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Alison Slaughter

Researcher at Ohio State University

Publications -  12
Citations -  950

Alison Slaughter is an academic researcher from Ohio State University. The author has contributed to research in topics: Integrase & Allosteric regulation. The author has an hindex of 10, co-authored 12 publications receiving 821 citations.

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Allosteric integrase inhibitor potency is determined through the inhibition of HIV-1 particle maturation.

TL;DR: It is demonstrated that ALLinI potency is unexpectedly accounted for during the late phase of HIV-1 replication, and cooperative multimerization of IN by ALLINIs together with the inability for LEDGF/p75 to effectively engage the virus during its egress from cells underscores the multimodal mechanism of ALLINI action.
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BET proteins promote efficient murine leukemia virus integration at transcription start sites

TL;DR: It is shown that purified recombinant Brd4(1-720) binds with high affinity to MLV integrase and stimulates correct concerted integration in vitro and elucidate the importance of BET proteins for MLV integration efficiency and targeting and provide a route to developing safer MLV-based vectors for human gene therapy.
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Multimode, cooperative mechanism of action of allosteric HIV-1 integrase inhibitors.

TL;DR: 2-(quinolin-3-yl) acetic acid derivatives impairs both integrase-LEDGF binding and LEDGF-independent integrase catalytic activities with similar IC50 values, defining them as bona fide allosteric inhibitors of integrase function.
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HIV-1 Integrase Binds the Viral RNA Genome and Is Essential during Virion Morphogenesis

TL;DR: It is demonstrated that IN directly binds the viral RNA genome in virions and these interactions have specificity, as IN exhibits distinct preference for select viral RNA structural elements.
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A New Class of Multimerization Selective Inhibitors of HIV-1 Integrase

TL;DR: Design of small molecules that allowed us to probe the role of HIV-1 IN multimerization independently from IN-LEDGF/p75 interactions in infected cells delineate the significance of correctly ordered IN structure for HIV- 1 particle morphogenesis and demonstrate feasibility of exploiting INMultimerization as a therapeutic target.