Biophysical Characterization of the C-propeptide Trimer from Human Procollagen III Reveals a Tri-lobed Structure-Reference-Cited by-同舟云学术

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Biophysical Characterization of the C-propeptide Trimer from Human Procollagen III Reveals a Tri-lobed Structure

Published:2001-12 Issue:52 Volume:276 Page:48930-48936
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Bernocco Simonetta,Finet Stéphanie,Ebel Christine,Eichenberger Denise,Mazzorana Marlène,Farjanel Jean,Hulmes David J.S.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference61 articles.

1. Protein Profile;Kadler,1995

2. Extracellular Matrix Assembly and Structure;Prockop,1994

3. Bone Morphogenetic Protein-1: The Type I Procollagen C-Proteinase

4. Procollagen N-proteinase and procollagen C-proteinase. Two unusual metalloproteinases that are essential for procollagen processing probably have important roles in development and cell signaling

5. Folding and activity of recombinant human procollagen C-proteinase enhancer

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2. Structural basis of homo- and heterotrimerization of collagen I;Nature Communications;2017-03-10

3. Procollagen C-proteinase enhancer grasps the stalk of the C-propeptide trimer to boost collagen precursor maturation;Proceedings of the National Academy of Sciences;2013-04-02

4. Production and crystallization of the C-propeptide trimer from human procollagen III;Acta Crystallographica Section F Structural Biology and Crystallization Communications;2012-09-26

5. Bone Matrix and Mineralization;Pediatric Bone;2012

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