Type XI collagen is a heterotrimer with the composition (1a,2a,3a) retaining non-triple-helical domains

Type XI collagen is a heterotrimer with the composition (1a,2a,3a) retaining non-triple-helical domains

Morris, N.P.; Bachinger, H.P.ter

The Journal of Biological Chemistry 262: 345-50

1987

(PDF emailed within 1 workday: $29.90)

Accession: 018196244

Download citation: RIS BibTeX Text

Related references

Type XI collagen is a heterotrimer with the composition (1 alpha, 2 alpha, 3 alpha) retaining non-triple-helical domains. Journal of Biological Chemistry 262(23): 11345-11350, 1987

The cloning and sequencing of alpha 1 viii collagen complementary dnas demonstrate that type viii collagen is a short chain collagen and contains triple helical and carboxyl terminal non triple helical domains similar to those of type x collagen. Journal of Biological Chemistry 264(27): 16022-16029, 1989

The cloning and sequencing of alpha 1(VIII) collagen cDNAs demonstrate that type VIII collagen is a short chain collagen and contains triple-helical and carboxyl-terminal non-triple-helical domains similar to those of type X collagen. Journal of Biological Chemistry 264(27): 16022-16029, 1989

The cloning and sequencing of a1 (VIII) collagen cDNAs demonstrate that type VIII collagen is a short chain collagen and contains triple-helical and carboxyl-terminal non-triple-helical domains similar to those of type X collagen. The Journal of Biological Chemistry 264: 022-9, 1989

Does the triple helical domain of type I collagen encode molecular recognition and fiber assembly while telopeptides serve as catalytic domains? Effect of proteolytic cleavage on fibrillogenesis and on collagen-collagen interaction in fibers. Journal of Biological Chemistry 274(51): 36083-36088, 1999

Differences between the thermal stabilities of the three triple-helical domains of type IX collagen. Journal of Molecular Biology 277(1): 135-144, 1998

Structure of N-linked oligosaccharide chains in the triple-helical domains of human type VI and mouse type IV collagen. Matrix 11(5): 307-312, 1991

The a1 (VIII) collagen gene is homologous to the a1(X) collagen gene and contains a large exon encoding the entire triple helical and carboxyl-terminal non-triple helical domains of the a1(VIII) polypeptide. The Journal of Biological Chemistry 266: 08-13, 1991

The structure of avian type XII collagen. a1(XII) chains contain 190-kDa non-triple helical amino-terminal domains and form homotrimeric molecules. The Journal of Biological Chemistry 264: 150-6, 1989

Cysteine residues mark the C-terminal triple-helical/non-triple-helical junction in type III collagen. Hoppe-Seyler's Zeitschrift für Physiologische Chemie 357(11): 1663-1665, 1976

The alpha 1 (VIII) collagen gene is homologous to the alpha 1 (X) collagen gene and contains a large exon encoding the entire triple helical and carboxyl-terminal non-triple helical domains of the alpha 1 (VIII) polypeptide. Journal of Biological Chemistry 266(7): 4508-4513, 1991

The structure of avian type XII collagen. Alpha 1 (XII) chains contain 190-kDa non-triple helical amino-terminal domains and form homotrimeric molecules. Journal of Biological Chemistry 264(22): 13150-13156, 1989

Type XIII collagen forms homotrimers with three triple helical collagenous domains and its association into disulfide-bonded trimers is enhanced by prolyl 4-hydroxylase. Journal of Biological Chemistry 275(12): 8936-8944, 2000

Deletions and duplications of Gly-Xaa-Yaa triplet repeats in the triple helical domains of type I collagen chains disrupt helix formation and result in several types of osteogenesis imperfecta. Human Mutation 18(4): 319-326, 2001

The type X collagen gene. Intron sequences split the 5'-untranslated region and separate the coding regions for the non-collagenous amino-terminal and triple-helical domains. Journal of Biological Chemistry 263(34): 18378-18385, 1988

< Previous

∧ Chapter

Next >

© 2022 EurekaMag OÜ, Sakala 7-2, 10141 Tallinn, Estonia, Tel: +372 69 91692
Registry code: , Legal Entity Identifier (LEI): 984500A2C1AE68HDA873
Privacy · Disclaimer · Terms · Contact · 浙ICP备10204677号-1