Structure of the membrane anchor of pestivirus glycoprotein E(rns), a long tilted amphipathic helix.
about
Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface MattersHost-derived apolipoproteins play comparable roles with viral secretory proteins Erns and NS1 in the infectious particle formation of FlaviviridaeLipid Binding of the Amphipathic Helix Serving as Membrane Anchor of Pestivirus Glycoprotein ErnsHydrophobic Mismatch Drives the Interaction of E5 with the Transmembrane Segment of PDGF Receptor.Complex Virus-Host Interactions Involved in the Regulation of Classical Swine Fever Virus Replication: A Minireview.Different evolutionary patterns of classical swine fever virus envelope proteins.Glycoprotein 3 of porcine reproductive and respiratory syndrome virus exhibits an unusual hairpin-like membrane topology.Homodimerisation-independent cleavage of dsRNA by a pestiviral nicking endoribonuclease.
P2860
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P2860
Structure of the membrane anchor of pestivirus glycoprotein E(rns), a long tilted amphipathic helix.
description
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2014年の論文
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2014年論文
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2014年論文
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2014年論文
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2014年論文
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2014年論文
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2014年论文
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name
Structure of the membrane anch ...... long tilted amphipathic helix.
@ast
Structure of the membrane anch ...... long tilted amphipathic helix.
@en
type
label
Structure of the membrane anch ...... long tilted amphipathic helix.
@ast
Structure of the membrane anch ...... long tilted amphipathic helix.
@en
prefLabel
Structure of the membrane anch ...... long tilted amphipathic helix.
@ast
Structure of the membrane anch ...... long tilted amphipathic helix.
@en
P2093
P2860
P50
P1433
P1476
Structure of the membrane anch ...... long tilted amphipathic helix.
@en
P2093
Burkhard Luy
Claudia Muhle-Goll
Daniel Aberle
Gregor Meyers
Moritz Wolf
Sabine Reißer
P2860
P304
P356
10.1371/JOURNAL.PPAT.1003973
P577
2014-02-27T00:00:00Z