Journal ArticleDOI
The Complete Sequence of Dystrophin Predicts a Rod-Shaped Cytoskeletal Protein
M. Koenig,M. Koenig,Anthony P. Monaco,Anthony P. Monaco,Louis M. Kunkel,Louis M. Kunkel,Louis M. Kunkel +6 more
TLDR
The complete sequence of the human Duchenne muscular dystrophy cDNA has been determined and dystrophin shares many features with the cytoskeletal protein spectrin and alpha-actinin and is likely to adopt a rod shape about 150 nm in length.About:
This article is published in Cell.The article was published on 1988-04-22. It has received 1506 citations till now. The article focuses on the topics: Dystrophin-associated protein complex & Utrophin.read more
Citations
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Journal ArticleDOI
Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix
Oxana Ibraghimov-Beskrovnaya,James M. Ervasti,Cynthia J. Leveille,Clive A. Slaughter,Suzanne W. Sernett,Kevin P. Campbell +5 more
TL;DR: The hypothesis that the dramatic reduction in the 156K DAG in Duchenne muscular dystrophy leads to a loss of a linkage between the sarcolemma and extra-cellular matrix and that this may render muscle fibres more susceptible to necrosis is supported.
Journal ArticleDOI
A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
TL;DR: The results support a role for the striated muscle dystrophin-glycoprotein complex in linking the actin- based cytoskeleton with the extracellular matrix and suggest that dystophin and dystroglycan may play substantially different functional roles in nonmuscle tissues.
Journal ArticleDOI
Membrane organization of the dystrophin-glycoprotein complex
TL;DR: It is demonstrated that dystrophin and its 59 kd associated protein are cytoskeletal elements that are tightly linked to a 156 kd extracellular glycoprotein by way of a complex of transmembrane proteins.
Journal ArticleDOI
The molecular basis of muscular dystrophy in the mdx mouse: a point mutation
Piotr Sicinski,Yan Geng,Allan S. Ryder-Cook,Eric A. Barnard,Mark G. Darlison,Pene J. Barnard +5 more
TL;DR: Sequence analysis of the amplification products showed that the mdx mouse has a single base substitution within an exon, which causes premature termination of the polypeptide chain.
Journal ArticleDOI
Function and genetics of dystrophin and dystrophin-related proteins in muscle
TL;DR: The role of the dystrophin complex and protein family in muscle is discussed and the physiological processes that are affected in Duchenne muscular dystrophy are described.
References
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Journal ArticleDOI
DNA sequencing with chain-terminating inhibitors
TL;DR: A new method for determining nucleotide sequences in DNA is described, which makes use of the 2',3'-dideoxy and arabinon nucleoside analogues of the normal deoxynucleoside triphosphates, which act as specific chain-terminating inhibitors of DNA polymerase.
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A simple method for displaying the hydropathic character of a protein
Jack Kyte,Russell F. Doolittle +1 more
TL;DR: A computer program that progressively evaluates the hydrophilicity and hydrophobicity of a protein along its amino acid sequence has been devised and its simplicity and its graphic nature make it a very useful tool for the evaluation of protein structures.
Journal ArticleDOI
A comprehensive set of sequence analysis programs for the VAX
TL;DR: A group of programs that will interact with each other has been developed for the Digital Equipment Corporation VAX computer using the VMS operating system.
Journal ArticleDOI
Identification of common molecular subsequences.
TL;DR: This letter extends the heuristic homology algorithm of Needleman & Wunsch (1970) to find a pair of segments, one from each of two long sequences, such that there is no other Pair of segments with greater similarity (homology).
Journal ArticleDOI
Dystrophin: The protein product of the duchenne muscular dystrophy locus
TL;DR: The identification of the mdx mouse as an animal model for DMD has important implications with regard to the etiology of the lethal DMD phenotype, and the protein dystrophin is named because of its identification via the isolation of the Duchenne muscular dystrophy locus.
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