H Rommelaere

Summary

Affiliation: Ghent University
Country: Belgium

Publications

  1. ncbi request reprint Prefoldin recognition motifs in the nonhomologous proteins of the actin and tubulin families
    H Rommelaere
    Flanders Interuniversity Institute for Biotechnology and Department of Biochemistry, Faculty of Medicine, Ghent University, K L Ledeganckstraat 35, B 9000 Gent, Belgium
    J Biol Chem 276:41023-8. 2001
  2. pmc Eukaryotic cytosolic chaperonin contains t-complex polypeptide 1 and seven related subunits
    H Rommelaere
    Laboratory of Physiological Chemistry, University Ghent, Belgium
    Proc Natl Acad Sci U S A 90:11975-9. 1993
  3. ncbi request reprint Cofactor A is a molecular chaperone required for beta-tubulin folding: functional and structural characterization
    R Melki
    Laboratoire d Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif sur Yvette, France
    Biochemistry 35:10422-35. 1996
  4. ncbi request reprint Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin
    I E Vainberg
    Department of Biochemistry, New York University Medical Center, New York 10016, USA
    Cell 93:863-73. 1998
  5. pmc A novel cochaperonin that modulates the ATPase activity of cytoplasmic chaperonin
    Y Gao
    Department of Biochemistry, New York University Medical Center, New York 10016
    J Cell Biol 125:989-96. 1994
  6. ncbi request reprint Pathway leading to correctly folded beta-tubulin
    G Tian
    Department of Biochemistry, New York University Medical Center, New York 10016, USA
    Cell 86:287-96. 1996
  7. pmc Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors
    G Tian
    Department of Biochemistry, New York University Medical Center 10016, USA
    J Cell Biol 138:821-32. 1997

Collaborators

Detail Information

Publications7

  1. ncbi request reprint Prefoldin recognition motifs in the nonhomologous proteins of the actin and tubulin families
    H Rommelaere
    Flanders Interuniversity Institute for Biotechnology and Department of Biochemistry, Faculty of Medicine, Ghent University, K L Ledeganckstraat 35, B 9000 Gent, Belgium
    J Biol Chem 276:41023-8. 2001
    ..In addition, they also compete with tubulins, suggesting that these target proteins contact similar prefoldin subunits...
  2. pmc Eukaryotic cytosolic chaperonin contains t-complex polypeptide 1 and seven related subunits
    H Rommelaere
    Laboratory of Physiological Chemistry, University Ghent, Belgium
    Proc Natl Acad Sci U S A 90:11975-9. 1993
    ..We propose that a highly conserved region in these polypeptides and in other chaperonins of the cpn60 chaperone family participates in ATP binding...
  3. ncbi request reprint Cofactor A is a molecular chaperone required for beta-tubulin folding: functional and structural characterization
    R Melki
    Laboratoire d Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif sur Yvette, France
    Biochemistry 35:10422-35. 1996
    ..Our data imply that cofactor A is a chaperone involved in tubulin folding...
  4. ncbi request reprint Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin
    I E Vainberg
    Department of Biochemistry, New York University Medical Center, New York 10016, USA
    Cell 93:863-73. 1998
    ..We show that by directing target proteins to chaperonin, prefoldin promotes folding in an environment in which there are many competing pathways for nonnative proteins...
  5. pmc A novel cochaperonin that modulates the ATPase activity of cytoplasmic chaperonin
    Y Gao
    Department of Biochemistry, New York University Medical Center, New York 10016
    J Cell Biol 125:989-96. 1994
    ..Moreover, while GroES functions as a heptameric ring, cofactor A behaves as a dimer. Thus, cofactor A is a novel cochaperonin that is structurally unrelated to GroES...
  6. ncbi request reprint Pathway leading to correctly folded beta-tubulin
    G Tian
    Department of Biochemistry, New York University Medical Center, New York 10016, USA
    Cell 86:287-96. 1996
    ..Sequence analysis identifies yeast homologs of cofactors D (cin1) and E (pac2), characterized by mutations that affect microtubule function...
  7. pmc Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors
    G Tian
    Department of Biochemistry, New York University Medical Center 10016, USA
    J Cell Biol 138:821-32. 1997
    ....