PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1953667-0	1991	Substitution of cysteine for glycine-alpha 1-691 in the pro alpha 1(I) chain of type I procollagen in a proband with lethal osteogenesis imperfecta destabilizes the triple helix at a site C-terminal to the substitution.	Glycine	29-36	collagen type I alpha 2 chain	Homo sapiens	80-98	
1953667-7	1991	Since the proteinase assay of helical stability generated a fragment of 700 residues that retained disulphide-bonded cysteine residues at alpha 1-691, the results provide one of the first indications that glycine substitutions in type I procollagen can alter the conformation of the triple helix at a site that is C-terminal to the site of the substitution.	Glycine	205-212	collagen type I alpha 2 chain	Homo sapiens	230-248