Nonhelical leash and alpha-helical structures determine the potency of a peptide antagonist of human T-cell leukemia virus entry.
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Charge-Surrounded Pockets and Electrostatic Interactions with Small Ions Modulate the Activity of Retroviral Fusion ProteinsCapturing a fusion intermediate of influenza hemagglutinin with a cholesterol-conjugated peptide, a new antiviral strategy for influenza virus.Cellular Factors Involved in HTLV-1 Entry and PathogenicitDiscovery and significance of new human T-lymphotropic viruses: HTLV-3 and HTLV-4.The six-helix bundle of human immunodeficiency virus Env controls pore formation and enlargement and is initiated at residues proximal to the hairpin turnHighly specific inhibition of leukaemia virus membrane fusion by interaction of peptide antagonists with a conserved region of the coiled coil of envelope.Basic residues are critical to the activity of peptide inhibitors of human T cell leukemia virus type 1 entry.
P2860
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P2860
Nonhelical leash and alpha-helical structures determine the potency of a peptide antagonist of human T-cell leukemia virus entry.
description
2008 nî lūn-bûn
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2008年の論文
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2008年学术文章
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2008年学术文章
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2008年学术文章
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2008年学术文章
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2008年学术文章
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2008年學術文章
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2008年學術文章
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2008年學術文章
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name
Nonhelical leash and alpha-hel ...... n T-cell leukemia virus entry.
@en
type
label
Nonhelical leash and alpha-hel ...... n T-cell leukemia virus entry.
@en
prefLabel
Nonhelical leash and alpha-hel ...... n T-cell leukemia virus entry.
@en
P2093
P2860
P356
P1433
P1476
Nonhelical leash and alpha-hel ...... n T-cell leukemia virus entry.
@en
P2093
Antonis Mirsaliotis
Daniel Lamb
David W Brighty
P2860
P304
P356
10.1128/JVI.02458-07
P407
P577
2008-02-27T00:00:00Z