Interaction of fibronectin with semen amyloids synergistically enhances HIV infection. - Wikidata - wikimedia - TriplyDB

Interaction of fibronectin with semen amyloids synergistically enhances HIV infection.

Interaction of fibronectin with semen amyloids synergistically enhances HIV infection.

http://www.wikidata.org/entity/Q34209036

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The long noncoding RNA Pnky regulates neuronal differentiation of embryonic and postnatal neural stem cells Bacterial Interactomes: Interacting Protein Partners Share Similar Function and Are Validated in Independent Assays More Frequently Than Previously Reported A Peptide Derived from the HIV-1 gp120 Coreceptor-Binding Region Promotes Formation of PAP248-286 Amyloid Fibrils to Enhance HIV-1 Infection.Amyloid formation: functional friend or fearful foe?Structural and functional diversity among amyloid proteins: Agents of disease, building blocks of biology, and implications for molecular engineering.

P2860

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Interaction of fibronectin with semen amyloids synergistically enhances HIV infection.

http://www.wikidata.org/entity/Q34209036

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2014 nî lūn-bûn

@nan

2014 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Interaction of fibronectin with semen amyloids synergistically enhances HIV infection.

@ast

Interaction of fibronectin with semen amyloids synergistically enhances HIV infection.

@en

Interaction of fibronectin with semen amyloids synergistically enhances HIV infection.

@nl

type

label

Interaction of fibronectin with semen amyloids synergistically enhances HIV infection.

@ast

Interaction of fibronectin with semen amyloids synergistically enhances HIV infection.

@en

Interaction of fibronectin with semen amyloids synergistically enhances HIV infection.

@nl

prefLabel

Interaction of fibronectin with semen amyloids synergistically enhances HIV infection.

@ast

Interaction of fibronectin with semen amyloids synergistically enhances HIV infection.

@en

Interaction of fibronectin with semen amyloids synergistically enhances HIV infection.

@nl

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P1433

The Journal of Infectious Diseases

P1476

Interaction of fibronectin with semen amyloids synergistically enhances HIV infection.

@en

P2093

H Ewa Witkowska

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

Haichuan Liu

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

Jason Neidleman

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

Nadia R Roan

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

Simon Chu

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

Warner C Greene

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

P2860

Semen-derived amyloid fibrils drastically enhance HIV infection

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

Semen-mediated enhancement of HIV infection is donor-dependent and correlates with the levels of SEVI.

Amyloid-binding small molecules efficiently block SEVI (semen-derived enhancer of virus infection)- and semen-mediated enhancement of HIV-1 infection

Interleukin-7 facilitates HIV-1 transmission to cervico-vaginal tissue ex vivo.

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 EGCG

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

The main green tea polyphenol epigallocatechin-3-gallate counteracts semen-mediated enhancement of HIV infection.

P304

1062-1066

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

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scholarly article

P356

10.1093/INFDIS/JIU220

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

P407

P433

7

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210

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2014-04-08T00:00:00Z

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24719472

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P932

4168303

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