Publications
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Evolutionary conservation of codon optimality reveals hidden signatures of cotranslational folding.
Pechmann S,
Frydman J.
Nat Struct Mol Biol.
2013;
20
(2):
237-43
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Exogenous delivery of chaperonin subunit fragment ApiCCT1 modulates mutant Huntingtin cellular phenotypes.
Sontag EM,
Joachimiak LA, Tan Z, Tomlinson A, Housman DE, Glabe CG, Potkin SG, Frydman J, Thompson LM.
Proc Natl Acad Sci U S A.
2013;
110
(8):
3077-82
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Hsp90 inhibitors exhibit resistance-free antiviral activity against respiratory syncytial virus.
Geller R,
Andino R, Frydman J.
PLoS One.
2013;
8
(2):
e56762
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Principles of cotranslational ubiquitination and quality control at the ribosome.
Duttler S,
Pechmann S, Frydman J.
Mol Cell.
2013;
50
(3):
379-93
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The cotranslational function of ribosome-associated Hsp70 in eukaryotic protein homeostasis.
Willmund F,
del Alamo M, Pechmann S, Chen T, Albanèse V, Dammer EB, Peng J, Frydman J.
Cell.
2013;
152
(1-2):
196-209
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The ribosome as a hub for protein quality control.
Pechmann S,
Willmund F, Frydman J.
Mol Cell.
2013;
49
(3):
411-21
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The role of mutational robustness in RNA virus evolution.
Lauring AS,
Frydman J, Andino R.
Nat Rev Microbiol.
2013;
11
(5):
327-36
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A gradient of ATP affinities generates an asymmetric power stroke driving the chaperonin TRIC/CCT folding cycle.
Reissmann S,
Joachimiak LA, Chen B, Meyer AS, Nguyen A, Frydman J.
Cell Rep.
2012;
2
(4):
866-77
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Broad action of Hsp90 as a host chaperone required for viral replication.
Geller R,
Taguwa S, Frydman J.
Biochim Biophys Acta.
2012;
1823
(3):
698-706
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Cellular inclusion bodies of mutant huntingtin exon 1 obscure small fibrillar aggregate species.
Sahl SJ,
Weiss LE, Duim WC, Frydman J, Moerner WE.
Sci Rep.
2012:
2
895
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Mechanism of nucleotide sensing in group II chaperonins.
Pereira JH,
Ralston CY, Douglas NR, Kumar R, Lopez T, McAndrew RP, Knee KM, King JA, Frydman J, Adams PD.
EMBO J.
2012;
31
(19):
3949-50
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State of the science: an update on renal cell carcinoma.
Jonasch E,
Futreal PA, Davis IJ, Bailey ST, Kim WY, Brugarolas J, Giaccia AJ, Kurban G, Pause A, Frydman J, Zurita AJ, Rini BI, Sharma P, Atkins MB, Walker CL, Rathmell WK.
Mol Cancer Res.
2012;
10
(7):
859-80
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Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle.
Cong Y,
Schröder GF, Meyer AS, Jakana J, Ma B, Dougherty MT, Schmid MF, Reissmann S, Levitt M, Ludtke SL, Frydman J, Chiu W.
EMBO J.
2012;
31
(3):
720-30
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Systematic functional prioritization of protein posttranslational modifications.
Beltrao P,
Albanèse V, Kenner LR, Swaney DL, Burlingame A, Villén J, Lim WA, Fraser JS, Frydman J, Krogan NJ.
Cell.
2012;
150
(2):
413-25
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The molecular architecture of the eukaryotic chaperonin TRiC/CCT.
Leitner A,
Joachimiak LA, Bracher A, Mönkemeyer L, Walzthoeni T, Chen B, Pechmann S, Holmes S, Cong Y, Ma B, Ludtke S, Chiu W, Hartl FU, Aebersold R, Frydman J.
Structure.
2012;
20
(5):
814-25
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Cellular strategies of protein quality control.
Chen B,
Retzlaff M, Roos T, Frydman J.
Cold Spring Harb Perspect Biol.
2011;
3
(8):
a004374
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Cryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure.
Zhang J,
Ma B, DiMaio F, Douglas NR, Joachimiak LA, Baker D, Frydman J, Levitt M, Chiu W.
Structure.
2011;
19
(5):
633-9
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Defining the specificity of cotranslationally acting chaperones by systematic analysis of mRNAs associated with ribosome-nascent chain complexes.
del Alamo M,
Hogan DJ, Pechmann S, Albanese V, Brown PO, Frydman J.
PLoS Biol.
2011;
9
(7):
e1001100
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Dual action of ATP hydrolysis couples lid closure to substrate release into the group II chaperonin chamber.
Douglas NR,
Reissmann S, Zhang J, Chen B, Jakana J, Kumar R, Chiu W, Frydman J.
Cell.
2011;
144
(2):
240-52
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Heterozygous yeast deletion collection screens reveal essential targets of Hsp90.
Franzosa EA,
Albanèse V, Frydman J, Xia Y, McClellan AJ.
PLoS One.
2011;
6
(11):
e28211
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Sensing cooperativity in ATP hydrolysis for single multisubunit enzymes in solution.
Jiang Y,
Douglas NR, Conley NR, Miller EJ, Frydman J, Moerner WE.
Proc Natl Acad Sci U S A.
2011;
108
(41):
16962-7
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Sub-diffraction imaging of huntingtin protein aggregates by fluorescence blink-microscopy and atomic force microscopy.
Duim WC,
Chen B, Frydman J, Moerner WE.
Chemphyschem.
2011;
12
(13):
2387-90
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4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement.
Cong Y,
Baker ML, Jakana J, Woolford D, Miller EJ, Reissmann S, Kumar RN, Redding-Johanson AM, Batth TS, Mukhopadhyay A, Ludtke SJ, Frydman J, Chiu W.
Proc Natl Acad Sci U S A.
2010;
107
(11):
4967-72
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A ribosome-anchored chaperone network that facilitates eukaryotic ribosome biogenesis.
Albanèse V,
Reissmann S, Frydman J.
J Cell Biol.
2010;
189
(1):
69-81
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Action of the chaperonin GroEL/ES on a non-native substrate observed with single-molecule FRET.
Kim SY,
Miller EJ, Frydman J, Moerner WE.
J Mol Biol.
2010;
401
(4):
553-63
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Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle.
Pereira JH,
Ralston CY, Douglas NR, Meyer D, Knee KM, Goulet DR, King JA, Frydman J, Adams PD.
J Biol Chem.
2010;
285
(36):
27958-66
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Mechanism of folding chamber closure in a group II chaperonin.
Zhang J,
Baker ML, Schröder GF, Douglas NR, Reissmann S, Jakana J, Dougherty M, Fu CJ, Levitt M, Ludtke SJ, Frydman J, Chiu W.
Nature.
2010;
463
(7279):
379-83
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Trivalent arsenic inhibits the functions of chaperonin complex.
Pan X,
Reissman S, Douglas NR, Huang Z, Yuan DS, Wang X, McCaffery JM, Frydman J, Boeke JD.
Genetics.
2010;
186
(2):
725-34
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The Hsp90 mosaic: a picture emerges.
Mayer MP,
Prodromou C, Frydman J.
Nat Struct Mol Biol.
2009;
16
(1):
2-6
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The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation.
Tam S,
Spiess C, Auyeung W, Joachimiak L, Chen B, Poirier MA, Frydman J.
Nat Struct Mol Biol.
2009;
16
(12):
1279-85
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The predicted structure of the headpiece of the Huntingtin protein and its implications on Huntingtin aggregation.
Kelley NW,
Huang X, Tam S, Spiess C, Frydman J, Pande VS.
J Mol Biol.
2009;
388
(5):
919-27
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Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies.
Yam AY,
Xia Y, Lin HT, Burlingame A, Gerstein M, Frydman J.
Nat Struct Mol Biol.
2008;
15
(12):
1255-62
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Hardware-based anti-Brownian electrokinetic trap (ABEL trap) for single molecules: Control loop simulations and application to ATP binding stoichiometry in multi-subunit enzymes.
Jiang Y,
Wang Q, Cohen AE, Douglas N, Frydman J, Moerner WE.
Proc Soc Photo Opt Instrum Eng.
2008:
7038
1-12
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Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT.
Booth CR,
Meyer AS, Cong Y, Topf M, Sali A, Ludtke SJ, Chiu W, Frydman J.
Nat Struct Mol Biol.
2008;
15
(7):
746-53
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Misfolded proteins partition between two distinct quality control compartments.
Kaganovich D,
Kopito R, Frydman J.
Nature.
2008;
454
(7208):
1088-95
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Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches.
McClellan AJ,
Xia Y, Deutschbauer AM, Davis RW, Gerstein M, Frydman J.
Cell.
2007;
131
(1):
121-35
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Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins.
Reissmann S,
Parnot C, Booth CR, Chiu W, Frydman J.
Nat Struct Mol Biol.
2007;
14
(5):
432-40
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Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance.
Geller R,
Vignuzzi M, Andino R, Frydman J.
Genes Dev.
2007;
21
(2):
195-205
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Chaperonin GroEL and its mutant D87K protect from ischemia in vivo and in vitro.
Xu L,
Dayal M, Ouyang YB, Sun Y, Yang CF, Frydman J, Giffard RG.
Neurobiol Aging.
2006;
27
(4):
562-9
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Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperonins.
Spiess C,
Miller EJ, McClellan AJ, Frydman J.
Mol Cell.
2006;
24
(1):
25-37
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Modeling of possible subunit arrangements in the eukaryotic chaperonin TRiC.
Miller EJ,
Meyer AS, Frydman J.
Protein Sci.
2006;
15
(6):
1522-6
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Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells.
Albanèse V,
Yam AY, Baughman J, Parnot C, Frydman J.
Cell.
2006;
124
(1):
75-88
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The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions.
Tam S,
Geller R, Spiess C, Frydman J.
Nat Cell Biol.
2006;
8
(10):
1155-62
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Actin mutations in hypertrophic and dilated cardiomyopathy cause inefficient protein folding and perturbed filament formation.
Vang S,
Corydon TJ, Børglum AD, Scott MD, Frydman J, Mogensen J, Gregersen N, Bross P.
FEBS J.
2005;
272
(8):
2037-49
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Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways.
McClellan AJ,
Scott MD, Frydman J.
Cell.
2005;
121
(5):
739-48
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Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding.
Yam AY,
Albanèse V, Lin HT, Frydman J.
J Biol Chem.
2005;
280
(50):
41252-61
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Probing the sequence of conformationally induced polarity changes in the molecular chaperonin GroEL with fluorescence spectroscopy.
Kim SY,
Semyonov AN, Twieg RJ, Horwich AL, Frydman J, Moerner WE.
J Phys Chem B.
2005;
109
(51):
24517-25
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Protein quality control: chaperones culling corrupt conformations.
McClellan AJ,
Tam S, Kaganovich D, Frydman J.
Nat Cell Biol.
2005;
7
(8):
736-41
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The cotranslational contacts between ribosome-bound nascent polypeptides and the subunits of the hetero-oligomeric chaperonin TRiC probed by photocross-linking.
Etchells SA,
Meyer AS, Yam AY, Roobol A, Miao Y, Shao Y, Carden MJ, Skach WR, Frydman J, Johnson AE.
J Biol Chem.
2005;
280
(30):
28118-26
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Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets.
Spiess C,
Meyer AS, Reissmann S, Frydman J.
Trends Cell Biol.
2004;
14
(11):
598-604
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Aberrant protein folding as the molecular basis of cancer.
Scott MD,
Frydman J.
Methods Mol Biol.
2003:
232
67-76
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Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis.
Meyer AS,
Gillespie JR, Walther D, Millet IS, Doniach S, Frydman J.
Cell.
2003;
113
(3):
369-81
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The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex.
Melville MW,
McClellan AJ, Meyer AS, Darveau A, Frydman J.
Mol Cell Biol.
2003;
23
(9):
3141-51
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Tumorigenic mutations in VHL disrupt folding in vivo by interfering with chaperonin binding.
Feldman DE,
Spiess C, Howard DE, Frydman J.
Mol Cell.
2003;
12
(5):
1213-24
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Where chaperones and nascent polypeptides meet.
Albanèse V,
Frydman J.
Nat Struct Biol.
2002;
9
(10):
716-8
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Folding of newly translated proteins in vivo: the role of molecular chaperones.
Frydman J,
Annu Rev Biochem.
2001:
70
603-47
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Molecular chaperones and the art of recognizing a lost cause.
McClellan AJ,
Frydman J.
Nat Cell Biol.
2001;
3
(2):
E51-3
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Review: cellular substrates of the eukaryotic chaperonin TRiC/CCT.
Dunn AY,
Melville MW, Frydman J.
J Struct Biol.
2001;
135
(2):
176-84
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Folding assays. Assessing the native conformation of proteins.
Thulasiraman V,
Ferreyra RG, Frydman J.
Methods Mol Biol.
2000:
140
169-77
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Monitoring actin folding. Purification protocols for labeled proteins and binding to DNase I-sepharose beads.
Thulasiraman V,
Ferreyra RG, Frydman J.
Methods Mol Biol.
2000:
140
161-7
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Protein folding in vivo: the importance of molecular chaperones.
Feldman DE,
Frydman J.
Curr Opin Struct Biol.
2000;
10
(1):
26-33
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Purification of the cytosolic chaperonin TRiC from bovine testis.
Ferreyra RG,
Frydman J.
Methods Mol Biol.
2000:
140
153-60
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The interaction of the chaperonin tailless complex polypeptide 1 (TCP1) ring complex (TRiC) with ribosome-bound nascent chains examined using photo-cross-linking.
McCallum CD,
Do H, Johnson AE, Frydman J.
J Cell Biol.
2000;
149
(3):
591-602
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Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase.
Frydman J,
Erdjument-Bromage H, Tempst P, Hartl FU.
Nat Struct Biol.
1999;
6
(7):
697-705
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Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC.
Feldman DE,
Thulasiraman V, Ferreyra RG, Frydman J.
Mol Cell.
1999;
4
(6):
1051-61
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In vivo newly translated polypeptides are sequestered in a protected folding environment.
Thulasiraman V,
Yang CF, Frydman J.
EMBO J.
1999;
18
(1):
85-95
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Directionality of polypeptide transfer in the mitochondrial pathway of chaperone-mediated protein folding.
Heyrovská N,
Frydman J, Höhfeld J, Hartl FU.
Biol Chem.
1998;
379
(3):
301-9
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Chaperones get in touch: the Hip-Hop connection.
Frydman J,
Höhfeld J.
Trends Biochem Sci.
1997;
22
(3):
87-92
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Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms.
Frydman J,
Hartl FU.
Science.
1996;
272
(5267):
1497-502
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Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones.
Frydman J,
Nimmesgern E, Ohtsuka K, Hartl FU.
Nature.
1994;
370
(6485):
111-7
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Tcp20, a subunit of the eukaryotic TRiC chaperonin from humans and yeast.
Li WZ,
Lin P, Frydman J, Boal TR, Cardillo TS, Richard LM, Toth D, Lichtman MA, Hartl FU, Sherman F.
J Biol Chem.
1994;
269
(28):
18616-22
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An ATP-stabilized inhibitor of the proteasome is a component of the 1500-kDa ubiquitin conjugate-degrading complex.
Driscoll J,
Frydman J, Goldberg AL.
Proc Natl Acad Sci U S A.
1992;
89
(11):
4986-90
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Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits.
Frydman J,
Nimmesgern E, Erdjument-Bromage H, Wall JS, Tempst P, Hartl FU.
EMBO J.
1992;
11
(13):
4767-78
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