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Structure and function of an unusual family of protein phosphatases: the bacterial chemotaxis proteins CheC and CheX

Academic Article
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Overview

authors

  • Park, S. Y.
  • Chao, X.
  • Gonzalez-Bonet, G.
  • Beel, B. D.
  • Bilwes, A. M.
  • Crane, Brian R

publication date

  • November 2004

journal

  • Molecular Cell  Journal

subject areas

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Bacillus subtilis
  • Bacterial Proteins
  • Binding Sites
  • Chemotaxis
  • Conserved Sequence
  • Crystallography, X-Ray
  • Dimerization
  • Escherichia coli
  • Flagella
  • Hydrogen Bonding
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation
  • Phosphoprotein Phosphatases
  • Phosphorus Radioisotopes
  • Phosphorylation
  • Protein Structure, Quaternary
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid
  • Temperature
  • Treponema
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Identity

International Standard Serial Number (ISSN)

  • 1097-2765

Digital Object Identifier (DOI)

  • 10.1016/j.molcel.2004.10.018

PubMed ID

  • 15546616
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Additional Document Info

start page

  • 563

end page

  • 574

volume

  • 16

issue

  • 4

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