High-resolution crystal structure of human asparagine synthetase enables analysis of inhibitor binding and selectivity

Zhu, W., Radadiya, A., Bisson, C. orcid.org/0000-0002-9430-6822 et al. (14 more authors) (2019) High-resolution crystal structure of human asparagine synthetase enables analysis of inhibitor binding and selectivity. Communications Biology, 2 (1). 345.

Abstract

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Copyright, Publisher and Additional Information: © 2019 The Authors. This article is licensed under a Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/.), which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder.
Keywords: Computational models; Enzymes; Medicinal chemistry; X-ray crystallography
Dates:
  • Accepted: 21 August 2019
  • Published: 17 September 2019
Institution: The University of Sheffield
Academic Units: The University of Sheffield > Faculty of Science (Sheffield) > School of Biological Sciences (Sheffield) > Department of Molecular Biology and Biotechnology (Sheffield)
Depositing User: Symplectic Sheffield
Date Deposited: 30 Oct 2019 13:32
Last Modified: 18 Mar 2020 15:41
Status: Published
Publisher: Springer Science and Business Media LLC
Refereed: Yes
Identification Number: https://doi.org/10.1038/s42003-019-0587-z
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