Actinohivin, a broadly neutralizing prokaryotic lectin, inhibits HIV-1 infection by specifically targeting high-mannose-type glycans on the gp120 envelope.
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Activity of and effect of subcutaneous treatment with the broad-spectrum antiviral lectin griffithsin in two laboratory rodent modelsStructural insights into the specific anti-HIV property of actinohivin: structure of its complex with the α(1–2)mannobiose moiety of gp120The characteristic structure of anti-HIV actinohivin in complex with three HMTG D1 chains of HIV-gp120HIV-1 gp120 as a therapeutic target: navigating a moving labyrinthThe lantibiotic peptide labyrinthopeptin A1 demonstrates broad anti-HIV and anti-HSV activity with potential for microbicidal applicationsThe Cellular Thioredoxin-1/Thioredoxin Reductase-1 Driven Oxidoreduction Represents a Chemotherapeutic Target for HIV-1 Entry InhibitionCurrent progress and challenges in HIV gene therapyBroad antiviral activity of carbohydrate-binding agents against the four serotypes of dengue virus in monocyte-derived dendritic cellsA strategy for phage display selection of functional domain-exchanged immunoglobulin scaffolds with high affinity for glycan targets.Complement and viral pathogenesisBroad anti-HIV activity of the Oscillatoria agardhii agglutinin homologue lectin family.Role of the carbohydrate-binding sites of griffithsin in the prevention of DC-SIGN-mediated capture and transmission of HIV-1.The highly conserved glycan at asparagine 260 of HIV-1 gp120 is indispensable for viral entryThe role of individual carbohydrate-binding sites in the function of the potent anti-HIV lectin griffithsin.Combinations of griffithsin with other carbohydrate-binding agents demonstrate superior activity against HIV Type 1, HIV Type 2, and selected carbohydrate-binding agent-resistant HIV Type 1 strainsThe 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.Lectin-Glycan Interaction Network-Based Identification of Host Receptors of Microbial Pathogenic AdhesinsThe lectin-like protein 1 in Lactobacillus rhamnosus GR-1 mediates tissue-specific adherence to vaginal epithelium and inhibits urogenital pathogens.Lectins, Interconnecting Proteins with Biotechnological/Pharmacological and Therapeutic Applications.HIV sexual transmission and microbicides.HIV-1 and its resistance to peptidic carbohydrate-binding agents (CBAs): an overview.Antiviral lectins: Selective inhibitors of viral entry.The role of N-glycans of HIV-1 gp41 in virus infectivity and susceptibility to the suppressive effects of carbohydrate-binding agents.Differences in the mannose oligomer specificities of the closely related lectins from Galanthus nivalis and Zea mays strongly determine their eventual anti-HIV activity.NICTABA and UDA, two GlcNAc-binding lectins with unique antiviral activity profiles.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.Lectins as Promising Therapeutics for the Prevention and Treatment of HIV and Other Potential Coinfections.
P2860
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P2860
Actinohivin, a broadly neutralizing prokaryotic lectin, inhibits HIV-1 infection by specifically targeting high-mannose-type glycans on the gp120 envelope.
description
2010 nî lūn-bûn
@nan
2010年の論文
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2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
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2010年论文
@zh-cn
name
Actinohivin, a broadly neutral ...... glycans on the gp120 envelope.
@en
type
label
Actinohivin, a broadly neutral ...... glycans on the gp120 envelope.
@en
prefLabel
Actinohivin, a broadly neutral ...... glycans on the gp120 envelope.
@en
P2093
P2860
P50
P356
P1476
Actinohivin, a broadly neutral ...... glycans on the gp120 envelope.
@en
P2093
Atsushi Takahashi
Bart Hoorelbeke
Dana Huskens
Geoffrey Férir
Haruo Tanaka
Katrien O François
P2860
P304
P356
10.1128/AAC.00254-10
P407
P577
2010-05-24T00:00:00Z