The L-VP35 and L-L interaction domains reside in the amino terminus of the Ebola virus L protein and are potential targets for antivirals.
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Mutual antagonism between the Ebola virus VP35 protein and the RIG-I activator PACT determines infection outcomeThe impact of "omic" and imaging technologies on assessing the host immune response to biodefence agents.Analysis of the highly diverse gene borders in Ebola virus reveals a distinct mechanism of transcriptional regulation.Antibodies to the core proteins of Nairobi sheep disease virus/Ganjam virus reveal details of the distribution of the proteins in infected cells and tissuesAssembly of the Ebola Virus Nucleoprotein from a Chaperoned VP35 ComplexAn Intrinsically Disordered Peptide from Ebola Virus VP35 Controls Viral RNA Synthesis by Modulating Nucleoprotein-RNA Interactions.HSP90 Chaperoning in Addition to Phosphoprotein Required for Folding but Not for Supporting Enzymatic Activities of Measles and Nipah Virus L Polymerases.Ebola Virus Does Not Induce Stress Granule Formation during Infection and Sequesters Stress Granule Proteins within Viral Inclusions.Reverse genetics systems as tools for the development of novel therapies against filoviruses.Ebola virus disease: societal challenges and new treatments.The Host E3-Ubiquitin Ligase TRIM6 Ubiquitinates the Ebola Virus VP35 Protein and Promotes Virus Replication.An RNA polymerase II-driven Ebola virus minigenome system as an advanced tool for antiviral drug screening.Modeling Ebola Virus Genome Replication and Transcription with Minigenome Systems.Molecular Function Analysis of Rabies Virus RNA Polymerase L Protein by Using an L Gene-Deficient Virus.Dynamic Phosphorylation of VP30 Is Essential for Ebola Virus Life Cycle.Inside the Cell: Assembly of Filoviruses.Characterization of the catalytic center of the Ebola virus L polymerase.Putative endogenous filovirus VP35-like protein potentially functions as an IFN antagonist but not a polymerase cofactor.Ebolaviruses: New roles for old proteins.Differential Mechanisms for the Involvement of Polyamines and Hypusinated eIF5A in Ebola Virus Gene ExpressionSofosbuvir: A Potential Treatment for Ebola
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The L-VP35 and L-L interaction domains reside in the amino terminus of the Ebola virus L protein and are potential targets for antivirals.
description
article científic
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article scientifique
@fr
articolo scientifico
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artigo científico
@pt
bilimsel makale
@tr
scientific article published on 11 April 2013
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
The L-VP35 and L-L interaction ...... ential targets for antivirals.
@en
The L-VP35 and L-L interaction ...... ential targets for antivirals.
@nl
type
label
The L-VP35 and L-L interaction ...... ential targets for antivirals.
@en
The L-VP35 and L-L interaction ...... ential targets for antivirals.
@nl
prefLabel
The L-VP35 and L-L interaction ...... ential targets for antivirals.
@en
The L-VP35 and L-L interaction ...... ential targets for antivirals.
@nl
P2093
P2860
P1433
P1476
The L-VP35 and L-L interaction ...... ential targets for antivirals.
@en
P2093
Dominik Conrad
Judith Olejnik
Kristina Brauburger
Martina Trunschke
Sven Enterlein
P2860
P304
P356
10.1016/J.VIROL.2013.03.013
P407
P577
2013-04-11T00:00:00Z