Title |
Aberrant Localization of FUS and TDP43 Is Associated with Misfolding of SOD1 in Amyotrophic Lateral Sclerosis
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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. |
X Demographics
Geographical breakdown
Country | Count | As % |
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Egypt | 1 | 100% |
Demographic breakdown
Type | Count | As % |
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Practitioners (doctors, other healthcare professionals) | 1 | 100% |
Mendeley readers
Geographical breakdown
Country | Count | As % |
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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 % |
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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% |
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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% |