about
Potent D-peptide inhibitors of HIV-1 entryHIV entry: a game of hide-and-fuse?Protease-resistant peptide design-empowering nature's fragile warriors against HIVA fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodiesStructural and biological mimicry of protein surface recognition by / -peptide foldamersDesign of a Potent D-Peptide HIV-1 Entry Inhibitor with a Strong Barrier to ResistanceDistinct conformational states of HIV-1 gp41 are recognized by neutralizing and non-neutralizing antibodiesStructural Basis of HIV-1 Neutralization by Affinity Matured Fabs Directed against the Internal Trimeric Coiled-Coil of gp41Asymmetric deactivation of HIV-1 gp41 following fusion inhibitor bindingAntibody elicited against the gp41 N-heptad repeat (NHR) coiled-coil can neutralize HIV-1 with modest potency but non-neutralizing antibodies also bind to NHR mimetics.Estimating the probability of polyreactive antibodies 4E10 and 2F5 disabling a gp41 trimer after T cell-HIV adhesion.A monoclonal Fab derived from a human nonimmune phage library reveals a new epitope on gp41 and neutralizes diverse human immunodeficiency virus type 1 strains.Sequestering of the prehairpin intermediate of gp41 by peptide N36Mut(e,g) potentiates the human immunodeficiency virus type 1 neutralizing activity of monoclonal antibodies directed against the N-terminal helical repeat of gp41Soluble CD4 and CD4-mimetic compounds inhibit HIV-1 infection by induction of a short-lived activated state.Affinity maturation by targeted diversification of the CDR-H2 loop of a monoclonal Fab derived from a synthetic naïve human antibody library and directed against the internal trimeric coiled-coil of gp41 yields a set of Fabs with improved HIV-1 neutSERINC5 protein inhibits HIV-1 fusion pore formation by promoting functional inactivation of envelope glycoproteins.Vaccination with peptide mimetics of the gp41 prehairpin fusion intermediate yields neutralizing antisera against HIV-1 isolates.Viral entry inhibitors targeted to the membrane site of action.Enhanced potency of bivalent small molecule gp41 inhibitors.Sub-inhibitory concentrations of human α-defensin potentiate neutralizing antibodies against HIV-1 gp41 pre-hairpin intermediates in the presence of serum.Kinetically coupled folding of a single HIV-1 glycoprotein 41 complex in viral membrane fusion and inhibition.Interactions between different generation HIV-1 fusion inhibitors and the putative mechanism underlying the synergistic anti-HIV-1 effect resulting from their combination.Trimeric, coiled-coil extension on peptide fusion inhibitor of HIV-1 influences selection of resistance pathwaysDesign of helical, oligomeric HIV-1 fusion inhibitor peptides with potent activity against enfuvirtide-resistant virusReceptor Activation of HIV-1 Env Leads to Asymmetric Exposure of the gp41 Trimer.Peptide mimic of the HIV envelope gp120-gp41 interfaceInteractions of HIV-1 inhibitory peptide T20 with the gp41 N-HR coiled coilMutations in gp120 contribute to the resistance of human immunodeficiency virus type 1 to membrane-anchored C-peptide maC46.Kinetic dependence of paramyxovirus entry inhibition.Detailed mechanistic insights into HIV-1 sensitivity to three generations of fusion inhibitors.HIV-1 tropism testing and clinical management of CCR5 antagonists: Quebec review and recommendations.Peptides in the treatment of AIDS.Surface plasmon resonance for vaccine design and efficacy studies: recent applications and future trends.Amphipathic properties of HIV-1 gp41 fusion inhibitors.Escape from human immunodeficiency virus type 1 (HIV-1) entry inhibitors.Designed protein mimics of the Ebola virus glycoprotein GP2 α-helical bundle: stability and pH effects.Evaluation of ligand-based NMR screening methods to characterize small molecule binding to HIV-1 glycoprotein-41.Complex interplay of kinetic factors governs the synergistic properties of HIV-1 entry inhibitors.Site-Specific Polymer Attachment to HR2 Peptide Fusion Inhibitors against HIV-1 Decreases Binding Association Rates and Dissociation Rates Rather Than Binding Affinity.Structure-activity relationship studies of indole-based compounds as small molecule HIV-1 fusion inhibitors targeting glycoprotein 41.
P2860
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P2860
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh
2006年學術文章
@zh-hant
name
Kinetic dependence to HIV-1 entry inhibition.
@en
Kinetic dependence to HIV-1 entry inhibition.
@nl
type
label
Kinetic dependence to HIV-1 entry inhibition.
@en
Kinetic dependence to HIV-1 entry inhibition.
@nl
prefLabel
Kinetic dependence to HIV-1 entry inhibition.
@en
Kinetic dependence to HIV-1 entry inhibition.
@nl
P2860
P356
P1476
Kinetic dependence to HIV-1 entry inhibition.
@en
P2093
H Kirby Steger
Michael J Root
P2860
P304
25813-25821
P356
10.1074/JBC.M601457200
P407
P577
2006-06-27T00:00:00Z