Research Topics
| J FrydmanSummaryAffiliation: Stanford University Country: USA Publications
Research Grants
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Detail Information
Publications
Modeling of possible subunit arrangements in the eukaryotic chaperonin TRiCErik 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...
Folding of newly translated proteins in vivo: the role of molecular chaperonesJ 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...- Chaperones get in touch: the Hip-Hop connectionJ 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... - Purification of the cytosolic chaperonin TRiC from bovine testisR G Ferreyra
Department of Biological Sciences, Stanford University, Stanford, CA, USA
Methods Mol Biol 140:153-60. 2000 - Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferaseJ 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... - Review: cellular substrates of the eukaryotic chaperonin TRiC/CCTA 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... - Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiCD 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... - Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cellsVéronique 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... - Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secretsChristoph 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... - Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo foldingAlice 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... - The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complexMark 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... - Where chaperones and nascent polypeptides meetVéronique Albanèse
Nat Struct Biol 9:716-8. 2002 - Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistanceRon 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... - Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperoninsChristoph 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... - Probing the sequence of conformationally induced polarity changes in the molecular chaperonin GroEL with fluorescence spectroscopySo Yeon Kim
Department of Chemistry, Stanford University, Stanford, California 94305, USA
J Phys Chem B 109:24517-25. 2005.... - Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperoninsStefanie 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... - Protein quality control: chaperones culling corrupt conformationsAmie 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... - Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathwaysAmie J McClellan
Department of Biological Sciences and BioX Program, Stanford University, CA 94305, USA
Cell 121:739-48. 2005.... - The cotranslational contacts between ribosome-bound nascent polypeptides and the subunits of the hetero-oligomeric chaperonin TRiC probed by photocross-linkingStephanie 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... - Actin mutations in hypertrophic and dilated cardiomyopathy cause inefficient protein folding and perturbed filament formationSøren 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... - Tumorigenic mutations in VHL disrupt folding in vivo by interfering with chaperonin bindingDouglas 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... - Aberrant protein folding as the molecular basis of cancerMelissa D Scott
Department of Biological Sciences, Stanford University, CA, USA
Methods Mol Biol 232:67-76. 2003 - Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysisAnne 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... - Misfolded proteins partition between two distinct quality control compartmentsDaniel 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 Grants
- PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOLJudith Frydman; Fiscal Year: 2009..Finally, our fourth specific aim will explore the interaction between chaperones and the translational machinery. ..
- Mechanism of the Eukaryotic Chaperonin in TRiC/CCTJudith 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. ..
- Mechanism of the eukaryotic chaperonin TRiC/CCTJudith 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. ..
- PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOLJudith Frydman; Fiscal Year: 2007..Finally, our fourth specific aim will explore the interaction between chaperones and the translational machinery. ..
- PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOLJudith Frydman; Fiscal Year: 2007..Finally, our fourth specific aim will explore the interaction between chaperones and the translational machinery. ..
- PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOLJudith Frydman; Fiscal Year: 2010..Finally, our fourth specific aim will explore the interaction between chaperones and the translational machinery. ..
- PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOLJudith Frydman; Fiscal Year: 2006..abstract_text> ..
- PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOLJudith Frydman; Fiscal Year: 2001....
- PROTEIN FOLDING IN THE EUKARYOTIC CYTOSOLJudith Frydman; Fiscal Year: 2003..abstract_text> ..