Crystal structure of the essential transcription antiterminator M2-1 protein of human respiratory syncytial virus and implications of its phosphorylation

Tanner, S, Ariza, A, Richard, CA et al. (12 more authors) (2014) Crystal structure of the essential transcription antiterminator M2-1 protein of human respiratory syncytial virus and implications of its phosphorylation. Proceedings of the National Academy of Sciences, 111 (4). pp. 1580-1585. ISSN 0027-8424

Abstract

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Authors/Creators:
Keywords: Biopolymers; Crystallography, X-Ray; Humans; Nuclear Magnetic Resonance, Biomolecular; Phosphorylation; Protein Conformation; RNA; Respiratory Syncytial Viruses; Viral Proteins
Dates:
  • Accepted: 9 December 2013
  • Published (online): 13 January 2014
  • Published: 28 January 2014
Institution: The University of Leeds
Academic Units: The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Crystallography (Leeds)
The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Synthetic Biology (Leed)
Depositing User: Symplectic Publications
Date Deposited: 23 Mar 2015 13:46
Last Modified: 04 Dec 2020 13:00
Published Version: http://dx.doi.org/10.1073/pnas.1317262111
Status: Published
Publisher: National Academy of Sciences
Identification Number: https://doi.org/10.1073/pnas.1317262111
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