id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
work_wp5rzk3a2vcvpcxwhzc4zfdaem	Isabelle Richard	Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A	1995.0	14	.pdf	application/pdf	16434	2889	88	splice site, frameshift, or missense calpain mutations the rat CANP3 amino acid sequence (Sorimachi et al., hormones; Minty and Kedes, 1986), and four E boxes (contact sites for basic-helix-loop-helix proteins found in members of the MyoD family; Blackwell and Weintraub, 1990). factor-binding sites in the regulation of CANP3 gene expression remains to be established. The DNA and protein sequences of the human CANP3 A comparison of the published CANP3 human cDNA (Sodmachi et al., 1989) with the corresponding genomic sequence led to the identification of 24 exons ranging in CANP3 Mutations in LGMD2A Families The corresponding sequence from a normal muscular CANP3 cDNA the same exon 22 mutation as the Amish LGMD2A patients (see Figure 6), but embedded in a completely different haplotype (Allamand et al., 1995b). Only four different mutations were identified by heteroduplex and sequence analyses in the families of La R~ Mutations in CANP3 Cause LGMD2A 	./cache/work_wp5rzk3a2vcvpcxwhzc4zfdaem.pdf	./txt/work_wp5rzk3a2vcvpcxwhzc4zfdaem.txt