J Frydman

Summary

Affiliation: Stanford University
Country: USA

Publications

  1. pmc Modeling of possible subunit arrangements in the eukaryotic chaperonin TRiC
    Erik J Miller
    Department of Biological Sciences, Stanford University, Stanford, California 94305, USA
    Protein Sci 15:1522-6. 2006
  2. 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
  3. 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
  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 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
  6. 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
  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 Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells
    Véronique Albanèse
    Department of Biological Sciences and BioX Program, Stanford University, Stanford, CA 94305, USA
    Cell 124:75-88. 2006
  9. pmc Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets
    Christoph Spiess
    Department of Biological Sciences and BioX Program, E200 Clark Center, Stanford University, Stanford, CA 94305, USA
    Trends Cell Biol 14:598-604. 2004
  10. ncbi request reprint Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding
    Alice Yen Wen Yam
    Department of Biological Sciences and BioX Program, Stanford University, Stanford, California 94305 5020, USA
    J Biol Chem 280:41252-61. 2005

Research Grants

  1. PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOL
    Judith Frydman; Fiscal Year: 2009
  2. Mechanism of the Eukaryotic Chaperonin in TRiC/CCT
    Judith Frydman; Fiscal Year: 2010
  3. Mechanism of the eukaryotic chaperonin TRiC/CCT
    Judith Frydman; Fiscal Year: 2007
  4. PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOL
    Judith Frydman; Fiscal Year: 2007
  5. PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOL
    Judith Frydman; Fiscal Year: 2007
  6. PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOL
    Judith Frydman; Fiscal Year: 2010
  7. PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOL
    Judith Frydman; Fiscal Year: 2006
  8. PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOL
    Judith Frydman; Fiscal Year: 2001
  9. PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOL
    Judith Frydman; Fiscal Year: 2003

Collaborators

  • F U Hartl
  • Arthur E Johnson
  • Arthur Horwich
  • WILLIAM SKACH
  • Amie J McClellan
  • Anne S Meyer
  • Christoph Spiess
  • Véronique Albanèse
  • Melissa D Scott
  • Daniel Kaganovich
  • Stefanie Reissmann
  • Erik J Miller
  • Alice Yen Wen Yam
  • Ron Geller
  • Charles Parnot
  • Søren Vang
  • So Yeon Kim
  • Stephanie A Etchells
  • R G Ferreyra
  • Mark W Melville
  • Douglas E Feldman
  • A Y Dunn
  • Ron Kopito
  • D E Feldman
  • Marco Vignuzzi
  • Christopher R Booth
  • Wah Chiu
  • Raul Andino
  • Joshua Baughman
  • Hen Tzu Jill Lin
  • Thomas J Corydon
  • Alexander N Semyonov
  • Anne Roobol
  • Robert J Twieg
  • Peter Bross
  • Stephen Tam
  • Yiwei Miao
  • Alice Y Yam
  • Anders D Børglum
  • W E Moerner
  • Yuanlong Shao
  • Niels Gregersen
  • Jens Mogensen
  • Martin J Carden
  • Ian S Millet
  • Daniel E Howard
  • Joel R Gillespie
  • Dirk Walther
  • Sebastian Doniach
  • Andre Darveau
  • M W Melville
  • V Thulasiraman

Detail Information

Publications24

  1. pmc Modeling of possible subunit arrangements in the eukaryotic chaperonin TRiC
    Erik J Miller
    Department of Biological Sciences, Stanford University, Stanford, California 94305, USA
    Protein Sci 15:1522-6. 2006
    ..This in turn will aid in the understanding of substrate binding and allosteric properties of this chaperonin...
  2. 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...
  3. 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...
  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 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...
  6. 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...
  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 Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells
    Véronique Albanèse
    Department of Biological Sciences and BioX Program, Stanford University, Stanford, CA 94305, USA
    Cell 124:75-88. 2006
    ..The emergence of a translation-linked chaperone network likely underlies the elaborate cotranslational folding process necessary for the evolution of larger multidomain proteins characteristic of eukaryotic cells...
  9. pmc Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets
    Christoph Spiess
    Department of Biological Sciences and BioX Program, E200 Clark Center, Stanford University, Stanford, CA 94305, USA
    Trends Cell Biol 14:598-604. 2004
    ..Although knowledge of this unique complex is in its infancy, we review recent advances that open the way to understanding the secrets of its folding chamber...
  10. ncbi request reprint Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding
    Alice Yen Wen Yam
    Department of Biological Sciences and BioX Program, Stanford University, Stanford, California 94305 5020, USA
    J Biol Chem 280:41252-61. 2005
    ..It, thus, appears that Hsp110 is an important regulator of Hsp70-substrate interactions. Based on our data, we propose that Hsp110 cooperates with the SSB and SSA Hsp70 subfamilies, which act sequentially during de novo folding...
  11. pmc The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex
    Mark W Melville
    Department of Biological Sciences, Stanford University, Stanford, California 94305, USA
    Mol Cell Biol 23:3141-51. 2003
    ..We conclude that, in vivo, folding of some polypeptides requires the cooperation of Hsp70 and TRiC and that Hsp70 acts to promote substrate binding to TRiC...
  12. ncbi request reprint Where chaperones and nascent polypeptides meet
    Véronique Albanèse
    Nat Struct Biol 9:716-8. 2002
  13. pmc Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance
    Ron Geller
    Department of Biological Sciences, Stanford University, Stanford, California 94305, USA
    Genes Dev 21:195-205. 2007
    ..We propose that targeting folding of viral proteins may provide a general antiviral strategy that is refractory to development of drug resistance...
  14. pmc Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperonins
    Christoph Spiess
    Department of Biological Sciences and BioX Program, Stanford University, Stanford, CA 94305, USA
    Mol Cell 24:25-37. 2006
    ..The unique combination of specificity and plasticity in TRiC substrate binding may diversify the range of motifs recognized by this chaperonin and contribute to its unique ability to fold eukaryotic proteins...
  15. pmc Probing the sequence of conformationally induced polarity changes in the molecular chaperonin GroEL with fluorescence spectroscopy
    So Yeon Kim
    Department of Chemistry, Stanford University, Stanford, California 94305, USA
    J Phys Chem B 109:24517-25. 2005
    ....
  16. pmc Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins
    Stefanie Reissmann
    Department of Biological Sciences and BioX Program, Stanford University, Stanford, California 94305, USA
    Nat Struct Mol Biol 14:432-40. 2007
    ..These regulatory functions of the lid may serve to allow the symmetrical chaperonins to function as 'two-stroke' motors and may also provide a timer for substrate encapsulation within the closed chamber...
  17. ncbi request reprint Protein quality control: chaperones culling corrupt conformations
    Amie J McClellan
    Department of Biological Sciences and BioX Program, E200 Clark Center, Stanford University, Stanford, CA 94305, USA
    Nat Cell Biol 7:736-41. 2005
    ..Here we discuss emerging links between folding and degradation machineries and highlight challenges for future research...
  18. ncbi request reprint Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways
    Amie J McClellan
    Department of Biological Sciences and BioX Program, Stanford University, CA 94305, USA
    Cell 121:739-48. 2005
    ....
  19. ncbi request reprint The cotranslational contacts between ribosome-bound nascent polypeptides and the subunits of the hetero-oligomeric chaperonin TRiC probed by photocross-linking
    Stephanie A Etchells
    Department of Biochemistry and Biophysics, Texas A and M University, College Station, Texas 77843, USA
    J Biol Chem 280:28118-26. 2005
    ..We conclude that elongating actin and luciferase nascent chains contact multiple TRiC subunits upon emerging from the ribosome, and that the TRiC subunits contacted by nascent actin change as it elongates and starts to fold...
  20. ncbi request reprint Actin mutations in hypertrophic and dilated cardiomyopathy cause inefficient protein folding and perturbed filament formation
    Søren Vang
    Research Unit for Molecular Medicine, Aarhus University Hospital and Faculty of Health Sciences, Denmark
    FEBS J 272:2037-49. 2005
    ..We propose that effects of mutations on folding and fiber assembly may play a role in the molecular disease mechanism...
  21. ncbi request reprint Tumorigenic mutations in VHL disrupt folding in vivo by interfering with chaperonin binding
    Douglas E Feldman
    Department of Biological Sciences and BioX Program, Stanford University, E200A James Clark Center, 318 Campus Drive, Stanford, CA 94305, USA
    Mol Cell 12:1213-24. 2003
    ..Our findings reveal a class of disease-causing mutations that inactivate protein function by disrupting chaperone-mediated folding in vivo...
  22. ncbi request reprint Aberrant protein folding as the molecular basis of cancer
    Melissa D Scott
    Department of Biological Sciences, Stanford University, CA, USA
    Methods Mol Biol 232:67-76. 2003
  23. ncbi request reprint Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis
    Anne S Meyer
    Department of Biological Sciences, Stanford University, Stanford, CA 94305, USA
    Cell 113:369-81. 2003
    ..Understanding the distinct mechanisms governing eukaryotic and bacterial chaperonin function may reveal how TRiC has evolved to fold specific eukaryotic proteins...
  24. pmc Misfolded proteins partition between two distinct quality control compartments
    Daniel Kaganovich
    Department of Biology and BioX Program, Stanford University, Stanford, California 94305, USA
    Nature 454:1088-95. 2008
    ..Our findings provide a framework for understanding the preferential accumulation of amyloidogenic proteins in inclusions linked to human disease...

Research Grants20

  1. PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOL
    Judith Frydman; Fiscal Year: 2009
    ..Finally, our fourth specific aim will explore the interaction between chaperones and the translational machinery. ..
  2. Mechanism of the Eukaryotic Chaperonin in TRiC/CCT
    Judith Frydman; Fiscal Year: 2010
    ..Thus our project will help deciphering the role of this chaperonin in cellular folding and provide therapies to ameliorate human misfolding disorders. ..
  3. Mechanism of the eukaryotic chaperonin TRiC/CCT
    Judith Frydman; Fiscal Year: 2007
    ..Characterize of the nucleotide cycle of the chaperonin TRiC; 2. Define the molecular basis of TRiC-substrate interactions; 3. Explore the mechanism of TRiC-assisted folding. ..
  4. PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOL
    Judith Frydman; Fiscal Year: 2007
    ..Finally, our fourth specific aim will explore the interaction between chaperones and the translational machinery. ..
  5. PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOL
    Judith Frydman; Fiscal Year: 2007
    ..Finally, our fourth specific aim will explore the interaction between chaperones and the translational machinery. ..
  6. PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOL
    Judith Frydman; Fiscal Year: 2010
    ..Finally, our fourth specific aim will explore the interaction between chaperones and the translational machinery. ..
  7. PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOL
    Judith Frydman; Fiscal Year: 2006
    ..abstract_text> ..
  8. PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOL
    Judith Frydman; Fiscal Year: 2001
    ....
  9. PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOL
    Judith Frydman; Fiscal Year: 2003
    ..abstract_text> ..