Peptides released by physiological cleavage of semen coagulum proteins form amyloids that enhance HIV infection. - Wikidata - wikimedia - TriplyDB

Peptides released by physiological cleavage of semen coagulum proteins form amyloids that enhance HIV infection.

Peptides released by physiological cleavage of semen coagulum proteins form amyloids that enhance HIV infection.

http://www.wikidata.org/entity/Q35669283

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Peptides derived from HIV-1 gp120 co-receptor binding domain form amyloid fibrils and enhance HIV-1 infection Blocking HIV-1 transmission in the female reproductive tract: from microbicide development to exploring local antiviral responses Predominant Role of Plasmacytoid Dendritic Cells in Stimulating Systemic Autoimmunity HIV, sexual violence and special populations: adolescence and pregnancy Bottlenecks in HIV-1 transmission: insights from the study of founder viruses Polyanionic candidate microbicides accelerate the formation of semen-derived amyloid fibrils to enhance HIV-1 infection Direct visualization of HIV-enhancing endogenous amyloid fibrils in human semen.Sexual violence and HIV transmission: summary proceedings of a scientific research planning meeting.Seminal plasma induces inflammation and enhances HIV-1 replication in human cervical tissue explants.The Surprising Role of Amyloid Fibrils in HIV Infection Seminal plasma induces global transcriptomic changes associated with cell migration, proliferation and viability in endometrial epithelial cells and stromal fibroblasts Friend or Foe: Innate Sensing of HIV in the Female Reproductive Tract.Effect of semen and seminal amyloid on vaginal transmission of simian immunodeficiency virus Structural 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.Semen amyloids participate in spermatozoa selection and clearance Interaction of fibronectin with semen amyloids synergistically enhances HIV infection.Innate and adaptive immune responses in male and female reproductive tracts in homeostasis and following HIV infection.Interleukin-7 facilitates HIV-1 transmission to cervico-vaginal tissue ex vivo.Semen enhances HIV infectivity and impairs the antiviral efficacy of microbicides.Discovery of modulators of HIV-1 infection from the human peptidome.Enhancement of herpes simplex virus (HSV) infection by seminal plasma and semen amyloids implicates a new target for the prevention of HSV 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.A Peptide Derived from the HIV-1 gp120 Coreceptor-Binding Region Promotes Formation of PAP248-286 Amyloid Fibrils to Enhance HIV-1 Infection.Seminal plasma accelerates semen-derived enhancer of viral infection (SEVI) fibril formation by the prostatic acid phosphatase (PAP248-286) peptide.HIV-1 vaginal transmission: cell-free or cell-associated virus?A 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 oligonucleotide Epigallocatechin-3-gallate rapidly remodels PAP85-120, SEM1(45-107), and SEM2(49-107) seminal amyloid fibrils.A novel role for APOBEC3: susceptibility to sexual transmission of murine acquired immunodeficiency virus (mAIDS) is aggravated in APOBEC3 deficient mice.Nucleic acid-containing amyloid fibrils potently induce type I interferon and stimulate systemic autoimmunity.Mucosal stromal fibroblasts markedly enhance HIV infection of CD4+ T cells.Epigallocatechin Gallate Inhibits Macaque SEVI-Mediated Enhancement of SIV or SHIV Infection.Core sequence of PAPf39 amyloid fibrils and mechanism of pH-dependent fibril formation: the role of monomer conformation No SEVI-mediated enhancement of rectal HIV-1 transmission of HIV-1 in two humanized mouse cohorts Improving preclinical models of HIV microbicide efficacy.Bacterial curli protein promotes the conversion of PAP248-286 into the amyloid SEVI: cross-seeding of dissimilar amyloid sequences

P2860

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P2860

Peptides released by physiological cleavage of semen coagulum proteins form amyloids that enhance HIV infection.

http://www.wikidata.org/entity/Q35669283

description

2011 nî lūn-bûn

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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2011年论文

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2011年论文

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name

Peptides released by physiolog ...... ds that enhance HIV infection.

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Peptides released by physiolog ...... ds that enhance HIV infection.

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type

label

Peptides released by physiolog ...... ds that enhance HIV infection.

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Peptides released by physiolog ...... ds that enhance HIV infection.

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Peptides released by physiolog ...... ds that enhance HIV infection.

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Peptides released by physiolog ...... ds that enhance HIV infection.

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J.CHOM.2011.10.010

P1433

Cell Host & Microbe

P1476

Peptides released by physiolog ...... ds that enhance HIV infection.

@en

P2093

Christina M Stürzel

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Franziska Arnold

http://www.w3.org/2001/XMLSchema#string

H Ewa Witkowska

http://www.w3.org/2001/XMLSchema#string

Haichuan Liu

http://www.w3.org/2001/XMLSchema#string

Jan Münch

http://www.w3.org/2001/XMLSchema#string

Janis A Müller

http://www.w3.org/2001/XMLSchema#string

Ming Dong

http://www.w3.org/2001/XMLSchema#string

Nadia R Roan

http://www.w3.org/2001/XMLSchema#string

Paul Walther

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Simon Chu

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P2860

Semen-derived amyloid fibrils drastically enhance HIV infection

The major bactericidal activity of human seminal plasma is zinc-dependent and derived from fragmentation of the semenogelins

Semenogelin I: a coagulum forming, multifunctional seminal vesicle protein

Opsonization of HIV-1 by semen complement enhances infection of human epithelial cells

Quantification of seminal plasma motility inhibitor/semenogelin in human seminal plasma

Distribution and tissue expression of semenogelin I and II in man as demonstrated by in situ hybridization and immunocytochemistry

Characterization of prostate-specific antigen proteolytic activity on its major physiological substrate, the sperm motility inhibitor precursor/semenogelin I

Senile seminal vesicle amyloid is derived from semenogelin I

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

Spermatozoa capture HIV-1 through heparan sulfate and efficiently transmit the virus to dendritic cells.

P304

541-550

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scholarly article

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10.1016/J.CHOM.2011.10.010

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P433

6

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P478

10

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Frank Kirchhoff

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2011-12-01T00:00:00Z

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51896149

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22177559

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3257029

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