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Nonconsecutive disulfide bond formation in an essential integral outer membrane protein

Nonconsecutive disulfide bond formation in an essential integral outer membrane protein

http://www.wikidata.org/entity/Q33982252

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Disulfide bond formation in the bacterial periplasm: major achievements and challenges ahead The Escherichia coli Lpt Transenvelope Protein Complex for Lipopolysaccharide Export Is Assembled via Conserved Structurally Homologous Domains LptE binds to and alters the physical state of LPS to catalyze its assembly at the cell surface.Structural basis for outer membrane lipopolysaccharide insertion Secretion of novel SEL1L endogenous variants is promoted by ER stress/UPR via endosomes and shed vesicles in human cancer cells Structural basis for lipopolysaccharide insertion in the bacterial outer membrane Characterization of a stalled complex on the β-barrel assembly machine.Classifying β-Barrel Assembly Substrates by Manipulating Essential Bam Complex Members.Lipopolysaccharide transport to the cell surface: periplasmic transport and assembly into the outer membrane.Outer membrane lipoprotein biogenesis: Lol is not the end.Transmembrane domain of surface-exposed outer membrane lipoprotein RcsF is threaded through the lumen of β-barrel proteins.Protease homolog BepA (YfgC) promotes assembly and degradation of β-barrel membrane proteins in Escherichia coli.Conformation-specific labeling of BamA and suppressor analysis suggest a cyclic mechanism for β-barrel assembly in Escherichia coli Max Bergmann lecture protein epitope mimetics in the age of structural vaccinology Dominant negative lptE mutation that supports a role for LptE as a plug in the LptD barrel.Disulfide rearrangement triggered by translocon assembly controls lipopolysaccharide export Outer membrane biogenesis in Escherichia coli, Neisseria meningitidis, and Helicobacter pylori: paradigm deviations in H. pylori Making a beta-barrel: assembly of outer membrane proteins in Gram-negative bacteria.BamE modulates the Escherichia coli beta-barrel assembly machine component BamA.The Bam machine: a molecular cooper.Lipoprotein LptE is required for the assembly of LptD by the beta-barrel assembly machine in the outer membrane of Escherichia coli.The complex that inserts lipopolysaccharide into the bacterial outer membrane forms a two-protein plug-and-barrel Factors affecting the folding of Pseudomonas aeruginosa OprF porin into the one-domain open conformer Bacterial thiol oxidoreductases - from basic research to new antibacterial strategies Electrical spiking in Escherichia coli probed with a fluorescent voltage-indicating protein.Inhibition of virulence-promoting disulfide bond formation enzyme DsbB is blocked by mutating residues in two distinct regions.A Peptidomimetic Antibiotic Targets Outer Membrane Proteins and Disrupts Selectively the Outer Membrane in Escherichia coli.The Activity of Escherichia coli Chaperone SurA Is Regulated by Conformational Changes Involving a Parvulin Domain.Lipopolysaccharide transport and assembly at the outer membrane: the PEZ model Role for Skp in LptD assembly in Escherichia coli.On the essentiality of lipopolysaccharide to Gram-negative bacteria.Prospects for new antibiotics: a molecule-centered perspective.The lipopolysaccharide export pathway in Escherichia coli: structure, organization and regulated assembly of the Lpt machinery Stress-induced remodeling of the bacterial proteome.Lipopolysaccharide is inserted into the outer membrane through an intramembrane hole, a lumen gate, and the lateral opening of LptD.Transport of lipopolysaccharide to the Gram-negative bacterial cell surface.The LptD chaperone LptE is not directly involved in lipopolysaccharide transport in Neisseria meningitidis The lipopolysaccharide transport (Lpt) machinery: a non-conventional transporter for lipopolysaccharide assembly at the outer membrane of Gram-negative bacteria.Structural and functional insights into the lipopolysaccharide ABC transporter LptB2FG.Ght protein of Neisseria meningitidis is involved in the regulation of lipopolysaccharide biosynthesis.

P2860

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P2860

Nonconsecutive disulfide bond formation in an essential integral outer membrane protein

http://www.wikidata.org/entity/Q33982252

description

2010 nî lūn-bûn

@nan

2010 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Nonconsecutive disulfide bond formation in an essential integral outer membrane protein

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Nonconsecutive disulfide bond formation in an essential integral outer membrane protein

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type

label

Nonconsecutive disulfide bond formation in an essential integral outer membrane protein

@ast

Nonconsecutive disulfide bond formation in an essential integral outer membrane protein

@en

prefLabel

Nonconsecutive disulfide bond formation in an essential integral outer membrane protein

@ast

Nonconsecutive disulfide bond formation in an essential integral outer membrane protein

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PNAS.1007319107

P1433

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

P1476

Nonconsecutive disulfide bond formation in an essential integral outer membrane protein

@en

P2093

Annie Hiniker

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

Daniel Kahne

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P2860

A pathway for disulfide bond formation in vivo

Transport of lipopolysaccharide across the cell envelope: the long road of discovery

Functional analysis of the protein machinery required for transport of lipopolysaccharide to the outer membrane of Escherichia coli

Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli

In vivo oxidative protein folding can be facilitated by oxidation-reduction cycling

Identification of two inner-membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coli

Reconstitution of outer membrane protein assembly from purified components

Contribution of proteomics toward solving the fascinating mysteries of the biogenesis of the envelope of Escherichia coli.

Characterization of the role of the Escherichia coli periplasmic chaperone SurA using differential proteomics.

Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli.

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12245-12250

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scholarly article

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10.1073/PNAS.1007319107

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27

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107

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Thomas J. Silhavy

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2010-06-21T00:00:00Z

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44691315

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