Retroviral insertional mutagenesis identifies a small protein required for synthesis of diphthamide, the target of bacterial ADP-ribosylating toxins
about
Chemogenomic approach identified yeast YLR143W as diphthamide synthetaseIdentification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2Haploid genetic screens in human cells identify host factors used by pathogensDiphthamide modification of eEF2 requires a J-domain protein and is essential for normal developmentMembrane insertion of anthrax protective antigen and cytoplasmic delivery of lethal factor occur at different stages of the endocytic pathwayThe diphthamide modification pathway from Saccharomyces cerevisiae--revisitedBiochemical and Structural Characterization of a Novel Family of Cystathionine β-Synthase Domain Proteins Fused to a Zn Ribbon-Like DomainStructure of the Elongator cofactor complex Kti11/Kti13 provides insight into the role of Kti13 in Elongator-dependent tRNA modificationYBR246W is required for the third step of diphthamide biosynthesisA genome-wide screen identifies genes required for formation of the wobble nucleoside 5-methoxycarbonylmethyl-2-thiouridine in Saccharomyces cerevisiae.The yeast elongator histone acetylase requires Sit4-dependent dephosphorylation for toxin-target capacity.The amidation step of diphthamide biosynthesis in yeast requires DPH6, a gene identified through mining the DPH1-DPH5 interaction networkA dominant-negative approach that prevents diphthamide formation confers resistance to Pseudomonas exotoxin A and diphtheria toxinMannosyl-diinositolphospho-ceramide, the major yeast plasma membrane sphingolipid, governs toxicity of Kluyveromyces lactis zymocin.Gene trap mutagenesis-based forward genetic approach reveals that the tumor suppressor OVCA1 is a component of the biosynthetic pathway of diphthamide on elongation factor 2.Quantitative high-throughput screening identifies inhibitors of anthrax-induced cell deathCharacterization of a Chinese hamster ovary cell mutant having a mutation in elongation factor-2.Allele-specific suppressors of lin-1(R175Opal) identify functions of MOC-3 and DPH-3 in tRNA modification complexes in Caenorhabditis elegansSilencing of diphthamide synthesis 3 (Dph3) reduces metastasis of murine melanoma.Anthrax toxin targeting of myeloid cells through the CMG2 receptor is essential for establishment of Bacillus anthracis infections in mice.Dph3, a small protein required for diphthamide biosynthesis, is essential in mouse developmentThe Bacillus cereus Hbl and Nhe tripartite enterotoxin components assemble sequentially on the surface of target cells and are not interchangeable.Anthrax edema toxin impairs clearance in mice.Mutation in the platelet-derived growth factor receptor alpha inhibits adeno-associated virus type 5 transduction.Diphthamide modification on eukaryotic elongation factor 2 is needed to assure fidelity of mRNA translation and mouse developmentThe receptors that mediate the direct lethality of anthrax toxinMatrix metalloproteinase-activated anthrax lethal toxin demonstrates high potency in targeting tumor vasculatureCharacterization of the interaction between anthrax toxin and its cellular receptorsThe diphthamide modification on elongation factor-2 renders mammalian cells resistant to ricin.ADP-ribosylation of translation elongation factor 2 by diphtheria toxin in yeast inhibits translation and cell separation.Unique modifications of translation elongation factors.Dph3 is an electron donor for Dph1-Dph2 in the first step of eukaryotic diphthamide biosynthesis.SILENCE: a new forward genetic technology.
P2860
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P2860
Retroviral insertional mutagenesis identifies a small protein required for synthesis of diphthamide, the target of bacterial ADP-ribosylating toxins
description
2003 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2003
@ast
im September 2003 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2003/09/01)
@sk
vědecký článek publikovaný v roce 2003
@cs
wetenschappelijk artikel (gepubliceerd op 2003/09/01)
@nl
наукова стаття, опублікована у вересні 2003
@uk
مقالة علمية (نشرت في سبتمبر 2003)
@ar
name
Retroviral insertional mutagen ...... terial ADP-ribosylating toxins
@ast
Retroviral insertional mutagen ...... terial ADP-ribosylating toxins
@en
Retroviral insertional mutagen ...... terial ADP-ribosylating toxins
@nl
type
label
Retroviral insertional mutagen ...... terial ADP-ribosylating toxins
@ast
Retroviral insertional mutagen ...... terial ADP-ribosylating toxins
@en
Retroviral insertional mutagen ...... terial ADP-ribosylating toxins
@nl
prefLabel
Retroviral insertional mutagen ...... terial ADP-ribosylating toxins
@ast
Retroviral insertional mutagen ...... terial ADP-ribosylating toxins
@en
Retroviral insertional mutagen ...... terial ADP-ribosylating toxins
@nl
P1433
P1476
Retroviral insertional mutagen ...... terial ADP-ribosylating toxins
@en
P304
P356
10.1016/J.MOLCEL.2003.08.003
P577
2003-09-01T00:00:00Z