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A kinesin-1 binding motif in vaccinia virus that is widespread throughout the human genomeCoupling viruses to dynein and kinesin-1Structure of B-MLV capsid amino-terminal domain reveals key features of viral tropism, gag assembly and core formationStructural Basis for Kinesin-1:Cargo RecognitionTRIM5 alpha cytoplasmic bodies are highly dynamic structures.F11-mediated inhibition of RhoA signalling enhances the spread of vaccinia virus in vitro and in vivo in an intranasal mouse model of infectionCapsid processing requirements for abrogation of Fv1 and Ref1 restrictionTrim-cyclophilin A fusion proteins can restrict human immunodeficiency virus type 1 infection at two distinct phases in the viral life cycle.The light chains of kinesin-1 are autoinhibited.The Dynamic Localization of Cytoplasmic Dynein in Neurons Is Driven by Kinesin-1.Folliculin directs the formation of a Rab34-RILP complex to control the nutrient-dependent dynamic distribution of lysosomes.Nck- and N-WASP-dependent actin-based motility is conserved in divergent vertebrate poxviruses.An E2-F12 complex is required for intracellular enveloped virus morphogenesis during vaccinia infection.Folliculin - A tumor suppressor at the intersection of metabolic signaling and membrane traffic.Vaccinia-induced epidermal growth factor receptor-MEK signalling and the anti-apoptotic protein F1L synergize to suppress cell death during infection.Backseat drivers: Regulation of dynein motilitySKIP controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain.Vaccinia virus F11 promotes viral spread by acting as a PDZ-containing scaffolding protein to bind myosin-9A and inhibit RhoA signaling.A small-molecule activator of kinesin-1 drives remodeling of the microtubule network.Structural basis for isoform-specific kinesin-1 recognition of Y-acidic cargo adaptorsClathrin Potentiates Vaccinia-Induced Actin Polymerization to Facilitate Viral Spread
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description
hulumtues
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researcher
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wetenschapper
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հետազոտող
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name
Mark Dodding
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Mark Dodding
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Mark Dodding
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Mark Dodding
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Mark Dodding
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type
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Mark Dodding
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Mark Dodding
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Mark Dodding
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Mark Dodding
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Mark Dodding
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Mark Dodding
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Mark Dodding
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Mark Dodding
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Mark Dodding
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Mark Dodding
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P1153
8679652400
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P31
P496
0000-0001-8091-6534