Aminoquinoline surfen inhibits the action of SEVI (semen-derived enhancer of viral infection). - Wikidata - awgldk - TriplyDB

Aminoquinoline surfen inhibits the action of SEVI (semen-derived enhancer of viral infection).

Aminoquinoline surfen inhibits the action of SEVI (semen-derived enhancer of viral infection).

http://www.wikidata.org/entity/Q33581944

about

Direct visualization of HIV-enhancing endogenous amyloid fibrils in human semen.Combinations of 3-hydroxyphthalic anhydride-modified ovalbumin with antiretroviral drug-based microbicide candidates display synergistic and complementary effects against HIV-1 infection.The Surprising Role of Amyloid Fibrils in HIV Infection Effect of semen and seminal amyloid on vaginal transmission of simian immunodeficiency virus Liquefaction of semen generates and later degrades a conserved semenogelin peptide that enhances HIV infection.A chemical biology approach demonstrates G protein βγ subunits are sufficient to mediate directional neutrophil chemotaxis.The amyloidogenic SEVI precursor, PAP248-286, is highly unfolded in solution despite an underlying helical tendency.Semen amyloids participate in spermatozoa selection and clearance Semen-mediated enhancement of HIV infection is donor-dependent and correlates with the levels of SEVI.Interaction of fibronectin with semen amyloids synergistically enhances HIV infection.Amyloid-binding small molecules efficiently block SEVI (semen-derived enhancer of virus infection)- and semen-mediated enhancement of HIV-1 infection Enhancement of HIV-1 infectivity by simple, self-assembling modular peptides Semen enhances HIV infectivity and impairs the antiviral efficacy of microbicides.Discovery of modulators of HIV-1 infection from the human peptidome.Inhibition of the enhancement of infection of human immunodeficiency virus by semen-derived enhancer of virus infection using amyloid-targeting polymeric nanoparticles.Characterization of the Influence of Semen-Derived Enhancer of Virus Infection on the Interaction of HIV-1 with Female Reproductive Tract Tissues.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.ADS-J1 inhibits semen-derived amyloid fibril formation and blocks fibril-mediated enhancement of HIV-1 infection.Amyloid formation: functional friend or fearful foe?No SEVI-mediated enhancement of rectal HIV-1 transmission of HIV-1 in two humanized mouse cohorts Bacterial curli protein promotes the conversion of PAP248-286 into the amyloid SEVI: cross-seeding of dissimilar amyloid sequences Gallic Acid Is an Antagonist of Semen Amyloid Fibrils That Enhance HIV-1 Infection.Glycosaminoglycans and infection.Seminal plasma and semen amyloids enhance cytomegalovirus infection in cell culture.The D-amino acid peptide D3 reduces amyloid fibril boosted HIV-1 infectivity.Small molecule antagonists of cell-surface heparan sulfate and heparin-protein interactions.Implications of the nucleocapsid and the microenvironment in retroviral reverse transcription.Peptide nanofibrils as enhancers of retroviral gene transfer.Glycosaminoglycan and DNA Binding Induced Intra- and Intermolecular Exciton Coupling of the bis-4-Aminoquinoline Surfen.Targeting heparin and heparan sulfate protein interactions.Oligovalent amyloid-binding agents reduce SEVI-mediated enhancement of HIV-1 infection.Brazilin Inhibits Prostatic Acidic Phosphatase Fibrillogenesis and Decreases its Cytotoxicity.The KT Jeang Retrovirology prize 2016: Frank Kirchhoff.Site specific interaction of the polyphenol EGCG with the SEVI amyloid precursor peptide PAP(248-286).Small Molecule Antagonist of Cell Surface Glycosaminoglycans Restricts Mouse Embryonic Stem Cells in a Pluripotent State.Sulfonated Compounds Bind with Prostatic Acid Phosphatase (PAP248–286) to Inhibit the Formation of Amyloid Fibrils.

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P2860

Aminoquinoline surfen inhibits the action of SEVI (semen-derived enhancer of viral infection).

http://www.wikidata.org/entity/Q33581944

description

2009 nî lūn-bûn

@nan

2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

@zh-hk

2009年論文

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2009年論文

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2009年论文

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name

Aminoquinoline surfen inhibits ...... enhancer of viral infection).

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Aminoquinoline surfen inhibits ...... enhancer of viral infection).

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Aminoquinoline surfen inhibits the action of SEVI

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type

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Aminoquinoline surfen inhibits ...... enhancer of viral infection).

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Aminoquinoline surfen inhibits ...... enhancer of viral infection).

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Aminoquinoline surfen inhibits the action of SEVI

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Aminoquinoline surfen inhibits ...... enhancer of viral infection).

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Aminoquinoline surfen inhibits ...... enhancer of viral infection).

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Aminoquinoline surfen inhibits the action of SEVI

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JBC.M109.066167

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Journal of Biological Chemistry

P1476

Aminoquinoline surfen inhibits ...... enhancer of viral infection).

@en

P2093

Jan Münch

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Nadia R Roan

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Stefanie Sowinski

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Warner C Greene

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P2860

Semen-derived amyloid fibrils drastically enhance HIV infection

Fibrils of prostatic acid phosphatase fragments boost infections with XMRV (xenotropic murine leukemia virus-related virus), a human retrovirus associated with prostate cancer

Identification of small molecule inhibitors of anthrax lethal factor

Animal cell mutants defective in glycosaminoglycan biosynthesis

Emergence of resistant human immunodeficiency virus type 1 in patients receiving fusion inhibitor (T-20) monotherapy.

Effects of CCR5 and CD4 cell surface concentrations on infections by macrophagetropic isolates of human immunodeficiency virus type 1.

Surfen, a small molecule antagonist of heparan sulfate

The cationic properties of SEVI underlie its ability to enhance human immunodeficiency virus infection.

Lack of effectiveness of cellulose sulfate gel for the prevention of vaginal HIV transmission.

Envelope-dependent, cyclophilin-independent effects of glycosaminoglycans on human immunodeficiency virus type 1 attachment and infection.

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1861-1869

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scholarly article

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10.1074/JBC.M109.066167

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3

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285

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Frank Kirchhoff

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2009-11-06T00:00:00Z

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19897482

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2804344

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