Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif. - Wikidata - wikimedia - TriplyDB

Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif.

Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif.

http://www.wikidata.org/entity/Q30159573

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Type V secretion: mechanism(s) of autotransport through the bacterial outer membrane Contribution of trimeric autotransporter C-terminal domains of oligomeric coiled-coil adhesin (Oca) family members YadA, UspA1, EibA, and Hia to translocation of the YadA passenger domain and virulence of Yersinia enterocolitica A growing toolbox of techniques for studying β-barrel outer membrane protein folding and biogenesis Analyzing the molecular mechanism of lipoprotein localization in Brucella Fold and function of polypeptide transport-associated domains responsible for delivering unfolded proteins to membranes Crystal Structure of YaeT: Conformational Flexibility and Substrate Recognition Conserved Properties of Polypeptide Transport-associated (POTRA) Domains Derived from Cyanobacterial Omp85 Omp85 from the Thermophilic Cyanobacterium Thermosynechococcus elongatus Differs from Proteobacterial Omp85 in Structure and Domain Composition Functional importance of a conserved sequence motif in FhaC, a prototypic member of the TpsB/Omp85 superfamily 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 Crystal Structure of BamB from Pseudomonas aeruginosa and Functional Evaluation of Its Conserved Structural Features Structural Determinants for Activity and Specificity of the Bacterial Toxin LlpA Crystal Structures of the Outer Membrane Domain of Intimin and Invasin from Enterohemorrhagic E. coli and Enteropathogenic Y. pseudotuberculosis Mitochondrial-bacterial hybrids of BamA/Tob55 suggest variable requirements for the membrane integration of β-barrel proteins.Outer membrane protein design.Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM.Secretion of the Intimin Passenger Domain Is Driven by Protein Folding.Recombinant expression of Chlamydia trachomatis major outer membrane protein in E. Coli outer membrane as a substrate for vaccine research From Constructs to Crystals - Towards Structure Determination of β-barrel Outer Membrane Proteins.Consensus computational network analysis for identifying candidate outer membrane proteins from Borrelia spirochetes.How does a β-barrel integral membrane protein insert into the membrane?Outer membrane protein biogenesis in Gram-negative bacteria Computational redesign of the lipid-facing surface of the outer membrane protein OmpA.The Borrelia afzelii outer membrane protein BAPKO_0422 binds human factor-H and is predicted to form a membrane-spanning β-barrel Evolution of the Translocation and Assembly Module (TAM)Cross-species chimeras reveal BamA POTRA and β-barrel domains must be fine-tuned for efficient OMP insertion Looks can be deceiving: recent insights into the mechanism of protein secretion by the autotransporter pathway.Bipartite Topology of Treponema pallidum Repeat Proteins C/D and I: OUTER MEMBRANE INSERTION, TRIMERIZATION, AND PORIN FUNCTION REQUIRE A C-TERMINAL β-BARREL DOMAIN Inhibition of the β-barrel assembly machine by a peptide that binds BamD.Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach.TtOmp85, a β-barrel assembly protein, functions by barrel augmentation Dynamics of Lewis b binding and sequence variation of the babA adhesin gene during chronic Helicobacter pylori infection in humans Versatile in vitro system to study translocation and functional integration of bacterial outer membrane proteins.Translocation path of a substrate protein through its Omp85 transporter.A mortise-tenon joint in the transmembrane domain modulates autotransporter assembly into bacterial outer membranes.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.Outer membrane β-barrel protein folding is physically controlled by periplasmic lipid head groups and BamA.Species-specificity of the BamA component of the bacterial outer membrane protein-assembly machinery.Structural modeling and physicochemical characterization provide evidence that P66 forms a β-barrel in the Borrelia burgdorferi outer membrane.

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P2860

Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif.

http://www.wikidata.org/entity/Q30159573

description

2006 nî lūn-bûn

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2006 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Assembly factor Omp85 recogniz ...... ies-specific C-terminal motif.

@ast

Assembly factor Omp85 recogniz ...... ies-specific C-terminal motif.

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type

label

Assembly factor Omp85 recogniz ...... ies-specific C-terminal motif.

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Assembly factor Omp85 recogniz ...... ies-specific C-terminal motif.

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prefLabel

Assembly factor Omp85 recogniz ...... ies-specific C-terminal motif.

@ast

Assembly factor Omp85 recogniz ...... ies-specific C-terminal motif.

@en

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Assembly factor Omp85 recogniz ...... ies-specific C-terminal motif.

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Freya Senf

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Jan Tommassen

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Martine P Bos

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Patrick Van Gelder

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Viviane Robert

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P2860

Identification of an outer membrane protein required for the transport of lipopolysaccharide to the bacterial cell surface

Crystal structures explain functional properties of two E. coli porins

An essential role of Sam50 in the protein sorting and assembly machinery of the mitochondrial outer membrane.

The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria.

Evolutionary conservation of biogenesis of beta-barrel membrane proteins.

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

Chemical conditionality: a genetic strategy to probe organelle assembly.

Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation.

Structure of the translocator domain of a bacterial autotransporter

POTRA: a conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins.

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scholarly article

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4

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Elena B Volokhina

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6707513

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17090219

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1634882

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