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Reconstitution of outer membrane protein assembly from purified components

Reconstitution of outer membrane protein assembly from purified components

http://www.wikidata.org/entity/Q30156906

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The translocation domain in trimeric autotransporter adhesins is necessary and sufficient for trimerization and autotransportation Protein-protein interactions and the spatiotemporal dynamics of bacterial outer membrane proteins From evolution to pathogenesis: the link between β-barrel assembly machineries in the outer membrane of mitochondria and gram-negative bacteria Structure and function of BamE within the outer membrane and the β-barrel assembly machine The Crystal Structure of BamB Suggests Interactions with BamA and Its Role within the BAM Complex Crystal Structure of BamD: An Essential Component of the β-Barrel Assembly Machinery of Gram-Negative Bacteria Structural Basis of Outer Membrane Protein Biogenesis in Bacteria Crystal Structure of BamB from Pseudomonas aeruginosa and Functional Evaluation of Its Conserved Structural Features Structural insight into the biogenesis of β-barrel membrane proteins Structure of Escherichia coli BamB and its interaction with POTRA domains of BamA Structural basis for the interaction of BamB with the POTRA3-4 domains of BamA Assembly of the mitochondrial protein import channel: role of Tom5 in two-stage interaction of Tom40 with the SAM complex The CpxQ sRNA Negatively Regulates Skp To Prevent Mistargeting of β-Barrel Outer Membrane Proteins into the Cytoplasmic Membrane Membrane integration of an essential β-barrel protein prerequires burial of an extracellular loop.The β-barrel assembly machinery in motion.Flexibility in the Periplasmic Domain of BamA Is Important for Function.Structural snapshots of the β-barrel assembly machinery.Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM.Recombinant expression of Chlamydia trachomatis major outer membrane protein in E. Coli outer membrane as a substrate for vaccine research From Chaperones to the Membrane with a BAM!Characterization of a stalled complex on the β-barrel assembly machine.BamA POTRA Domain Interacts with a Native Lipid Membrane Surface A Supercomplex Spanning the Inner and Outer Membranes Mediates the Biogenesis of β-Barrel Outer Membrane Proteins in Bacteria.Classifying β-Barrel Assembly Substrates by Manipulating Essential Bam Complex Members.Outer membrane protein biogenesis in Gram-negative bacteria A combined kinetic push and thermodynamic pull as driving forces for outer membrane protein sorting and folding in bacteria.Computational redesign of the lipid-facing surface of the outer membrane protein OmpA.Looks can be deceiving: recent insights into the mechanism of protein secretion by the autotransporter pathway.Inhibition of the β-barrel assembly machine by a peptide that binds BamD.Characterization of the insertase BamA in three different membrane mimetics by solution NMR spectroscopy.Versatile in vitro system to study translocation and functional integration of bacterial outer membrane proteins.Reconstitution of bacterial autotransporter assembly using purified components.Lateral opening and exit pore formation are required for BamA function In vivo roles of BamA, BamB and BamD in the biogenesis of BamA, a core protein of the β-barrel assembly machine of Escherichia coli.Refolding, crystallization and preliminary X-ray crystallographic studies of the β-barrel domain of BamA, a membrane protein essential for outer membrane protein biogenesis DegP primarily functions as a protease for the biogenesis of β-barrel outer membrane proteins in the Gram-negative bacterium Escherichia coli.Identification of FkpA as a key quality control factor for the biogenesis of outer membrane proteins under heat shock conditions Lateral gates: β-barrels get in on the act.Stepwise folding of an autotransporter passenger domain is not essential for its secretion Charge-dependent secretion of an intrinsically disordered protein via the autotransporter pathway.

P2860

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P2860

Reconstitution of outer membrane protein assembly from purified components

http://www.wikidata.org/entity/Q30156906

description

2010 nî lūn-bûn

@nan

2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Reconstitution of outer membrane protein assembly from purified components

@ast

Reconstitution of outer membrane protein assembly from purified components

@en

type

label

Reconstitution of outer membrane protein assembly from purified components

@ast

Reconstitution of outer membrane protein assembly from purified components

@en

prefLabel

Reconstitution of outer membrane protein assembly from purified components

@ast

Reconstitution of outer membrane protein assembly from purified components

@en

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SCIENCE.1188919

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P1476

Reconstitution of outer membrane protein assembly from purified components

@en

P2093

Christine L Hagan

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

Seokhee Kim

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

P2860

Structure and function of an essential component of the outer membrane protein assembly machine

The Periplasmic Bacterial Molecular Chaperone SurA Adapts its Structure to Bind Peptides in Different Conformations to Assert a Sequence Preference for Aromatic Residues

Machinery for protein sorting and assembly in the mitochondrial outer membrane.

Evolutionary conservation of biogenesis of beta-barrel membrane proteins.

The versatile beta-barrel membrane protein

Role of a highly conserved bacterial protein in outer membrane protein assembly

Interaction of an autotransporter passenger domain with BamA during its translocation across the bacterial outer membrane.

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

Beta-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro.

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

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890-892

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scholarly article

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10.1126/SCIENCE.1188919

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5980

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43080101

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20378773

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P921

chaperone-mediated protein transport

chaperone-mediated protein transport across periplasmic space

Bam protein complex

P932

2873164

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