Literature DB >> 23037594

Solving the mystery of procollagen chain selectivity.

Neil J Bulleid1.   

Abstract

The recently solved crystal structure of the procollagen C propeptide reveals the basis for chain selectivity as well as an unexpected asymmetry to this homotrimeric molecule. In addition, mapping disease-causing mutations to the structure demonstrates clear correlation between severity of disease and mutation location.

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Year:  2012        PMID： 23037594     DOI： 10.1038/nsmb.2397

Source DB:  PubMed          Journal:  Nat Struct Mol Biol        ISSN： 1545-9985            Impact factor:   15.369


  10 in total

Review 1.  Folding defects in fibrillar collagens.

Authors:  P H Byers
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2001-02-28       Impact factor: 6.237

Review 2.  The crucial role of trimerization domains in collagen folding.

Authors:  Sergei P Boudko; Jürgen Engel; Hans Peter Bächinger
Journal:  Int J Biochem Cell Biol       Date:  2011-10-05       Impact factor: 5.085

Review 3.  Procollagen trafficking, processing and fibrillogenesis.

Authors:  Elizabeth G Canty; Karl E Kadler
Journal:  J Cell Sci       Date:  2005-04-01       Impact factor: 5.285

4.  Peptide-binding specificity of the molecular chaperone BiP.

Authors:  G C Flynn; J Pohl; M T Flocco; J E Rothman
Journal:  Nature       Date:  1991-10-24       Impact factor: 49.962

5.  Protein disulfide isomerase acts as a molecular chaperone during the assembly of procollagen.

Authors:  R Wilson; J F Lees; N J Bulleid
Journal:  J Biol Chem       Date:  1998-04-17       Impact factor: 5.157

6.  Identification of the molecular recognition sequence which determines the type-specific assembly of procollagen.

Authors:  J F Lees; M Tasab; N J Bulleid
Journal:  EMBO J       Date:  1997-03-03       Impact factor: 11.598

Review 7.  N-glycan processing in ER quality control.

Authors:  Lloyd W Ruddock; Maurizio Molinari
Journal:  J Cell Sci       Date:  2006-11-01       Impact factor: 5.285

8.  BiP binds type I procollagen pro alpha chains with mutations in the carboxyl-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta.

Authors:  S D Chessler; P H Byers
Journal:  J Biol Chem       Date:  1993-08-25       Impact factor: 5.157

9.  The role of cysteine residues in the folding and association of the COOH-terminal propeptide of types I and III procollagen.

Authors:  J F Lees; N J Bulleid
Journal:  J Biol Chem       Date:  1994-09-30       Impact factor: 5.157

10.  Structural basis of fibrillar collagen trimerization and related genetic disorders.

Authors:  Jean-Marie Bourhis; Natacha Mariano; Yuguang Zhao; Karl Harlos; Jean-Yves Exposito; E Yvonne Jones; Catherine Moali; Nushin Aghajari; David J S Hulmes
Journal:  Nat Struct Mol Biol       Date:  2012-09-23       Impact factor: 15.369
  10 in total
  1 in total

1.  Heterozygous mutation of c.3521C>T in COL1A1 may cause mild osteogenesis imperfecta/Ehlers-Danlos syndrome in a Chinese family.

Authors:  Xianlong Shi; Yanqin Lu; Yanzhou Wang; Yu-Ang Zhang; Yuanwei Teng; Wanshui Han; Zhenzhong Han; Tianyou Li; Mei Chen; Junlong Liu; Fengling Fang; Conghui Dou; Xiuzhi Ren; Jinxiang Han
Journal:  Intractable Rare Dis Res       Date:  2015-02
  1 in total

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