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

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

http://www.wikidata.org/entity/Q24644906

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Bcl-x(L) retrotranslocates Bax from the mitochondria into the cytosol Disruption of reducing pathways is not essential for efficient disulfide bond formation in the cytoplasm of E. coli Oxidative switches in functioning of mammalian copper chaperone Cox17 Bacterial autoinduction: looking outside the cell for new metabolic engineering targets Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli Production of soluble mammalian proteins in Escherichia coli: identification of protein features that correlate with successful expression Characterisation of methionine adenosyltransferase from Mycobacterium smegmatis and M. tuberculosis The genomics of disulfide bonding and protein stabilization in thermophiles Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system Crystal structure of the global regulator FlhD from Escherichia coli at 1.8 A resolution Molecular recognition of parathyroid hormone by its G protein-coupled receptor An Extracellular Disulfide Bond Forming Protein (DsbF) from Mycobacterium tuberculosis: Structural, Biochemical, and Gene Expression Analysis Structure of catalytically competent intein caught in a redox trap with functional and evolutionary implications A conserved threonine spring-loads precursor for intein splicing Structural and biochemical characterization of the essential DsbA-like disulfide bond forming protein from Mycobacterium tuberculosis An Extended Active-site Motif Controls the Reactivity of the Thioredoxin Fold A current perspective on applications of macrocyclic-peptide-based high-affinity ligands Cellular disulfide bond formation in bioactive peptides and proteins Crystal structures of MBP fusion proteins Functional insights from the structure of the multifunctional C345C domain of C5 of complement.Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli.Genetic toggling of alkaline phosphatase folding reveals signal peptides for all major modes of transport across the inner membrane of bacteria.Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli.Disulfide bond formation and activation of Escherichia coli β-galactosidase under oxidizing conditions Rapid isolation of high-affinity protein binding peptides using bacterial display.Amino acid residues on the surface of soybean 4-kDa peptide involved in the interaction with its binding protein.Matrix-assisted refolding and purification of placenta-derived recombinant human interleukin-6 produced in Escherichia coli.The PLAC1-homology region of the ZP domain is sufficient for protein polymerisation.In vivo drafting of single-chain antibodies for regulatory duty on the sigma54-promoter Pu of the TOL plasmid.A simple vector system to improve performance and utilisation of recombinant antibodies Conjugative transfer can be inhibited by blocking relaxase activity within recipient cells with intrabodies.A scFv antibody mutant isolated in a genetic screen for improved export via the twin arginine transporter pathway exhibits faster folding.Genetic selection for peptide inhibitors of angiogenin.Identification of soluble protein fragments by gene fragmentation and genetic selection.Versatile selection technology for intracellular protein-protein interactions mediated by a unique bacterial hitchhiker transport mechanism Relationship between recombinant protein expression and host metabolome as determined by two-dimensional NMR spectroscopy Biochemical characterization of Plasmodium falciparum dipeptidyl aminopeptidase 1 Expression of active recombinant human tissue-type plasminogen activator by using in vivo polyhydroxybutyrate granule display.Disulfide bond formation in prokaryotes: history, diversity and design Peptide-based Antifungal Therapies against Emerging Infections.

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P2860

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

http://www.wikidata.org/entity/Q24644906

description

1999 nî lūn-bûn

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1999 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

1999 թվականի նոյեմբերին հրատարակված գիտական հոդված

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1999年の論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年论文

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name

Efficient folding of proteins ...... the Escherichia coli cytoplasm

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Efficient folding of proteins ...... the Escherichia coli cytoplasm

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Efficient folding of proteins ...... the Escherichia coli cytoplasm

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type

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Efficient folding of proteins ...... the Escherichia coli cytoplasm

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Efficient folding of proteins ...... the Escherichia coli cytoplasm

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Efficient folding of proteins ...... the Escherichia coli cytoplasm

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Efficient folding of proteins ...... the Escherichia coli cytoplasm

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Efficient folding of proteins ...... the Escherichia coli cytoplasm

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Efficient folding of proteins ...... the Escherichia coli cytoplasm

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PNAS.96.24.13703

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

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Efficient folding of proteins ...... the Escherichia coli cytoplasm

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F Aslund

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

G Georgiou

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J Beckwith

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P H Bessette

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P2860

Methods for generating precise deletions and insertions in the genome of wild-type Escherichia coli: application to open reading frame characterization

Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter

RsrA, an anti-sigma factor regulated by redox change

The thioredoxin superfamily: redundancy, specificity, and gray-area genomics.

Characterization of a periplasmic thiol:disulfide interchange protein required for the functional maturation of secreted virulence factors of Vibrio cholerae

Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins.

Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme.

A signal sequence is not required for protein export in prlA mutants of Escherichia coli

Determinants of membrane protein topology

Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.

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13703-8

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scholarly article

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10.1073/PNAS.96.24.13703

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24

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96

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1999-11-23T00:00:00Z

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12731376

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10570136

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Escherichia coli

protein folding

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24128

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