Abnormal extracellular matrix in Ehlers-Danlos syndrome type IV due to the substitution of glycine 934 by glutamic acid in the triple helical domain of type III collagen

Clinical Genetics

Volumn 50, Issue 6, 1996, Pages 442-445

  McGrory, J ^a   Weksberg, R ^a   Thorner, P ^a   Cole, W G ^a  

^a HOSPITAL FOR SICK CHILDREN   (Canada)

Author keywords

Analysis; Conformation; Detection; Mutation; Polymorphism; Single strand

Indexed keywords

COLLAGEN TYPE 3; COMPLEMENTARY DNA; GLUTAMIC ACID; GLYCINE;

ADULT; AMINO ACID SUBSTITUTION; ARTICLE; CASE REPORT; COLLAGEN DISEASE; DERMIS; DNA DETERMINATION; DNA SEQUENCE; EHLERS DANLOS SYNDROME; ENDOPLASMIC RETICULUM; EXON; EXTRACELLULAR MATRIX; FEMALE; FIBROBLAST CULTURE; HUMAN; HUMAN CELL; PRIORITY JOURNAL; SINGLE STRAND CONFORMATION POLYMORPHISM; TRIPLE HELIX;

EID: 0030453694     PISSN: 00099163     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1399-0004.1996.tb02709.x     Document Type: Article

References (13)

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10. Madhatheri S, Tromp G, Gustavson K-H, Kuivaniemi H. Substitution of glutamic acid for glycine 589 in the triple-helical domain of type III procollagen (COL3A1 ) in a family with variable phenotype of the Ehlers-Danlos syndrome type IV. Hum Mol Genet 1994: 3: 511-512.
11. Narcisi P, Wu Y, Tromp G, Earley JJ, Richards AJ, Pope FM, Kuivaniemi H. Single base mutation that substitutes glutamic acid for glycine 1021 in the COL3A1 gene and causes Ehlers-Danlos syndrome type IV. Am J Med Genet 1993: 46: 278-283.
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