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Aberrant Localization of FUS and TDP43 Is Associated with Misfolding of SOD1 in Amyotrophic Lateral Sclerosis

Overview of attention for article published in PLOS ONE, April 2012
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Title
Aberrant Localization of FUS and TDP43 Is Associated with Misfolding of SOD1 in Amyotrophic Lateral Sclerosis
Published in
PLOS ONE, April 2012
DOI 10.1371/journal.pone.0035050
Pubmed ID
Authors

Edward Pokrishevsky, Leslie I. Grad, Masoud Yousefi, Jing Wang, Ian R. Mackenzie, Neil R. Cashman

Abstract

Amyotrophic lateral sclerosis (ALS) is incurable and characterized by progressive paralysis of the muscles of the limbs, speech and swallowing, and respiration due to the progressive degeneration of voluntary motor neurons. Clinically indistinguishable ALS can be caused by genetic mutations of Cu/Zn superoxide dismutase (SOD1), TAR-DNA binding protein 43 (TDP43), or fused in sarcoma/translocated in liposarcoma (FUS/TLS), or can occur in the absence of known mutation as sporadic disease. In this study, we tested the hypothesis that FUS/TLS and TDP43 gain new pathogenic functions upon aberrant accumulation in the cytosol that directly or indirectly include misfolding of SOD1.

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Mendeley readers

The data shown below were compiled from readership statistics for 245 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Australia 2 <1%
Germany 1 <1%
Italy 1 <1%
United Kingdom 1 <1%
Belgium 1 <1%
Spain 1 <1%
United States 1 <1%
Unknown 237 97%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 50 20%
Researcher 38 16%
Student > Bachelor 34 14%
Student > Master 33 13%
Student > Doctoral Student 24 10%
Other 31 13%
Unknown 35 14%
Readers by discipline Count As %
Agricultural and Biological Sciences 90 37%
Biochemistry, Genetics and Molecular Biology 38 16%
Neuroscience 29 12%
Medicine and Dentistry 28 11%
Pharmacology, Toxicology and Pharmaceutical Science 5 2%
Other 14 6%
Unknown 41 17%