Mechanism by which the lectin actinohivin blocks HIV infection of target cells
about
HIV-1 neutralization profile and plant-based recombinant expression of actinohivin, an Env glycan-specific lectin devoid of T-cell mitogenic activityMonomerization of Viral Entry Inhibitor Griffithsin Elucidates the Relationship between Multivalent Binding to Carbohydrates and anti-HIV ActivityNovel Fold and Carbohydrate Specificity of the Potent Anti-HIV Cyanobacterial Lectin from Oscillatoria agardhiiSolution Structure of the Monovalent Lectin Microvirin in Complex with Man (1-2)Man Provides a Basis for Anti-HIV Activity with Low ToxicityStructural Insights into the Anti-HIV Activity of the Oscillatoria agardhii Agglutinin Homolog Lectin FamilyStructural Basis of the Anti-HIV Activity of the Cyanobacterial Oscillatoria Agardhii AgglutininStructural insights into the specific anti-HIV property of actinohivin: structure of its complex with the α(1–2)mannobiose moiety of gp120X-ray Crystallographic Structures of Trimers and Higher-Order Oligomeric Assemblies of a Peptide Derived from Aβ 17–36The characteristic structure of anti-HIV actinohivin in complex with three HMTG D1 chains of HIV-gp120High mannose-binding lectin with preference for the cluster of alpha1-2-mannose from the green alga Boodlea coacta is a potent entry inhibitor of HIV-1 and influenza viruses.Endothelial galectin-1 binds to specific glycans on nipah virus fusion protein and inhibits maturation, mobility, and function to block syncytia formation.An insight into the sialotranscriptome of Simulium nigrimanum, a black fly associated with fogo selvagem in South America.Broad antiviral activity of carbohydrate-binding agents against the four serotypes of dengue virus in monocyte-derived dendritic cellsDomain swapping proceeds via complete unfolding: a 19F- and 1H-NMR study of the Cyanovirin-N proteinModification of Asparagine-Linked Glycan Density for the Design of Hepatitis B Virus Virus-Like Particles with Enhanced Immunogenicity.The griffithsin dimer is required for high-potency inhibition of HIV-1: evidence for manipulation of the structure of gp120 as part of the griffithsin dimer mechanism.Identification, Characterization, and X-ray Crystallographic Analysis of a Novel Type of Mannose-Specific Lectin CGL1 from the Pacific Oyster Crassostrea gigas.Potential of carbohydrate-binding agents as therapeutics against enveloped viruses.HIV sexual transmission and microbicides.Nanoengineered glycan sensors enabling native glycoprofiling for medicinal applications: towards profiling glycoproteins without labeling or liberation steps.HIV-1 and its resistance to peptidic carbohydrate-binding agents (CBAs): an overview.Insights into animal and plant lectins with antimicrobial activities.Lectins with anti-HIV activity: a review.Actinohivin, a broadly neutralizing prokaryotic lectin, inhibits HIV-1 infection by specifically targeting high-mannose-type glycans on the gp120 envelope.Antiviral lectins: Selective inhibitors of viral entry.A new Phaseolus vulgaris lectin induces selective toxicity on human liver carcinoma Hep G2 cells.Differences in the mannose oligomer specificities of the closely related lectins from Galanthus nivalis and Zea mays strongly determine their eventual anti-HIV activity.Cloning, expression, purification, crystallization and preliminary X-ray studies of a secreted lectin (Rv1419) from Mycobacterium tuberculosisCrystallographic study of the interaction of the anti-HIV lectin actinohivin with the α(1-2)mannobiose moiety of gp120 HMTG.Actinohivin: specific amino acid residues essential for anti-HIV activity.HIV-1 envelope trimer has similar binding characteristics for carbohydrate-binding agents as monomeric gp120.Pyrrolic tripodal receptors for the molecular recognition of carbohydrates: ditopic receptors for dimannosides.Peculiarity in crystal packing of anti-HIV lectin actinohivin in complex with α(1-2)mannobiose.The high mannose-type glycan binding lectin actinohivin: dimerization greatly improves anti-HIV activity.Two carbohydrate recognizing domains from Cycas revoluta leaf lectin show the distinct sugar-binding specificity-A unique mannooligosaccharide recognition by N-terminal domain.Lectins as Promising Therapeutics for the Prevention and Treatment of HIV and Other Potential Coinfections.
P2860
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P2860
Mechanism by which the lectin actinohivin blocks HIV infection of target cells
description
2009 nî lūn-bûn
@nan
2009 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
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2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
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name
Mechanism by which the lectin actinohivin blocks HIV infection of target cells
@ast
Mechanism by which the lectin actinohivin blocks HIV infection of target cells
@en
Mechanism by which the lectin actinohivin blocks HIV infection of target cells
@nl
type
label
Mechanism by which the lectin actinohivin blocks HIV infection of target cells
@ast
Mechanism by which the lectin actinohivin blocks HIV infection of target cells
@en
Mechanism by which the lectin actinohivin blocks HIV infection of target cells
@nl
prefLabel
Mechanism by which the lectin actinohivin blocks HIV infection of target cells
@ast
Mechanism by which the lectin actinohivin blocks HIV infection of target cells
@en
Mechanism by which the lectin actinohivin blocks HIV infection of target cells
@nl
P2093
P2860
P3181
P356
P1476
Mechanism by which the lectin actinohivin blocks HIV infection of target cells
@en
P2093
Akio Takénaka
Atsushi Takahashi
Harumi Chiba
Haruo Tanaka
Hideaki Umeyama
Jun Hirabayashi
Junji Inokoshi
Kaoru Suzuki
Masaru Tsunoda
Satoshi Omura
P2860
P304
15633-15638
P3181
P356
10.1073/PNAS.0907572106
P407
P577
2009-08-26T00:00:00Z