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Involvement of Lipids in Different Steps of the Flavivirus Fusion Mechanism
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title
Involvement of Lipids in Different Steps of the Flavivirus Fusion Mechanism
(English)
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main subject
virology
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lipid
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author
Karin Stiasny
series ordinal
1
object named as
Karin Stiasny
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author name string
Christian Koessl
series ordinal
2
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Franz X Heinz
series ordinal
3
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publication date
July 2003
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published in
Journal of Virology
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volume
77
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page(s)
7856-62
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issue
14
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cites work
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The Fusion glycoprotein shell of Semliki Forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH
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Formation and characterization of the trimeric form of the fusion protein of Semliki Forest Virus
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Recombinant subviral particles from tick-borne encephalitis virus are fusogenic and provide a model system for studying flavivirus envelope glycoprotein functions
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Cholesterol is required for infection by Semliki Forest virus
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Membrane fusion of Semliki Forest virus involves homotrimers of the fusion protein
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HIV-1 entry into T-cells is not dependent on CD4 and CCR5 localization to sphingolipid-enriched, detergent-resistant, raft membrane domains
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The machinery for flavivirus fusion with host cell membranes
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Biochemical consequences of a mutation that controls the cholesterol dependence of Semliki Forest virus fusion
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The neutral glycosphingolipid globotriaosylceramide promotes fusion mediated by a CD4-dependent CXCR4-utilizing HIV type 1 envelope glycoprotein
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A single point mutation controls the cholesterol dependence of Semliki Forest virus entry and exit
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Membrane fusion of Semliki Forest virus requires sphingolipids in the target membrane
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Sterols and sphingolipids strongly affect the growth of fusion pores induced by the hemagglutinin of influenza virus
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Membrane fusion activity of tick-borne encephalitis virus and recombinant subviral particles in a liposomal model system
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Homogeneity of the Structural Glycoprotein from European Isolates of Tick-borne Encephalitis Virus: Comparison with Other Flaviviruses
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Streptolysin O: a proposed model of allosteric interaction between a pore-forming protein and its target lipid bilayer
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12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1128/JVI.77.14.7856-7862.2003
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3066247
OpenCitations bibliographic resource ID
3066247
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3066247
PMCID
161939
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3066247
PubMed ID
12829825
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3066247
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