Literature DB >> 4371812

Biosynthesis of cartilage procollagen. Influence of chain association and hydroxylation of prolyl residues on the folding of the polypeptides into the triple-helical conformation.

J Uitto, D J Prockop.   

Abstract

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Year:  1974        PMID： 4371812     DOI： 10.1021/bi00719a018

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


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  11 in total

1.  Biochemical characteristics and biological significance of the genetically-distinct collagens.

Authors:  E J Miller
Journal:  Mol Cell Biochem       Date:  1976-12-10       Impact factor: 3.396

2.  The disulphide-bonded nature of procollagen and the role of the extension peptides in the assembly of the molecule.

Authors:  R Harwood; A H Merry; D E Woolley; M E Grant; D S Jackson
Journal:  Biochem J       Date:  1977-02-01       Impact factor: 3.857

3.  Underhydroxylated minor cartilage collagen precursors cannot form stable triple helices.

Authors:  C C Clark; C F Richards
Journal:  Biochem J       Date:  1988-02-15       Impact factor: 3.857

4.  Hydroxylation of lysine and glycosylation of hydroxylysine during collagen biosynthesis in isolated chick-embryo cartilage cells.

Authors:  A Oikarinen; H Anttinen; K I Kivirikko
Journal:  Biochem J       Date:  1976-06-15       Impact factor: 3.857

5.  Amino acid sequence of the N-terminal 108 amino acid residues of the B chain of subcomponent C1q of the first component of human complement.

Authors:  K B Reid; E O Thompson
Journal:  Biochem J       Date:  1978-09-01       Impact factor: 3.857

6.  The subcellular fractionation of embryonic chick tendon and cartilage cells: a re-examination.

Authors:  M E Grant; D S Jackson
Journal:  Biochem J       Date:  1979-05-15       Impact factor: 3.857

7.  Abnormal properties of collagen lysyl hydroxylase from skin fibroblasts of siblings with hydroxylysine-deficient collagen.

Authors:  R S Quinn; S M Krane
Journal:  J Clin Invest       Date:  1976-01       Impact factor: 14.808

8.  Kniest dysplasia is characterized by an apparent abnormal processing of the C-propeptide of type II cartilage collagen resulting in imperfect fibril assembly.

Authors:  A R Poole; I Pidoux; A Reiner; L Rosenberg; D Hollister; L Murray; D Rimoin
Journal:  J Clin Invest       Date:  1988-02       Impact factor: 14.808

9.  Chondrocalcin is identical with the C-propeptide of type II procollagen.

Authors:  M Van der Rest; L C Rosenberg; B R Olsen; A R Poole
Journal:  Biochem J       Date:  1986-08-01       Impact factor: 3.857

10.  Effect of prevention of procollagen triple-helix formation on proline 3-hydroxylation in freshly isolated chick-embryo tendon cells.

Authors:  K Majamaa
Journal:  Biochem J       Date:  1981-04-15       Impact factor: 3.857
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