The main green tea polyphenol epigallocatechin-3-gallate counteracts semen-mediated enhancement of HIV infection.
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Binding of epigallocatechin-3-gallate to transthyretin modulates its amyloidogenicityPeptides derived from HIV-1 gp120 co-receptor binding domain form amyloid fibrils and enhance HIV-1 infectionAnti-infective properties of epigallocatechin-3-gallate (EGCG), a component of green teaNMR Structure in a Membrane Environment Reveals Putative Amyloidogenic Regions of the SEVI Precursor Peptide PAP 248−286Direct visualization of HIV-enhancing endogenous amyloid fibrils in human semen.Structural and functional analysis of human prostatic acid phosphatase.The Surprising Role of Amyloid Fibrils in HIV InfectionSeminal plasma induces global transcriptomic changes associated with cell migration, proliferation and viability in endometrial epithelial cells and stromal fibroblastsEffect of semen and seminal amyloid on vaginal transmission of simian immunodeficiency virusStructural characterization of semen coagulum-derived SEM1(86-107) amyloid fibrils that enhance HIV-1 infection.Liquefaction of semen generates and later degrades a conserved semenogelin peptide that enhances HIV infection.The amyloidogenic SEVI precursor, PAP248-286, is highly unfolded in solution despite an underlying helical tendency.HIV-1 enhancing effect of prostatic acid phosphatase peptides is reduced in human seminal plasma.EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity.Semen-mediated enhancement of HIV infection is donor-dependent and correlates with the levels of SEVI.Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanolsInteraction of fibronectin with semen amyloids synergistically enhances HIV infection.Morin hydrate inhibits amyloid formation by islet amyloid polypeptide and disaggregates amyloid fibers.An overview of drugs currently under investigation for the treatment of transthyretin-related hereditary amyloidosis.Semen enhances HIV infectivity and impairs the antiviral efficacy of microbicides.Discovery of modulators of HIV-1 infection from the human peptidome.Morphology-Dependent HIV-Enhancing Effect of Semen-Derived Enhancer of Viral Infection.Inhibition of the enhancement of infection of human immunodeficiency virus by semen-derived enhancer of virus infection using amyloid-targeting polymeric nanoparticles.Naturally occurring fragments from two distinct regions of the prostatic acid phosphatase form amyloidogenic enhancers of HIV infection.Peptides released by physiological cleavage of semen coagulum proteins form amyloids that enhance HIV infection.Assessment of the range of the HIV-1 infectivity enhancing effect of individual human semen specimen and the range of inhibition by EGCGA molecular tweezer antagonizes seminal amyloids and HIV infection.ADS-J1 inhibits semen-derived amyloid fibril formation and blocks fibril-mediated enhancement of HIV-1 infection.Amyloid formation: functional friend or fearful foe?Abolishing HIV-1 infectivity using a polypurine tract-specific G-quadruplex-forming oligonucleotideEpigallocatechin-3-gallate rapidly remodels PAP85-120, SEM1(45-107), and SEM2(49-107) seminal amyloid fibrils.NMR characterization of monomeric and oligomeric conformations of human calcitonin and its interaction with EGCG.Indication of Horizontal DNA Gene Transfer by Extracellular Vesicles.Epigallocatechin Gallate Inhibits Macaque SEVI-Mediated Enhancement of SIV or SHIV Infection.Alternative pathways of human islet amyloid polypeptide aggregation distinguished by (19)f nuclear magnetic resonance-detected kinetics of monomer consumption.No SEVI-mediated enhancement of rectal HIV-1 transmission of HIV-1 in two humanized mouse cohortsBacterial curli protein promotes the conversion of PAP248-286 into the amyloid SEVI: cross-seeding of dissimilar amyloid sequencesNatural compounds may open new routes to treatment of amyloid diseasesProtein folding and aggregation into amyloid: the interference by natural phenolic compoundsGallic Acid Is an Antagonist of Semen Amyloid Fibrils That Enhance HIV-1 Infection.
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The main green tea polyphenol epigallocatechin-3-gallate counteracts semen-mediated enhancement of HIV infection.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on 18 May 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
The main green tea polyphenol ...... enhancement of HIV infection.
@en
The main green tea polyphenol ...... enhancement of HIV infection.
@nl
type
label
The main green tea polyphenol ...... enhancement of HIV infection.
@en
The main green tea polyphenol ...... enhancement of HIV infection.
@nl
prefLabel
The main green tea polyphenol ...... enhancement of HIV infection.
@en
The main green tea polyphenol ...... enhancement of HIV infection.
@nl
P2093
P2860
P356
P1476
The main green tea polyphenol ...... enhancement of HIV infection.
@en
P2093
Barbara Holstermann
Heinrich Hohenberg
Ilona Hauber
Joachim Hauber
Werner Hunstein
P2860
P304
P356
10.1073/PNAS.0811827106
P407
P577
2009-05-18T00:00:00Z