Literature DB >> 10047579

Folding of peptide models of collagen and misfolding in disease.

J Baum1, B Brodsky.   

Abstract

The misfolding of the triple helix has been shown to play a critical role in collagen diseases. Normal and mutated collagen triple helices can be modeled by short, synthetic peptides of varying design. NMR spectroscopy and circular dichroism studies on the assembly of these peptide models have recently been used to isolate specific steps in the folding pathway and have provided information on the alterations resulting from mutations.

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Year:  1999        PMID: 10047579     DOI: 10.1016/s0959-440x(99)80016-5

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN: 0959-440X            Impact factor:   6.809


  35 in total

1.  Equilibrium thermal transitions of collagen model peptides.

Authors:  Anton V Persikov; Yujia Xu; Barbara Brodsky
Journal:  Protein Sci       Date:  2004-03-09       Impact factor: 6.725

2.  Location of glycine mutations within a bacterial collagen protein affects degree of disruption of triple-helix folding and conformation.

Authors:  Haiming Cheng; Shayan Rashid; Zhuoxin Yu; Ayumi Yoshizumi; Eileen Hwang; Barbara Brodsky
Journal:  J Biol Chem       Date:  2010-11-11       Impact factor: 5.157

3.  CD and NMR investigation of collagen peptides mimicking a pathological Gly-Ser mutation and a natural interruption in a similar highly charged sequence context.

Authors:  Xiuxia Sun; Songqing Liu; Wenyuan Yu; Shaoru Wang; Jianxi Xiao
Journal:  Protein Sci       Date:  2015-11-26       Impact factor: 6.725

Review 4.  Protein misfolding, aggregation, and degradation in disease.

Authors:  Niels Gregersen; Lars Bolund; Peter Bross
Journal:  Mol Biotechnol       Date:  2005-10       Impact factor: 2.695

Review 5.  The role of collagen in bone strength.

Authors:  S Viguet-Carrin; P Garnero; P D Delmas
Journal:  Osteoporos Int       Date:  2005-12-09       Impact factor: 4.507

6.  Analysis of the kinetics of folding of proteins and peptides using circular dichroism.

Authors:  Norma J Greenfield
Journal:  Nat Protoc       Date:  2006       Impact factor: 13.491

7.  FTIR studies of collagen model peptides: complementary experimental and simulation approaches to conformation and unfolding.

Authors:  Michael A Bryan; Joseph W Brauner; Gloria Anderle; Carol R Flach; Barbara Brodsky; Richard Mendelsohn
Journal:  J Am Chem Soc       Date:  2007-06-06       Impact factor: 15.419

8.  Folding and misfolding of the collagen triple helix: Markov analysis of molecular dynamics simulations.

Authors:  Sanghyun Park; Teri E Klein; Vijay S Pande
Journal:  Biophys J       Date:  2007-08-31       Impact factor: 4.033

9.  Activin A suppresses osteoblast mineralization capacity by altering extracellular matrix (ECM) composition and impairing matrix vesicle (MV) production.

Authors:  Rodrigo D A M Alves; Marco Eijken; Karel Bezstarosti; Jeroen A A Demmers; Johannes P T M van Leeuwen
Journal:  Mol Cell Proteomics       Date:  2013-06-17       Impact factor: 5.911

10.  Structural biology: Modelling collagen diseases.

Authors:  Barbara Brodsky; Jean Baum
Journal:  Nature       Date:  2008-06-19       Impact factor: 49.962

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