Judith Frydman
Publications
- Evolutionary conservation of codon optimality reveals hidden signatures of cotranslational folding. Nat Struct Mol Biol. 2013; (2): 237-43
- Exogenous delivery of chaperonin subunit fragment ApiCCT1 modulates mutant Huntingtin cellular phenotypes. Proc Natl Acad Sci U S A. 2013; (8): 3077-82
- Hsp90 inhibitors exhibit resistance-free antiviral activity against respiratory syncytial virus. PLoS One. 2013; (2): e56762
- Principles of cotranslational ubiquitination and quality control at the ribosome. Mol Cell. 2013; (3): 379-93
- The cotranslational function of ribosome-associated Hsp70 in eukaryotic protein homeostasis. Cell. 2013; (1-2): 196-209
- The ribosome as a hub for protein quality control. Mol Cell. 2013; (3): 411-21
- The role of mutational robustness in RNA virus evolution. Nat Rev Microbiol. 2013; (5): 327-36
- A gradient of ATP affinities generates an asymmetric power stroke driving the chaperonin TRIC/CCT folding cycle. Cell Rep. 2012; (4): 866-77
- Broad action of Hsp90 as a host chaperone required for viral replication. Biochim Biophys Acta. 2012; (3): 698-706
- Cellular inclusion bodies of mutant huntingtin exon 1 obscure small fibrillar aggregate species. Sci Rep. 2012: 895
- Mechanism of nucleotide sensing in group II chaperonins. EMBO J. 2012; (19): 3949-50
- State of the science: an update on renal cell carcinoma. Mol Cancer Res. 2012; (7): 859-80
- Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle. EMBO J. 2012; (3): 720-30
- Systematic functional prioritization of protein posttranslational modifications. Cell. 2012; (2): 413-25
- The molecular architecture of the eukaryotic chaperonin TRiC/CCT. Structure. 2012; (5): 814-25
- Cellular strategies of protein quality control. Cold Spring Harb Perspect Biol. 2011; (8): a004374
- Cryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure. Structure. 2011; (5): 633-9
- Defining the specificity of cotranslationally acting chaperones by systematic analysis of mRNAs associated with ribosome-nascent chain complexes. PLoS Biol. 2011; (7): e1001100
- Dual action of ATP hydrolysis couples lid closure to substrate release into the group II chaperonin chamber. Cell. 2011; (2): 240-52
- Heterozygous yeast deletion collection screens reveal essential targets of Hsp90. PLoS One. 2011; (11): e28211
- Sensing cooperativity in ATP hydrolysis for single multisubunit enzymes in solution. Proc Natl Acad Sci U S A. 2011; (41): 16962-7
- Sub-diffraction imaging of huntingtin protein aggregates by fluorescence blink-microscopy and atomic force microscopy. Chemphyschem. 2011; (13): 2387-90
- 4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement. Proc Natl Acad Sci U S A. 2010; (11): 4967-72
- A ribosome-anchored chaperone network that facilitates eukaryotic ribosome biogenesis. J Cell Biol. 2010; (1): 69-81
- Action of the chaperonin GroEL/ES on a non-native substrate observed with single-molecule FRET. J Mol Biol. 2010; (4): 553-63
- Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle. J Biol Chem. 2010; (36): 27958-66
- Mechanism of folding chamber closure in a group II chaperonin. Nature. 2010; (7279): 379-83
- Trivalent arsenic inhibits the functions of chaperonin complex. Genetics. 2010; (2): 725-34
- The Hsp90 mosaic: a picture emerges. Nat Struct Mol Biol. 2009; (1): 2-6
- The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation. Nat Struct Mol Biol. 2009; (12): 1279-85
- The predicted structure of the headpiece of the Huntingtin protein and its implications on Huntingtin aggregation. J Mol Biol. 2009; (5): 919-27
- Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies. Nat Struct Mol Biol. 2008; (12): 1255-62
- Hardware-based anti-Brownian electrokinetic trap (ABEL trap) for single molecules: Control loop simulations and application to ATP binding stoichiometry in multi-subunit enzymes. Proc Soc Photo Opt Instrum Eng. 2008: 1-12
- Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT. Nat Struct Mol Biol. 2008; (7): 746-53
- Misfolded proteins partition between two distinct quality control compartments. Nature. 2008; (7208): 1088-95
- Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches. Cell. 2007; (1): 121-35
- Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins. Nat Struct Mol Biol. 2007; (5): 432-40
- Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance. Genes Dev. 2007; (2): 195-205
- Chaperonin GroEL and its mutant D87K protect from ischemia in vivo and in vitro. Neurobiol Aging. 2006; (4): 562-9
- Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperonins. Mol Cell. 2006; (1): 25-37
- Modeling of possible subunit arrangements in the eukaryotic chaperonin TRiC. Protein Sci. 2006; (6): 1522-6
- Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells. Cell. 2006; (1): 75-88
- The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat Cell Biol. 2006; (10): 1155-62
- Actin mutations in hypertrophic and dilated cardiomyopathy cause inefficient protein folding and perturbed filament formation. FEBS J. 2005; (8): 2037-49
- Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways. Cell. 2005; (5): 739-48
- Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding. J Biol Chem. 2005; (50): 41252-61
- Probing the sequence of conformationally induced polarity changes in the molecular chaperonin GroEL with fluorescence spectroscopy. J Phys Chem B. 2005; (51): 24517-25
- Protein quality control: chaperones culling corrupt conformations. Nat Cell Biol. 2005; (8): 736-41
- The cotranslational contacts between ribosome-bound nascent polypeptides and the subunits of the hetero-oligomeric chaperonin TRiC probed by photocross-linking. J Biol Chem. 2005; (30): 28118-26
- Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets. Trends Cell Biol. 2004; (11): 598-604
- Aberrant protein folding as the molecular basis of cancer. Methods Mol Biol. 2003: 67-76
- Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis. Cell. 2003; (3): 369-81
- The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex. Mol Cell Biol. 2003; (9): 3141-51
- Tumorigenic mutations in VHL disrupt folding in vivo by interfering with chaperonin binding. Mol Cell. 2003; (5): 1213-24
- Where chaperones and nascent polypeptides meet. Nat Struct Biol. 2002; (10): 716-8
- Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu Rev Biochem. 2001: 603-47
- Molecular chaperones and the art of recognizing a lost cause. Nat Cell Biol. 2001; (2): E51-3
- Review: cellular substrates of the eukaryotic chaperonin TRiC/CCT. J Struct Biol. 2001; (2): 176-84
- Folding assays. Assessing the native conformation of proteins. Methods Mol Biol. 2000: 169-77
- Monitoring actin folding. Purification protocols for labeled proteins and binding to DNase I-sepharose beads. Methods Mol Biol. 2000: 161-7
- Protein folding in vivo: the importance of molecular chaperones. Curr Opin Struct Biol. 2000; (1): 26-33
- Purification of the cytosolic chaperonin TRiC from bovine testis. Methods Mol Biol. 2000: 153-60
- The interaction of the chaperonin tailless complex polypeptide 1 (TCP1) ring complex (TRiC) with ribosome-bound nascent chains examined using photo-cross-linking. J Cell Biol. 2000; (3): 591-602
- Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase. Nat Struct Biol. 1999; (7): 697-705
- Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC. Mol Cell. 1999; (6): 1051-61
- In vivo newly translated polypeptides are sequestered in a protected folding environment. EMBO J. 1999; (1): 85-95
- Directionality of polypeptide transfer in the mitochondrial pathway of chaperone-mediated protein folding. Biol Chem. 1998; (3): 301-9
- Chaperones get in touch: the Hip-Hop connection. Trends Biochem Sci. 1997; (3): 87-92
- Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms. Science. 1996; (5267): 1497-502
- Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature. 1994; (6485): 111-7
- Tcp20, a subunit of the eukaryotic TRiC chaperonin from humans and yeast. J Biol Chem. 1994; (28): 18616-22
- An ATP-stabilized inhibitor of the proteasome is a component of the 1500-kDa ubiquitin conjugate-degrading complex. Proc Natl Acad Sci U S A. 1992; (11): 4986-90
- Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits. EMBO J. 1992; (13): 4767-78
Help
Trial Administration