(Q50636467)

17 March 2018

title

Alleviation of deleterious effects of protein mutation through inactivation of molecular chaperones. (English)

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17 March 2018

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Ryszard Korona

2

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author name string

Katarzyna Tomala

series ordinal

1

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17 March 2018

publication date

2 September 2008

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17 March 2018

Molecular Genetics and Genomics

published in

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17 March 2018

volume

280

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17 March 2018

issue

5

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17 March 2018

page(s)

409-417

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17 March 2018

https://scigraph.springernature.com/pub.10.1007/s00438-008-0374-x

exact match

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cites work

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Functional specificity among Hsp70 molecular chaperones

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Why molecular chaperones buffer mutational damage: a case study with a yeast Hsp40/70 system.

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GroEL and GroES control of substrate flux in the in vivo folding pathway of phage P22 coat protein.

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Endosymbiotic bacteria: groEL buffers against deleterious mutations

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Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease

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RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin.

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The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex

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Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli

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Molecular chaperones and protein quality control

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Molecular chaperones and selection against mutations

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Hsp90 as a capacitor for morphological evolution

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Chaperone rings in protein folding and degradation.

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Under cover: causes, effects and implications of Hsp90-mediated genetic capacitance

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Cooperation of molecular chaperones with the ubiquitin/proteasome system

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Functional characterization of the atypical Hsp70 subunit of yeast ribosome-associated complex

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Specific effects of ribosome-tethered molecular chaperones on programmed -1 ribosomal frameshifting.

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Genetic analysis of protein stability and function

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A functional chaperone triad on the yeast ribosome

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Network of general and specialty J protein chaperones of the yeast cytosol

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Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis

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The HSP90 chaperone complex, an emerging force in plant development and phenotypic plasticity

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Evidence for an epigenetic mechanism by which Hsp90 acts as a capacitor for morphological evolution.

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The ribosome-bound chaperones RAC and Ssb1/2p are required for accurate translation in Saccharomyces cerevisiae

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Structural insights into translational fidelity

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Demonstration by genetic suppression of interaction of GroE products with many proteins.

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The synthetic genetic interaction spectrum of essential genes

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12 December 2020

10.1007/S00438-008-0374-X

Identifiers

DOI

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17 March 2018

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17 March 2018