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    Wyświetlanie 1-3 z 3
    Tytuł:
    Switching of Receptor Binding Poses between Closely Related Enteroviruses.
    Autorzy:
    Zhou D; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford OX3 7BN, UK.; Chinese Academy of Medical Sciences Oxford Institute, University of Oxford, Oxford OX3 7FZ, UK.
    Qin L; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford OX3 7BN, UK.
    Duyvesteyn HME; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford OX3 7BN, UK.
    Zhao Y; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford OX3 7BN, UK.
    Lin TY; Division of Pediatric Infectious Diseases, Department of Pediatrics, Chang Gung Memorial Hospital, Taoyuan 333, Taiwan.
    Fry EE; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford OX3 7BN, UK.
    Ren J; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford OX3 7BN, UK.
    Huang KA; Graduate Institute of Immunology and Department of Pediatrics, National Taiwan University Hospital, College of Medicine, National Taiwan University, Taipei 100, Taiwan.
    Stuart DI; Division of Structural Biology, Nuffield Department of Medicine, University of Oxford, The Wellcome Centre for Human Genetics, Headington, Oxford OX3 7BN, UK.; Chinese Academy of Medical Sciences Oxford Institute, University of Oxford, Oxford OX3 7FZ, UK.; Diamond Light Source Ltd., Harwell Science & Innovation Campus, Didcot OX11 0DE, UK.
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    Źródło:
    Viruses [Viruses] 2022 Nov 24; Vol. 14 (12). Date of Electronic Publication: 2022 Nov 24.
    Typ publikacji:
    Journal Article; Research Support, Non-U.S. Gov't
    MeSH Terms:
    Enterovirus*/metabolism
    Enterovirus Infections*
    Infant, Newborn ; Humans ; Cryoelectron Microscopy ; CD55 Antigens ; Enterovirus B, Human/metabolism
    Czasopismo naukowe
    Pełny tekst  Link otwiera się w nowym oknie Pełny tekstSzczegóły
    Tytuł:
    Nonlytic cellular release of hepatitis A virus requires dual capsid recruitment of the ESCRT-associated Bro1 domain proteins HD-PTP and ALIX.
    Autorzy:
    Shirasaki T; Lineberger Comprehensive Cancer Center, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.
    Feng H; Lineberger Comprehensive Cancer Center, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.
    Duyvesteyn HME; Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, United Kingdom.; Diamond Light Source, Didcot, United Kingdom.
    Fusco WG; Department of Medicine, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.
    McKnight KL; Lineberger Comprehensive Cancer Center, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.
    Xie L; Lineberger Comprehensive Cancer Center, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.; Department of Biochemistry and Biophysics, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.
    Boyce M; Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, United Kingdom.
    Kumar S; Division of Infectious Diseases and Geographic Medicine, Department of Medicine, Stanford University School of Medicine, Stanford, California, United States of America.; Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, California, United States of America.
    Barouch-Bentov R; Division of Infectious Diseases and Geographic Medicine, Department of Medicine, Stanford University School of Medicine, Stanford, California, United States of America.; Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, California, United States of America.
    González-López O; Lineberger Comprehensive Cancer Center, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.
    McNamara R; Lineberger Comprehensive Cancer Center, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.
    Wang L; Lineberger Comprehensive Cancer Center, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.; Department of Biochemistry and Biophysics, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.
    Hertel-Wulff A; Lineberger Comprehensive Cancer Center, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.
    Chen X; Lineberger Comprehensive Cancer Center, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.; Department of Biochemistry and Biophysics, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.
    Einav S; Division of Infectious Diseases and Geographic Medicine, Department of Medicine, Stanford University School of Medicine, Stanford, California, United States of America.; Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, California, United States of America.; Chan-Zuckerberg BioHub, San Francisco, California, United States of America.
    Duncan JA; Lineberger Comprehensive Cancer Center, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.; Department of Medicine, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.; Department of Pharmacology, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.
    Kapustina M; Department of Cell Biology & Physiology, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.
    Fry EE; Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, United Kingdom.
    Stuart DI; Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, United Kingdom.; Diamond Light Source, Didcot, United Kingdom.
    Lemon SM; Lineberger Comprehensive Cancer Center, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.; Department of Medicine, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.; Department of Microbiology & Immunology, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, United States of America.
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    Źródło:
    PLoS pathogens [PLoS Pathog] 2022 Aug 15; Vol. 18 (8), pp. e1010543. Date of Electronic Publication: 2022 Aug 15 (Print Publication: 2022).
    Typ publikacji:
    Journal Article; Research Support, Non-U.S. Gov't; Research Support, N.I.H., Extramural
    MeSH Terms:
    Endosomal Sorting Complexes Required for Transport*/genetics
    Endosomal Sorting Complexes Required for Transport*/metabolism
    Hepatitis A virus*/genetics
    Hepatitis A virus*/metabolism
    Animals ; Calcium-Binding Proteins/metabolism ; Capsid/metabolism ; Capsid Proteins/genetics ; Capsid Proteins/metabolism ; Cell Cycle Proteins/metabolism ; Mammals ; Viral Proteins/metabolism
    Czasopismo naukowe
    Pełny tekst  Link otwiera się w nowym oknie Pełny tekstSzczegóły
    Tytuł:
    Glutathione facilitates enterovirus assembly by binding at a druggable pocket.
    Autorzy:
    Duyvesteyn HME; 1Division of Structural Biology, University of Oxford, The Henry Wellcome Building for Genomic Medicine, Headington, Oxford OX3 7BN UK.; 2Diamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE UK.
    Ren J; 1Division of Structural Biology, University of Oxford, The Henry Wellcome Building for Genomic Medicine, Headington, Oxford OX3 7BN UK.
    Walter TS; 1Division of Structural Biology, University of Oxford, The Henry Wellcome Building for Genomic Medicine, Headington, Oxford OX3 7BN UK.
    Fry EE; 1Division of Structural Biology, University of Oxford, The Henry Wellcome Building for Genomic Medicine, Headington, Oxford OX3 7BN UK.
    Stuart DI; 1Division of Structural Biology, University of Oxford, The Henry Wellcome Building for Genomic Medicine, Headington, Oxford OX3 7BN UK.; 2Diamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE UK.
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    Źródło:
    Communications biology [Commun Biol] 2020 Jan 03; Vol. 3, pp. 9. Date of Electronic Publication: 2020 Jan 03 (Print Publication: 2020).
    Typ publikacji:
    Journal Article; Research Support, Non-U.S. Gov't
    MeSH Terms:
    Capsid Proteins/*genetics
    Enterovirus/*physiology
    Glutathione/*metabolism
    Amino Acid Sequence ; Capsid Proteins/chemistry ; Capsid Proteins/metabolism ; Enterovirus/genetics ; Sequence Alignment
    Czasopismo naukowe
    Pełny tekst  Link otwiera się w nowym oknie Pełny tekstSzczegóły
      Wyświetlanie 1-3 z 3

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