604 research outputs found

    Categorical notions of fibration

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    Fibrations over a category BB, introduced to category theory by Grothendieck, encode pseudo-functors BopCatB^{op} \rightsquigarrow {\bf Cat}, while the special case of discrete fibrations encode presheaves BopSetB^{op} \to {\bf Set}. A two-sided discrete variation encodes functors Bop×ASetB^{op} \times A \to {\bf Set}, which are also known as profunctors from AA to BB. By work of Street, all of these fibration notions can be defined internally to an arbitrary 2-category or bicategory. While the two-sided discrete fibrations model profunctors internally to Cat{\bf Cat}, unexpectedly, the dual two-sided codiscrete cofibrations are necessary to model V\cal V-profunctors internally to V\cal V-Cat\bf Cat.Comment: These notes were initially written by the second-named author to accompany a talk given in the Algebraic Topology and Category Theory Proseminar in the fall of 2010 at the University of Chicago. A few years later, the now first-named author joined to expand and improve in minor ways the exposition. To appear on "Expositiones Mathematicae

    t-structures are normal torsion theories

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    We characterize tt-structures in stable \infty-categories as suitable quasicategorical factorization systems. More precisely we show that a tt-structure t\mathfrak{t} on a stable \infty-category C\mathbf{C} is equivalent to a normal torsion theory F\mathbb{F} on C\mathbf{C}, i.e. to a factorization system F=(E,M)\mathbb{F}=(\mathcal{E},\mathcal{M}) where both classes satisfy the 3-for-2 cancellation property, and a certain compatibility with pullbacks/pushouts.Comment: Minor typographical corrections from v1; 25 pages; to appear in "Applied Categorical Structures

    Human Cytomegalovirus Inhibitor AL18 Also Possesses Activity against Influenza A and B Viruses

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    AL18, an inhibitor of human cytomegalovirus DNA polymerase, was serendipitously found to also block the interaction between the PB1 and PA polymerase subunits of influenza A virus. Furthermore, AL18 effectively inhibited influenza A virus polymerase activity and the overall replication of influenza A and B viruses. A molecular model to explain the binding of AL18 to both cytomegalovirus and influenza targets is proposed. Thus, AL18 represents an interesting lead for the development of new antivirals
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