Judith Frydman - Publications

Stanford University, Palo Alto, CA 
Biology and of Genetics

99 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2019 Shen K, Gamerdinger M, Chan R, Gense K, Martin EM, Sachs N, Knight PD, Schlömer R, Calabrese AN, Stewart KL, Leiendecker L, Baghel A, Radford SE, Frydman J, Deuerling E. Dual Role of Ribosome-Binding Domain of NAC as a Potent Suppressor of Protein Aggregation and Aging-Related Proteinopathies. Molecular Cell. PMID 30982745 DOI: 10.1016/j.molcel.2019.03.012  0.32
2019 Gestaut D, Roh SH, Ma B, Pintilie G, Joachimiak LA, Leitner A, Walzthoeni T, Aebersold R, Chiu W, Frydman J. The Chaperonin TRiC/CCT Associates with Prefoldin through a Conserved Electrostatic Interface Essential for Cellular Proteostasis. Cell. PMID 30955883 DOI: 10.1016/j.cell.2019.03.012  0.32
2019 Taguwa S, Yeh MT, Rainbolt TK, Nayak A, Shao H, Gestwicki JE, Andino R, Frydman J. Zika Virus Dependence on Host Hsp70 Provides a Protective Strategy against Infection and Disease. Cell Reports. 26: 906-920.e3. PMID 30673613 DOI: 10.1016/j.celrep.2018.12.095  0.52
2018 Nayak A, Kim DY, Trnka MJ, Kerr CH, Lidsky PV, Stanley DJ, Rivera BM, Li KH, Burlingame AL, Jan E, Frydman J, Gross JD, Andino R. A Viral Protein Restricts Drosophila RNAi Immunity by Regulating Argonaute Activity and Stability. Cell Host & Microbe. 24: 542-557.e9. PMID 30308158 DOI: 10.1016/j.chom.2018.09.006  0.52
2018 Levy GR, Shen K, Gavrilov Y, Smith PES, Levy Y, Chan R, Frydman J, Frydman L. Huntingtin's N-terminus rearrangements in the presence of membranes: A joint spectroscopic and computational perspective. Acs Chemical Neuroscience. PMID 30149694 DOI: 10.1021/acschemneuro.8b00353  0.32
2018 Geller R, Pechmann S, Acevedo A, Andino R, Frydman J. Hsp90 shapes protein and RNA evolution to balance trade-offs between protein stability and aggregation. Nature Communications. 9: 1781. PMID 29725062 DOI: 10.1038/s41467-018-04203-x  0.52
2017 Sweeney P, Park H, Baumann M, Dunlop J, Frydman J, Kopito R, McCampbell A, Leblanc G, Venkateswaran A, Nurmi A, Hodgson R. Protein misfolding in neurodegenerative diseases: implications and strategies. Translational Neurodegeneration. 6: 6. PMID 28293421 DOI: 10.1186/s40035-017-0077-5  0.48
2017 Baias M, Smith PE, Shen K, Joachimiak LA, Żerko S, Koźmiński W, Frydman J, Frydman L. Structure and Dynamics of the Huntingtin Exon-1 N-Terminus: A Solution NMR Perspective. Journal of the American Chemical Society. PMID 28085263 DOI: 10.1021/jacs.6b10893  0.32
2016 Shen K, Calamini B, Fauerbach JA, Ma B, Shahmoradian SH, Serrano Lachapel IL, Chiu W, Lo DC, Frydman J. Control of the structural landscape and neuronal proteotoxicity of mutant Huntingtin by domains flanking the polyQ tract. Elife. 5. PMID 27751235 DOI: 10.7554/eLife.18065  0.32
2015 Taguwa S, Maringer K, Li X, Bernal-Rubio D, Rauch JN, Gestwicki JE, Andino R, Fernandez-Sesma A, Frydman J. Defining Hsp70 Subnetworks in Dengue Virus Replication Reveals Key Vulnerability in Flavivirus Infection. Cell. PMID 26582131 DOI: 10.1016/j.cell.2015.10.046  0.88
2015 Walzthoeni T, Joachimiak LA, Rosenberger G, Röst HL, Malmström L, Leitner A, Frydman J, Aebersold R. xTract: software for characterizing conformational changes of protein complexes by quantitative cross-linking mass spectrometry. Nature Methods. PMID 26501516 DOI: 10.1038/nmeth.3631  0.88
2015 Sahl SJ, Lau L, Vonk WI, Weiss LE, Frydman J, Moerner WE. Delayed emergence of subdiffraction-sized mutant huntingtin fibrils following inclusion body formation. Quarterly Reviews of Biophysics. 1-13. PMID 26350150 DOI: 10.1017/S0033583515000219  0.88
2015 Lopez T, Dalton K, Frydman J. The Mechanism and Function of Group II Chaperonins. Journal of Molecular Biology. 427: 2919-30. PMID 25936650 DOI: 10.1016/j.jmb.2015.04.013  0.88
2015 Dhungel N, Eleuteri S, Li LB, Kramer NJ, Chartron JW, Spencer B, Kosberg K, Fields JA, Stafa K, Adame A, Lashuel H, Frydman J, Shen K, Masliah E, Gitler AD. Parkinson's disease genes VPS35 and EIF4G1 interact genetically and converge on α-synuclein. Neuron. 85: 76-87. PMID 25533483 DOI: 10.1016/j.neuron.2014.11.027  0.88
2015 Dalton KM, Frydman J, Pande VS. The dynamic conformational cycle of the group I chaperonin C-termini revealed via molecular dynamics simulation Plos One. 10. DOI: 10.1371/journal.pone.0117724  0.88
2014 Freund A, Zhong FL, Venteicher AS, Meng Z, Veenstra TD, Frydman J, Artandi SE. Proteostatic control of telomerase function through TRiC-mediated folding of TCAB1. Cell. 159: 1389-403. PMID 25467444 DOI: 10.1016/j.cell.2014.10.059  0.88
2014 Neef DW, Jaeger AM, Gomez-Pastor R, Willmund F, Frydman J, Thiele DJ. A direct regulatory interaction between chaperonin TRiC and stress-responsive transcription factor HSF1. Cell Reports. 9: 955-66. PMID 25437552 DOI: 10.1016/j.celrep.2014.09.056  0.88
2014 Pechmann S, Chartron JW, Frydman J. Local slowdown of translation by nonoptimal codons promotes nascent-chain recognition by SRP in vivo. Nature Structural & Molecular Biology. 21: 1100-5. PMID 25420103 DOI: 10.1038/nsmb.2919  0.88
2014 Joachimiak LA, Walzthoeni T, Liu CW, Aebersold R, Frydman J. The structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCT. Cell. 159: 1042-55. PMID 25416944 DOI: 10.1016/j.cell.2014.10.042  0.88
2014 Duim WC, Jiang Y, Shen K, Frydman J, Moerner WE. Super-resolution fluorescence of huntingtin reveals growth of globular species into short fibers and coexistence of distinct aggregates. Acs Chemical Biology. 9: 2767-78. PMID 25330023 DOI: 10.1021/cb500335w  0.88
2014 Pechmann S, Frydman J. Interplay between chaperones and protein disorder promotes the evolution of protein networks. Plos Computational Biology. 10: e1003674. PMID 24968255 DOI: 10.1371/journal.pcbi.1003674  0.88
2014 Leitner A, Joachimiak LA, Unverdorben P, Walzthoeni T, Frydman J, Förster F, Aebersold R. Chemical cross-linking/mass spectrometry targeting acidic residues in proteins and protein complexes. Proceedings of the National Academy of Sciences of the United States of America. 111: 9455-60. PMID 24938783 DOI: 10.1073/pnas.1320298111  0.88
2014 Kasembeli M, Lau WC, Roh SH, Eckols TK, Frydman J, Chiu W, Tweardy DJ. Modulation of STAT3 folding and function by TRiC/CCT chaperonin. Plos Biology. 12: e1001844. PMID 24756126 DOI: 10.1371/journal.pbio.1001844  0.88
2014 Sontag EM, Vonk WI, Frydman J. Sorting out the trash: the spatial nature of eukaryotic protein quality control. Current Opinion in Cell Biology. 26: 139-46. PMID 24463332 DOI: 10.1016/j.ceb.2013.12.006  0.88
2013 Escusa-Toret S, Vonk WI, Frydman J. Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress. Nature Cell Biology. 15: 1231-43. PMID 24036477 DOI: 10.1038/ncb2838  0.88
2013 Shahmoradian SH, Galaz-Montoya JG, Schmid MF, Cong Y, Ma B, Spiess C, Frydman J, Ludtke SJ, Chiu W. TRiC's tricks inhibit huntingtin aggregation. Elife. 2: e00710. PMID 23853712 DOI: 10.7554/eLife.00710  0.88
2013 Duttler S, Pechmann S, Frydman J. Principles of cotranslational ubiquitination and quality control at the ribosome. Molecular Cell. 50: 379-93. PMID 23583075 DOI: 10.1016/j.molcel.2013.03.010  0.88
2013 Lauring AS, Frydman J, Andino R. The role of mutational robustness in RNA virus evolution. Nature Reviews. Microbiology. 11: 327-36. PMID 23524517 DOI: 10.1038/nrmicro3003  0.88
2013 Geller R, Andino R, Frydman J. Hsp90 inhibitors exhibit resistance-free antiviral activity against respiratory syncytial virus. Plos One. 8: e56762. PMID 23460813 DOI: 10.1371/journal.pone.0056762  0.88
2013 Pechmann S, Willmund F, Frydman J. The ribosome as a hub for protein quality control. Molecular Cell. 49: 411-21. PMID 23395271 DOI: 10.1016/j.molcel.2013.01.020  0.88
2013 Sontag EM, Joachimiak LA, Tan Z, Tomlinson A, Housman DE, Glabe CG, Potkin SG, Frydman J, Thompson LM. Exogenous delivery of chaperonin subunit fragment ApiCCT1 modulates mutant Huntingtin cellular phenotypes. Proceedings of the National Academy of Sciences of the United States of America. 110: 3077-82. PMID 23365139 DOI: 10.1073/pnas.1222663110  0.88
2013 Willmund F, del Alamo M, Pechmann S, Chen T, Albanèse V, Dammer EB, Peng J, Frydman J. The cotranslational function of ribosome-associated Hsp70 in eukaryotic protein homeostasis. Cell. 152: 196-209. PMID 23332755 DOI: 10.1016/j.cell.2012.12.001  0.88
2013 Pechmann S, Frydman J. Evolutionary conservation of codon optimality reveals hidden signatures of cotranslational folding. Nature Structural & Molecular Biology. 20: 237-43. PMID 23262490 DOI: 10.1038/nsmb.2466  0.88
2012 Sahl SJ, Weiss LE, Duim WC, Frydman J, Moerner WE. Cellular inclusion bodies of mutant huntingtin exon 1 obscure small fibrillar aggregate species. Scientific Reports. 2: 895. PMID 23193437 DOI: 10.1038/srep00895  0.88
2012 Reissmann S, Joachimiak LA, Chen B, Meyer AS, Nguyen A, Frydman J. A gradient of ATP affinities generates an asymmetric power stroke driving the chaperonin TRIC/CCT folding cycle. Cell Reports. 2: 866-77. PMID 23041314 DOI: 10.1016/j.celrep.2012.08.036  0.88
2012 Beltrao P, Albanèse V, Kenner LR, Swaney DL, Burlingame A, Villén J, Lim WA, Fraser JS, Frydman J, Krogan NJ. Systematic functional prioritization of protein posttranslational modifications. Cell. 150: 413-25. PMID 22817900 DOI: 10.1016/j.cell.2012.05.036  0.88
2012 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, et al. State of the science: an update on renal cell carcinoma. Molecular Cancer Research : McR. 10: 859-80. PMID 22638109 DOI: 10.1158/1541-7786.MCR-12-0117  0.88
2012 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. The molecular architecture of the eukaryotic chaperonin TRiC/CCT. Structure (London, England : 1993). 20: 814-25. PMID 22503819 DOI: 10.1016/j.str.2012.03.007  0.88
2012 Pereira JH, Ralston CY, Douglas NR, Kumar R, Lopez T, McAndrew RP, Knee KM, King JA, Frydman J, Adams PD. Mechanism of nucleotide sensing in group II chaperonins. The Embo Journal. 31: 731-40. PMID 22193720 DOI: 10.1038/emboj.2011.468  0.88
2012 Geller R, Taguwa S, Frydman J. Broad action of Hsp90 as a host chaperone required for viral replication. Biochimica Et Biophysica Acta. 1823: 698-706. PMID 22154817 DOI: 10.1016/j.bbamcr.2011.11.007  0.88
2012 Cong Y, Schröder GF, Meyer AS, Jakana J, Ma B, Dougherty MT, Schmid MF, Reissmann S, Levitt M, Ludtke SL, Frydman J, Chiu W. Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle. The Embo Journal. 31: 720-30. PMID 22045336 DOI: 10.1038/emboj.2011.366  0.88
2011 Franzosa EA, Albanèse V, Frydman J, Xia Y, McClellan AJ. Heterozygous yeast deletion collection screens reveal essential targets of Hsp90. Plos One. 6: e28211. PMID 22140548 DOI: 10.1371/journal.pone.0028211  0.88
2011 Jiang Y, Douglas NR, Conley NR, Miller EJ, Frydman J, Moerner WE. Sensing cooperativity in ATP hydrolysis for single multisubunit enzymes in solution. Proceedings of the National Academy of Sciences of the United States of America. 108: 16962-7. PMID 21896715 DOI: 10.1073/pnas.1112244108  0.88
2011 del Alamo M, Hogan DJ, Pechmann S, Albanese V, Brown PO, Frydman J. Defining the specificity of cotranslationally acting chaperones by systematic analysis of mRNAs associated with ribosome-nascent chain complexes. Plos Biology. 9: e1001100. PMID 21765803 DOI: 10.1371/journal.pbio.1001100  0.88
2011 Chen B, Retzlaff M, Roos T, Frydman J. Cellular strategies of protein quality control. Cold Spring Harbor Perspectives in Biology. 3: a004374. PMID 21746797 DOI: 10.1101/cshperspect.a004374  0.88
2011 Duim WC, Chen B, Frydman J, Moerner WE. Sub-diffraction imaging of huntingtin protein aggregates by fluorescence blink-microscopy and atomic force microscopy. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 12: 2387-90. PMID 21735512 DOI: 10.1002/cphc.201100392  0.88
2011 Zhang J, Ma B, DiMaio F, Douglas NR, Joachimiak LA, Baker D, Frydman J, Levitt M, Chiu W. Cryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure. Structure (London, England : 1993). 19: 633-9. PMID 21565698 DOI: 10.1016/j.str.2011.03.005  0.88
2011 Douglas NR, Reissmann S, Zhang J, Chen B, Jakana J, Kumar R, Chiu W, Frydman J. Dual action of ATP hydrolysis couples lid closure to substrate release into the group II chaperonin chamber. Cell. 144: 240-52. PMID 21241893 DOI: 10.1016/j.cell.2010.12.017  0.88
2011 Jiang Y, Douglas N, Conley N, Miller E, Frydman J, Moerner WE. Studying subunit cooperativity by counting hydrolyzed ATP on single chaperonin nanomachines in solution Optics Infobase Conference Papers 0.88
2010 Pan X, Reissman S, Douglas NR, Huang Z, Yuan DS, Wang X, McCaffery JM, Frydman J, Boeke JD. Trivalent arsenic inhibits the functions of chaperonin complex. Genetics. 186: 725-34. PMID 20660648 DOI: 10.1534/genetics.110.117655  0.88
2010 Kim SY, Miller EJ, Frydman J, Moerner WE. Action of the chaperonin GroEL/ES on a non-native substrate observed with single-molecule FRET. Journal of Molecular Biology. 401: 553-63. PMID 20600107 DOI: 10.1016/j.jmb.2010.06.050  0.88
2010 Pereira JH, Ralston CY, Douglas NR, Meyer D, Knee KM, Goulet DR, King JA, Frydman J, Adams PD. Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle. The Journal of Biological Chemistry. 285: 27958-66. PMID 20573955 DOI: 10.1074/jbc.M110.125344  0.88
2010 Albanèse V, Reissmann S, Frydman J. A ribosome-anchored chaperone network that facilitates eukaryotic ribosome biogenesis. The Journal of Cell Biology. 189: 69-81. PMID 20368619 DOI: 10.1083/jcb.201001054  0.88
2010 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. 4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement. Proceedings of the National Academy of Sciences of the United States of America. 107: 4967-72. PMID 20194787 DOI: 10.1073/pnas.0913774107  0.88
2010 Zhang J, Baker ML, Schröder GF, Douglas NR, Reissmann S, Jakana J, Dougherty M, Fu CJ, Levitt M, Ludtke SJ, Frydman J, Chiu W. Mechanism of folding chamber closure in a group II chaperonin. Nature. 463: 379-83. PMID 20090755 DOI: 10.1038/nature08701  0.88
2010 Jiang Y, Douglas N, Conley N, Miller E, Frydman J, Moerner WE. Suppression of brownian motion explores cooperativity for single multi-subunit enzymes in solution Optics Infobase Conference Papers 0.88
2009 Tam S, Spiess C, Auyeung W, Joachimiak L, Chen B, Poirier MA, Frydman J. The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation. Nature Structural & Molecular Biology. 16: 1279-85. PMID 19915590 DOI: 10.1038/nsmb.1700  0.88
2009 Kelley NW, Huang X, Tam S, Spiess C, Frydman J, Pande VS. The predicted structure of the headpiece of the Huntingtin protein and its implications on Huntingtin aggregation. Journal of Molecular Biology. 388: 919-27. PMID 19361448 DOI: 10.1016/j.jmb.2009.01.032  0.88
2009 Jiang Y, Cohen A, Douglas N, Frydman J, Moerner WE. Determining single-molecule ATP binding stoichiometry in a multi-subunit enzyme with a hardware-based anti-brownian electrokinetic trap Optics Infobase Conference Papers 0.88
2008 Jiang Y, Wang Q, Cohen AE, Douglas N, Frydman J, Moerner WE. Hardware-based anti-Brownian electrokinetic trap (ABEL trap) for single molecules: Control loop simulations and application to ATP binding stoichiometry in multi-subunit enzymes. Proceedings of Spie--the International Society For Optical Engineering. 7038: 1-12. PMID 19823693 DOI: 10.1117/12.798093  0.32
2008 Kaganovich D, Kopito R, Frydman J. Misfolded proteins partition between two distinct quality control compartments. Nature. 454: 1088-95. PMID 18756251 DOI: 10.1038/nature07195  0.88
2008 Booth CR, Meyer AS, Cong Y, Topf M, Sali A, Ludtke SJ, Chiu W, Frydman J. Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT. Nature Structural & Molecular Biology. 15: 746-53. PMID 18536725 DOI: 10.1038/nsmb.1436  0.88
2007 McClellan AJ, Xia Y, Deutschbauer AM, Davis RW, Gerstein M, Frydman J. Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches. Cell. 131: 121-35. PMID 17923092 DOI: 10.1016/j.cell.2007.07.036  0.88
2007 Reissmann S, Parnot C, Booth CR, Chiu W, Frydman J. Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins. Nature Structural & Molecular Biology. 14: 432-40. PMID 17460696 DOI: 10.1038/nsmb1236  0.88
2007 Geller R, Vignuzzi M, Andino R, Frydman J. Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance. Genes & Development. 21: 195-205. PMID 17234885 DOI: 10.1101/gad.1505307  0.88
2006 Spiess C, Miller EJ, McClellan AJ, Frydman J. Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperonins. Molecular Cell. 24: 25-37. PMID 17018290 DOI: 10.1016/j.molcel.2006.09.003  0.88
2006 Tam S, Geller R, Spiess C, Frydman J. The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nature Cell Biology. 8: 1155-62. PMID 16980959 DOI: 10.1038/ncb1477  0.88
2006 Miller EJ, Meyer AS, Frydman J. Modeling of possible subunit arrangements in the eukaryotic chaperonin TRiC. Protein Science : a Publication of the Protein Society. 15: 1522-6. PMID 16672233 DOI: 10.1110/ps.052001606  0.88
2006 Albanèse V, Yam AY, Baughman J, Parnot C, Frydman J. Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells. Cell. 124: 75-88. PMID 16413483 DOI: 10.1016/j.cell.2005.11.039  0.88
2006 Xu L, Dayal M, Ouyang YB, Sun Y, Yang CF, Frydman J, Giffard RG. Chaperonin GroEL and its mutant D87K protect from ischemia in vivo and in vitro. Neurobiology of Aging. 27: 562-9. PMID 16257478 DOI: 10.1016/j.neurobiolaging.2005.09.032  0.88
2005 Kim SY, Semyonov AN, Twieg RJ, Horwich AL, Frydman J, Moerner WE. Probing the sequence of conformationally induced polarity changes in the molecular chaperonin GroEL with fluorescence spectroscopy. The Journal of Physical Chemistry. B. 109: 24517-25. PMID 16375456 DOI: 10.1021/jp0534232  0.88
2005 Yam AY, Albanèse V, Lin HT, Frydman J. Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding. The Journal of Biological Chemistry. 280: 41252-61. PMID 16219770 DOI: 10.1074/jbc.M503615200  0.88
2005 McClellan AJ, Tam S, Kaganovich D, Frydman J. Protein quality control: chaperones culling corrupt conformations. Nature Cell Biology. 7: 736-41. PMID 16056264 DOI: 10.1038/ncb0805-736  0.88
2005 McClellan AJ, Scott MD, Frydman J. Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways. Cell. 121: 739-48. PMID 15935760 DOI: 10.1016/j.cell.2005.03.024  0.88
2005 Etchells SA, Meyer AS, Yam AY, Roobol A, Miao Y, Shao Y, Carden MJ, Skach WR, Frydman J, Johnson AE. The cotranslational contacts between ribosome-bound nascent polypeptides and the subunits of the hetero-oligomeric chaperonin TRiC probed by photocross-linking. The Journal of Biological Chemistry. 280: 28118-26. PMID 15929940 DOI: 10.1074/jbc.M504110200  0.88
2005 Vang S, Corydon TJ, Børglum AD, Scott MD, Frydman J, Mogensen J, Gregersen N, Bross P. Actin mutations in hypertrophic and dilated cardiomyopathy cause inefficient protein folding and perturbed filament formation. The Febs Journal. 272: 2037-49. PMID 15819894 DOI: 10.1111/j.1742-4658.2005.04630.x  0.88
2004 Spiess C, Meyer AS, Reissmann S, Frydman J. Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets. Trends in Cell Biology. 14: 598-604. PMID 15519848 DOI: 10.1016/j.tcb.2004.09.015  0.88
2003 Feldman DE, Spiess C, Howard DE, Frydman J. Tumorigenic mutations in VHL disrupt folding in vivo by interfering with chaperonin binding. Molecular Cell. 12: 1213-24. PMID 14636579 DOI: 10.1016/S1097-2765(03)00423-4  0.88
2003 Scott MD, Frydman J. Aberrant protein folding as the molecular basis of cancer. Methods in Molecular Biology (Clifton, N.J.). 232: 67-76. PMID 12840540 DOI: 10.1385/1-59259-394-1:67  0.88
2003 Meyer AS, Gillespie JR, Walther D, Millet IS, Doniach S, Frydman J. Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis. Cell. 113: 369-81. PMID 12732144 DOI: 10.1016/S0092-8674(03)00307-6  0.88
2003 Melville MW, McClellan AJ, Meyer AS, Darveau A, Frydman J. The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex. Molecular and Cellular Biology. 23: 3141-51. PMID 12697815 DOI: 10.1128/MCB.23.9.3141-3151.2003  0.88
2002 Albanèse V, Frydman J. Where chaperones and nascent polypeptides meet. Nature Structural Biology. 9: 716-8. PMID 12352951 DOI: 10.1038/nsb1002-716  0.88
2001 Dunn AY, Melville MW, Frydman J. Review: Cellular substrates of the eukaryotic chaperonin TRiC/CCT Journal of Structural Biology. 135: 176-184. PMID 11580267 DOI: 10.1006/jsbi.2001.4380  0.88
2001 McClellan AJ, Frydman J. Molecular chaperones and the art of recognizing a lost cause Nature Cell Biology. 3: E51-E53. PMID 11175763 DOI: 10.1038/35055162  0.88
2000 Thulasiraman V, Ferreyra RG, Frydman J. Folding assays. Assessing the native conformation of proteins Methods in Molecular Biology (Clifton, N.J.). 140: 169-177. PMID 11484486  0.88
2000 Thulasiraman V, Ferreyra RG, Frydman J. Monitoring actin folding. Purification protocols for labeled proteins and binding to DNase I-sepharose beads Methods in Molecular Biology (Clifton, N.J.). 140: 161-167. PMID 11484485  0.88
2000 Ferreyra RG, Frydman J. Purification of the cytosolic chaperonin TRiC from bovine testis Methods in Molecular Biology (Clifton, N.J.). 140: 153-160. PMID 11484484  0.88
2000 McCallum CD, Do H, Johnson AE, Frydman J. The interaction of the chaperonin tailless complex polypeptide 1 (TCP1) ring complex (TRiC) with ribosome-bound nascent chains examined using photo- cross-linking Journal of Cell Biology. 149: 591-601. PMID 10791973 DOI: 10.1083/jcb.149.3.591  0.88
2000 Feldman DE, Frydman J. Protein folding in vivo: the importance of molecular chaperones. Current Opinion in Structural Biology. 10: 26-33. PMID 10679467 DOI: 10.1016/S0959-440X(99)00044-5  0.88
1999 Feldman DE, Thulasiraman V, Ferreyra RG, Frydman J. Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC. Molecular Cell. 4: 1051-61. PMID 10635329  0.88
1999 Frydman J, Erdjument-Bromage H, Tempst P, Ulrich Hartl F. Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase Nature Structural Biology. 6: 697-705. PMID 10404229 DOI: 10.1038/10754  0.88
1999 Thulasiraman V, Yang CF, Frydman J. In vivo newly translated polypeptides are sequestered in a protected folding environment Embo Journal. 18: 85-95. PMID 9878053 DOI: 10.1093/emboj/18.1.85  0.88
1998 Heyrovská N, Frydman J, Höhfeld J, Hartl FU. Directionality of polypeptide transfer in the mitochondrial pathway of chaperone-mediated protein folding Biological Chemistry. 379: 301-309. PMID 9563826  0.88
1997 Frydman J, Höhfeld J. Chaperones get in touch: The Hip-Hop connection Trends in Biochemical Sciences. 22: 87-92. PMID 9066258 DOI: 10.1016/S0968-0004(97)01005-0  0.88
1996 Frydman J, Hartl FU. Principles of chaperone-assisted protein folding: Differences between in vitro and in vivo mechanisms Science. 272: 1497-1502. PMID 8633246  0.88
1994 Li WZ, Lin P, Frydman J, Boal TR, Cardillo TS, Richard LM, Toth D, Lichtman MA, Hartl FU, Sherman F, Segel GB. Tcp20, a subunit of the eukaryotic TRiC chaperonin from humans and yeast Journal of Biological Chemistry. 269: 18616-18622. PMID 8034610  0.88
1994 Frydman J, Nimmesgern E, Ohtsuka K, Hartl FU. Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones Nature. 370: 111-117. PMID 8022479 DOI: 10.1038/370111a0  0.88
1992 Frydman J, Nimmesgern E, Erdjument-Bromage H, Wall JS, Tempst P, Hartl FU. Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits Embo Journal. 11: 4767-4778. PMID 1361170  0.88
1992 Driscoll J, Frydman J, Goldberg AL. An ATP-stabilized inhibitor of the proteasome is a component of the 1500-kDa ubiquitin conjugate-degrading complex Proceedings of the National Academy of Sciences of the United States of America. 89: 4986-4990. PMID 1317579  0.88
Show low-probability matches.