Judith Frydman
Cited by
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Folding of newly translated proteins in vivo: the role of molecular chaperones
J Frydman
Annual review of biochemistry 70, 603, 2001
Misfolded proteins partition between two distinct quality control compartments
D Kaganovich, R Kopito, J Frydman
Nature 454 (7208), 1088-1095, 2008
Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
J Frydman, E Nimmesgern, K Ohtsuka, FU Hartl
Nature 370 (6485), 111-117, 1994
Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches
AJ McClellan, Y Xia, AM Deutschbauer, RW Davis, M Gerstein, J Frydman
Cell 131 (1), 121-135, 2007
Function in protein folding of TRiC, a cytosolic ring complex containing TCP‐1 and structurally related subunits.
J Frydman, E Nimmesgern, H Erdjument‐Bromage, JS Wall, P Tempst, ...
The EMBO journal 11 (13), 4767-4778, 1992
Evolutionary conservation of codon optimality reveals hidden signatures of cotranslational folding
S Pechmann, J Frydman
Nature structural & molecular biology 20 (2), 237-243, 2013
Cellular strategies of protein quality control
B Chen, M Retzlaff, T Roos, J Frydman
Cold Spring Harbor perspectives in biology 3 (8), a004374, 2011
Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets
C Spiess, AS Meyer, S Reissmann, J Frydman
Trends in cell biology 14 (11), 598-604, 2004
Protein misfolding in neurodegenerative diseases: implications and strategies
P Sweeney, H Park, M Baumann, J Dunlop, J Frydman, R Kopito, ...
Translational neurodegeneration 6 (1), 1-13, 2017
In vivo newly translated polypeptides are sequestered in a protected folding environment
V Thulasiraman, CF Yang, J Frydman
The EMBO journal 18 (1), 85-95, 1999
Systematic functional prioritization of protein posttranslational modifications
P Beltrao, V Albanèse, LR Kenner, DL Swaney, A Burlingame, J Villén, ...
Cell 150 (2), 413-425, 2012
Chaperones get in touch: the Hip-Hop connection
J Frydman, J Höhfeld
Trends in biochemical sciences 22 (3), 87-92, 1997
Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies
AY Yam, Y Xia, HTJ Lin, A Burlingame, M Gerstein, J Frydman
Nature structural & molecular biology 15 (12), 1255-1262, 2008
The role of mutational robustness in RNA virus evolution
AS Lauring, J Frydman, R Andino
Nature Reviews Microbiology 11 (5), 327-336, 2013
Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms
J Frydman, FU Hartl
Science 272 (5267), 1497-1502, 1996
The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions
S Tam, R Geller, C Spiess, J Frydman
Nature cell biology 8 (10), 1155-1162, 2006
Protein quality control: chaperones culling corrupt conformations
AJ McClellan, S Tam, D Kaganovich, J Frydman
Nature cell biology 7 (8), 736-741, 2005
Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells
V Albanese, AYW Yam, J Baughman, C Parnot, J Frydman
Cell 124 (1), 75-88, 2006
Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress
S Escusa-Toret, WIM Vonk, J Frydman
Nature cell biology 15 (10), 1231-1243, 2013
Protein folding in vivo: the importance of molecular chaperones
DE Feldman, J Frydman
Current opinion in structural biology 10 (1), 26-33, 2000
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