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HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation

Article Abstract:

Research reveals that the antiviral pathway in human T lymphocytes and leukemic T-cell lines is neutralized by the viral infectivity factor (Vif) encoded by HIV-1. Results show that without Vif, the antiviral pathway inactivates HIV-1. Data indicate that APOBEC3G, a cytidine deaminase, confers the antiviral phenotype and that Vif binds to it inducing its degradation.

Author: Marin, Mariana, Rose, Kristine M., Kozak, Susan L., Kabat, David
Publisher: Nature America, Inc.
Publication Name: Nature Medicine
Subject: Health
ISSN: 1078-8956
Year: 2003
HIV infection, HIV infections, Proteolysis, Antiviral agent structure-activity relationships, Neutralization (Chemistry)

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Toll-like receptor-4 (TLR) signaling augments chemokine-induced neutrophil migration by modulating cell surface expression of chemokine receptors

Article Abstract:

Results demonstrate that regulation of polymorphonuclear leukocyte migration is contolled through Toll-like receptor-4-mediated reduction in chemokine receptor internalization, which reduces the expression of G-protein-coupled receptor kinase 2 and 5 by the chemokine macrophage inflammatory protein-2.

Author: Fan, Jie, Malik, Asrar B.Research
Publisher: Nature America, Inc.
Publication Name: Nature Medicine
Subject: Health
ISSN: 1078-8956
Year: 2003
G proteins, Cell migration, Neutrophils, Chemokine receptors

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Tolerance is dependent on complement C3 fragment iC3b binding to antigen-presenting cells

Article Abstract:

The induction of tolerance is mediated by the transforming growth factor-beta2 and interleukin-10, which are produced by the ligation of the complement C3 activated product iC3b to the iC3b receptor on antigen-presenting cells.

Author: Molina, Hector, Sohn, Jeong-Hyeon, Bora, Puran S., Sur, Hye-Jung, Kaplan, Henry J., Bora, Nalini S.
Publisher: Nature America, Inc.
Publication Name: Nature Medicine
Subject: Health
ISSN: 1078-8956
Year: 2003
Immunity, Immunity (Physiology), Complement (Immunology), Complement (Protein)

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Subjects list: United States, Physiological aspects, Protein binding, Immune response
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