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Structure-activity relationships in flexible protein domains: Regulation of Rho GTPases by RhoGDI and D4 GDI

Academic Article
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  • Overview
  • Research
  • Identity
  • Additional Document Info
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Overview

authors

  • Golovanov, A. P.
  • Chuang, T. H.
  • DerMardirossian, Celine
  • Barsukov, I.
  • Hawkins, D.
  • Badii, R.
  • Bokoch, G. M.
  • Lian, L. Y.
  • Roberts, G. C. K.

publication date

  • January 2001

journal

  • Journal of Molecular Biology  Journal

subject areas

  • Amides
  • Amino Acid Sequence
  • Binding Sites
  • Cloning, Molecular
  • Guanine Nucleotide Dissociation Inhibitors
  • Guanosine Diphosphate
  • Guanosine Triphosphate
  • HeLa Cells
  • Humans
  • Hydrolysis
  • Models, Molecular
  • Molecular Sequence Data
  • NADPH Oxidase
  • Nuclear Magnetic Resonance, Biomolecular
  • Pliability
  • Protein Binding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Sequence Deletion
  • Solvents
  • Structure-Activity Relationship
  • Transfection
  • rac1 GTP-Binding Protein
  • rho GTP-Binding Proteins
  • rho Guanine Nucleotide Dissociation Inhibitor alpha
  • rho Guanine Nucleotide Dissociation Inhibitor beta
  • rho-Specific Guanine Nucleotide Dissociation Inhibitors
  • rhoA GTP-Binding Protein
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Research

keywords

  • D4/LyGDI
  • GTPase
  • Rac1
  • RhoGDI
  • dissociation inhibitor
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1006/jmbi.2000.4262

PubMed ID

  • 11114252
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Additional Document Info

start page

  • 121

end page

  • 135

volume

  • 305

issue

  • 1

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