J Frydman

Summary

Affiliation: Stanford University
Country: USA

Publications

  1. pmc 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 request reprint 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 request reprint 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 request reprint 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 request reprint 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 request reprint 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 request reprint 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 request reprint 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 request reprint 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 request reprint 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
  • D Toth
  • P Lin
  • F Sherman
  • T R Boal
  • L M Richard
  • M A Lichtman
  • T S Cardillo

Detail Information

Publications10

  1. pmc 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 request reprint 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 request reprint 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 request reprint 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 request reprint 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 request reprint 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 request reprint 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 request reprint 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 request reprint 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 request reprint 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...