Publication Type:

Journal Article

Source:

Advances in Experimental Medicine and Biology, Volume 685, p.9-20 (2010)

ISBN:

9781441964472

URL:

http://www.scopus.com/inward/record.url?eid=2-s2.0-77955889112&partnerID=40&md5=b744408158b832f124107ca13b5a64bf

Keywords:

amyotrophic lateral sclerosis, article, clinical feature, copper zinc superoxide dismutase, DNA synthesis, gene mutation, human, molecular genetics, priority journal, protein aggregation, protein function, protein FUS, Protein Structure, protein TLS, riluzole, RNA synthesis, TAR DNA binding protein, tumor protein, unclassified drug

Abstract:

Abstract Amyotrophic lateral sclerosis (ALS) is a common neurological disorder that results in loss of motor neurons, leading to a rapidly progressive form of muscle paralysis that is fatal. There is no available cure and current therapies only provide minimal benefit at best. The disease is predominantly sporadic and until very recently only the Cu,Zn superoxide dismutase (Cu,ZnSOD), which is involved in a small number of sporadic cases and a larger component of familial ones, have been analyzed in any detail. Here we describe the clinical aspects of ALS and highlight the genetics and molecular mechanisms behind the disease. We discuss the current understanding and controversies of how mutations in Cu,ZnSOD may cause the disease. We also focus on the recent discovery that mutations in either TDP-43 or FUS/TLS, which are both involved in DNA/RNA synthesis, are likely the cause behind many cases of ALS that are not linked to Cu,ZnSOD. © 2010 Landes Bioscience and Springer Science+Business Media.

Notes:

cited By (since 1996)18

Cite this Research Publication

J. J. Pab Perry, Shin, D. Sc, and Tainer, J. Ac, “Amyotrophic lateral sclerosis”, Advances in Experimental Medicine and Biology, vol. 685, pp. 9-20, 2010.