Literature DB >> 10679316

Protein folding: Thickening the broth.

A P Minton1.   

Abstract

Recent results support the notion that macromolecular 'crowding' enhances protein aggregation, at the expense of correct folding. The results can be rationalised in terms of kinetic competition between distinct processes, taking into account the relative influence of crowding on each process.

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Year:  2000        PMID： 10679316     DOI： 10.1016/s0960-9822(00)00301-8

Source DB:  PubMed          Journal:  Curr Biol        ISSN： 0960-9822            Impact factor:   10.834


  12 in total

1.  Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell.

Authors:  B van den Berg; R Wain; C M Dobson; R J Ellis
Journal:  EMBO J       Date:  2000-08-01       Impact factor: 11.598

Review 2.  Intrinsically disordered proteins and their environment: effects of strong denaturants, temperature, pH, counter ions, membranes, binding partners, osmolytes, and macromolecular crowding.

Authors:  Vladimir N Uversky
Journal:  Protein J       Date:  2009-10       Impact factor: 2.371

Review 3.  Intrinsically disordered proteins in crowded milieu: when chaos prevails within the cellular gumbo.

Authors:  Alexander V Fonin; April L Darling; Irina M Kuznetsova; Konstantin K Turoverov; Vladimir N Uversky
Journal:  Cell Mol Life Sci       Date:  2018-07-31       Impact factor: 9.261

4.  Quantification of Entropic Excluded Volume Effects Driving Crowding-Induced Collapse and Folding of a Disordered Protein.

Authors:  Divya Rajendran; Shrutarshi Mitra; Hiroyuki Oikawa; Kulkarni Madhurima; Ashok Sekhar; Satoshi Takahashi; Athi N Naganathan
Journal:  J Phys Chem Lett       Date:  2022-03-31       Impact factor: 6.888

5.  Concerted action of metals and macromolecular crowding on the fibrillation of alpha-synuclein.

Authors:  Larissa A Munishkina; Anthony L Fink; Vladimir N Uversky
Journal:  Protein Pept Lett       Date:  2008       Impact factor: 1.890

Review 6.  Intrinsic disorder in scaffold proteins: getting more from less.

Authors:  Marc S Cortese; Vladimir N Uversky; A Keith Dunker
Journal:  Prog Biophys Mol Biol       Date:  2008-06-20       Impact factor: 3.667

Review 7.  The roles of intrinsic disorder-based liquid-liquid phase transitions in the "Dr. Jekyll-Mr. Hyde" behavior of proteins involved in amyotrophic lateral sclerosis and frontotemporal lobar degeneration.

Authors:  Vladimir N Uversky
Journal:  Autophagy       Date:  2017-12-17       Impact factor: 16.016

Review 8.  What macromolecular crowding can do to a protein.

Authors:  Irina M Kuznetsova; Konstantin K Turoverov; Vladimir N Uversky
Journal:  Int J Mol Sci       Date:  2014-12-12       Impact factor: 5.923

9.  Structure and stability of recombinant bovine odorant-binding protein: III. Peculiarities of the wild type bOBP unfolding in crowded milieu.

Authors:  Olga V Stepanenko; Denis O Roginskii; Olesya V Stepanenko; Irina M Kuznetsova; Vladimir N Uversky; Konstantin K Turoverov
Journal:  PeerJ       Date:  2016-04-18       Impact factor: 2.984

10.  Folding of newly translated membrane protein CCR5 is assisted by the chaperonin GroEL-GroES.

Authors:  Haixia Chi; Xiaoqiang Wang; Jiqiang Li; Hao Ren; Fang Huang
Journal:  Sci Rep       Date:  2015-11-20       Impact factor: 4.379
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