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Human glutathione transferase a4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products

Academic Article
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  • Research
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Overview

authors

  • Bruns, C. M.
  • Hubatsch, I.
  • Ridderstrom, M.
  • Mannervik, Bengt
  • Tainer, John

publication date

  • May 1999

journal

  • Journal of Molecular Biology  Journal

subject areas

  • Aldehydes
  • Amino Acid Sequence
  • Base Sequence
  • Binding Sites
  • Catalysis
  • Crystallography, X-Ray
  • DNA Primers
  • Glutathione
  • Glutathione Transferase
  • Glycine
  • Humans
  • Isoenzymes
  • Lipid Peroxidation
  • Models, Molecular
  • Molecular Sequence Data
  • Mutagenesis
  • Protein Conformation
  • Sequence Homology, Amino Acid
  • Tyrosine
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Research

keywords

  • alkenals
  • glutathione transferase
  • modular active site structure
  • oxidative stress
  • protein evolution
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1006/jmbi.1999.2697

PubMed ID

  • 10329152
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Additional Document Info

start page

  • 427

end page

  • 439

volume

  • 288

issue

  • 3

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