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Nancy Ruffing

Researcher at Takeda Pharmaceutical Company

Publications -  7
Citations -  2805

Nancy Ruffing is an academic researcher from Takeda Pharmaceutical Company. The author has contributed to research in topics: Chemokine receptor & Chemokine receptor CCR5. The author has an hindex of 6, co-authored 7 publications receiving 2767 citations. Previous affiliations of Nancy Ruffing include Aaron Diamond AIDS Research Center.

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Journal ArticleDOI

CD4-induced interaction of primary HIV-1 gp120 glycoproteins with the chemokine receptor CCR-5

TL;DR: It is suggested that HIV-1 attachment to CD4 creates a high-affinity binding site for CCR-5, leading to membrane fusion and virus entry.
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CCR5 Levels and Expression Pattern Correlate with Infectability by Macrophage-tropic HIV-1, In Vitro

TL;DR: Anti-CCR5 mAbs were poor inhibitors of chemokine binding, indicating that HIV-1 and ligands bind to separate, but overlapping regions of CCR5, and demonstrate the feasibility of blocking macrophage-tropic HIV- 1 entry into cells with an anti-CCr5 reagent.
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Interaction of chemokine receptor CCR5 with its ligands: multiple domains for HIV-1 gp120 binding and a single domain for chemokine binding.

TL;DR: The second extracellular loop of CCR5 is an ideal target site for the development of inhibitors of either chemokine or HIV-1 binding to CCR4, suggesting a complicated pattern of HIV- 1 gp120 binding to different regions of C CR5, but a relatively simple pattern for chemokin binding.
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A tyrosine-rich region in the N terminus of CCR5 is important for human immunodeficiency virus type 1 entry and mediates an association between gp120 and CCR5.

TL;DR: A small tyrosine-rich region of CCR5 proximal to the N-terminal cysteine that is critical for entry of macrophage- Tropic and dual-tropic variants of HIV-1 is identified and identified as necessary for the physical association of the gp120 envelope glycoprotein with C CR5 and for HIV- 1 infection.
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Discrete Steps in Binding and Signaling of Interleukin-8 with Its Receptor

TL;DR: The results support a model in which the binding and signaling of IL-8 with its receptor occur in at least two discrete steps involving distinct domains of the receptor, consistent with the notion that discrete conformational changes of the receptors secondary to ligand binding are required to trigger various biological responses.