Chaperonin overexpression promotes genetic variation and enzyme evolution (Q28247346)

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scientific article (publication date: 4 June 2009)

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English	Chaperonin overexpression promotes genetic variation and enzyme evolution	scientific article (publication date: 4 June 2009)

Statements

instance of

scholarly article

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title

Chaperonin overexpression promotes genetic variation and enzyme evolution (English)

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main subject

overexpression

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based on heuristic

inferred from title

genetic variation

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inferred from title

author name string

Nobuhiko Tokuriki

series ordinal

1

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Dan S Tawfik

series ordinal

2

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language of work or name

English

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publication date

4 June 2009

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published in

Nature

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volume

459

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issue

7247

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page(s)

668-73

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cites work

Between genotype and phenotype: protein chaperones and evolvability

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Directed evolution of phosphotriesterase from Pseudomonas diminuta for heterologous expression in Escherichia coli results in stabilization of the metal-free state.

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Asymmetric segregation of protein aggregates is associated with cellular aging and rejuvenation.

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GroEL and the maintenance of bacterial endosymbiosis

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Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations

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Chaperonin-mediated protein folding

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Shared promiscuous activities and evolutionary features in various members of the amidohydrolase superfamily.

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The stability effects of protein mutations appear to be universally distributed

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Continuity in evolution: on the nature of transitions

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Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research

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

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Evolution of an antibiotic resistance enzyme constrained by stability and activity trade-offs

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Evolutionary potential of hidden genetic variation.

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Low folding propensity and high translation efficiency distinguish in vivo substrates of GroEL from other Escherichia coli proteins

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Endosymbiotic bacteria: groEL buffers against deleterious mutations

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Transient kinetic analysis of adenosine 5'-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL

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Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL.

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Directed evolution of the promiscuous esterase activity of carbonic anhydrase II.

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Simultaneous purification of hexokinase, class-I fructose-bisphosphate aldolase, triosephosphate isomerase and phosphoglycerate kinase from Trypanosoma brucei

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Latent evolutionary potentials under the neutral mutational drift of an enzyme

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Intense neutral drifts yield robust and evolvable consensus proteins

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Hsp90 as a capacitor for morphological evolution

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Loss of protein structure stability as a major causative factor in monogenic disease.

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A compromise required by gene sharing enables survival: Implications for evolution of new enzyme activities

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

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Hsp90 potentiates the rapid evolution of new traits: drug resistance in diverse fungi

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The selection of acceptable protein mutations

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reference URL

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GroEL reversibly binds to, and causes rapid inactivation of, human carbonic anhydrase II at high temperatures

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Predicting the tolerance of proteins to random amino acid substitution

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How protein stability and new functions trade off

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

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Genomic buffering mitigates the effects of deleterious mutations in bacteria

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based on heuristic

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Evolution of evolvability.

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/19494908

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based on heuristic

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Robustness-epistasis link shapes the fitness landscape of a randomly drifting protein.

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Missense meanderings in sequence space: a biophysical view of protein evolution

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The FoldX web server: an online force field

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reference URL

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Chaperone coexpression plasmids: differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli

1 reference

stated in

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reference URL

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based on heuristic

inferred from PubMed ID database lookup

Hsp90 as a capacitor of phenotypic variation

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/19494908

retrieved

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based on heuristic

inferred from PubMed ID database lookup

Role of mutator alleles in adaptive evolution.

1 reference

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PubMed

reference URL

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retrieved

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based on heuristic

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Protein stability imposes limits on organism complexity and speed of molecular evolution

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stated in

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reference URL

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Directed evolution of mammalian paraoxonases PON1 and PON3 for bacterial expression and catalytic specialization

1 reference

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reference URL

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

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PubMed

reference URL

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retrieved

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based on heuristic

inferred from PubMed ID database lookup

Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/19494908

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Chaperone-assisted protein folding.

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/19494908

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1038/NATURE08009

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stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1102862

Dimensions Publication ID

1049245007

0 references

OpenCitations bibliographic resource ID

1102862

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1102862

PubMed publication ID

19494908

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1102862

ResearchGate publication ID

26265280

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