J Frydman

Summary

Affiliation: Stanford University
Country: USA

Publications

  1. ncbi The interaction of the chaperonin tailless complex polypeptide 1 (TCP1) ring complex (TRiC) with ribosome-bound nascent chains examined using photo-cross-linking
    C D McCallum
    Department of Medical Biochemistry and Genetics, Texas A and M University, College Station, Texas 77843 1114, USA
    J Cell Biol 149:591-602. 2000
  2. ncbi Chaperones get in touch: the Hip-Hop connection
    J Frydman
    Department of Biological Sciences, Stanford University, CA 94305 5020, USA
    Trends Biochem Sci 22:87-92. 1997
  3. ncbi Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase
    J Frydman
    Department of Biological Sciences, Stanford University, California 94305, USA
    Nat Struct Biol 6:697-705. 1999
  4. ncbi Purification of the cytosolic chaperonin TRiC from bovine testis
    R G Ferreyra
    Department of Biological Sciences, Stanford University, Stanford, CA, USA
    Methods Mol Biol 140:153-60. 2000
  5. ncbi Review: cellular substrates of the eukaryotic chaperonin TRiC/CCT
    A Y Dunn
    Department of Biological Sciences, Stanford University, Stanford, California 94305-5020, USA
    J Struct Biol 135:176-84. 2001
  6. ncbi Folding of newly translated proteins in vivo: the role of molecular chaperones
    J Frydman
    Department of Biological Sciences, Stanford University, Stanford, California 94305 5020, USA
    Annu Rev Biochem 70:603-47. 2001
  7. ncbi Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC
    D E Feldman
    Department of Biological Sciences, Stanford University, California 94305, USA
    Mol Cell 4:1051-61. 1999
  8. ncbi Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms
    J Frydman
    Howard Hughes Medical Institute, Memorial Sloan Kettering Cancer Center, New York 10021, USA
    Science 272:1497-502. 1996
  9. ncbi Directionality of polypeptide transfer in the mitochondrial pathway of chaperone-mediated protein folding
    N Heyrovska
    Cellular Biochemistry and Biophysics Program and Howard Hughes Medical Institute, Memorial Sloan Kettering Cancer Center, New York, NY 10021, USA
    Biol Chem 379:301-9. 1998
  10. ncbi Tcp20, a subunit of the eukaryotic TRiC chaperonin from humans and yeast
    W Z Li
    Department of Medicine, University of Rochester, School of Medicine and Dentistry, New York 14642
    J Biol Chem 269:18616-22. 1994

Collaborators

  • F U Hartl
  • Arthur E Johnson
  • R G Ferreyra
  • A Y Dunn
  • C D McCallum
  • D E Feldman
  • N Heyrovska
  • M W Melville
  • H Do
  • V Thulasiraman
  • J Hohfeld
  • W Z Li
  • F Sherman
  • T S Cardillo
  • M A Lichtman
  • D Toth
  • P Lin
  • T R Boal
  • L M Richard

Detail Information

Publications10

  1. ncbi The interaction of the chaperonin tailless complex polypeptide 1 (TCP1) ring complex (TRiC) with ribosome-bound nascent chains examined using photo-cross-linking
    C D McCallum
    Department of Medical Biochemistry and Genetics, Texas A and M University, College Station, Texas 77843 1114, USA
    J Cell Biol 149:591-602. 2000
    ..Our results indicate that TRiC/CCT associates with the translating polypeptide shortly after it emerges from the ribosome and suggest a close association between the chaperonin and the translational apparatus...
  2. ncbi Chaperones get in touch: the Hip-Hop connection
    J Frydman
    Department of Biological Sciences, Stanford University, CA 94305 5020, USA
    Trends Biochem Sci 22:87-92. 1997
    ..Efficient cooperation appears to be achieved through a defined regulation of Hsc70 activity by the chaperone cofactors Hip and Hop...
  3. ncbi Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase
    J Frydman
    Department of Biological Sciences, Stanford University, California 94305, USA
    Nat Struct Biol 6:697-705. 1999
    ..We propose that co-translational domain formation avoids intramolecular misfolding and may be critical in the folding of multidomain proteins...
  4. ncbi Purification of the cytosolic chaperonin TRiC from bovine testis
    R G Ferreyra
    Department of Biological Sciences, Stanford University, Stanford, CA, USA
    Methods Mol Biol 140:153-60. 2000
  5. ncbi Review: cellular substrates of the eukaryotic chaperonin TRiC/CCT
    A Y Dunn
    Department of Biological Sciences, Stanford University, Stanford, California 94305-5020, USA
    J Struct Biol 135:176-84. 2001
    ..Here we review the current understanding of a role for TRiC in the folding of newly synthesized polypeptides, with a focus on some of the individual proteins that require TRiC...
  6. ncbi Folding of newly translated proteins in vivo: the role of molecular chaperones
    J Frydman
    Department of Biological Sciences, Stanford University, Stanford, California 94305 5020, USA
    Annu Rev Biochem 70:603-47. 2001
    ..In addition, initiation of folding during translation appears to be important for efficient folding of multidomain proteins...
  7. ncbi Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC
    D E Feldman
    Department of Biological Sciences, Stanford University, California 94305, USA
    Mol Cell 4:1051-61. 1999
    ..Our results define a novel role for TRiC in mediating oligomerization and suggest that inactivating mutations can impair polypeptide function by interfering with chaperone-mediated folding...
  8. ncbi Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms
    J Frydman
    Howard Hughes Medical Institute, Memorial Sloan Kettering Cancer Center, New York 10021, USA
    Science 272:1497-502. 1996
    ..Thus, folding, oligomerization, and degradation are linked hierarchically to ensure the correct fate of newly synthesized polypeptides...
  9. ncbi Directionality of polypeptide transfer in the mitochondrial pathway of chaperone-mediated protein folding
    N Heyrovska
    Cellular Biochemistry and Biophysics Program and Howard Hughes Medical Institute, Memorial Sloan Kettering Cancer Center, New York, NY 10021, USA
    Biol Chem 379:301-9. 1998
    ....
  10. ncbi Tcp20, a subunit of the eukaryotic TRiC chaperonin from humans and yeast
    W Z Li
    Department of Medicine, University of Rochester, School of Medicine and Dentistry, New York 14642
    J Biol Chem 269:18616-22. 1994
    ..The amino acid sequence similarities and the derived evolutionary relationships established that the human and yeast Tcp20 proteins represent members of a new family of subunits of TRiC chaperonins...