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:

TDP‐43 and FUS en route from the nucleus to the cytoplasm
Helena Ederle, Dorothee Dormann
FEBS Letters (2017) Vol. 591, Iss. 11, pp. 1489-1507
Open Access | Times Cited: 150

Showing 1-25 of 150 citing articles:

Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis
A. Aditya Prasad, Vidhya Bharathi, Vishwanath Sivalingam, et al.
Frontiers in Molecular Neuroscience (2019) Vol. 12
Open Access | Times Cited: 636

Nuclear Import Receptor Inhibits Phase Separation of FUS through Binding to Multiple Sites
Takuya Yoshizawa, Rustam Ali, Jenny Jiou, et al.
Cell (2018) Vol. 173, Iss. 3, pp. 693-705.e22
Open Access | Times Cited: 303

Triad of TDP43 control in neurodegeneration: autoregulation, localization and aggregation
Paraskevi Tziortzouda, Ludo Van Den Bosch, Frank Hirth
Nature reviews. Neuroscience (2021) Vol. 22, Iss. 4, pp. 197-208
Closed Access | Times Cited: 174

The interface of condensates of the hnRNPA1 low-complexity domain promotes formation of amyloid fibrils
Miriam Linsenmeier, Lenka Faltova, Chiara Morelli, et al.
Nature Chemistry (2023) Vol. 15, Iss. 10, pp. 1340-1349
Open Access | Times Cited: 80

TDP-43 extracted from frontotemporal lobar degeneration subject brains displays distinct aggregate assemblies and neurotoxic effects reflecting disease progression rates
Florent Laferrière, Zuzanna Maniecka, Manuela Pérez‐Berlanga, et al.
Nature Neuroscience (2018) Vol. 22, Iss. 1, pp. 65-77
Open Access | Times Cited: 155

Mice with endogenous TDP ‐43 mutations exhibit gain of splicing function and characteristics of amyotrophic lateral sclerosis
Pietro Fratta, Prasanth Sivakumar, Jack Humphrey, et al.
The EMBO Journal (2018) Vol. 37, Iss. 11
Open Access | Times Cited: 148

Review: Neuropathology of non‐tau frontotemporal lobar degeneration
Manuela Neumann, Ian R. Mackenzie
Neuropathology and Applied Neurobiology (2018) Vol. 45, Iss. 1, pp. 19-40
Closed Access | Times Cited: 123

ALS-linked FUS mutations confer loss and gain of function in the nucleus by promoting excessive formation of dysfunctional paraspeckles
Haiyan An, Lucy Skelt, Antonietta Notaro, et al.
Acta Neuropathologica Communications (2019) Vol. 7, Iss. 1
Open Access | Times Cited: 122

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: 106

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

TDP-43 and Tau Oligomers in Alzheimer's Disease, Amyotrophic Lateral Sclerosis, and Frontotemporal Dementia
Mauro Montalbano, Salomé McAllen, Filippa Lo Cascio, et al.
Neurobiology of Disease (2020) Vol. 146, pp. 105130-105130
Open Access | Times Cited: 73

Nuclear RNA binding regulates TDP-43 nuclear localization and passive nuclear export
Lauren Duan, Benjamin L. Zaepfel, Vasilisa Aksenova, et al.
Cell Reports (2022) Vol. 40, Iss. 3, pp. 111106-111106
Open Access | Times Cited: 69

Nearly 30 Years of Animal Models to Study Amyotrophic Lateral Sclerosis: A Historical Overview and Future Perspectives
Tiziana Bonifacino, Roberta Arianna Zerbo, Matilde Balbi, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 22, pp. 12236-12236
Open Access | Times Cited: 64

Cell environment shapes TDP-43 function with implications in neuronal and muscle disease
Urša Šušnjar, Neva Škrabar, Anna‐Leigh Brown, et al.
Communications Biology (2022) Vol. 5, Iss. 1
Open Access | Times Cited: 41

Molecular mechanisms of amyloid formation in living systems
Tessa Sinnige
Chemical Science (2022) Vol. 13, Iss. 24, pp. 7080-7097
Open Access | Times Cited: 41

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

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

Targeting 14-3-3θ-mediated TDP-43 pathology in amyotrophic lateral sclerosis and frontotemporal dementia mice
Yazi D. Ke, Annika van Hummel, Carol G. Au, et al.
Neuron (2024) Vol. 112, Iss. 8, pp. 1249-1264.e8
Closed Access | Times Cited: 10

The potential mechanism maintaining transactive response DNA binding protein 43kDa in the mouse stroke model
Yuting Bian, Yusuke Fukui, Ricardo Satoshi Ota-Elliott, et al.
Neuroscience Research (2025)
Open Access | Times Cited: 1

A feedback loop between dipeptide-repeat protein, TDP-43 and karyopherin-α mediates C9orf72-related neurodegeneration
Daniel A. Solomon, Alan Stepto, Wing Hei Au, et al.
Brain (2018) Vol. 141, Iss. 10, pp. 2908-2924
Open Access | Times Cited: 78

C9orf72-FTD/ALS pathogenesis: evidence from human neuropathological studies
Sarat C. Vatsavayai, Alissa L. Nana, Jennifer S. Yokoyama, et al.
Acta Neuropathologica (2018) Vol. 137, Iss. 1, pp. 1-26
Open Access | Times Cited: 67

Cell‐to‐cell transmission of C9orf72 poly‐(Gly‐Ala) triggers key features of ALS / FTD
Bahram Khosravi, Kathrine D LaClair, Henrick Riemenschneider, et al.
The EMBO Journal (2020) Vol. 39, Iss. 8
Open Access | Times Cited: 64

mRNP assembly, axonal transport, and local translation in neurodegenerative diseases
Bilal Khalil, Dmytro Morderer, Phillip L. Price, et al.
Brain Research (2018) Vol. 1693, pp. 75-91
Open Access | Times Cited: 61

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: 61

FUS-ALS mutants alter FMRP phase separation equilibrium and impair protein translation
Nicol Birsa, Agnieszka M Ule, Maria Giovanna Garone, et al.
Science Advances (2021) Vol. 7, Iss. 30
Open Access | Times Cited: 53

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