Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway. - Wikidata - wikimedia - TriplyDB

Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway.

Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway.

http://www.wikidata.org/entity/Q35022917

about

The transcriptionally active regions in the genome of Bacillus subtilis Protein quality control in the bacterial periplasm Prediction of twin-arginine signal peptides A microbial sensor for discovering structural probes of protein misfolding and aggregation Structural diversity in twin-arginine signal peptide-binding proteins The 1.38 Å crystal structure of DmsD protein fromSalmonella typhimurium, a proofreading chaperone on the Tat pathway Conserved Signal Peptide Recognition Systems across the Prokaryotic Domains Directed evolution of Mycobacterium tuberculosis β-lactamase reveals gatekeeper residue that regulates antibiotic resistance and catalytic efficiency Directed Evolution of Human Heavy Chain Variable Domain (VH) Using In Vivo Protein Fitness Filter Prerequisites for terminal processing of thylakoidal Tat substrates Identification of functional Tat signal sequences in Mycobacterium tuberculosis proteins Role of the Pseudomonas aeruginosa PlcH Tat signal peptide in protein secretion, transcription, and cross-species Tat secretion system compatibility Contribution of Phe-7 to Tat-dependent export of β-lactamase in Xanthomonas campestris.Genetic toggling of alkaline phosphatase folding reveals signal peptides for all major modes of transport across the inner membrane of bacteria.Efficient isolation of soluble intracellular single-chain antibodies using the twin-arginine translocation machinery.Phage shock protein PspA of Escherichia coli relieves saturation of protein export via the Tat pathway.Genetic selection for protein solubility enabled by the folding quality control feature of the twin-arginine translocation pathway.A scFv antibody mutant isolated in a genetic screen for improved export via the twin arginine transporter pathway exhibits faster folding.LocateP: genome-scale subcellular-location predictor for bacterial proteins.Identification of protein secretion systems and novel secreted proteins in Rhizobium leguminosarum bv. viciae.Laboratory evolution of fast-folding green fluorescent protein using secretory pathway quality control.Versatile selection technology for intracellular protein-protein interactions mediated by a unique bacterial hitchhiker transport mechanism Visualizing interactions along the Escherichia coli twin-arginine translocation pathway using protein fragment complementation.A filamentous phage display system for N-linked glycoproteins.Signal peptide-chaperone interactions on the twin-arginine protein transport pathway.Environmental salinity determines the specificity and need for Tat-dependent secretion of the YwbN protein in Bacillus subtilis.Rejection of impassable substrates by Yersinia type III secretion machines Engineering antibody fitness and function using membrane-anchored display of correctly folded proteins.Redesigning the NEDD8 pathway with a bacterial genetic screen for ubiquitin-like molecule transfer.The hydrophobic core of twin-arginine signal sequences orchestrates specific binding to Tat-pathway related chaperones.Identification of a twin-arginine translocation system in Pseudomonas syringae pv. tomato DC3000 and its contribution to pathogenicity and fitness.Industrial production of recombinant therapeutics in Escherichia coli and its recent advancements.Optimizing recombinant antibodies for intracellular function using hitchhiker-mediated survival selection Tat-dependent translocation of an F420-binding protein of Mycobacterium tuberculosis.Production of secretory and extracellular N-linked glycoproteins in Escherichia coli.Envelope stress is a trigger of CRISPR RNA-mediated DNA silencing in Escherichia coli Effect of signal peptide on stability and folding of Escherichia coli thioredoxin.Discovery of plant phenolic compounds that act as type III secretion system inhibitors or inducers of the fire blight pathogen, Erwinia amylovora.Glycoarrays with engineered phages displaying structurally diverse oligosaccharides enable high-throughput detection of glycan-protein interactions Secretome of obligate intracellular Rickettsia.

P2860

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P2860

Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway.

http://www.wikidata.org/entity/Q35022917

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2003 nî lūn-bûn

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2003 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2003 թվականի ապրիլին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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

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Folding quality control in the ...... rginine translocation pathway.

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Danielle Tullman

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George Georgiou

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Matthew P DeLisa

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P2860

Overlapping functions of components of a bacterial Sec-independent protein export pathway

Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm

A common export pathway for proteins binding complex redox cofactors?

The complete general secretory pathway in gram-negative bacteria

Isolation of high-affinity ligand-binding proteins by periplasmic expression with cytometric screening (PECS).

Genetic analysis of the twin arginine translocator secretion pathway in bacteria.

Translocation of jellyfish green fluorescent protein via the Tat system of Escherichia coli and change of its periplasmic localization in response to osmotic up-shock.

Export of active green fluorescent protein to the periplasm by the twin-arginine translocase (Tat) pathway in Escherichia coli.

Protein translocation into and across the bacterial plasma membrane and the plant thylakoid membrane.

Protein import and routing systems of chloroplasts.

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quality control

protein folding

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