Laboratory evolution of one disulfide isomerase to resemble another - Wikidata - awgldk - TriplyDB

Laboratory evolution of one disulfide isomerase to resemble another

Laboratory evolution of one disulfide isomerase to resemble another

http://www.wikidata.org/entity/Q30362756

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Staphylococcus aureus DsbA does not have a destabilizing disulfide. A new paradigm for bacterial oxidative folding Structural and biochemical characterization of the oxidoreductase NmDsbA3 from Neisseria meningitidis Properties of the Thioredoxin Fold Superfamily Are Modulated by a Single Amino Acid Residue The Structure of the Bacterial Oxidoreductase Enzyme DsbA in Complex with a Peptide Reveals a Basis for Substrate Specificity in the Catalytic Cycle of DsbA Enzymes Following evolutionary paths to protein-protein interactions with high affinity and selectivity Structural and functional characterization of Helicobacter pylori DsbG Diversity of the Epsilonproteobacteria Dsb (disulfide bond) systems.Bacterial thiol oxidoreductases - from basic research to new antibacterial strategies Identification of disulfide bond isomerase substrates reveals bacterial virulence factors.Functional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA.The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner.Engineering of Helicobacter pylori Dimeric Oxidoreductase DsbK (HP0231)Mechanisms of oxidative protein folding in the bacterial cell envelope.Sulfur Denitrosylation by an Engineered Trx-like DsbG Enzyme Identifies Nucleophilic Cysteine Hydrogen Bonds as Key Functional Determinant.Engineered pathways for correct disulfide bond oxidation.Converting a Sulfenic Acid Reductase into a Disulfide Bond Isomerase.

P2860

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P2860

Laboratory evolution of one disulfide isomerase to resemble another

http://www.wikidata.org/entity/Q30362756

description

2007 nî lūn-bûn

@nan

2007 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

name

Laboratory evolution of one disulfide isomerase to resemble another

@ast

Laboratory evolution of one disulfide isomerase to resemble another

@en

type

label

Laboratory evolution of one disulfide isomerase to resemble another

@ast

Laboratory evolution of one disulfide isomerase to resemble another

@en

prefLabel

Laboratory evolution of one disulfide isomerase to resemble another

@ast

Laboratory evolution of one disulfide isomerase to resemble another

@en

P1433

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P356

PNAS.0704692104

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Laboratory evolution of one disulfide isomerase to resemble another

@en

P2093

Annie Hiniker

http://www.w3.org/2001/XMLSchema#string

Guoping Ren

http://www.w3.org/2001/XMLSchema#string

James C A Bardwell

http://www.w3.org/2001/XMLSchema#string

Jeanne A Stuckey

http://www.w3.org/2001/XMLSchema#string

Richard W Jobson

http://www.w3.org/2001/XMLSchema#string

Stephanie Laurinec

http://www.w3.org/2001/XMLSchema#string

Ying Zheng

http://www.w3.org/2001/XMLSchema#string

P2860

The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex.

Mimicking natural evolution in vitro: An N-acetylneuraminate lyase mutant with an increased dihydrodipicolinate synthase activity

Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter

Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

Dehydration converts DsbG crystal diffraction from low to high resolution.

How does an enzyme evolved in vitro compare to naturally occurring homologs possessing the targeted function? Tyrosine aminotransferase from aspartate aminotransferase.

Laboratory-directed protein evolution

The evolution of catalytic efficiency and substrate promiscuity in human theta class 1-1 glutathione transferase.

Interactions of glutaredoxins, ribonucleotide reductase, and components of the DNA replication system of Escherichia coli.

Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide.

P304

11670-11675

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scholarly article

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10.1073/PNAS.0704692104

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P433

28

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P478

104

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P50

Jennifer L Martin

P577

2007-07-03T00:00:00Z

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P5875

6229119

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P698

17609373

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P932

1906722

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