Proteolytic processing of the Ebola virus glycoprotein is not critical for Ebola virus replication in nonhuman primates.
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The Ebola virus glycoprotein contributes to but is not sufficient for virulence in vivoStructures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeEbolavirus glycoprotein structure and mechanism of entryEbola virus: A gap in drug design and discovery - experimental and computational perspective.Inhibition of proprotein convertases abrogates processing of the middle eastern respiratory syndrome coronavirus spike protein in infected cells but does not reduce viral infectivity.A new player in the puzzle of filovirus entry.Recovery of Recombinant Crimean Congo Hemorrhagic Fever Virus Reveals a Function for Non-structural Glycoproteins Cleavage by Furin.Inhibition of Lassa virus glycoprotein cleavage and multicycle replication by site 1 protease-adapted alpha(1)-antitrypsin variants.Human Ebola virus infection in West Africa: a review of available therapeutic agents that target different steps of the life cycle of Ebola virus.Cathepsin B & L are not required for ebola virus replicationComparative analysis of Ebola virus glycoprotein interactions with human and bat cells.The role of antigen-presenting cells in filoviral hemorrhagic fever: gaps in current knowledge.Filovirus entry into cells - new insights.The Glycoproteins of All Filovirus Species Use the Same Host Factors for Entry into Bat and Human Cells but Entry Efficiency Is Species Dependent.Crimean-Congo hemorrhagic fever virus glycoprotein processing by the endoprotease SKI-1/S1P is critical for virus infectivityMinigenomes, transcription and replication competent virus-like particles and beyond: reverse genetics systems for filoviruses and other negative stranded hemorrhagic fever virusesNovel mutations in Marburg virus glycoprotein associated with viral evasion from antibody mediated immune pressure.Host cell factors in filovirus entry: novel players, new insightsA mutation in the Ebola virus envelope glycoprotein restricts viral entry in a host species- and cell-type-specific manner.Forty Years of Ebolavirus Molecular Biology: Understanding a Novel Disease Agent Through the Development and Application of New Technologies.Characterization of the receptor-binding domain of Ebola glycoprotein in viral entry.A forward genetic strategy reveals destabilizing mutations in the Ebolavirus glycoprotein that alter its protease dependence during cell entryReverse Genetics of Filoviruses.Production and Purification of Filovirus Glycoproteins in Insect and Mammalian Cell Lines.Proteases and protease inhibitors in infectious diseases.Statins Suppress Ebola Virus Infectivity by Interfering with Glycoprotein Processing.
P2860
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P2860
Proteolytic processing of the Ebola virus glycoprotein is not critical for Ebola virus replication in nonhuman primates.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Proteolytic processing of the ...... lication in nonhuman primates.
@ast
Proteolytic processing of the ...... lication in nonhuman primates.
@en
type
label
Proteolytic processing of the ...... lication in nonhuman primates.
@ast
Proteolytic processing of the ...... lication in nonhuman primates.
@en
prefLabel
Proteolytic processing of the ...... lication in nonhuman primates.
@ast
Proteolytic processing of the ...... lication in nonhuman primates.
@en
P2860
P50
P356
P1433
P1476
Proteolytic processing of the ...... lication in nonhuman primates.
@en
P2093
Gabriele Neumann
Joan B Geisbert
P2860
P304
P356
10.1128/JVI.02486-06
P407
P577
2007-01-17T00:00:00Z