Invariant surface glycoprotein 65 of Trypanosoma brucei is a complement C3 receptor.

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Title: Invariant surface glycoprotein 65 of Trypanosoma brucei is a complement C3 receptor.
Authors: Macleod OJS; Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK., Cook AD; Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.; Kavli Institute for Nanoscience Discovery, Dorothy Crowfoot Hodgkin Building, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK., Webb H; Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK., Crow M; Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK., Burns R; Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK., Redpath M; Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK., Seisenberger S; Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK., Trevor CE; Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK., Peacock L; Bristol Veterinary School and School of Biological Sciences, University of Bristol, Bristol, UK., Schwede A; Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK., Kimblin N; Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK., Francisco AF; Faculty of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, London, WC1E 7HT, UK., Pepperl J; Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK., Rust S; Antibody Discovery and Protein Engineering, Biopharmaceuticals R&D, AstraZeneca, Cambridge, UK., Voorheis P; School of Biochemistry and Immunology, Trinity Biomedical Sciences Institute, Trinity College Dublin, Dublin, Ireland., Gibson W; Bristol Veterinary School and School of Biological Sciences, University of Bristol, Bristol, UK., Taylor MC; Faculty of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, London, WC1E 7HT, UK., Higgins MK; Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK. matthew.higgins@bioch.ox.ac.uk.; Kavli Institute for Nanoscience Discovery, Dorothy Crowfoot Hodgkin Building, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK. matthew.higgins@bioch.ox.ac.uk., Carrington M; Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, UK. mc115@cam.ac.uk.
Source: Nature communications [Nat Commun] 2022 Aug 29; Vol. 13 (1), pp. 5085. Date of Electronic Publication: 2022 Aug 29.
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
Journal Info: Publisher: Nature Pub. Group Country of Publication: England NLM ID: 101528555 Publication Model: Electronic Cited Medium: Internet ISSN: 2041-1723 (Electronic) Linking ISSN: 20411723 NLM ISO Abbreviation: Nat Commun Subsets: MEDLINE
Database: MEDLINE Ultimate
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ISSN:2041-1723
DOI:10.1038/s41467-022-32728-9