Literature DB >> 12581666

Protein unfolding--an important process in vivo?

Andreas Matouschek1.   

Abstract

Protein unfolding is an important step in several cellular processes, most interestingly protein degradation by ATP-dependent proteases and protein translocation across some membranes. Unfolding can be catalyzed when the unfoldases change the unfolding pathway of substrate proteins by pulling at their polypeptide chains. The resistance of a protein to unraveling during these processes is not determined by the protein's stability against global unfolding, as measured by temperature or solvent denaturation in vitro. Instead, resistance to unfolding is determined by the local structure that the unfoldase encounters first as it follows the substrate's polypeptide chain from the targeting signal. As unfolding is a necessary step in protein degradation and translocation, the susceptibility to unfolding of substrate proteins contributes to the specificity of these important cellular processes.

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Year:  2003        PMID: 12581666     DOI: 10.1016/s0959-440x(03)00010-1

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


  39 in total

1.  Protein topology determines binding mechanism.

Authors:  Yaakov Levy; Peter G Wolynes; José N Onuchic
Journal:  Proc Natl Acad Sci U S A       Date:  2003-12-23       Impact factor: 11.205

2.  Conformation and orientation of a protein folding intermediate trapped by adsorption.

Authors:  Maarten F M Engel; Antonie J W G Visser; Carlo P M van Mierlo
Journal:  Proc Natl Acad Sci U S A       Date:  2004-07-19       Impact factor: 11.205

3.  Reversible mechanical unfolding of single ubiquitin molecules.

Authors:  Chia-Lin Chyan; Fan-Chi Lin; Haibo Peng; Jian-Min Yuan; Chung-Hung Chang; Sheng-Hsien Lin; Guoliang Yang
Journal:  Biophys J       Date:  2004-09-10       Impact factor: 4.033

4.  Fast and faster: a designed variant of the B-domain of protein A folds in 3 microsec.

Authors:  Pooja Arora; Terrence G Oas; Jeffrey K Myers
Journal:  Protein Sci       Date:  2004-04       Impact factor: 6.725

Review 5.  Ratcheting up protein translocation with anthrax toxin.

Authors:  Geoffrey K Feld; Michael J Brown; Bryan A Krantz
Journal:  Protein Sci       Date:  2012-03-30       Impact factor: 6.725

6.  Atomic Structures of Anthrax Prechannel Bound with Full-Length Lethal and Edema Factors.

Authors:  Kang Zhou; Shiheng Liu; Nathan J Hardenbrook; Yanxiang Cui; Bryan A Krantz; Z Hong Zhou
Journal:  Structure       Date:  2020-06-09       Impact factor: 5.006

7.  Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers.

Authors:  Geoffrey K Feld; Katie L Thoren; Alexander F Kintzer; Harry J Sterling; Iok I Tang; Shoshana G Greenberg; Evan R Williams; Bryan A Krantz
Journal:  Nat Struct Mol Biol       Date:  2010-10-31       Impact factor: 15.369

8.  Blood compatible carbon nanotubes--nano-based neoproteoglycans.

Authors:  Saravanababu Murugesan; Tae-Joon Park; Hoichang Yang; Shaker Mousa; Robert J Linhardt
Journal:  Langmuir       Date:  2006-04-11       Impact factor: 3.882

Review 9.  Genetics of sarcoidosis: candidate genes and genome scans.

Authors:  Michael C Iannuzzi; Benjamin A Rybicki
Journal:  Proc Am Thorac Soc       Date:  2007-01

10.  Ligand binding modulates the mechanical stability of dihydrofolate reductase.

Authors:  Sri Rama Koti Ainavarapu; Lewyn Li; Carmen L Badilla; Julio M Fernandez
Journal:  Biophys J       Date:  2005-08-12       Impact factor: 4.033

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