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Structures of mammalian ER α-glucosidase II capture the binding modes of broad-spectrum iminosugar antivirals.

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Title: Structures of mammalian ER α-glucosidase II capture the binding modes of broad-spectrum iminosugar antivirals.
Authors: Caputo AT; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom;, Alonzi DS; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom;, Marti L; Institute of Sciences of Food Production, Consiglio Nazionale delle Ricerche Unit of Lecce, 73100 Lecce, Italy;, Reca IB; Institute of Sciences of Food Production, Consiglio Nazionale delle Ricerche Unit of Lecce, 73100 Lecce, Italy;, Kiappes JL; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom;, Struwe WB; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom;, Cross A; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom;, Basu S; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom;, Lowe ED; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom;, Darlot B; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom; Ecole Nationale Supérieure de Chimie de Montpellier, 34296 Montpellier Cedex 5, France., Santino A; Institute of Sciences of Food Production, Consiglio Nazionale delle Ricerche Unit of Lecce, 73100 Lecce, Italy;, Roversi P; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom; pietro.roversi@bioch.ox.ac.uk nicole.zitzmann@bioch.ox.ac.uk., Zitzmann N; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom; pietro.roversi@bioch.ox.ac.uk nicole.zitzmann@bioch.ox.ac.uk.
Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2016 Aug 09; Vol. 113 (32), pp. E4630-8. Date of Electronic Publication: 2016 Jul 26.
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
Journal Info: Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1091-6490 (Electronic) Linking ISSN: 00278424 NLM ISO Abbreviation: Proc Natl Acad Sci U S A Subsets: MEDLINE
Database: MEDLINE Ultimate
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  Data: Structures of mammalian ER α-glucosidase II capture the binding modes of broad-spectrum iminosugar antivirals.
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  Data: <searchLink fieldCode="AU" term="%22Caputo+AT%22">Caputo AT</searchLink>; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom;<br /><searchLink fieldCode="AU" term="%22Alonzi+DS%22">Alonzi DS</searchLink>; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom;<br /><searchLink fieldCode="AU" term="%22Marti+L%22">Marti L</searchLink>; Institute of Sciences of Food Production, Consiglio Nazionale delle Ricerche Unit of Lecce, 73100 Lecce, Italy;<br /><searchLink fieldCode="AU" term="%22Reca+IB%22">Reca IB</searchLink>; Institute of Sciences of Food Production, Consiglio Nazionale delle Ricerche Unit of Lecce, 73100 Lecce, Italy;<br /><searchLink fieldCode="AU" term="%22Kiappes+JL%22">Kiappes JL</searchLink>; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom;<br /><searchLink fieldCode="AU" term="%22Struwe+WB%22">Struwe WB</searchLink>; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom;<br /><searchLink fieldCode="AU" term="%22Cross+A%22">Cross A</searchLink>; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom;<br /><searchLink fieldCode="AU" term="%22Basu+S%22">Basu S</searchLink>; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom;<br /><searchLink fieldCode="AU" term="%22Lowe+ED%22">Lowe ED</searchLink>; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom;<br /><searchLink fieldCode="AU" term="%22Darlot+B%22">Darlot B</searchLink>; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom; Ecole Nationale Supérieure de Chimie de Montpellier, 34296 Montpellier Cedex 5, France.<br /><searchLink fieldCode="AU" term="%22Santino+A%22">Santino A</searchLink>; Institute of Sciences of Food Production, Consiglio Nazionale delle Ricerche Unit of Lecce, 73100 Lecce, Italy;<br /><searchLink fieldCode="AU" term="%22Roversi+P%22">Roversi P</searchLink>; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom; pietro.roversi@bioch.ox.ac.uk nicole.zitzmann@bioch.ox.ac.uk.<br /><searchLink fieldCode="AU" term="%22Zitzmann+N%22">Zitzmann N</searchLink>; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom; pietro.roversi@bioch.ox.ac.uk nicole.zitzmann@bioch.ox.ac.uk.
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