Extensive homology between the carboxyl-terminal peptides of mouse alpha 1(IV) and alpha 2(IV) collagen.
Open Access
- 1 June 1987
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 262 (18) , 8496-8499
- https://doi.org/10.1016/s0021-9258(18)47441-8
Abstract
No abstract availableThis publication has 30 references indexed in Scilit:
- Structure of mouse type IV collagen. Amino-acid sequence of the C-terminal 511-residue-long triple-helical segment of the alpha2(IV) chain and its comparison with the alpha1(IV) chainEuropean Journal of Biochemistry, 1986
- Isolation and Characterization of the Human Fibrillar Collagen GenesaAnnals of the New York Academy of Sciences, 1985
- Synthesis of [pro-.alpha.1(IV)]3 collagen molecules by cultured embryo-derived parietal yolk sac cellsBiochemistry, 1985
- Characterization of 64-, 123- and 182-base-pair exons in the mouse α2(IV) collagen geneNature, 1985
- Amino acid sequence of the non‐collagenous globular domain (NC1) of the α1 (IV) chain of basement membrane collagen as derived from complementary DNAEuropean Journal of Biochemistry, 1985
- Structure of human‐basement‐membrane (type IV) collagenEuropean Journal of Biochemistry, 1984
- Heritable Diseases of CollagenNew England Journal of Medicine, 1984
- Conservation of the sizes for one but not another class of exons in two chick collagen genesNature, 1984
- Self-assembly of basement membrane collagenBiochemistry, 1984
- Subunit structure and assembly of the globular domain of basement-membrane collagen type IVEuropean Journal of Biochemistry, 1984