Structure of human endo-α-1,2-mannosidase (MANEA), an antiviral host-glycosylation target.

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Bibliographic Details
Title: Structure of human endo-α-1,2-mannosidase (MANEA), an antiviral host-glycosylation target.
Authors: Sobala ŁF; Department of Chemistry, University of York, York YO10 5DD, United Kingdom., Fernandes PZ; School of Chemistry, University of Melbourne, Parkville, VIC 3010, Australia.; Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia., Hakki Z; School of Chemistry, University of Melbourne, Parkville, VIC 3010, Australia.; Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia., Thompson AJ; Department of Chemistry, University of York, York YO10 5DD, United Kingdom., Howe JD; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom., Hill M; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom., Zitzmann N; Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom., Davies S; Institute for Immunology and Immunotherapy, University of Birmingham, Birmingham B15 2TT, United Kingdom., Stamataki Z; Institute for Immunology and Immunotherapy, University of Birmingham, Birmingham B15 2TT, United Kingdom., Butters TD; 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., Williams SJ; School of Chemistry, University of Melbourne, Parkville, VIC 3010, Australia; sjwill@unimelb.edu.au gideon.davies@york.ac.uk.; Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia., Davies GJ; Department of Chemistry, University of York, York YO10 5DD, United Kingdom; sjwill@unimelb.edu.au gideon.davies@york.ac.uk.
Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2020 Nov 24; Vol. 117 (47), pp. 29595-29601. Date of Electronic Publication: 2020 Nov 05.
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
Description
ISSN:1091-6490
DOI:10.1073/pnas.2013620117