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An aminoquinazoline inhibitor of the essential bacterial cell wall synthetic enzyme GlmU has a unique non-protein-kinase-like binding mode

Academic Article
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Overview

authors

  • Larsen, Nicholas
  • Nash, T. J.
  • Morningstar, M.
  • Shapiro, A. B.
  • Joubran, C.
  • Blackett, C. J.
  • Patten, A. D.
  • Boriack-Sjodin, P. A.
  • Doig, P.

publication date

  • September 2012

journal

  • Biochemical Journal  Journal

subject areas

  • Acetylglucosamine
  • Acetyltransferases
  • Bacterial Proteins
  • Binding Sites
  • Cell Wall
  • Crystallography, X-Ray
  • Haemophilus influenzae
  • Models, Molecular
  • Multienzyme Complexes
  • Nucleotidyltransferases
  • Quinazolines
  • Structure-Activity Relationship
  • Uridine Triphosphate
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Research

keywords

  • GlmU
  • N-acetylglucosamine-1-phosphate uridyltransferase
  • aminoquinazoline
  • cell wall biosynthesis
  • high-throughput screening
  • inhibitor
  • kinase
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Identity

International Standard Serial Number (ISSN)

  • 0264-6021

Digital Object Identifier (DOI)

  • 10.1042/bj20120596

PubMed ID

  • 22721802
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Additional Document Info

start page

  • 405

end page

  • 413

volume

  • 446

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