about
Structural and functional comparisons of retroviral envelope protein C-terminal domains: still much to learnFluctuating Nonlinear Spring Model of Mechanical Deformation of Biological ParticlesCyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site.Structures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeTopology of the C-terminal tail of HIV-1 gp41: differential exposure of the Kennedy epitope on cell and viral membranesC-terminal tail of human immunodeficiency virus gp41: functionally rich and structurally enigmatic.Herpes virus genome, the pressure is on.Sampling protein form and function with the atomic force microscope.How cells tune viral mechanics--insights from biophysical measurements of influenza virus.Glycosphingolipid-functionalized nanoparticles recapitulate CD169-dependent HIV-1 uptake and trafficking in dendritic cellsMaturation-induced cloaking of neutralization epitopes on HIV-1 particles.Effect of envelope proteins on the mechanical properties of influenza virusBending and puncturing the influenza lipid envelope.Detailed topology mapping reveals substantial exposure of the "cytoplasmic" C-terminal tail (CTT) sequences in HIV-1 Env proteins at the cell surface.Mechanism of multivalent nanoparticle encounter with HIV-1 for potency enhancement of peptide triazole virus inactivation.Mutagenesis of tyrosine and di-leucine motifs in the HIV-1 envelope cytoplasmic domain results in a loss of Env-mediated fusion and infectivity.Poly(trimethylene carbonate-co-ε-caprolactone) promotes axonal growth.HIV-1 envelope glycoprotein biosynthesis, trafficking, and incorporation.[Atomic force microscopy: a tool to analyze the viral cycle].Mechanical elasticity as a physical signature of conformational dynamics in a virus particleVertex-Specific Proteins pUL17 and pUL25 Mechanically Reinforce Herpes Simplex Virus Capsids.CRAC motif peptide of the HIV-1 gp41 protein thins SOPC membranes and interacts with cholesterol.Manipulation of the mechanical properties of a virus by protein engineering.Analysis of the mechanical properties of wild type and hyperstable mutants of the HIV-1 capsid.The frantic play of the concealed HIV envelope cytoplasmic tail.Membrane structure correlates to function of LLP2 on the cytoplasmic tail of HIV-1 gp41 protein.Depletion effect and biomembrane budding.Biophysics of viral infectivity: matching genome length with capsid size.Structural transitions and energy landscape for Cowpea Chlorotic Mottle Virus capsid mechanics from nanomanipulation in vitro and in silico.Scaffold expulsion and genome packaging trigger stabilization of herpes simplex virus capsidsMechanisms of receptor/coreceptor-mediated entry of enveloped viruses.Maturation of the Gag core decreases the stability of retroviral lipid membranes.Elucidating the mechanism behind irreversible deformation of viral capsids.HIV-1 Gag processing intermediates trans-dominantly interfere with HIV-1 infectivity."Marker of Self" CD47 on lentiviral vectors decreases macrophage-mediated clearance and increases delivery to SIRPA-expressing lung carcinoma tumorsEvidence showing that tetraspanins inhibit HIV-1-induced cell-cell fusion at a post-hemifusion stageCompetition between Bending and Internal Pressure Governs the Mechanics of Fluid Nanovesicles.Virus engineering: functionalization and stabilization.Biosensors based on nanomechanical systems.Lipid polymer hybrid as emerging tool in nanocarriers for oral drug delivery.
P2860
Q26862369-0C1749E0-8561-4E89-8879-92CC0068231DQ27316776-A802284F-1082-47EF-9C82-EBD47234F871Q27332017-79859BAD-7EB3-4E2B-83F1-67EEAA6C8E84Q27487974-0F9DB030-4741-4AD1-87FA-5304DFDF37CFQ28476449-0D07265D-1840-40B6-885D-914328D9EFB9Q30422545-73BE6E0E-0993-4D6D-A9C1-59207124D128Q33603854-C0E144C6-F65F-43AE-9DB4-B7C02106C527Q33609572-89D68C42-ED9F-47B5-BFB0-A1776F3500FAQ33736593-AF8F0CE1-9B76-4E46-A2B1-5F06ED5CDAA5Q33943688-D3B51E30-0905-4662-A575-567ACA592E8DQ34023008-BEDB96E0-A94A-4CF9-9F39-F65C21877C76Q34437352-6A42B604-4063-4AEB-97E4-059746E1743BQ34535972-39585626-E322-43B2-B2E5-E2742D53002EQ34750051-7FA71AAC-F6D0-4E0F-9D8B-82D25AA0FD05Q34801630-50833CA1-56B9-4872-8AC3-F4B5D0F4B682Q35052938-609CDEA1-2D3F-4728-8237-2C887152DBDBQ35106147-078248A3-2742-4511-AB40-5420A4EA58E5Q35113720-13441323-9233-475A-99F0-ED3FE45AE7EDQ35658883-BBBF7DF8-E299-44CB-89F5-11332BAA3B85Q36132864-C33AE90A-6930-4697-8FF0-1CD8A868A0E2Q36337316-A0E1FE10-80E6-4DF1-B64C-5664F1C539D5Q36570805-93F97CF9-CB62-4E21-A6EB-5ADD57BEDCCAQ36670177-E63DE682-BFD2-41DE-BE9D-6F5B4BB59C45Q36691472-996B640A-A92E-4A48-ABA7-D69A9DC1AD71Q36940646-B786C412-194A-44F8-95E5-E905E3B8D76DQ37078294-AFC32168-A0BE-401F-9BEB-009EBF221649Q37136401-9C39B9C7-73C8-471C-A114-69BA30CFC247Q37142304-E7D09C94-B9E9-464D-82A7-A9063336F3FBQ37232099-E8F6C651-7E05-4DC1-BA1E-9F59BD78CACAQ37238943-59024E37-3C25-4064-810B-4082DAF784AAQ37263225-105A46A2-968F-4C6A-99E9-EF1EAE0320AEQ37359745-F80C7533-2AAA-4B29-9422-9B988EA4AB10Q37373455-27E00D9A-6FBA-4F5A-A7E3-5122805AF774Q37447762-E80DB202-C73A-4879-B1FB-87A6044590BFQ37490583-8AA18B65-9432-49DC-9811-9DC0AAF1EF07Q37673129-B788EADD-5BEB-4FAB-A9DA-B4CB723EBB55Q37728045-3F267369-C30E-484D-B657-C17BF47AE08EQ37798083-26BA5A00-1367-4FD2-9840-64C5AAF0460AQ38059825-3AAD05D7-8592-4C9D-BAAD-E054B44AEAA2Q38252593-0C3AE2E1-7A91-4D52-B280-DE2C566809F5
P2860
description
2006 nî lūn-bûn
@nan
2006 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
A stiffness switch in human immunodeficiency virus.
@ast
A stiffness switch in human immunodeficiency virus.
@en
type
label
A stiffness switch in human immunodeficiency virus.
@ast
A stiffness switch in human immunodeficiency virus.
@en
prefLabel
A stiffness switch in human immunodeficiency virus.
@ast
A stiffness switch in human immunodeficiency virus.
@en
P2093
P2860
P1433
P1476
A stiffness switch in human immunodeficiency virus.
@en
P2093
David Barlam
Itay Rousso
Marianna Tsvitov
Michael S Kay
Nitzan Kol
Roni Z Shneck
P2860
P304
P356
10.1529/BIOPHYSJ.106.093914
P407
P577
2006-12-08T00:00:00Z