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Adam J. Fletcher

Researcher at University of Dundee

Publications -  21
Citations -  2040

Adam J. Fletcher is an academic researcher from University of Dundee. The author has contributed to research in topics: Ubiquitin ligase & Viral replication. The author has an hindex of 16, co-authored 21 publications receiving 1690 citations. Previous affiliations of Adam J. Fletcher include University of Oxford & University College London.

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HIV-1 capsid-cyclophilin interactions determine nuclear import pathway, integration targeting and replication efficiency.

TL;DR: It is reported that HIV-1 capsid binds directly to the cyclophilin domain of Nup358/RanBP2, and inhibition of CypA reduced dependence on Nup 358 and the nuclear basket protein Nup153, suggesting that CypA regulates the choice of the nuclear import machinery that is engaged by the virus.
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HIV-1 evades innate immune recognition through specific cofactor recruitment

TL;DR: It is concluded that HIV-1 has evolved to use CPSF6 and cyclophilins to cloak its replication, allowing evasion of innate immune sensors and induction of a cell-autonomous innate immune response in primary human macrophages.
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CPSF6 defines a conserved capsid interface that modulates HIV-1 replication.

TL;DR: A novel protein-protein interface in the N-terminal domain of HIV-1 CA is determined by X-ray crystallography, which mediates both viral restriction and host cofactor dependence, and is highly conserved across lentiviruses and is accessible in the context of a hexameric lattice.
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Host Cofactors and Pharmacologic Ligands Share an Essential Interface in HIV-1 Capsid That Is Lost upon Disassembly.

TL;DR: It is shown that a multi-subunit interface formed exclusively within CA hexamers mediates binding to linear epitopes within cellular cofactors NUP153 and CPSF6, and is competed for by the antiretroviral compounds PF74 and BI-2.
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Sequential ubiquitination and deubiquitination enzymes synchronize the dual sensor and effector functions of TRIM21

TL;DR: The stepwise ubiquitination mechanism catalyzed by TRIM21, as well as the various cofactors required, that allows these two antiviral activities to occur synchronously at the proteasome are uncovered.