Rationally designed anti-HIV peptides containing multifunctional domains as molecule probes for studying the mechanisms of action of the first and second generation HIV fusion inhibitors.
about
Rational improvement of gp41-targeting HIV-1 fusion inhibitors: an innovatively designed Ile-Asp-Leu tail with alternative conformations.Binding of a potent small-molecule inhibitor of six-helix bundle formation requires interactions with both heptad-repeats of the RSV fusion proteinHIV-1 fusion inhibitor peptides enfuvirtide and T-1249 interact with erythrocyte and lymphocyte membranesComputational methods for de novo protein design and its applications to the human immunodeficiency virus 1, purine nucleoside phosphorylase, ubiquitin specific protease 7, and histone demethylases.Discovery of entry inhibitors for HIV-1 via a new de novo protein design framework.Covalent fusion inhibitors targeting HIV-1 gp41 deep pocket.Resistance profiles of novel electrostatically constrained HIV-1 fusion inhibitors.Identification of a human protein-derived HIV-1 fusion inhibitor targeting the gp41 fusion core structure.DNA duplexes with hydrophobic modifications inhibit fusion between HIV-1 and cell membranes.Biochemistry and biophysics of HIV-1 gp41 - membrane interactions and implications for HIV-1 envelope protein mediated viral-cell fusion and fusion inhibitor designSite-specific Isopeptide Bridge Tethering of Chimeric gp41 N-terminal Heptad Repeat Helical Trimers for the Treatment of HIV-1 Infection.Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors.Peptides in the treatment of AIDS.Computer-Aided Approaches for Targeting HIVgp41.Peptide fusion inhibitors targeting the HIV-1 gp41: a patent review (2009 - 2014).Proteins, peptides, polysaccharides, and nucleotides with inhibitory activity on human immunodeficiency virus and its enzymes.Artificial peptides conjugated with cholesterol and pocket-specific small molecules potently inhibit infection by laboratory-adapted and primary HIV-1 isolates and enfuvirtide-resistant HIV-1 strains.Mutations of Gln64 in the HIV-1 gp41 N-terminal heptad repeat render viruses resistant to peptide HIV fusion inhibitors targeting the gp41 pocket.ADS-J1 inhibits human immunodeficiency virus type 1 entry by interacting with the gp41 pocket region and blocking fusion-active gp41 core formation.Combinations of the first and next generations of human immunodeficiency virus (HIV) fusion inhibitors exhibit a highly potent synergistic effect against enfuvirtide- sensitive and -resistant HIV type 1 strains.A novel bispecific peptide HIV-1 fusion inhibitor targeting the N-terminal heptad repeat and fusion peptide domains in gp41.An effective conjugation strategy for designing short peptide-based HIV-1 fusion inhibitors.Design of highly potent HIV fusion inhibitors based on artificial peptide sequences.
P2860
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P2860
Rationally designed anti-HIV peptides containing multifunctional domains as molecule probes for studying the mechanisms of action of the first and second generation HIV fusion inhibitors.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Rationally designed anti-HIV p ...... eration HIV fusion inhibitors.
@en
type
label
Rationally designed anti-HIV p ...... eration HIV fusion inhibitors.
@en
prefLabel
Rationally designed anti-HIV p ...... eration HIV fusion inhibitors.
@en
P2093
P2860
P356
P1476
Rationally designed anti-HIV p ...... eration HIV fusion inhibitors.
@en
P2093
P2860
P304
30376-30384
P356
10.1074/JBC.M804672200
P407
P50
P577
2008-07-28T00:00:00Z