Literature DB >> 23530255

Assembly chaperones: a perspective.

R John Ellis1.   

Abstract

The historical origins and current interpretation of the molecular chaperone concept are presented, with the emphasis on the distinction between folding chaperones and assembly chaperones. Definitions of some basic terms in this field are offered and misconceptions pointed out. Two examples of assembly chaperone are discussed in more detail: the role of numerous histone chaperones in fundamental nuclear processes and the co-operation of assembly chaperones with folding chaperones in the production of the world's most important enzyme.

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Year:  2013        PMID: 23530255      PMCID: PMC3638391          DOI: 10.1098/rstb.2011.0398

Source DB:  PubMed          Journal:  Philos Trans R Soc Lond B Biol Sci        ISSN: 0962-8436            Impact factor:   6.237


  38 in total

1.  Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin.

Authors:  Jose M Barral; Alex H Hutagalung; Achim Brinker; F Ulrich Hartl; Henry F Epstein
Journal:  Science       Date:  2002-01-25       Impact factor: 47.728

2.  Advancing our understanding and capacity to engineer nature's CO2-sequestering enzyme, Rubisco.

Authors:  Spencer M Whitney; Robert L Houtz; Hernan Alonso
Journal:  Plant Physiol       Date:  2010-10-25       Impact factor: 8.340

Review 3.  Molecular chaperones in protein folding and proteostasis.

Authors:  F Ulrich Hartl; Andreas Bracher; Manajit Hayer-Hartl
Journal:  Nature       Date:  2011-07-20       Impact factor: 49.962

Review 4.  The role of Hsp90 in protein complex assembly.

Authors:  Taras Makhnevych; Walid A Houry
Journal:  Biochim Biophys Acta       Date:  2011-09-16

5.  What have we learned from 15 years of free-air CO2 enrichment (FACE)? A meta-analytic review of the responses of photosynthesis, canopy properties and plant production to rising CO2.

Authors:  Elizabeth A Ainsworth; Stephen P Long
Journal:  New Phytol       Date:  2005-02       Impact factor: 10.151

6.  Homologous plant and bacterial proteins chaperone oligomeric protein assembly.

Authors:  S M Hemmingsen; C Woolford; S M van der Vies; K Tilly; D T Dennis; C P Georgopoulos; R W Hendrix; R J Ellis
Journal:  Nature       Date:  1988-05-26       Impact factor: 49.962

7.  Proteins as molecular chaperones.

Authors:  J Ellis
Journal:  Nature       Date:  1987 Jul 30-Aug 5       Impact factor: 49.962

8.  Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells.

Authors:  Andrija Finka; Rayees U H Mattoo; Pierre Goloubinoff
Journal:  Cell Stress Chaperones       Date:  2010-08-09       Impact factor: 3.667

9.  Co-expression of plastid chaperonin genes and a synthetic plant Rubisco operon in Escherichia coli.

Authors:  L P Cloney; D R Bekkaoui; S M Hemmingsen
Journal:  Plant Mol Biol       Date:  1993-12       Impact factor: 4.076

10.  Alpha-hemoglobin-stabilizing protein: an erythroid molecular chaperone.

Authors:  Maria Emília Favero; Fernando Ferreira Costa
Journal:  Biochem Res Int       Date:  2011-03-24
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  18 in total

1.  Structure and mechanism of the Rubisco-assembly chaperone Raf1.

Authors:  Thomas Hauser; Javaid Y Bhat; Goran Miličić; Petra Wendler; F Ulrich Hartl; Andreas Bracher; Manajit Hayer-Hartl
Journal:  Nat Struct Mol Biol       Date:  2015-08-03       Impact factor: 15.369

Review 2.  Adapting to stress - chaperome networks in cancer.

Authors:  Suhasini Joshi; Tai Wang; Thaís L S Araujo; Sahil Sharma; Jeffrey L Brodsky; Gabriela Chiosis
Journal:  Nat Rev Cancer       Date:  2018-09       Impact factor: 60.716

Review 3.  The role of protein-protein interactions in the intracellular traffic of the potassium channels TASK-1 and TASK-3.

Authors:  Markus Kilisch; Olga Lytovchenko; Blanche Schwappach; Vijay Renigunta; Jürgen Daut
Journal:  Pflugers Arch       Date:  2015-01-07       Impact factor: 3.657

Review 4.  Classical chaperone-usher (CU) adhesive fimbriome: uropathogenic Escherichia coli (UPEC) and urinary tract infections (UTIs).

Authors:  Payam Behzadi
Journal:  Folia Microbiol (Praha)       Date:  2019-06-05       Impact factor: 2.099

5.  Chaperones: needed for both the good times and the bad times.

Authors:  Roy A Quinlan; R John Ellis
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2013-03-25       Impact factor: 6.237

6.  Structure of GPN-Loop GTPase Npa3 and Implications for RNA Polymerase II Assembly.

Authors:  Jürgen Niesser; Felix R Wagner; Dirk Kostrewa; Wolfgang Mühlbacher; Patrick Cramer
Journal:  Mol Cell Biol       Date:  2015-12-28       Impact factor: 4.272

7.  Chloroplast Proteome of Nicotiana benthamiana Infected by Tomato Blistering Mosaic Virus.

Authors:  Esau Megias; Lílian Silveira Travassos do Carmo; Cícero Nicolini; Luciano Paulino Silva; Rosana Blawid; Tatsuya Nagata; Angela Mehta
Journal:  Protein J       Date:  2018-06       Impact factor: 2.371

8.  Molecular Stressors Engender Protein Connectivity Dysfunction through Aberrant N-Glycosylation of a Chaperone.

Authors:  Pengrong Yan; Hardik J Patel; Sahil Sharma; Adriana Corben; Tai Wang; Palak Panchal; Chenghua Yang; Weilin Sun; Thais L Araujo; Anna Rodina; Suhasini Joshi; Kenneth Robzyk; Srinivasa Gandu; Julie R White; Elisa de Stanchina; Shanu Modi; Yelena Y Janjigian; Elizabeth G Hill; Bei Liu; Hediye Erdjument-Bromage; Thomas A Neubert; Nanette L S Que; Zihai Li; Daniel T Gewirth; Tony Taldone; Gabriela Chiosis
Journal:  Cell Rep       Date:  2020-06-30       Impact factor: 9.423

9.  The non-prion SUP35 preexists in large chaperone-containing molecular complexes.

Authors:  Shiwha Park; Xin Wang; Wen Xi; Roy Richardson; Thomas M Laue; Clyde L Denis
Journal:  Proteins       Date:  2021-12-02

Review 10.  Mutations, protein homeostasis, and epigenetic control of genome integrity.

Authors:  Jinglin Lucy Xie; Daniel F Jarosz
Journal:  DNA Repair (Amst)       Date:  2018-08-23
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