| Year |
Citation |
Score |
| 2024 |
Aviner R, Lee TT, Masto VB, Li KH, Andino R, Frydman J. Polyglutamine-mediated ribotoxicity disrupts proteostasis and stress responses in Huntington's disease. Nature Cell Biology. PMID 38741019 DOI: 10.1038/s41556-024-01414-x |
0.546 |
|
| 2024 |
Aviner R, Lidsky PV, Xiao Y, Tassetto M, Kim D, Zhang L, McAlpine PL, Elias J, Frydman J, Andino R. SARS-CoV-2 Nsp1 cooperates with initiation factors EIF1 and 1A to selectively enhance translation of viral RNA. Plos Pathogens. 20: e1011535. PMID 38335237 DOI: 10.1371/journal.ppat.1011535 |
0.569 |
|
| 2024 |
Park J, Kim H, Gestaut D, Lim S, Opoku-Nsiah KA, Leitner A, Frydman J, Roh SH. A structural vista of phosducin-like PhLP2A-chaperonin TRiC cooperation during the ATP-driven folding cycle. Nature Communications. 15: 1007. PMID 38307855 DOI: 10.1038/s41467-024-45242-x |
0.776 |
|
| 2023 |
Betancourt Moreira K, Collier MP, Leitner A, Li KH, Lachapel ILS, McCarthy F, Opoku-Nsiah KA, Morales-Polanco F, Barbosa N, Gestaut D, Samant RS, Roh SH, Frydman J. A hierarchical assembly pathway directs the unique subunit arrangement of TRiC/CCT. Molecular Cell. PMID 37625406 DOI: 10.1016/j.molcel.2023.07.031 |
0.773 |
|
| 2023 |
Aguilar Rangel M, Dolan PT, Taguwa S, Xiao Y, Andino R, Frydman J. High-resolution mapping reveals the mechanism and contribution of genome insertions and deletions to RNA virus evolution. Proceedings of the National Academy of Sciences of the United States of America. 120: e2304667120. PMID 37487061 DOI: 10.1073/pnas.2304667120 |
0.717 |
|
| 2023 |
Aviner R, Lidsky PV, Xiao Y, Tasseto M, Zhang L, McAlpine PL, Elias J, Frydman J, Andino R. SARS-CoV-2 Nsp1 regulates translation start site fidelity to promote infection. Biorxiv : the Preprint Server For Biology. PMID 37461541 DOI: 10.1101/2023.07.05.547902 |
0.565 |
|
| 2023 |
Sontag EM, Morales-Polanco F, Chen JH, McDermott G, Dolan PT, Gestaut D, Le Gros MA, Larabell C, Frydman J. Nuclear and cytoplasmic spatial protein quality control is coordinated by nuclear-vacuolar junctions and perinuclear ESCRT. Nature Cell Biology. PMID 37081164 DOI: 10.1038/s41556-023-01128-6 |
0.778 |
|
| 2023 |
Park J, Kim H, Gestaut D, Lim S, Leitner A, Frydman J, Roh SH. A structural vista of phosducin-like PhLP2A-chaperonin TRiC cooperation during the ATP-driven folding cycle. Biorxiv : the Preprint Server For Biology. PMID 37016670 DOI: 10.1101/2023.03.25.534239 |
0.301 |
|
| 2023 |
Elsasser S, Elia LP, Morimoto RI, Powers ET, Elsasser S, Finley D, Costa B, Budron M, Tokuno Z, Wang S, Iyer RG, Barth B, Mockler E, Elia LP, Finkbeiner S, ... ... Frydman J, et al. A Comprehensive Enumeration of the Human Proteostasis Network. 2. Components of the Autophagy-Lysosome Pathway. Biorxiv : the Preprint Server For Biology. PMID 36993380 DOI: 10.1101/2023.03.22.533675 |
0.544 |
|
| 2022 |
Shao H, Taguwa S, Gilbert L, Shkedi A, Sannino S, Guerriero CJ, Gale-Day ZJ, Young ZT, Brodsky JL, Weissman J, Gestwicki JE, Frydman J. A campaign targeting a conserved Hsp70 binding site uncovers how subcellular localization is linked to distinct biological activities. Cell Chemical Biology. PMID 35830852 DOI: 10.1016/j.chembiol.2022.06.006 |
0.501 |
|
| 2022 |
Morales-Polanco F, Lee JH, Barbosa NM, Frydman J. Cotranslational Mechanisms of Protein Biogenesis and Complex Assembly in Eukaryotes. Annual Review of Biomedical Data Science. PMID 35472290 DOI: 10.1146/annurev-biodatasci-121721-095858 |
0.81 |
|
| 2022 |
Stein KC, Morales-Polanco F, van der Lienden J, Rainbolt TK, Frydman J. Ageing exacerbates ribosome pausing to disrupt cotranslational proteostasis. Nature. 601: 637-642. PMID 35046576 DOI: 10.1038/s41586-021-04295-4 |
0.772 |
|
| 2022 |
Cable J, Weber-Ban E, Clausen T, Walters KJ, Sharon M, Finley DJ, Gu Y, Hanna J, Feng Y, Martens S, Simonsen A, Hansen M, Zhang H, Goodwin JM, Reggio A, ... ... Frydman J, et al. Targeted protein degradation: from small molecules to complex organelles-a Keystone Symposia report. Annals of the New York Academy of Sciences. PMID 35000205 DOI: 10.1111/nyas.14745 |
0.316 |
|
| 2021 |
Xiao Y, Lidsky PV, Shirogane Y, Aviner R, Wu CT, Li W, Zheng W, Talbot D, Catching A, Doitsh G, Su W, Gekko CE, Nayak A, Ernst JD, Brodsky L, ... ... Frydman J, et al. A defective viral genome strategy elicits broad protective immunity against respiratory viruses. Cell. PMID 34852237 DOI: 10.1016/j.cell.2021.11.023 |
0.485 |
|
| 2021 |
Aviner R, Li KH, Frydman J, Andino R. Author Correction: Cotranslational prolyl hydroxylation is essential for flavivirus biogenesis. Nature. PMID 34675396 DOI: 10.1038/s41586-021-04102-0 |
0.447 |
|
| 2021 |
Aviner R, Li KH, Frydman J, Andino R. Cotranslational prolyl hydroxylation is essential for flavivirus biogenesis. Nature. PMID 34408324 DOI: 10.1038/s41586-021-03851-2 |
0.528 |
|
| 2021 |
Galaz-Montoya JG, Shahmoradian SH, Shen K, Frydman J, Chiu W. Cryo-electron tomography provides topological insights into mutant huntingtin exon 1 and polyQ aggregates. Communications Biology. 4: 849. PMID 34239038 DOI: 10.1038/s42003-021-02360-2 |
0.761 |
|
| 2021 |
Knowlton JJ, Gestaut D, Ma B, Taylor G, Seven AB, Leitner A, Wilson GJ, Shanker S, Yates NA, Prasad BVV, Aebersold R, Chiu W, Frydman J, Dermody TS. Structural and functional dissection of reovirus capsid folding and assembly by the prefoldin-TRiC/CCT chaperone network. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 33836586 DOI: 10.1073/pnas.2018127118 |
0.365 |
|
| 2021 |
Dolan PT, Taguwa S, Rangel MA, Acevedo A, Hagai T, Andino R, Frydman J. Principles of dengue virus evolvability derived from genotype-fitness maps in human and mosquito cells. Elife. 10. PMID 33491648 DOI: 10.7554/eLife.61921 |
0.71 |
|
| 2020 |
Lee CYD, Wang N, Shen K, Stricos M, Langfelder P, Cheon KH, Cortés EP, Vinters HV, Vonsattel JP, Wexler NS, Damoiseaux R, Frydman J, Yang XW. Disease-related Huntingtin seeding activities in cerebrospinal fluids of Huntington's disease patients. Scientific Reports. 10: 20295. PMID 33219289 DOI: 10.1038/s41598-020-77164-1 |
0.723 |
|
| 2020 |
Vonk WIM, Rainbolt TK, Dolan PT, Webb AE, Brunet A, Frydman J. Differentiation Drives Widespread Rewiring of the Neural Stem Cell Chaperone Network. Molecular Cell. PMID 32268122 DOI: 10.1016/J.Molcel.2020.03.009 |
0.695 |
|
| 2020 |
Dalton K, Lopez T, Pande V, Frydman J. REP-X: An Evolution-guided Strategy for the Rational Design of Cysteine-less Protein Variants. Scientific Reports. 10: 2193. PMID 32042106 DOI: 10.1038/S41598-020-58794-X |
0.402 |
|
| 2020 |
Rainbolt TK, Frydman J. Dynamics and clustering of IRE1α during ER stress. Proceedings of the National Academy of Sciences of the United States of America. 117: 3352-3354. PMID 32019880 DOI: 10.1073/Pnas.1921799117 |
0.396 |
|
| 2019 |
Stein KC, Kriel A, Frydman J. Nascent Polypeptide Domain Topology and Elongation Rate Direct the Cotranslational Hierarchy of Hsp70 and TRiC/CCT. Molecular Cell. PMID 31400849 DOI: 10.1016/J.Molcel.2019.06.036 |
0.419 |
|
| 2019 |
Samant RS, Masto VB, Frydman J. Dosage compensation plans: protein aggregation provides additional insurance against aneuploidy. Genes & Development. 33: 1027-1030. PMID 31371460 DOI: 10.1101/Gad.329383.119 |
0.456 |
|
| 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 |
0.806 |
|
| 2019 |
Gestaut D, Limatola A, Joachimiak L, Frydman J. The ATP-powered gymnastics of TRiC/CCT: an asymmetric protein folding machine with a symmetric origin story. Current Opinion in Structural Biology. 55: 50-58. PMID 30978594 DOI: 10.1016/J.Sbi.2019.03.002 |
0.486 |
|
| 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 |
0.441 |
|
| 2019 |
Samant RS, Frydman J. Methods for measuring misfolded protein clearance in the budding yeast Saccharomyces cerevisiae. Methods in Enzymology. 619: 27-45. PMID 30910025 DOI: 10.1016/Bs.Mie.2018.12.039 |
0.442 |
|
| 2019 |
Aviner R, Frydman J. Proteostasis in Viral Infection: Unfolding the Complex Virus-Chaperone Interplay. Cold Spring Harbor Perspectives in Biology. PMID 30858229 DOI: 10.1101/Cshperspect.A034090 |
0.437 |
|
| 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 |
0.664 |
|
| 2018 |
Stein KC, Frydman J. The stop and go traffic regulating protein biogenesis: how translation kinetics control proteostasis. The Journal of Biological Chemistry. PMID 30504455 DOI: 10.1074/Jbc.Rev118.002814 |
0.418 |
|
| 2018 |
Samant RS, Livingston CM, Sontag EM, Frydman J. Distinct proteostasis circuits cooperate in nuclear and cytoplasmic protein quality control. Nature. 563: 407-411. PMID 30429547 DOI: 10.1038/S41586-018-0678-X |
0.448 |
|
| 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 |
0.573 |
|
| 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 |
0.77 |
|
| 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 |
0.79 |
|
| 2018 |
Leeman DS, Hebestreit K, Ruetz T, Webb AE, McKay A, Pollina EA, Dulken BW, Zhao X, Yeo RW, Ho TT, Mahmoudi S, Devarajan K, Passegué E, Rando TA, Frydman J, et al. Lysosome activation clears aggregates and enhances quiescent neural stem cell activation during aging. Science (New York, N.Y.). 359: 1277-1283. PMID 29590078 DOI: 10.1126/Science.Aag3048 |
0.373 |
|
| 2018 |
Knowlton JJ, Fernández de Castro I, Ashbrook AW, Gestaut DR, Zamora PF, Bauer JA, Forrest JC, Frydman J, Risco C, Dermody TS. The TRiC chaperonin controls reovirus replication through outer-capsid folding. Nature Microbiology. PMID 29531365 DOI: 10.1038/S41564-018-0122-X |
0.43 |
|
| 2017 |
Lopez T, Dalton K, Tomlinson A, Pande V, Frydman J. An information theoretic framework reveals a tunable allosteric network in group II chaperonins. Nature Structural & Molecular Biology. PMID 28741612 DOI: 10.1038/Nsmb.3440 |
0.313 |
|
| 2017 |
Mitchell Sontag E, Samant RS, Frydman J. Mechanisms and Functions of Spatial Protein Quality Control. Annual Review of Biochemistry. PMID 28489421 DOI: 10.1146/Annurev-Biochem-060815-014616 |
0.435 |
|
| 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 |
0.38 |
|
| 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 |
0.763 |
|
| 2017 |
Sontag E, Chen J, McDermott G, Gestaut D, Larabell C, Frydman J. Sorting Out the JUNQ: the Spatial Nature of Protein Quality Control Microscopy and Microanalysis. 23: 994-995. DOI: 10.1017/S1431927617005633 |
0.313 |
|
| 2016 |
Hanebuth MA, Kityk R, Fries SJ, Jain A, Kriel A, Albanese V, Frickey T, Peter C, Mayer MP, Frydman J, Deuerling E. Multivalent contacts of the Hsp70 Ssb contribute to its architecture on ribosomes and nascent chain interaction. Nature Communications. 7: 13695. PMID 27917864 DOI: 10.1038/Ncomms13695 |
0.414 |
|
| 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 |
0.771 |
|
| 2016 |
Chartron JW, Hunt KC, Frydman J. Cotranslational signal-independent SRP preloading during membrane targeting. Nature. PMID 27487213 DOI: 10.1038/Nature19309 |
0.336 |
|
| 2016 |
Shen K, Calamini B, Fauerbach JA, Ma B, Shahmoradian SH, Lachapel ILS, Chiu W, Lo DC, Frydman J. Author response: Control of the structural landscape and neuronal proteotoxicity of mutant Huntingtin by domains flanking the polyQ tract Elife. DOI: 10.7554/Elife.18065.024 |
0.736 |
|
| 2016 |
Baias M, Smith P, Shen K, Joachimiak L, Zerko S, Kozminski W, Frydman J, Frydman L. Backbone 1H, 13C, and 15N Chemical Shift Assignments for an Exon-1 Fragment of Huntingtin at pH = 1.7 and T = 25 C. Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr26964 |
0.709 |
|
| 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 |
0.688 |
|
| 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 |
0.335 |
|
| 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 |
0.409 |
|
| 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 |
0.439 |
|
| 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: e0117724. PMID 25822285 DOI: 10.1371/Journal.Pone.0117724 |
0.385 |
|
| 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 |
0.373 |
|
| 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 |
0.395 |
|
| 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 |
0.34 |
|
| 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 |
0.383 |
|
| 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 |
0.75 |
|
| 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 |
0.442 |
|
| 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 |
0.309 |
|
| 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 |
0.338 |
|
| 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 |
0.444 |
|
| 2014 |
Sahl SJ, Vonk WI, Weiss LE, Lau L, Frydman J, Moerner W. The Aggregation-Prone Mutant Huntingtin Protein in a Cellular Context - Approaches by Super-Resolution Imaging Biophysical Journal. 106: 683a. DOI: 10.1016/J.Bpj.2013.11.3780 |
0.372 |
|
| 2014 |
Shen K, Calamini B, Lo D, Frydman J. Polyglutamine Flanking Regions in Huntingtin Highlight Key Structural Intermediates Relevant for Molecular Chaperone Interaction and Huntington's Disease Pathogenesis Biophysical Journal. 106: 682a. DOI: 10.1016/J.Bpj.2013.11.3774 |
0.763 |
|
| 2014 |
Frydman J. The Machines that Fold Proteins in the Eukaryotic Cytosol Biophysical Journal. 106: 6a. DOI: 10.1016/J.Bpj.2013.11.073 |
0.357 |
|
| 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 |
0.416 |
|
| 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 |
0.42 |
|
| 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 |
0.366 |
|
| 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 |
0.535 |
|
| 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 |
0.757 |
|
| 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 |
0.44 |
|
| 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 |
0.413 |
|
| 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 |
0.474 |
|
| 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 |
0.321 |
|
| 2013 |
Sahl SJ, Weiss LE, Lau L, Frydman J, Moerner W. Super-resolution fluorescence imaging of intracellular mutant huntingtin protein reveals a population of fibrillar aggregates co-existing with compact perinuclear inclusion bodies Molecular Neurodegeneration. 8: O18. DOI: 10.1186/1750-1326-8-S1-O18 |
0.369 |
|
| 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 |
0.375 |
|
| 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 |
0.584 |
|
| 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 |
0.392 |
|
| 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 |
0.54 |
|
| 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 |
0.405 |
|
| 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 |
0.725 |
|
| 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 |
0.56 |
|
| 2012 |
Frydman J. Mechanism and Function of the Eukaryotic Ring-Shaped Chaperonin TRiC/CCT Biophysical Journal. 102: 428a. DOI: 10.1016/J.Bpj.2011.11.2340 |
0.475 |
|
| 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 |
0.337 |
|
| 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: 10.1016/J.Bpj.2011.11.967 |
0.578 |
|
| 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 |
0.449 |
|
| 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 |
0.43 |
|
| 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 |
0.385 |
|
| 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 |
0.368 |
|
| 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 |
0.34 |
|
| 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. DOI: 10.1364/Fio.2011.Ftuo6 |
0.584 |
|
| 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 |
0.367 |
|
| 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 |
0.619 |
|
| 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 |
0.381 |
|
| 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 |
0.468 |
|
| 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 |
0.625 |
|
| 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 |
0.364 |
|
| 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. DOI: 10.1364/Fio.2010.Ftum1 |
0.545 |
|
| 2010 |
Zhang J, Baker ML, Schroeder G, Douglas NR, Jakana J, Fu CJ, Levitt M, Ludtke SJ, Frydman J, Chiu W. Rocking Motion of a Protein-Folding Nano-Machine Revealed By Single-Particle Cryo-Em Biophysical Journal. 98: 33a. DOI: 10.1016/J.Bpj.2009.12.192 |
0.355 |
|
| 2010 |
Cong Y, Baker M, Jakana J, Woolford D, Reissmann S, Ludtke SJ, Frydman J, Chiu W. 4.0 Å Cryo-EM Structure of the Mammalian Chaperonin: TRiC/CCT Biophysical Journal. 98: 222a-223a. DOI: 10.1016/J.Bpj.2009.12.1202 |
0.381 |
|
| 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 |
0.394 |
|
| 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 |
0.343 |
|
| 2009 |
Mayer MP, Prodromou C, Frydman J. The Hsp90 mosaic: a picture emerges. Nature Structural & Molecular Biology. 16: 2-6. PMID 19125165 DOI: 10.1038/Nsmb0109-2 |
0.325 |
|
| 2008 |
Yam AY, Xia Y, Lin HT, Burlingame A, Gerstein M, Frydman J. Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies. Nature Structural & Molecular Biology. 15: 1255-62. PMID 19011634 DOI: 10.1038/Nsmb.1515 |
0.796 |
|
| 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 |
0.751 |
|
| 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 |
0.578 |
|
| 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 |
0.339 |
|
| 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 |
0.392 |
|
| 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 |
0.773 |
|
| 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 |
0.627 |
|
| 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 |
0.743 |
|
| 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 |
0.679 |
|
| 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 |
0.757 |
|
| 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 |
0.403 |
|
| 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 |
0.344 |
|
| 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 |
0.76 |
|
| 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 |
0.751 |
|
| 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 |
0.406 |
|
| 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 |
0.776 |
|
| 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 |
0.423 |
|
| 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 |
0.635 |
|
| 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 |
0.763 |
|
| 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 |
0.353 |
|
| 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 |
0.579 |
|
| 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 |
0.609 |
|
| 2002 |
Albanèse V, Frydman J. Where chaperones and nascent polypeptides meet. Nature Structural Biology. 9: 716-8. PMID 12352951 DOI: 10.1038/Nsb1002-716 |
0.347 |
|
| 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 |
0.462 |
|
| 2001 |
Frydman J. Folding of newly translated proteins in vivo: The role of molecular chaperones Annual Review of Biochemistry. 70: 603-648. PMID 11395418 DOI: 10.1146/Annurev.Biochem.70.1.603 |
0.479 |
|
| 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 |
0.442 |
|
| 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 DOI: 10.1385/1-59259-061-6:161 |
0.353 |
|
| 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 |
0.374 |
|
| 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 |
0.775 |
|
| 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 DOI: 10.1016/S1097-2765(00)80233-6 |
0.762 |
|
| 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 |
0.434 |
|
| 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 |
0.471 |
|
| 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 |
0.543 |
|
| 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 |
0.389 |
|
| 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 DOI: 10.1126/Science.272.5267.1497 |
0.635 |
|
| 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 |
0.526 |
|
| 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 |
0.592 |
|
| 1994 |
Frydman J, Hartl F. 10 Molecular Chaperone Functions of hsp70 and hsp60 in Protein Folding Cold Spring Harbor Monograph Archive. 26: 251-283. DOI: 10.1101/087969427.26.251 |
0.464 |
|
| 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 DOI: 10.1002/J.1460-2075.1992.Tb05582.X |
0.638 |
|
| 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 DOI: 10.1073/Pnas.89.11.4986 |
0.54 |
|
| 1992 |
Frydman J, Nimmesgern E, Erdjument-Bromage H, Wall J, Tempst P, Hartl F. Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits. The Embo Journal. 11: 4767-4778. DOI: 10.1002/j.1460-2075.1992.tb05582.x |
0.304 |
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