An α2(I) glycine to aspartate substitution is responsible for the presence of a kink in type I collagen in a lethal case of Osteogenesis Imperfecta

Matrix Biology

Volumn 17, Issue 8-9, 1998, Pages 575-584

  Forlino, Antonella ^a   Keene, Douglas R ^b   Schmidt, Karen ^c   Marini, Joan C ^a,d  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

^b SHRINERS HOSPITAL FOR CHILDREN   (United States)

^c Rockford Memorial Hospital   (United States)

^d SCTD   (United States)

Author keywords

Extracellular matrix; Kink; Osteogenesis Imperfecta

Indexed keywords

ASPARTIC ACID; BIPYRIDINE; COLLAGEN TYPE 1; CYANOGEN BROMIDE; DNA; GLYCINE; MUTANT PROTEIN; PROCOLLAGEN; COLLAGEN;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; CASE REPORT; CONTROLLED STUDY; DNA POLYMORPHISM; ELECTRON MICROSCOPY; ELECTROPHORETIC MOBILITY; EXTRACELLULAR MATRIX; FATHER; FIBROBLAST CULTURE; HUMAN; HUMAN CELL; MOLECULAR CLONING; NUCLEOTIDE SEQUENCE; OSTEOGENESIS IMPERFECTA; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN CONFORMATION; SKIN FIBROBLAST; FATALITY; GENETICS; INFANT; MALE; PHYSIOLOGY;

AMINO ACID SUBSTITUTION; ASPARTIC ACID; COLLAGEN; FATAL OUTCOME; GLYCINE; HUMANS; INFANT; MALE; OSTEOGENESIS IMPERFECTA;

EID: 0032217327     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0945-053X(98)90109-3     Document Type: Article

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