Modulating protein stability - directed evolution strategies for improved protein function (Q38109676)

29 August 2017

title

Modulating protein stability - directed evolution strategies for improved protein function (English)

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29 August 2017

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Raymond D Socha

1

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29 August 2017

Nobuhiko Tokuriki

series ordinal

2

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29 August 2017

language of work or name

English

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publication date

18 June 2013

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29 August 2017

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29 August 2017

volume

280

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29 August 2017

issue

22

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29 August 2017

page(s)

5582-5595

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Engineering the third wave of biocatalysis

29 August 2017

cites work

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Directed evolution drives the next generation of biocatalysts

21 January 2018

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Strategy and success for the directed evolution of enzymes

21 January 2018

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Finding better protein engineering strategies

21 January 2018

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Evolving strategies for enzyme engineering

21 January 2018

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https://api.crossref.org/works/10.1111%2FFEBS.12354

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

21 January 2018

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https://api.crossref.org/works/10.1111%2FFEBS.12354

Protein stability promotes evolvability

21 January 2018

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https://api.crossref.org/works/10.1111%2FFEBS.12354

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

21 January 2018

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https://api.crossref.org/works/10.1111%2FFEBS.12354

Chaperonin overexpression promotes genetic variation and enzyme evolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Stability effects of mutations and protein evolvability

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Identification and analysis of deleterious human SNPs.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

In the light of directed evolution: pathways of adaptive protein evolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

The stability effects of protein mutations appear to be universally distributed

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

How protein stability and new functions trade off

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Relative tolerance of an enzymatic molten globule and its thermostable counterpart to point mutation

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Correlation of levels of folded recombinant p53 in escherichia coli with thermodynamic stability in vitro.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Using model proteins to quantify the effects of pathogenic mutations in Ig-like proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Protein kinetic stability.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Converging concepts of protein folding in vitro and in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Protein folding and misfolding

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Soluble oligomerization provides a beneficial fitness effect on destabilizing mutations

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Protein quality control acts on folding intermediates to shape the effects of mutations on organismal fitness

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Computational design and selections for an engineered, thermostable terpene synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Evolutionary transitions to new DNA methyltransferases through target site expansion and shrinkage

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Directed evolution of serum paraoxonase PON3 by family shuffling and ancestor/consensus mutagenesis, and its biochemical characterization

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Bridging the gaps in design methodologies by evolutionary optimization of the stability and proficiency of designed Kemp eliminase KE59

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

The transition of human estrogen sulfotransferase from generalist to specialist using directed enzyme evolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Intense neutral drifts yield robust and evolvable consensus proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Evolutionary history of a specialized p450 propane monooxygenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Utilizing natural diversity to evolve protein function: applications towards thermostability

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Protein stability by number: high-throughput and statistical approaches to one of protein science's most difficult problems.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Ancestral residues stabilizing 3-isopropylmalate dehydrogenase of an extreme thermophile: experimental evidence supporting the thermophilic common ancestor hypothesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Engineering proteins with tunable thermodynamic and kinetic stabilities.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Design of highly stable functional GroEL minichaperones.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

The design of a hyperstable mutant of the Abp1p SH3 domain by sequence alignment analysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

The consensus concept for thermostability engineering of proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Construction of stabilized proteins by combinatorial consensus mutagenesis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Structure-guided consensus approach to create a more thermostable penicillin G acylase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Development of a thermostable glucose dehydrogenase by a structure-guided consensus concept

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Improved thermostability of Clostridium thermocellum endoglucanase Cel8A by using consensus-guided mutagenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Advanced evolutionary molecular engineering to produce thermostable cellulase by using a small but efficient library

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Improvement of the Thermostability and Activity of a Pectate Lyase by Single Amino Acid Substitutions, Using a Strategy Based on Melting-Temperature-Guided Sequence Alignment

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Thermostability of ancestral mutants of Caldococcus noboribetus isocitrate dehydrogenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Designing thermostable proteins: ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Extremely thermophilic translation system in the common ancestor commonote: ancestral mutants of Glycyl-tRNA synthetase from the extreme thermophile Thermus thermophilus

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Improvement of Bacillus circulans beta-amylase activity attained using the ancestral mutation method.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Energy functions for protein design: adjustment with protein-protein complex affinities, models for the unfolded state, and negative design of solubility and specificity.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

I-Mutant2.0: predicting stability changes upon mutation from the protein sequence or structure

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

CUPSAT: prediction of protein stability upon point mutations.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

SPROUTS: a database for the evaluation of protein stability upon point mutation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

PoPMuSiC 2.1: a web server for the estimation of protein stability changes upon mutation and sequence optimality

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

RosettaBackrub--a web server for flexible backbone protein structure modeling and design

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

SDM--a server for predicting effects of mutations on protein stability and malfunction

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

PROTS-RF: a robust model for predicting mutation-induced protein stability changes

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

The linear interaction energy method for the prediction of protein stability changes upon mutation

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

SNPeffect 4.0: on-line prediction of molecular and structural effects of protein-coding variants

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Performance of protein stability predictors.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Assessing predictors of changes in protein stability upon mutation using self-consistency

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Assessing computational methods for predicting protein stability upon mutation: good on average but not in the details.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Enhancing the stability and solubility of TEV protease using in silico design

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Improving the thermostability of lipase Lip2 from Yarrowia lipolytica

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Improved thermostability of AEH by combining B-FIT analysis and structure-guided consensus method.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Highly thermostable fungal cellobiohydrolase I (Cel7A) engineered using predictive methods.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Thermostabilization of a cytochrome p450 peroxygenase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Increasing activity and thermal resistance of Bacillus gibsonii alkaline protease (BgAP) by directed evolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Directed evolution of a highly active Yersinia mollaretii phytase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Increased thermostability of microbial transglutaminase by combination of several hot spots evolved by random and saturation mutagenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Evolving thermostability in mutant libraries of ligninolytic oxidoreductases expressed in yeast

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Directed evolution of a thermostable esterase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Proteolytic selection for protein folding using filamentous bacteriophages

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Selecting proteins with improved stability by a phage-based method

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Genetic selection for enhanced folding in vivo targets the Cys14-Cys38 disulfide bond in bovine pancreatic trypsin inhibitor

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

In vitro evolution of a hyperstable Gbeta1 variant

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Increased folding stability of TEM-1 beta-lactamase by in vitro selection

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Directed evolution of proteins for heterologous expression and stability.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Evolutionary optimization of computationally designed enzymes: Kemp eliminases of the KE07 series

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Screening for soluble expression constructs using cell-free protein synthesis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Rational improvement of simvastatin synthase solubility in Escherichia coli leads to higher whole-cell biocatalytic activity.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Identification of soluble protein fragments by gene fragmentation and genetic selection.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

A simple in vivo assay for increased protein solubility

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Optimizing protein stability in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

New molecular reporters for rapid protein folding assays

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

In vivo protein stabilization based on fragment complementation and a split GFP system

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Enhancing the stability and solubility of the glucocorticoid receptor ligand-binding domain by high-throughput library screening

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Directed evolution and structural analysis of N-carbamoyl-D-amino acid amidohydrolase provide insights into recombinant protein solubility in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

A systematic survey of in vivo obligate chaperonin-dependent substrates

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

A survey of proteins encoded by non-synonymous single nucleotide polymorphisms reveals a significant fraction with altered stability and activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Molecular chaperones: structure of a protein disaggregase

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Disaggregating chaperones: an unfolding story.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Chemical chaperones assist intracellular folding to buffer mutational variations.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Chemical and pharmacological chaperones: application for recombinant protein production and protein folding diseases

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Global analysis of chaperone effects using a reconstituted cell-free translation system.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Enhancing the solubility of recombinant proteins in Escherichia coli by using hexahistidine-tagged maltose-binding protein as a fusion partner

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Iterative saturation mutagenesis on the basis of B factors as a strategy for increasing protein thermostability

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Rapid protein-folding assay using green fluorescent protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

Sequence statistics reliably predict stabilizing mutations in a protein domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12354

21 January 2018

Identifiers

DOI

10.1111/FEBS.12354

1 reference

29 August 2017

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