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The a1(VIII) and a2(VIII) chains of type VIII collagen can form stable homotrimeric molecules


The a1(VIII) and a2(VIII) chains of type VIII collagen can form stable homotrimeric molecules



The Journal of Biological Chemistry 273(34): 091-5




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Related references

The alpha1(VIII) and alpha2(VIII) chains of type VIII collagen can form stable homotrimeric molecules. Journal of Biological Chemistry 273(34): 22091-22095, 1998

The alpha1 and alpha2 chains of type VIII collagen can form stable homotrimeric molecules. Journal of Biological Chemistry 273(34): 22091-22095, 1998

The alpha1(VIII) and alpha2(VIII) collagen chains form two distinct homotrimeric proteins in vivo. Matrix Biology: Journal of the International Society for Matrix Biology 19(1): 19-28, 2000

Cloning and sequencing of alpha 1 viii collagen complementary dna type viii collagen contains a short triple helical domain similar to that of type x collagen. Fleischmajer, R , B R Olsen And K Kuehn (Ed ) Annals Of The New York Academy Of Sciences, Vol 580 Structure, Molecular Biology, And Pathology Of Collagen; Second New York Academy Of Sciences Conference on Collagen, Bethesda, Maryland, Usa, April 3-5, 1989 Xv+592p New York Academy Of Sciences: New York, New York, Usa Illus 433-435, 1990

Cloning and sequencing of α1 (VIII) collagen cDNAs : type VIII collagen contains a short triple-helical domain similar to that of type X collagen. New York Academy of Sciences Conference 2 580: 433-435, 1990

Altered serum factor VIII-related antigen (VIII : AGN)/von Willebrand factor (VIII : vWf) in haemophiliacs with inhibitors to factor VIII procoagulant activity (VIII : C). Thrombosis and Haemostasis 45(1): 68-72, 1981

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

Alpha 1 viii and alpha 2 viii collagen chains major constituents of descemets membrane are encoded by genes located on the human chromosomes 3 and 1. IOVS Investigative Ophthalmology and Visual Science 32(4): 1140, 1991

The cloning and sequencing of α1(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(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

Chalcolithic and early bronze age pottery and other finds from Caves VIII/9 and VIII/28 - La céramique du Chalcolithique et de l'Age du Bronze ancien ainsi que d'autres découvertes provenant des grottes VIII/9 et VIII/28. ‘atiqot (Jerusalem 1991) 41: 129-141, 2002

Von Willebrand's disease: studies of platelet functions, factor VIII procoagulant activity (F VIII C) and factor VIII-related antigen (F VIII RAg) in three families. Southeast Asian Journal of Tropical Medicine and Public Health 10(2): 243-247, 1979

Recombinant alpha 1(VIII) collagen chains form homotrimers in vitro. Biochemical and Biophysical Research Communications 227(1): 205-210, 1996

Porzellane hoher Festigkeit. VIII - Porcelaine à haute résistance. VIII - High-strength porcelain. VIII. Sprechsaal (1976) 122(3): 246-251, 1989