) in amyotrophic lateral sclerosis (ALS)
Phillip Smethurst, Katie Claire Louise Sidle, John Hardy
Neuropathology and Applied Neurobiology (2014) Vol. 41, Iss. 5, pp. 578-597
Closed Access | Times Cited: 87

Page 1 - Next Page

Scroll to top