Literature DB >> 14685248

Protein folding and misfolding.

Christopher M Dobson1.   

Abstract

The manner in which a newly synthesized chain of amino acids transforms itself into a perfectly folded protein depends both on the intrinsic properties of the amino-acid sequence and on multiple contributing influences from the crowded cellular milieu. Folding and unfolding are crucial ways of regulating biological activity and targeting proteins to different cellular locations. Aggregation of misfolded proteins that escape the cellular quality-control mechanisms is a common feature of a wide range of highly debilitating and increasingly prevalent diseases.

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Year:  2003        PMID: 14685248     DOI: 10.1038/nature02261

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  1088 in total

1.  Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding.

Authors:  Apratim Dhar; Antonios Samiotakis; Simon Ebbinghaus; Lea Nienhaus; Dirar Homouz; Martin Gruebele; Margaret S Cheung
Journal:  Proc Natl Acad Sci U S A       Date:  2010-10-04       Impact factor: 11.205

2.  High cell density cultivation of a recombinant Escherichia coli strain expressing a 6-O-sulfotransferase for the production of bioengineered heparin.

Authors:  J Zhang; M Suflita; C M Fiaschetti; G Li; L Li; F Zhang; J S Dordick; R J Linhardt
Journal:  J Appl Microbiol       Date:  2014-12-02       Impact factor: 3.772

3.  Observation of sequence specificity in the seeding of protein amyloid fibrils.

Authors:  Mark R H Krebs; Ludmilla A Morozova-Roche; Katie Daniel; Carol V Robinson; Christopher M Dobson
Journal:  Protein Sci       Date:  2004-07       Impact factor: 6.725

4.  Oligomerization of amyloid Abeta16-22 peptides using hydrogen bonds and hydrophobicity forces.

Authors:  Giorgio Favrin; Anders Irbäck; Sandipan Mohanty
Journal:  Biophys J       Date:  2004-09-17       Impact factor: 4.033

5.  Expansion and compression of a protein folding intermediate by GroEL.

Authors:  Zong Lin; Hays S Rye
Journal:  Mol Cell       Date:  2004-10-08       Impact factor: 17.970

6.  Aqueous urea solution destabilizes Abeta(16-22) oligomers.

Authors:  D K Klimov; John E Straub; D Thirumalai
Journal:  Proc Natl Acad Sci U S A       Date:  2004-10-01       Impact factor: 11.205

7.  Molecular basis for evolving modularity in the yeast protein interaction network.

Authors:  Ariel Fernández
Journal:  PLoS Comput Biol       Date:  2007-11       Impact factor: 4.475

8.  Do amyloid structures formed by Staphylococcus aureus phenol-soluble modulins have a biological function?

Authors:  Yue Zheng; Hwang-Soo Joo; Vinod Nair; Katherine Y Le; Michael Otto
Journal:  Int J Med Microbiol       Date:  2017-09-01       Impact factor: 3.473

9.  Protective hinge in insulin opens to enable its receptor engagement.

Authors:  John G Menting; Yanwu Yang; Shu Jin Chan; Nelson B Phillips; Brian J Smith; Jonathan Whittaker; Nalinda P Wickramasinghe; Linda J Whittaker; Vijay Pandyarajan; Zhu-li Wan; Satya P Yadav; Julie M Carroll; Natalie Strokes; Charles T Roberts; Faramarz Ismail-Beigi; Wieslawa Milewski; Donald F Steiner; Virander S Chauhan; Colin W Ward; Michael A Weiss; Michael C Lawrence
Journal:  Proc Natl Acad Sci U S A       Date:  2014-08-04       Impact factor: 11.205

10.  Exploring the aggregation propensity of γS-crystallin protein variants using two-dimensional spectroscopic tools.

Authors:  Jun Jiang; Kory J Golchert; Carolyn N Kingsley; William D Brubaker; Rachel W Martin; Shaul Mukamel
Journal:  J Phys Chem B       Date:  2013-11-12       Impact factor: 2.991

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