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LARGE can functionally bypass alpha-dystroglycan glycosylation defects in distinct congenital muscular dystrophies.

Barresi, Rita (author)
Michele, Daniel E (author)
Kanagawa, Motoi (author)
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Harper, Hollie A (author)
Dovico, Sherri A (author)
Satz, Jakob S (author)
Moore, Steven A (author)
Zhang, Wenli (author)
Schachter, Harry (author)
Dumanski, Jan P (author)
Uppsala universitet,Institutionen för genetik och patologi
Cohn, Ronald D (author)
Nishino, Ichizo (author)
Campbell, Kevin P (author)
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 (creator_code:org_t)
2004
2004
English.
In: Nat Med. - 1078-8956. ; 10:7, s. 696-703
  • Journal article (peer-reviewed)
Subject headings
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Keyword

Animals
Cytoskeletal Proteins/*metabolism
Dystroglycans
Gene Therapy
Glycosylation
Glycosyltransferases/*deficiency
Humans
Laminin/metabolism
Membrane Glycoproteins/*metabolism
Mice
Muscular Dystrophies/*congenital/genetics/therapy
N-Acetylglucosaminyltransferases/genetics/*physiology
Neoplasm Proteins/genetics/*physiology
Research Support; Non-U.S. Gov't
Research Support; U.S. Gov't; P.H.S.

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art (subject category)

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