Literature DB >> 27384188

Molecular chaperones: providing a safe place to weather a midlife protein-folding crisis.

Patricia L Clark1, Adrian H Elcock2.   

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Year:  2016        PMID： 27384188     DOI： 10.1038/nsmb.3255

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


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  22 in total

Review 1.  Hsp90 & Co. - a holding for folding.

Authors:  J Buchner
Journal:  Trends Biochem Sci       Date:  1999-04       Impact factor: 13.807

Review 2.  The heat shock response: systems biology of proteotoxic stress in aging and disease.

Authors:  Richard I Morimoto
Journal:  Cold Spring Harb Symp Quant Biol       Date:  2012-02-27

Review 3.  The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum.

Authors:  Kunio Nakatsukasa; Jeffrey L Brodsky
Journal:  Traffic       Date:  2008-02-24       Impact factor: 6.215

Review 4.  Hsp70 chaperone dynamics and molecular mechanism.

Authors:  Matthias P Mayer
Journal:  Trends Biochem Sci       Date:  2013-09-05       Impact factor: 13.807

5.  Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements.

Authors:  Andrew K Shiau; Seth F Harris; Daniel R Southworth; David A Agard
Journal:  Cell       Date:  2006-10-20       Impact factor: 41.582

6.  Residues in chaperonin GroEL required for polypeptide binding and release.

Authors:  W A Fenton; Y Kashi; K Furtak; A L Horwich
Journal:  Nature       Date:  1994-10-13       Impact factor: 49.962

7.  Chaperonin complex with a newly folded protein encapsulated in the folding chamber.

Authors:  D K Clare; P J Bakkes; H van Heerikhuizen; S M van der Vies; H R Saibil
Journal:  Nature       Date:  2009-01-01       Impact factor: 49.962

Review 8.  Fundamental aspects of protein-protein association kinetics.

Authors:  G Schreiber; G Haran; H-X Zhou
Journal:  Chem Rev       Date:  2009-03-11       Impact factor: 60.622

9.  Forces Driving Chaperone Action.

Authors:  Philipp Koldewey; Frederick Stull; Scott Horowitz; Raoul Martin; James C A Bardwell
Journal:  Cell       Date:  2016-06-09       Impact factor: 41.582

10.  Substrate protein folds while it is bound to the ATP-independent chaperone Spy.

Authors:  Frederick Stull; Philipp Koldewey; Julia R Humes; Sheena E Radford; James C A Bardwell
Journal:  Nat Struct Mol Biol       Date:  2015-11-30       Impact factor: 15.369
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  5 in total

1.  Increased surface charge in the protein chaperone Spy enhances its anti-aggregation activity.

Authors:  Wei He; Jiayin Zhang; Veronika Sachsenhauser; Lili Wang; James C A Bardwell; Shu Quan
Journal:  J Biol Chem       Date:  2020-08-17       Impact factor: 5.157

2.  Artificial Intelligence Set to Reverse Engineer Drug Targeting in the Cell.

Authors:  Ariel Fernández
Journal:  ACS Pharmacol Transl Sci       Date:  2021-04-28

3.  Artificial Intelligence Deconstructs Drug Targeting In Vivo by Leveraging a Transformer Platform.

Authors:  Ariel Fernández
Journal:  ACS Med Chem Lett       Date:  2021-06-07       Impact factor: 4.632

4.  Laser-Triggered Small Interfering RNA Releasing Gold Nanoshells against Heat Shock Protein for Sensitized Photothermal Therapy.

Authors:  Zhaohui Wang; Siwen Li; Min Zhang; Yi Ma; Yuxi Liu; Weidong Gao; Jiaqi Zhang; Yueqing Gu
Journal:  Adv Sci (Weinh)       Date:  2016-10-19       Impact factor: 16.806

5.  Modeling protein folding in vivo.

Authors:  Irina Sorokina; Arcady Mushegian
Journal:  Biol Direct       Date:  2018-07-06       Impact factor: 4.540
  5 in total

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