Post-translational modification of type IV collagen with 3-hydroxyproline affects its interactions with glycoprotein VI and nidogens 1 and 2-Reference-Cited by-同舟云学术

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Post-translational modification of type IV collagen with 3-hydroxyproline affects its interactions with glycoprotein VI and nidogens 1 and 2

Published:2018-04 Issue:16 Volume:293 Page:5987-5999
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Montgomery Nathan T.,Zientek Keith D.,Pokidysheva Elena N.,Bächinger Hans Peter

Funder

Shriners Hospitals for Children

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference40 articles.

1. Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta;Cabral;Nat. Genet,2007

2. Prolyl 4-hydroxylase;Gorres;Crit. Rev. Biochem. Mol. Biol,2010

3. Effect of the -Gly-3(S)-hydroxyprolyl-4(R)-hydroxyprolyl-tripeptide unit on the stability of collagen model peptides;Mizuno;FEBS J,2008

4. CRTAP is required for prolyl 3-hydroxylation and mutations cause recessive osteogenesis imperfecta;Morello;Cell,2006

5. PPIB mutations cause severe osteogenesis imperfecta;van Dijk;Am. J. Hum. Genet,2009

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