An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteins. - Wikidata - awgldk - TriplyDB

An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteins.

An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteins.

http://www.wikidata.org/entity/Q34756523

about

Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge Bcl-x(L) retrotranslocates Bax from the mitochondria into the cytosol A novel function of tissue-type transglutaminase: protein disulphide isomerase A duplicated motif controls assembly of zona pellucida domain proteins Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm Cloak and Dagger: Alternative Immune Evasion and Modulation Strategies of Poxviruses Whole cell cryo-electron tomography reveals distinct disassembly intermediates of vaccinia virus Shedding light on disulfide bond formation: engineering a redox switch in green fluorescent protein Disulfide bond formation at the C termini of vaccinia virus A26 and A27 proteins does not require viral redox enzymes and suppresses glycosaminoglycan-mediated cell fusion.Disulfide bond formation and activation of Escherichia coli β-galactosidase under oxidizing conditions A glutaredoxin, encoded by the G4L gene of vaccinia virus, is essential for virion morphogenesis.Kinetics and intracellular location of intramolecular disulfide bond formation mediated by the cytoplasmic redox system encoded by vaccinia virus.Disulfide bonds and membrane topology of the vaccinia virus A17L envelope protein Characterization of vaccinia virus intracellular cores: implications for viral uncoating and core structure Disulfide-mediated oligomerization of Peripherin/Rds and Rom-1 in photoreceptor disk membranes. Implications for photoreceptor outer segment morphogenesis and degeneration.Endoplasmic reticulum-Golgi intermediate compartment membranes and vimentin filaments participate in vaccinia virus assembly Native disulfide bond formation in proteins Complete pathway for protein disulfide bond formation encoded by poxviruses Formation and transfer of disulphide bonds in living cells.Cell-type specific requirements for thiol/disulfide exchange during HIV-1 entry and infection Molecular chaperone Hsp90 is important for vaccinia virus growth in cells Vaccinia virus G4L glutaredoxin is an essential intermediate of a cytoplasmic disulfide bond pathway required for virion assembly.Hepatitis B virus HBx protein interactions with the ubiquitin proteasome system.Structure of intracellular mature vaccinia virus visualized by in situ atomic force microscopy Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis.Investigation of structural and functional motifs within the vaccinia virus A14 phosphoprotein, an essential component of the virion membrane.A viral member of the ERV1/ALR protein family participates in a cytoplasmic pathway of disulfide bond formation.Thiol/disulfide exchange is required for membrane fusion directed by the Newcastle disease virus fusion protein.Two Cys residues essential for von Willebrand factor multimer assembly in the Golgi.SHuffle, a novel Escherichia coli protein expression strain capable of correctly folding disulfide bonded proteins in its cytoplasm Overexpression of thiol/disulfide isomerases enhances membrane fusion directed by the Newcastle disease virus fusion protein Poxvirus proteomics and virus-host protein interactions.Entry of the two infectious forms of vaccinia virus at the plasma membane is signaling-dependent for the IMV but not the EEV.Hepatitis B Virus X and Regulation of Viral Gene Expression.Structure and assembly of intracellular mature vaccinia virus: isolated-particle analysis.Structure and assembly of intracellular mature vaccinia virus: thin-section analyses Differences in virus-induced cell morphology and in virus maturation between MVA and other strains (WR, Ankara, and NYCBH) of vaccinia virus in infected human cells.Plectin repeats and modules: strategic cysteines and their presumed impact on cytolinker functions.Chemistry and Enzymology of Disulfide Cross-Linking in Proteins.

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P2860

An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteins.

http://www.wikidata.org/entity/Q34756523

description

1999 nî lūn-bûn

@nan

1999 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

1999 թվականի հունվարին հրատարակված գիտական հոդված

@hy

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

An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteins.

@ast

An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteins.

@en

An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteins.

@nl

type

label

An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteins.

@ast

An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteins.

@en

An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteins.

@nl

prefLabel

An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteins.

@ast

An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteins.

@en

An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteins.

@nl

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An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteins.

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G Griffiths

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J K Locker

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P2860

Folding and assembly of viral membrane proteins.

Thioredoxin and glutaredoxin systems

Assembly of vaccinia virus: role of the intermediate compartment between the endoplasmic reticulum and the Golgi stacks

Oxidized redox state of glutathione in the endoplasmic reticulum

Formation of a vaccinia virus structural polypeptide from a higher molecular weight precursor: inhibition by rifampicin.

Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum.

A class of membrane proteins with a C-terminal anchor.

The small envelope glycoprotein (GS) of equine arteritis virus folds into three distinct monomers and a disulfide-linked dimer

Assembly of vaccinia virus: incorporation of p14 and p32 into the membrane of the intracellular mature virus.

Vaccinia virus A17L gene product is essential for an early step in virion morphogenesis

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