Structural and functional characterization of Helicobacter pylori DsbG - Wikidata - wikimedia - TriplyDB

Structural and functional characterization of Helicobacter pylori DsbG

Structural and functional characterization of Helicobacter pylori DsbG

http://www.wikidata.org/entity/Q27675432

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Structural and functional characterization of HP0377, a thioredoxin-fold protein from Helicobacter pylori A novel insight into the oxidoreductase activity of Helicobacter pylori HP0231 protein Diversity of the Epsilonproteobacteria Dsb (disulfide bond) systems.Comparative Roles of the Two Helicobacter pylori Thioredoxins in Preventing Macromolecule Damage Helicobacter pylori HP0231 Influences Bacterial Virulence and Is Essential for Gastric Colonization Functional and evolutionary analyses of Helicobacter pylori HP0231 (DsbK) protein with strong oxidative and chaperone activity characterized by a highly diverged dimerization domain Engineering of Helicobacter pylori Dimeric Oxidoreductase DsbK (HP0231)Structural and functional aspects of the Helicobacter pylori secretome.Characterization of Helicobacter pylori HP0231 (DsbK): role in disulfide bond formation, redox homeostasis and production of Helicobacter cystein-rich protein HcpE.

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Structural and functional characterization of Helicobacter pylori DsbG

http://www.wikidata.org/entity/Q27675432

description

2011 nî lūn-bûn

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2011 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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2011 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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Structural and functional characterization of Helicobacter pylori DsbG

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Structural and functional characterization of Helicobacter pylori DsbG

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Structural and functional characterization of Helicobacter pylori DsbG

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Structural and functional characterization of Helicobacter pylori DsbG

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Structural and functional characterization of Helicobacter pylori DsbG

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Structural and functional characterization of Helicobacter pylori DsbG

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Structural and functional characterization of Helicobacter pylori DsbG

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Structural and functional characterization of Helicobacter pylori DsbG

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Structural and functional characterization of Helicobacter pylori DsbG

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Structural and functional characterization of Helicobacter pylori DsbG

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Byung Woo Han

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Ha Na Im

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Hye-Jin Yoon

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Hyoun Sook Kim

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Ji Young Yoon

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Jieun Kim

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Kyoung Hoon Kim

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Sang Jae Lee

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

Se Won Suh

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

Soon-Jong Kim

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P2860

Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli

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

DsbL and DsbI form a specific dithiol oxidase system for periplasmic arylsulfate sulfotransferase in uropathogenic Escherichia coli

Properties of the Thioredoxin Fold Superfamily Are Modulated by a Single Amino Acid Residue

Structural and functional characterization of three DsbA paralogues from Salmonella enterica serovar Typhimurium

Reassessment of Ellman's reagent

Thioredoxin--a fold for all reasons

Laboratory evolution of one disulfide isomerase to resemble another

DsbA: a protein-folding catalyst contributing to bacterial virulence.

Protein disulfide bond formation in prokaryotes.

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Helicobacter pylori