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Dani P. Bolognesi

Researcher at Duke University

Publications -  263
Citations -  19414

Dani P. Bolognesi is an academic researcher from Duke University. The author has contributed to research in topics: Virus & Antibody. The author has an hindex of 65, co-authored 261 publications receiving 19001 citations. Previous affiliations of Dani P. Bolognesi include Max Planck Society & Repligen Corporation.

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3'-Azido-3'-deoxythymidine (BW A509U): an antiviral agent that inhibits the infectivity and cytopathic effect of human T-lymphotropic virus type III/lymphadenopathy-associated virus in vitro.

TL;DR: The antiviral effects of a thymidine analogue,3'-azido-3'-deoxythymidine (BW A509U), which, as a triphosphate, inhibits the reverse transcriptase of HTLV-III/LAV, and the in vitro immune functions of normal T cells remain basically intact.
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Phosphorylation of 3'-azido-3'-deoxythymidine and selective interaction of the 5'-triphosphate with human immunodeficiency virus reverse transcriptase.

TL;DR: The results reported here suggest that azidothymidine is nonselectively phosphorylated but that the triphosphate derivative efficiently and selectively binds to the HIV reverse transcriptase.
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Potent suppression of hiv-1 replication in humans by t-20, a peptide inhibitor of gp41-mediated virus entry

TL;DR: Proof-of-concept that viral entry can be successfully blocked in vivo is provided, and short-term administration of T-20 seems safe and provides potent inhibition of HIV replication comparable to anti-retroviral regimens approved at present.
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Principal neutralizing domain of the human immunodeficiency virus type 1 envelope protein

TL;DR: The principal neutralizing determinant of human immunodeficiency virus type 1 (HIV-1) is located in the external envelope protein, gp120, and has been mapped to a 24-amino acid-long sequence (denoted RP135), and deletion of this sequence renders the envelope unable to elicit neutralizing antibodies.