Procollagen Triple Helix Assembly: An Unconventional Chaperone-Assisted Folding Paradigm-Reference-Cited by-同舟云学术

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Procollagen Triple Helix Assembly: An Unconventional Chaperone-Assisted Folding Paradigm

Published:2007-10-10 Issue:10 Volume:2 Page:e1029
ISSN:1932-6203
Container-title:PLoS ONE
language:en
Short-container-title:PLoS ONE

Author:

Makareeva Elena,Leikin Sergey

Publisher

Public Library of Science (PLoS)

Subject

Multidisciplinary

Reference56 articles.

1. Collagens: molecular biology, diseases, and potentials for therapy.;DJ Prockop;Annu Rev Biochem,1995

2. Folding defects in fibrillar collagens.;PH Byers;Philos Trans R Soc Lond B Biol Sci,2001

3. Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans.;JC Marini;Hum Mutat,2007

4. Procollagen folding and assembly: the role of endoplasmic reticulum enzymes and molecular chaperones.;SR Lamande;Semin Cell Dev Biol,1999

5. HSP47 as a collagen-specific molecular chaperone: function and expression in normal mouse development.;K Nagata;Semin Cell Dev Biol,2003

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