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

Volumn 275, Issue 12, 2000, Pages 8936-8944

  Snellman, Anne ^a   Keränen, Marja Riitta ^a   Hägg, Pasi O ^a   Lamberg, Arja ^a   Hiltunen, J Kalervo ^a   Kivirikko, Kari I ^a   Pihlajaniemi, Taina ^a  

^a UNIVERSITY OF OULU   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

CHYMOTRYPSIN; COLLAGEN TYPE 13; COMPLEMENTARY DNA; CYSTEINE; MEMBRANE PROTEIN; MESSENGER RNA; PEPSIN A; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; PROLINE; TRYPSIN;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DISULFIDE BOND; HYDROXYLATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN POLYMERIZATION; THERMOSTABILITY;

ANIMALS; ANTIBODY SPECIFICITY; CHYMOTRYPSIN; COLLAGEN; CYSTINE; HEAT; HUMANS; HYDROXYLATION; MEMBRANE PROTEINS; NUCLEOPOLYHEDROVIRUS; PROCOLLAGEN-PROLINE DIOXYGENASE; PROTEIN DENATURATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SPODOPTERA; TRYPSIN;

ANIMALIA; INSECTA;

EID: 0039599048     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.275.12.8936     Document Type: Article

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