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J

J. D. Lifson

Researcher at Science Applications International Corporation

Publications -  28
Citations -  1964

J. D. Lifson is an academic researcher from Science Applications International Corporation. The author has contributed to research in topics: Virus & Simian immunodeficiency virus. The author has an hindex of 17, co-authored 21 publications receiving 1925 citations.

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Inactivation of human immunodeficiency virus type 1 infectivity with preservation of conformational and functional integrity of virion surface proteins.

TL;DR: Findings indicate that inactivation via this method results in elimination of infectivity with preservation of conformational and functional integrity of virion surface proteins, including both virally encoded determinants and proteins derived from the host cells in which the virus was produced.
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Vpx is required for dissemination and pathogenesis of SIV(SM) PBj: evidence of macrophage-dependent viral amplification

TL;DR: Vpx-dependent viral amplification at local sites of initial infection, perhaps through a macrophage-dependent mechanism, may be a prerequisite for efficient dissemination of infection and pathogenic consequences after exposure through either mucosal or intravenous routes.
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Infectious and Whole Inactivated Simian Immunodeficiency Viruses Interact Similarly with Primate Dendritic Cells (DCs): Differential Intracellular Fate of Virions in Mature and Immature DCs

TL;DR: Compared chemically inactivated SIV having conformationally and functionally intact envelope glycoproteins (2,2′-dithiodipyridine [AT-2] SIV) to infectious and heat-treated SIV, both immature and mature DCs contained similar amounts of viral RNA, suggesting that different uptake/virus entry mechanisms are active in immature and maturity DCs.
Journal Article

Chemical inactivation of retroviral infectivity by targeting nucleocapsid protein zinc fingers: a candidate SIV vaccine

TL;DR: Inactivation and processing of primate immunodeficiency viruses by methods described here results in highly concentrated virus preparations that retain their envelope proteins in a native configuration.