ADP-ribosylation of elongation factor 2 by diphtheria toxin. Isolation and properties of the novel ribosyl-amino acid and its hydrolysis products
about
Chemogenomic approach identified yeast YLR143W as diphthamide synthetaseDiphthamide modification of eEF2 requires a J-domain protein and is essential for normal developmentToxin-based targeted therapy for malignant brain tumorsStructural basis of actin recognition and arginine ADP-ribosylation by Clostridium perfringens -toxinArginine ADP-ribosylation mechanism based on structural snapshots of iota-toxin and actin complexYBR246W is required for the third step of diphthamide biosynthesisDPH5, a methyltransferase gene required for diphthamide biosynthesis in Saccharomyces cerevisiae.Dph7 catalyzes a previously unknown demethylation step in diphthamide biosynthesis.The amidation step of diphthamide biosynthesis in yeast requires DPH6, a gene identified through mining the DPH1-DPH5 interaction networkLoss of diphthamide pre-activates NF-κB and death receptor pathways and renders MCF7 cells hypersensitive to tumor necrosis factorThe biosynthesis and biological function of diphthamideA structural domain mediates attachment of ethanolamine phosphoglycerol to eukaryotic elongation factor 1A in Trypanosoma bruceiA dominant-negative approach that prevents diphthamide formation confers resistance to Pseudomonas exotoxin A and diphtheria toxinInactivation of the elongation factor Tu by mosquitocidal toxin-catalyzed mono-ADP-ribosylationCharacterization of a Chinese hamster ovary cell mutant having a mutation in elongation factor-2.A type VI secretion system effector protein, VgrG1, from Aeromonas hydrophila that induces host cell toxicity by ADP ribosylation of actin.Expression of diphtheria toxin fragment A and hormone-toxin fusion proteins in toxin-resistant yeast mutantsReconstitution of diphthine synthase activity in vitro.Towards a systems approach in the genetic analysis of archaea: Accelerating mutant construction and phenotypic analysis in Haloferax volcaniiGenome-Scale CRISPR-Mediated Control of Gene Repression and ActivationAntibody fusion proteins: anti-CD22 recombinant immunotoxin moxetumomab pasudotoxMatching two independent cohorts validates DPH1 as a gene responsible for autosomal recessive intellectual disability with short stature, craniofacial, and ectodermal anomaliesImmunoconjugates in the management of hairy cell leukemia.Occurrence of diphthamide in archaebacteria.Comparative genomic analysis of the DUF71/COG2102 family predicts roles in diphthamide biosynthesis and B12 salvage.Host cell cytotoxicity and cytoskeleton disruption by CerADPr, an ADP-ribosyltransferase of Bacillus cereus G9241The diphthamide modification on elongation factor-2 renders mammalian cells resistant to ricin.In vitro biosynthesis of diphthamide, studied with mutant Chinese hamster ovary cells resistant to diphtheria toxinDiphtheria toxin-resistant mutants of Saccharomyces cerevisiae.Saccharomyces cerevisiae spheroplasts are sensitive to the action of diphtheria toxin.Hairy cell leukemia - immunotargets and therapiesADP-ribosylation of translation elongation factor 2 by diphtheria toxin in yeast inhibits translation and cell separation.Recombinant immunotoxins containing truncated bacterial toxins for the treatment of hematologic malignanciesAutoradiographic assay of mutants resistant to diphtheria toxin in mammalian cells in vitro.Radical S-adenosylmethionine enzymes.Clostridium perfringens iota-toxin: structure and function.Macrophage-targeted therapy: CD64-based immunotoxins for treatment of chronic inflammatory diseases.Novel bacterial ADP-ribosylating toxins: structure and function.Dph3 is an electron donor for Dph1-Dph2 in the first step of eukaryotic diphthamide biosynthesis.Functions of Murine Dendritic Cells.
P2860
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P2860
ADP-ribosylation of elongation factor 2 by diphtheria toxin. Isolation and properties of the novel ribosyl-amino acid and its hydrolysis products
description
1980 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1980 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1980
@ast
im November 1980 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1980/11/25)
@sk
vědecký článek publikovaný v roce 1980
@cs
wetenschappelijk artikel (gepubliceerd op 1980/11/25)
@nl
наукова стаття, опублікована в листопаді 1980
@uk
name
ADP-ribosylation of elongation ...... id and its hydrolysis products
@ast
ADP-ribosylation of elongation ...... id and its hydrolysis products
@en
ADP-ribosylation of elongation ...... id and its hydrolysis products
@nl
type
label
ADP-ribosylation of elongation ...... id and its hydrolysis products
@ast
ADP-ribosylation of elongation ...... id and its hydrolysis products
@en
ADP-ribosylation of elongation ...... id and its hydrolysis products
@nl
prefLabel
ADP-ribosylation of elongation ...... id and its hydrolysis products
@ast
ADP-ribosylation of elongation ...... id and its hydrolysis products
@en
ADP-ribosylation of elongation ...... id and its hydrolysis products
@nl
P2093
P1476
ADP-ribosylation of elongation ...... id and its hydrolysis products
@en
P2093
B. G. Van Ness
J. B. Howard
J. W. Bodley
P304
10717–10720
P407
P577
1980-11-25T00:00:00Z