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The LEM domain proteins emerin and LAP2α are dispensable for human immunodeficiency virus type 1 and murine leukemia virus infections
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Solution NMR structure of the barrier-to-autointegration factor-emerin complex
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Poxviral b1 kinase overcomes barrier to autointegration factor, a host Defense against virus replication
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Caenorhabditis elegans BAF-1 and its kinase VRK-1 participate directly in post-mitotic nuclear envelope assembly
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The vaccinia-related kinases phosphorylate the N′ terminus of BAF, regulating its interaction with DNA and its retention in the nucleus
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Barrier-to-autointegration factor phosphorylation on Ser-4 regulates emerin binding to lamin A in vitro and emerin localization in vivo
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Low-force DNA condensation and discontinuous high-force decondensation reveal a loop-stabilizing function of the protein Fis
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Structural basis for DNA bridging by barrier-to-autointegration factor
CM Bradley et al.
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Barrier-to-autointegration factor is required to segregate and enclose chromosomes within the nuclear envelope and assemble the nuclear lamina
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LAP2α and BAF collaborate to organize the Moloney murine leukemia virus preintegration complex
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Micromechanical analysis of the binding of DNA-bending proteins HMGB1, NHP6A, and HU reveals their ability to form highly stable DNA-protein complexes
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How do site-specific DNA-binding proteins find their targets?
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Barrier-to-autointegration factor plays crucial roles in cell cycle progression and nuclear organization in Drosophila
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Barrier-to-autointegration factor: major roles in chromatin decondensation and nuclear assembly
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Direct observation of single MuB polymers: Evidence for a DNA-dependent conformational change for generating an active target complex
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Structural basis of DNA bridging by barrier-to-autointegration factor
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Barrier-to-autointegration factor (BAF) bridges DNA in a discrete, higher-order nucleoprotein complex
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