| Year |
Citation |
Score |
| 2022 |
Hallacli E, Kayatekin C, Nazeen S, Wang XH, Sheinkopf Z, Sathyakumar S, Sarkar S, Jiang X, Dong X, Di Maio R, Wang W, Keeney MT, Felsky D, Sandoe J, Vahdatshoar A, ... ... Lindquist S, et al. The Parkinson's disease protein alpha-synuclein is a modulator of processing bodies and mRNA stability. Cell. 185: 2035-2056.e33. PMID 35688132 DOI: 10.1016/j.cell.2022.05.008 |
0.769 |
|
| 2021 |
Sienski G, Narayan P, Bonner JM, Kory N, Boland S, Arczewska AA, Ralvenius WT, Akay L, Lockshin E, He L, Milo B, Graziosi A, Baru V, Lewis CA, Kellis M, ... ... Lindquist S, et al. disrupts intracellular lipid homeostasis in human iPSC-derived glia. Science Translational Medicine. 13. PMID 33658354 DOI: 10.1126/scitranslmed.aaz4564 |
0.762 |
|
| 2020 |
Narayan P, Sienski G, Bonner JM, Lin YT, Seo J, Baru V, Haque A, Milo B, Akay LA, Graziosi A, Freyzon Y, Landgraf D, Hesse WR, Valastyan J, Barrasa MI, ... ... Lindquist S, et al. PICALM Rescues Endocytic Defects Caused by the Alzheimer's Disease Risk Factor APOE4. Cell Reports. 33: 108224. PMID 33027662 DOI: 10.1016/j.celrep.2020.108224 |
0.721 |
|
| 2020 |
Tsvetkov P, Eisen TJ, Heinrich SU, Brune Z, Hallacli E, Newby GA, Kayatekin C, Pincus D, Lindquist S. Persistent Activation of mRNA Translation by Transient Hsp90 Inhibition. Cell Reports. 32: 108001. PMID 32783929 DOI: 10.1016/J.Celrep.2020.108001 |
0.404 |
|
| 2020 |
Gaglia G, Rashid R, Yapp C, Joshi GN, Li CG, Lindquist SL, Sarosiek KA, Whitesell L, Sorger PK, Santagata S. HSF1 phase transition mediates stress adaptation and cell fate decisions. Nature Cell Biology. PMID 32015439 DOI: 10.1038/S41556-019-0458-3 |
0.3 |
|
| 2019 |
Whitesell L, Robbins N, Huang DS, McLellan CA, Shekhar-Guturja T, LeBlanc EV, Nation CS, Hui R, Hutchinson A, Collins C, Chatterjee S, Trilles R, Xie JL, Krysan DJ, Lindquist S, et al. Structural basis for species-selective targeting of Hsp90 in a pathogenic fungus. Nature Communications. 10: 402. PMID 30679438 DOI: 10.1038/s41467-018-08248-w |
0.746 |
|
| 2018 |
Fanning S, Haque A, Imberdis T, Baru V, Barrasa MI, Nuber S, Termine D, Ramalingam N, Ho GPH, Noble T, Sandoe J, Lou Y, Landgraf D, Freyzon Y, Newby G, ... ... Lindquist S, et al. Lipidomic Analysis of α-Synuclein Neurotoxicity Identifies Stearoyl CoA Desaturase as a Target for Parkinson Treatment. Molecular Cell. PMID 30527540 DOI: 10.1016/J.Molcel.2018.11.028 |
0.656 |
|
| 2018 |
Pedley AM, Karras GI, Zhang X, Lindquist SL, Benkovic SJ. The Role of HSP90 in the Regulation of de novo Purine Biosynthesis. Biochemistry. PMID 29553718 DOI: 10.1021/Acs.Biochem.8B00140 |
0.802 |
|
| 2018 |
Kritzer JA, Freyzon Y, Lindquist S. Yeast can accommodate phosphotyrosine: v-Src toxicity in yeast arises from a single disrupted pathway. Fems Yeast Research. PMID 29546391 DOI: 10.1093/Femsyr/Foy027 |
0.674 |
|
| 2018 |
Kayatekin C, Amasino A, Gaglia G, Flannick J, Bonner JM, Fanning S, Narayan P, Barrasa MI, Pincus D, Landgraf D, Nelson J, Hesse WR, Costanzo M, Myers CL, ... ... Lindquist S, et al. Translocon Declogger Ste24 Protects against IAPP Oligomer-Induced Proteotoxicity. Cell. PMID 29526462 DOI: 10.1016/J.Cell.2018.02.026 |
0.731 |
|
| 2017 |
Caraveo G, Soste M, Cappelleti V, Fanning S, van Rossum DB, Whitesell L, Huang Y, Chung CY, Baru V, Zaichick S, Picotti P, Lindquist S. FKBP12 contributes to α-synuclein toxicity by regulating the calcineurin-dependent phosphoproteome. Proceedings of the National Academy of Sciences of the United States of America. PMID 29229832 DOI: 10.1073/pnas.1711926115 |
0.56 |
|
| 2017 |
Newby GA, Lindquist S. Pioneer cells established by the [SWI+] prion can promote dispersal and out-crossing in yeast. Plos Biology. 15: e2003476. PMID 29135981 DOI: 10.1371/journal.pbio.2003476 |
0.32 |
|
| 2017 |
Newby GA, Kiriakov S, Hallacli E, Kayatekin C, Tsvetkov P, Mancuso CP, Bonner JM, Hesse WR, Chakrabortee S, Manogaran AL, Liebman SW, Lindquist S, Khalil AS. A Genetic Tool to Track Protein Aggregates and Control Prion Inheritance. Cell. PMID 29056345 DOI: 10.1016/J.Cell.2017.09.041 |
0.421 |
|
| 2017 |
Dettmer U, Ramalingam N, von Saucken VE, Kim TE, Newman AJ, Terry-Kantor E, Nuber S, Ericsson M, Fanning S, Bartels T, Lindquist S, Levy OA, Selkoe D. Loss of native α-synuclein multimerization by strategically mutating its amphipathic helix causes abnormal vesicle interactions in neuronal cells. Human Molecular Genetics. 26: 3466-3481. PMID 28911198 DOI: 10.1093/hmg/ddx227 |
0.328 |
|
| 2017 |
Silvers R, Colvin MT, Frederick KK, Jacavone AC, Lindquist SL, Linse S, Griffin RG. Aggregation and Fibril Structure of AβM01-42 and Aβ1-42. Biochemistry. PMID 28792214 DOI: 10.1021/Acs.Biochem.7B00729 |
0.334 |
|
| 2017 |
Tardiff DF, Brown LE, Yan X, Trilles R, Jui NT, Barrasa MI, Caldwell KA, Caldwell GA, Schaus SE, Lindquist S. Dihydropyrimidine-thiones and clioquinol synergize to target β-amyloid cellular pathologies through a metal-dependent mechanism. Acs Chemical Neuroscience. PMID 28628299 DOI: 10.1021/Acschemneuro.7B00187 |
0.325 |
|
| 2017 |
Frederick KK, Michaelis VK, Caporini MA, Andreas LB, Debelouchina GT, Griffin RG, Lindquist S. Combining DNP NMR with segmental and specific labeling to study a yeast prion protein strain that is not parallel in-register. Proceedings of the National Academy of Sciences of the United States of America. PMID 28330994 DOI: 10.1073/Pnas.1619051114 |
0.347 |
|
| 2017 |
Karras GI, Yi S, Sahni N, Fischer M, Xie J, Vidal M, D'Andrea AD, Whitesell L, Lindquist S. HSP90 Shapes the Consequences of Human Genetic Variation. Cell. PMID 28215707 DOI: 10.1016/J.Cell.2017.01.023 |
0.811 |
|
| 2017 |
Chung CY, Khurana V, Yi S, Sahni N, Loh KH, Auluck PK, Baru V, Udeshi ND, Freyzon Y, Carr SA, Hill DE, Vidal M, Ting AY, Lindquist S. In Situ Peroxidase Labeling and Mass-Spectrometry Connects Alpha-Synuclein Directly to Endocytic Trafficking and mRNA Metabolism in Neurons. Cell Systems. PMID 28131823 DOI: 10.1016/J.Cels.2017.01.002 |
0.806 |
|
| 2017 |
Khurana V, Peng J, Chung CY, Auluck PK, Fanning S, Tardiff DF, Bartels T, Koeva M, Eichhorn SW, Benyamini H, Lou Y, Nutter-Upham A, Baru V, Freyzon Y, Tuncbag N, ... ... Lindquist S, et al. Genome-Scale Networks Link Neurodegenerative Disease Genes to α-Synuclein through Specific Molecular Pathways. Cell Systems. PMID 28131822 DOI: 10.1016/J.Cels.2016.12.011 |
0.797 |
|
| 2016 |
Tsvetkov P, Sokol E, Jin D, Brune Z, Thiru P, Ghandi M, Garraway LA, Gupta PB, Santagata S, Whitesell L, Lindquist S. Suppression of 19S proteasome subunits marks emergence of an altered cell state in diverse cancers. Proceedings of the National Academy of Sciences of the United States of America. PMID 28028240 DOI: 10.1073/Pnas.1619067114 |
0.311 |
|
| 2016 |
Landgraf D, Huh D, Hallacli E, Lindquist S. Scarless Gene Tagging with One-Step Transformation and Two-Step Selection in Saccharomyces cerevisiae and Schizosaccharomyces pombe. Plos One. 11: e0163950. PMID 27736907 DOI: 10.1371/Journal.Pone.0163950 |
0.326 |
|
| 2016 |
Chakrabortee S, Byers JS, Jones S, Garcia DM, Bhullar B, Chang A, She R, Lee L, Fremin B, Lindquist S, Jarosz DF. Intrinsically Disordered Proteins Drive Emergence and Inheritance of Biological Traits. Cell. PMID 27693355 DOI: 10.1016/J.Cell.2016.09.017 |
0.81 |
|
| 2016 |
Chakrabortee S, Kayatekin C, Newby GA, Mendillo ML, Lancaster A, Lindquist S. Luminidependens (LD) is an Arabidopsis protein with prion behavior. Proceedings of the National Academy of Sciences of the United States of America. PMID 27114519 DOI: 10.1073/Pnas.1604478113 |
0.407 |
|
| 2016 |
Zhong Q, Pevzner SJ, Hao T, Wang Y, Mosca R, Menche J, Taipale M, Taşan M, Fan C, Yang X, Haley P, Murray RR, Mer F, Gebreab F, Tam S, ... ... Lindquist S, et al. An inter-species protein-protein interaction network across vast evolutionary distance. Molecular Systems Biology. 12: 865. PMID 27107014 DOI: 10.15252/Msb.20156484 |
0.301 |
|
| 2015 |
Frederick KK, Michaelis VK, Corzilius B, Ong TC, Jacavone AC, Griffin RG, Lindquist S. Sensitivity-Enhanced NMR Reveals Alterations in Protein Structure by Cellular Milieus. Cell. 163: 620-8. PMID 26456111 DOI: 10.1016/J.Cell.2015.09.024 |
0.369 |
|
| 2015 |
Tsvetkov P, Mendillo ML, Zhao J, Carette JE, Merrill PH, Cikes D, Varadarajan M, van Diemen FR, Penninger JM, Goldberg AL, Brummelkamp TR, Santagata S, Lindquist S. Compromising the 19S proteasome complex protects cells from reduced flux through the proteasome. Elife. 4. PMID 26327695 DOI: 10.7554/Elife.08467 |
0.391 |
|
| 2015 |
Khurana V, Tardiff DF, Chung CY, Lindquist S. Toward stem cell-based phenotypic screens for neurodegenerative diseases. Nature Reviews. Neurology. 11: 339-50. PMID 25986505 DOI: 10.1038/Nrneurol.2015.79 |
0.67 |
|
| 2015 |
Sahni N, Yi S, Taipale M, Fuxman Bass JI, Coulombe-Huntington J, Yang F, Peng J, Weile J, Karras GI, Wang Y, Kovács IA, Kamburov A, Krykbaeva I, Lam MH, Tucker G, ... ... Lindquist S, et al. Widespread macromolecular interaction perturbations in human genetic disorders. Cell. 161: 647-60. PMID 25910212 DOI: 10.1016/J.Cell.2015.04.013 |
0.818 |
|
| 2015 |
Ishizawa J, Jacamo RO, Kojima K, Chachad D, Ruvolo V, Ruvolo P, Zang W, Tabe Y, Konopleva M, Devine W, Lindquist S, Porco JA, Whitesell L, Andreeff M. Inactivating Heat Shock Factor 1 (HSF1) in Acute Myeloid Leukemia By Pharmacological Inhibition of eIF4a: A Promising Therapeutic Approach Blood. 126: 2548-2548. DOI: 10.1182/Blood.V126.23.2548.2548 |
0.306 |
|
| 2015 |
Narayan P, Ehsani S, Lindquist S. Corrigendum: Combating neurodegenerative disease with chemical probes and model systems Nature Chemical Biology. 11: 172-172. DOI: 10.1038/Nchembio0215-172C |
0.701 |
|
| 2014 |
Whitesell L, Santagata S, Mendillo ML, Lin NU, Proia DA, Lindquist S. HSP90 empowers evolution of resistance to hormonal therapy in human breast cancer models. Proceedings of the National Academy of Sciences of the United States of America. 111: 18297-302. PMID 25489079 DOI: 10.1073/Pnas.1421323111 |
0.317 |
|
| 2014 |
Reymer A, Frederick KK, Rocha S, Beke-Somfai T, Kitts CC, Lindquist S, Nordén B. Orientation of aromatic residues in amyloid cores: structural insights into prion fiber diversity. Proceedings of the National Academy of Sciences of the United States of America. 111: 17158-63. PMID 25404291 DOI: 10.1073/Pnas.1415663111 |
0.344 |
|
| 2014 |
Narayan P, Ehsani S, Lindquist S. Combating neurodegenerative disease with chemical probes and model systems. Nature Chemical Biology. 10: 911-20. PMID 25325702 DOI: 10.1038/Nchembio.1663 |
0.751 |
|
| 2014 |
Jarosz DF, Brown JC, Walker GA, Datta MS, Ung WL, Lancaster AK, Rotem A, Chang A, Newby GA, Weitz DA, Bisson LF, Lindquist S. Cross-kingdom chemical communication drives a heritable, mutually beneficial prion-based transformation of metabolism. Cell. 158: 1083-93. PMID 25171409 DOI: 10.1016/J.Cell.2014.07.025 |
0.657 |
|
| 2014 |
Jarosz DF, Lancaster AK, Brown JC, Lindquist S. An evolutionarily conserved prion-like element converts wild fungi from metabolic specialists to generalists. Cell. 158: 1072-82. PMID 25171408 DOI: 10.1016/J.Cell.2014.07.024 |
0.673 |
|
| 2014 |
Tardiff DF, Khurana V, Chung CY, Lindquist S. From yeast to patient neurons and back again: powerful new discovery platform. Movement Disorders : Official Journal of the Movement Disorder Society. 29: 1231-40. PMID 25131316 DOI: 10.1002/Mds.25989 |
0.706 |
|
| 2014 |
Caraveo G, Auluck PK, Whitesell L, Chung CY, Baru V, Mosharov EV, Yan X, Ben-Johny M, Soste M, Picotti P, Kim H, Caldwell KA, Caldwell GA, Sulzer D, Yue DT, ... Lindquist S, et al. Calcineurin determines toxic versus beneficial responses to α-synuclein. Proceedings of the National Academy of Sciences of the United States of America. 111: E3544-52. PMID 25122673 DOI: 10.1073/Pnas.1413201111 |
0.758 |
|
| 2014 |
Kayatekin C, Matlack KE, Hesse WR, Guan Y, Chakrabortee S, Russ J, Wanker EE, Shah JV, Lindquist S. Prion-like proteins sequester and suppress the toxicity of huntingtin exon 1. Proceedings of the National Academy of Sciences of the United States of America. 111: 12085-90. PMID 25092318 DOI: 10.1073/Pnas.1412504111 |
0.463 |
|
| 2014 |
Taipale M, Tucker G, Peng J, Krykbaeva I, Lin ZY, Larsen B, Choi H, Berger B, Gingras AC, Lindquist S. A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways. Cell. 158: 434-48. PMID 25036637 DOI: 10.1016/J.Cell.2014.05.039 |
0.416 |
|
| 2014 |
Shalgi R, Hurt JA, Lindquist S, Burge CB. Widespread inhibition of posttranscriptional splicing shapes the cellular transcriptome following heat shock. Cell Reports. 7: 1362-70. PMID 24857664 DOI: 10.1016/J.Celrep.2014.04.044 |
0.349 |
|
| 2014 |
Lancaster AK, Nutter-Upham A, Lindquist S, King OD. PLAAC: a web and command-line application to identify proteins with prion-like amino acid composition. Bioinformatics (Oxford, England). 30: 2501-2. PMID 24825614 DOI: 10.1093/Bioinformatics/Btu310 |
0.319 |
|
| 2014 |
Petschnigg J, Groisman B, Kotlyar M, Taipale M, Zheng Y, Kurat CF, Sayad A, Sierra JR, Mattiazzi Usaj M, Snider J, Nachman A, Krykbaeva I, Tsao MS, Moffat J, Pawson T, ... Lindquist S, et al. The mammalian-membrane two-hybrid assay (MaMTH) for probing membrane-protein interactions in human cells. Nature Methods. 11: 585-92. PMID 24658140 DOI: 10.1038/Nmeth.2895 |
0.329 |
|
| 2014 |
Wijeratne EM, Xu YM, Scherz-Shouval R, Marron MT, Rocha DD, Liu MX, Costa-Lotufo LV, Santagata S, Lindquist S, Whitesell L, Gunatilaka AA. Structure-activity relationships for withanolides as inducers of the cellular heat-shock response. Journal of Medicinal Chemistry. 57: 2851-63. PMID 24625088 DOI: 10.1021/Jm401279N |
0.328 |
|
| 2014 |
Matlack KE, Tardiff DF, Narayan P, Hamamichi S, Caldwell KA, Caldwell GA, Lindquist S. Clioquinol promotes the degradation of metal-dependent amyloid-β (Aβ) oligomers to restore endocytosis and ameliorate Aβ toxicity. Proceedings of the National Academy of Sciences of the United States of America. 111: 4013-8. PMID 24591589 DOI: 10.1073/Pnas.1402228111 |
0.737 |
|
| 2014 |
Valastyan JS, Termine DJ, Lindquist S. Splice isoform and pharmacological studies reveal that sterol depletion relocalizes α-synuclein and enhances its toxicity Proceedings of the National Academy of Sciences of the United States of America. 111: 3014-3019. PMID 24516169 DOI: 10.1073/Pnas.1324209111 |
0.302 |
|
| 2014 |
Frederick KK, Debelouchina GT, Kayatekin C, Dorminy T, Jacavone AC, Griffin RG, Lindquist S. Distinct prion strains are defined by amyloid core structure and chaperone binding site dynamics. Chemistry & Biology. 21: 295-305. PMID 24485763 DOI: 10.1016/J.Chembiol.2013.12.013 |
0.353 |
|
| 2014 |
Valastyan JS, Lindquist S. Mechanisms of protein-folding diseases at a glance. Disease Models & Mechanisms. 7: 9-14. PMID 24396149 DOI: 10.1242/dmm.013474 |
0.46 |
|
| 2013 |
Rohner N, Jarosz DF, Kowalko JE, Yoshizawa M, Jeffery WR, Borowsky RL, Lindquist S, Tabin CJ. Cryptic variation in morphological evolution: HSP90 as a capacitor for loss of eyes in cavefish. Science (New York, N.Y.). 342: 1372-5. PMID 24337296 DOI: 10.1126/Science.1240276 |
0.346 |
|
| 2013 |
Lambert JP, Ivosev G, Couzens AL, Larsen B, Taipale M, Lin ZY, Zhong Q, Lindquist S, Vidal M, Aebersold R, Pawson T, Bonner R, Tate S, Gingras AC. Mapping differential interactomes by affinity purification coupled with data-independent mass spectrometry acquisition. Nature Methods. 10: 1239-45. PMID 24162924 DOI: 10.1038/Nmeth.2702 |
0.374 |
|
| 2013 |
Tardiff DF, Jui NT, Khurana V, Tambe MA, Thompson ML, Chung CY, Kamadurai HB, Kim HT, Lancaster AK, Caldwell KA, Caldwell GA, Rochet JC, Buchwald SL, Lindquist S. Yeast reveal a "druggable" Rsp5/Nedd4 network that ameliorates α-synuclein toxicity in neurons. Science (New York, N.Y.). 342: 979-83. PMID 24158909 DOI: 10.1126/Science.1245321 |
0.693 |
|
| 2013 |
Chung CY, Khurana V, Auluck PK, Tardiff DF, Mazzulli JR, Soldner F, Baru V, Lou Y, Freyzon Y, Cho S, Mungenast AE, Muffat J, Mitalipova M, Pluth MD, Jui NT, ... ... Lindquist S, et al. Identification and rescue of α-synuclein toxicity in Parkinson patient-derived neurons. Science (New York, N.Y.). 342: 983-7. PMID 24158904 DOI: 10.1126/Science.1245296 |
0.802 |
|
| 2013 |
Tardiff DF, Lindquist S. Phenotypic screens for compounds that target the cellular pathologies underlying Parkinson's disease. Drug Discovery Today. Technologies. 10: e121-8. PMID 24050240 DOI: 10.1016/J.Ddtec.2012.02.003 |
0.315 |
|
| 2013 |
Jackson WS, Borkowski AW, Watson NE, King OD, Faas H, Jasanoff A, Lindquist S. Profoundly different prion diseases in knock-in mice carrying single PrP codon substitutions associated with human diseases. Proceedings of the National Academy of Sciences of the United States of America. 110: 14759-64. PMID 23959875 DOI: 10.1073/Pnas.1312006110 |
0.714 |
|
| 2013 |
Santagata S, Mendillo ML, Tang YC, Subramanian A, Perley CC, Roche SP, Wong B, Narayan R, Kwon H, Koeva M, Amon A, Golub TR, Porco JA, Whitesell L, Lindquist S. Tight coordination of protein translation and HSF1 activation supports the anabolic malignant state. Science (New York, N.Y.). 341: 1238303. PMID 23869022 DOI: 10.1126/Science.1238303 |
0.354 |
|
| 2013 |
Holmes DL, Lancaster AK, Lindquist S, Halfmann R. Heritable remodeling of yeast multicellularity by an environmentally responsive prion. Cell. 153: 153-65. PMID 23540696 DOI: 10.1016/J.Cell.2013.02.026 |
0.754 |
|
| 2013 |
Newby GA, Lindquist S. Blessings in disguise: Biological benefits of prion-like mechanisms Trends in Cell Biology. 23: 251-259. PMID 23485338 DOI: 10.1016/j.tcb.2013.01.007 |
0.424 |
|
| 2013 |
Shalgi R, Hurt JA, Krykbaeva I, Taipale M, Lindquist S, Burge CB. Widespread Regulation of Translation by Elongation Pausing in Heat Shock Molecular Cell. 49: 439-452. PMID 23290915 DOI: 10.1016/J.Molcel.2012.11.028 |
0.365 |
|
| 2013 |
Scherz-Shouval R, Santagata S, Koeva M, Whitesell L, Lindquist S. Abstract A23: Cell autonomous and nonautonomous activities of heat shock factor 1 support tumor initiation, progression, and metastasis Cancer Research. 73. DOI: 10.1158/1538-7445.Tim2013-A23 |
0.304 |
|
| 2013 |
Scherz-Shouval R, Bagley AF, Whitesell L, Bhatia SN, Lindquist S. Abstract C132: Targeting heat shock factor 1 improves the antitumor efficiency of hyperthermia. Molecular Cancer Therapeutics. 12. DOI: 10.1158/1535-7163.Targ-13-C132 |
0.33 |
|
| 2013 |
Serebryany E, Schafheimer N, Lindquist SL, King JA. Aggregation of Trp>Glu Mutants of the Human Gamma-D Crystallin: A Model for Hereditary or UV-Induced Cataract Biophysical Journal. 104. DOI: 10.1016/J.Bpj.2012.11.307 |
0.408 |
|
| 2012 |
Muralidharan V, Oksman A, Pal P, Lindquist S, Goldberg DE. Plasmodium falciparum heat shock protein 110 stabilizes the asparagine repeat-rich parasite proteome during malarial fevers. Nature Communications. 3: 1310. PMID 23250440 DOI: 10.1038/Ncomms2306 |
0.407 |
|
| 2012 |
Taipale M, Krykbaeva I, Koeva M, Kayatekin C, Westover KD, Karras GI, Lindquist S. Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition. Cell. 150: 987-1001. PMID 22939624 DOI: 10.1016/J.Cell.2012.06.047 |
0.783 |
|
| 2012 |
Saibil HR, Seybert A, Habermann A, Winkler J, Eltsov M, Perkovic M, Castaño-Diez D, Scheffer MP, Haselmann U, Chlanda P, Lindquist S, Tyedmers J, Frangakis AS. Heritable yeast prions have a highly organized three-dimensional architecture with interfiber structures Proceedings of the National Academy of Sciences of the United States of America. 109: 14906-14911. PMID 22927413 DOI: 10.1073/Pnas.1211976109 |
0.456 |
|
| 2012 |
Mendillo ML, Santagata S, Koeva M, Bell GW, Hu R, Tamimi RM, Fraenkel E, Ince TA, Whitesell L, Lindquist S. HSF1 drives a transcriptional program distinct from heat shock to support highly malignant human cancers. Cell. 150: 549-62. PMID 22863008 DOI: 10.1016/J.Cell.2012.06.031 |
0.308 |
|
| 2012 |
Krishnan R, Goodman JL, Mukhopadhyay S, Pacheco CD, Lemke EA, Deniz AA, Lindquist S. Conserved features of intermediates in amyloid assembly determine their benign or toxic states. Proceedings of the National Academy of Sciences of the United States of America. 109: 11172-7. PMID 22745165 DOI: 10.1073/Pnas.1209527109 |
0.788 |
|
| 2012 |
McLellan CA, Whitesell L, King OD, Lancaster AK, Mazitschek R, Lindquist S. Inhibiting GPI anchor biosynthesis in fungi stresses the endoplasmic reticulum and enhances immunogenicity. Acs Chemical Biology. 7: 1520-8. PMID 22724584 DOI: 10.1021/Cb300235M |
0.343 |
|
| 2012 |
Halfmann R, Wright JR, Alberti S, Lindquist S, Rexach M. Prion formation by a yeast GLFG nucleoporin. Prion. 6: 391-9. PMID 22561191 DOI: 10.4161/pri.20199 |
0.752 |
|
| 2012 |
Treusch S, Lindquist S. An intrinsically disordered yeast prion arrests the cell cycle by sequestering a spindle pole body component Journal of Cell Biology. 197: 369-379. PMID 22529103 DOI: 10.1083/Jcb.201108146 |
0.432 |
|
| 2012 |
Halfmann R, Jarosz DF, Jones SK, Chang A, Lancaster AK, Lindquist S. Prions are a common mechanism for phenotypic inheritance in wild yeasts. Nature. 482: 363-8. PMID 22337056 DOI: 10.1038/Nature10875 |
0.804 |
|
| 2012 |
Donmez G, Arun A, Chung CY, McLean PJ, Lindquist S, Guarente L. SIRT1 protects against α-synuclein aggregation by activating molecular chaperones. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 32: 124-32. PMID 22219275 DOI: 10.1523/Jneurosci.3442-11.2012 |
0.592 |
|
| 2012 |
Tardiff DF, Tucci ML, Caldwell KA, Caldwell GA, Lindquist S. Different 8-hydroxyquinolines protect models of TDP-43 protein, α-synuclein, and polyglutamine proteotoxicity through distinct mechanisms. The Journal of Biological Chemistry. 287: 4107-20. PMID 22147697 DOI: 10.1074/Jbc.M111.308668 |
0.437 |
|
| 2012 |
Santagata S, Xu YM, Wijeratne EM, Kontnik R, Rooney C, Perley CC, Kwon H, Clardy J, Kesari S, Whitesell L, Lindquist S, Gunatilaka AA. Using the heat-shock response to discover anticancer compounds that target protein homeostasis. Acs Chemical Biology. 7: 340-9. PMID 22050377 DOI: 10.1021/Cb200353M |
0.349 |
|
| 2011 |
Treusch S, Hamamichi S, Goodman JL, Matlack KE, Chung CY, Baru V, Shulman JM, Parrado A, Bevis BJ, Valastyan JS, Han H, Lindhagen-Persson M, Reiman EM, Evans DA, Bennett DA, ... ... Lindquist S, et al. Functional links between Aβ toxicity, endocytic trafficking, and Alzheimer's disease risk factors in yeast. Science (New York, N.Y.). 334: 1241-5. PMID 22033521 DOI: 10.1126/Science.1213210 |
0.535 |
|
| 2011 |
Lindquist SL, Kelly JW. Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis. Cold Spring Harbor Perspectives in Biology. 3. PMID 21900404 DOI: 10.1101/Cshperspect.A004507 |
0.454 |
|
| 2011 |
Valastyan JS, Lindquist S. Torsina and the Torsina-Interacting protein printor have no impact on endoplasmic reticulum stress or protein trafficking in yeast Plos One. 6. PMID 21818381 DOI: 10.1371/journal.pone.0022744 |
0.463 |
|
| 2011 |
Soldner F, Laganière J, Cheng AW, Hockemeyer D, Gao Q, Alagappan R, Khurana V, Golbe LI, Myers RH, Lindquist S, Zhang L, Guschin D, Fong LK, Vu BJ, Meng X, et al. Generation of isogenic pluripotent stem cells differing exclusively at two early onset Parkinson point mutations. Cell. 146: 318-31. PMID 21757228 DOI: 10.1016/J.Cell.2011.06.019 |
0.662 |
|
| 2011 |
Halfmann R, Alberti S, Krishnan R, Lyle N, O'Donnell CW, King OD, Berger B, Pappu RV, Lindquist S. Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins. Molecular Cell. 43: 72-84. PMID 21726811 DOI: 10.1016/J.Molcel.2011.05.013 |
0.744 |
|
| 2011 |
O'Donnell CW, Waldispühl J, Lis M, Halfmann R, Devadas S, Lindquist S, Berger B. A method for probing the mutational landscape of amyloid structure Bioinformatics. 27: i34-i42. PMID 21685090 DOI: 10.1093/bioinformatics/btr238 |
0.707 |
|
| 2011 |
Manogaran AL, Hong JY, Hufana J, Tyedmers J, Lindquist S, Liebman SW. Prion formation and polyglutamine aggregation are controlled by two classes of genes Plos Genetics. 7. PMID 21625618 DOI: 10.1371/journal.pgen.1001386 |
0.41 |
|
| 2011 |
Lindquist S. A flurry of folding problems: an interview with Susan Lindquist by Jane Gitschier Plos Genetics. 7: e1002076. PMID 21589898 DOI: 10.1371/Journal.Pgen.1002076 |
0.301 |
|
| 2011 |
Ju S, Tardiff DF, Han H, Divya K, Zhong Q, Maquat LE, Bosco DA, Hayward LJ, Brown RH, Lindquist S, Ringe D, Petsko GA. A yeast model of FUS/TLS-dependent cytotoxicity. Plos Biology. 9: e1001052. PMID 21541368 DOI: 10.1371/Journal.Pbio.1001052 |
0.42 |
|
| 2011 |
Resenberger UK, Harmeier A, Woerner AC, Goodman JL, Müller V, Krishnan R, Vabulas RM, Kretzschmar HA, Lindquist S, Hartl FU, Multhaup G, Winklhofer KF, Tatzelt J. The cellular prion protein mediates neurotoxic signalling of β-sheet-rich conformers independent of prion replication. The Embo Journal. 30: 2057-70. PMID 21441896 DOI: 10.1038/emboj.2011.86 |
0.373 |
|
| 2011 |
Heinrich SU, Lindquist S. Protein-only mechanism induces self-perpetuating changes in the activity of neuronal Aplysia cytoplasmic polyadenylation element binding protein (CPEB). Proceedings of the National Academy of Sciences of the United States of America. 108: 2999-3004. PMID 21270333 DOI: 10.1073/pnas.1019368108 |
0.379 |
|
| 2011 |
Dumitriu A, Pacheco CD, Wilk JB, Strathearn KE, Latourelle JC, Goldwurm S, Pezzoli G, Rochet JC, Lindquist S, Myers RH. Cyclin-G-associated kinase modifies α-synuclein expression levels and toxicity in Parkinson's disease: results from the GenePD Study. Human Molecular Genetics. 20: 1478-87. PMID 21258085 DOI: 10.1093/Hmg/Ddr026 |
0.778 |
|
| 2011 |
Mendillo M, Santagata S, Koeva M, Fraenkel E, Ince T, Whitesell L, Lindquist S. P3-01-09: Oncogenic Activation of HSF1 Enables the Malignant Progression of Breast Carcinoma. Cancer Research. 71. DOI: 10.1158/0008-5472.Sabcs11-P3-01-09 |
0.301 |
|
| 2010 |
Jarosz DF, Lindquist S. Hsp90 and environmental stress transform the adaptive value of natural genetic variation. Science (New York, N.Y.). 330: 1820-4. PMID 21205668 DOI: 10.1126/science.1195487 |
0.696 |
|
| 2010 |
Dong J, Castro CE, Boyce MC, Lang MJ, Lindquist S. Optical trapping with high forces reveals unexpected behaviors of prion fibrils Nature Structural and Molecular Biology. 17: 1422-1430. PMID 21113168 DOI: 10.1038/Nsmb.1954 |
0.33 |
|
| 2010 |
Jarosz DF, Taipale M, Lindquist S. Protein homeostasis and the phenotypic manifestation of genetic diversity: principles and mechanisms. Annual Review of Genetics. 44: 189-216. PMID 21047258 DOI: 10.1146/annurev.genet.40.110405.090412 |
0.706 |
|
| 2010 |
Halfmann R, Lindquist S. Epigenetics in the extreme: Prions and the inheritance of environmentally acquired traits Science. 330: 629-632. PMID 21030648 DOI: 10.1126/Science.1191081 |
0.756 |
|
| 2010 |
Alberti S, Halfmann R, Lindquist S. Biochemical, cell biological, and genetic assays to analyze amyloid and prion aggregation in yeast. Methods in Enzymology. 470: 709-34. PMID 20946833 DOI: 10.1016/S0076-6879(10)70030-6 |
0.767 |
|
| 2010 |
Lewandowski NM, Ju S, Verbitsky M, Ross B, Geddie ML, Rockenstein E, Adame A, Muhammad A, Vonsattel JP, Ringe D, Cote L, Lindquist S, Masliah E, Petsko GA, Marder K, et al. Polyamine pathway contributes to the pathogenesis of Parkinson disease. Proceedings of the National Academy of Sciences of the United States of America. 107: 16970-5. PMID 20837543 DOI: 10.1073/Pnas.1011751107 |
0.358 |
|
| 2010 |
Taipale M, Jarosz DF, Lindquist S. HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nature Reviews. Molecular Cell Biology. 11: 515-28. PMID 20531426 DOI: 10.1038/nrm2918 |
0.732 |
|
| 2010 |
Auluck PK, Caraveo G, Lindquist S. α-Synuclein: membrane interactions and toxicity in Parkinson's disease. Annual Review of Cell and Developmental Biology. 26: 211-33. PMID 20500090 DOI: 10.1146/Annurev.Cellbio.042308.113313 |
0.733 |
|
| 2010 |
Garrity SJ, Sivanathan V, Dong J, Lindquist S, Hochschild A. Conversion of a yeast prion protein to an infectious form in bacteria. Proceedings of the National Academy of Sciences of the United States of America. 107: 10596-601. PMID 20484678 DOI: 10.1073/Pnas.0913280107 |
0.659 |
|
| 2010 |
Khurana V, Lindquist S. Modelling neurodegeneration in Saccharomyces cerevisiae: why cook with baker's yeast? Nature Reviews. Neuroscience. 11: 436-49. PMID 20424620 DOI: 10.1038/Nrn2809 |
0.602 |
|
| 2010 |
Tyedmers J, Treusch S, Dong J, McCaffery JM, Bevis B, Lindquist S. Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentation. Proceedings of the National Academy of Sciences of the United States of America. 107: 8633-8. PMID 20421488 DOI: 10.1073/pnas.1003895107 |
0.425 |
|
| 2010 |
Halfmann R, Alberti S, Lindquist S. Prions, protein homeostasis, and phenotypic diversity. Trends in Cell Biology. 20: 125-33. PMID 20071174 DOI: 10.1016/j.tcb.2009.12.003 |
0.768 |
|
| 2010 |
Su LJ, Auluck PK, Outeiro TF, Yeger-Lotem E, Kritzer JA, Tardiff DF, Strathearn KE, Liu F, Cao S, Hamamichi S, Hill KJ, Caldwell KA, Bell GW, Fraenkel E, Cooper AA, ... ... Lindquist S, et al. Compounds from an unbiased chemical screen reverse both ER-to-Golgi trafficking defects and mitochondrial dysfunction in Parkinson's disease models. Disease Models & Mechanisms. 3: 194-208. PMID 20038714 DOI: 10.1242/Dmm.004267 |
0.783 |
|
| 2010 |
Faas H, Jackson WS, Borkowski AW, Wang X, Ma J, Lindquist S, Jasanoff A. Context-dependent perturbation of neural systems in transgenic mice expressing a cytosolic prion protein. Neuroimage. 49: 2607-17. PMID 19835963 DOI: 10.1016/J.Neuroimage.2009.10.009 |
0.698 |
|
| 2010 |
Castro CE, Dong J, Boyce MC, Lindquist S, Lang MJ. Physical Properties of Yeast Prion Proteins Studied with Optical Tweezers Biophysical Journal. 98: 424a. DOI: 10.1016/J.Bpj.2009.12.2296 |
0.373 |
|
| 2009 |
Lindquist S. Protein folding sculpting evolutionary change Cold Spring Harbor Symposia On Quantitative Biology. 74: 103-108. PMID 20375316 DOI: 10.1101/sqb.2009.74.043 |
0.468 |
|
| 2009 |
Steele AD, Zhou Z, Jackson WS, Zhu C, Auluck P, Moskowitz MA, Chesselet MF, Lindquist S. Context dependent neuroprotective properties of prion protein (PrP). Prion. 3: 240-9. PMID 19901559 DOI: 10.4161/Pri.3.4.10135 |
0.806 |
|
| 2009 |
Brown JC, Lindquist S. A heritable switch in carbon source utilization driven by an unusual yeast prion. Genes & Development. 23: 2320-32. PMID 19797769 DOI: 10.1101/gad.1839109 |
0.395 |
|
| 2009 |
Sénéchal P, Arseneault G, Leroux A, Lindquist S, Rokeach LA. The Schizosaccharomyces pombe Hsp104 disaggregase is unable to propagate the [PSI] prion. Plos One. 4: e6939. PMID 19759825 DOI: 10.1371/journal.pone.0006939 |
0.42 |
|
| 2009 |
Jackson WS, Borkowski AW, Faas H, Steele AD, King OD, Watson N, Jasanoff A, Lindquist S. Spontaneous generation of prion infectivity in fatal familial insomnia knockin mice. Neuron. 63: 438-50. PMID 19709627 DOI: 10.1016/J.Neuron.2009.07.026 |
0.734 |
|
| 2009 |
Wacker JL, Huang SY, Steele AD, Aron R, Lotz GP, Nguyen Q, Giorgini F, Roberson ED, Lindquist S, Masliah E, Muchowski PJ. Loss of Hsp70 exacerbates pathogenesis but not levels of fibrillar aggregates in a mouse model of Huntington's disease. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 29: 9104-14. PMID 19605647 DOI: 10.1523/Jneurosci.2250-09.2009 |
0.625 |
|
| 2009 |
Kritzer JA, Hamamichi S, McCaffery JM, Santagata S, Naumann TA, Caldwell KA, Caldwell GA, Lindquist S. Rapid selection of cyclic peptides that reduce alpha-synuclein toxicity in yeast and animal models. Nature Chemical Biology. 5: 655-63. PMID 19597508 DOI: 10.1038/Nchembio.193 |
0.679 |
|
| 2009 |
Tessier PM, Lindquist S. Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI+]. Nature Structural & Molecular Biology. 16: 598-605. PMID 19491937 DOI: 10.1038/Nsmb.1617 |
0.376 |
|
| 2009 |
Treusch S, Cyr DM, Lindquist S. Amyloid deposits: protection against toxic protein species? Cell Cycle (Georgetown, Tex.). 8: 1668-74. PMID 19411847 DOI: 10.4161/Cc.8.11.8503 |
0.414 |
|
| 2009 |
Wendler P, Shorter J, Snead D, Plisson C, Clare DK, Lindquist S, Saibil HR. Motor Mechanism for Protein Threading through Hsp104 Molecular Cell. 34: 81-92. PMID 19362537 DOI: 10.1016/J.Molcel.2009.02.026 |
0.563 |
|
| 2009 |
Beauregard PB, Guérin R, Turcotte C, Lindquist S, Rokeach LA. A nucleolar protein allows viability in the absence of the essential ER-residing molecular chaperone calnexin Journal of Cell Science. 122: 1342-1351. PMID 19351719 DOI: 10.1242/jcs.040949 |
0.397 |
|
| 2009 |
Alberti S, Halfmann R, King O, Kapila A, Lindquist S. A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell. 137: 146-58. PMID 19345193 DOI: 10.1016/J.Cell.2009.02.044 |
0.768 |
|
| 2009 |
Whitesell L, Lindquist S. Inhibiting the transcription factor HSF1 as an anticancer strategy Expert Opinion On Therapeutic Targets. 13: 469-478. PMID 19335068 DOI: 10.1517/14728220902832697 |
0.339 |
|
| 2009 |
Yeger-Lotem E, Riva L, Su LJ, Gitler AD, Cashikar AG, King OD, Auluck PK, Geddie ML, Valastyan JS, Karger DR, Lindquist S, Fraenkel E. Bridging high-throughput genetic and transcriptional data reveals cellular responses to alpha-synuclein toxicity. Nature Genetics. 41: 316-23. PMID 19234470 DOI: 10.1038/Ng.337 |
0.778 |
|
| 2009 |
Cowen LE, Singh SD, Köhler JR, Collins C, Zaas AK, Schell WA, Aziz H, Mylonakis E, Perfect JR, Whitesell L, Lindquist S. Harnessing Hsp90 function as a powerful, broadly effective therapeutic strategy for fungal infectious disease Proceedings of the National Academy of Sciences of the United States of America. 106: 2818-2823. PMID 19196973 DOI: 10.1073/Pnas.0813394106 |
0.69 |
|
| 2009 |
Gitler AD, Chesi A, Geddie ML, Strathearn KE, Hamamichi S, Hill KJ, Caldwell KA, Caldwell GA, Cooper AA, Rochet JC, Lindquist S. Alpha-synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity. Nature Genetics. 41: 308-15. PMID 19182805 DOI: 10.1038/Ng.300 |
0.563 |
|
| 2009 |
Rappley I, Gitler AD, Selvy PE, LaVoie MJ, Levy BD, Brown HA, Lindquist S, Selkoe DJ. Evidence that alpha-synuclein does not inhibit phospholipase D. Biochemistry. 48: 1077-83. PMID 19146388 DOI: 10.1021/Bi801871H |
0.628 |
|
| 2008 |
Heikenwalder M, Kurrer MO, Margalith I, Kranich J, Zeller N, Haybaeck J, Polymenidou M, Matter M, Bremer J, Jackson WS, Lindquist S, Sigurdson CJ, Aguzzi A. Lymphotoxin-dependent prion replication in inflammatory stromal cells of granulomas. Immunity. 29: 998-1008. PMID 19100703 DOI: 10.1016/J.Immuni.2008.10.014 |
0.69 |
|
| 2008 |
Tyedmers J, Madariaga ML, Lindquist S. Prion switching in response to environmental stress Plos Biology. 6: 2605-2613. PMID 19067491 DOI: 10.1371/journal.pbio.0060294 |
0.323 |
|
| 2008 |
Lindquist S. Interview: Protein Folding and Studies of Neurodegenerative Diseases Journal of Visualized Experiments. 616-623. PMID 19066516 DOI: 10.3791/786 |
0.447 |
|
| 2008 |
Halfmann R, Lindquist S. Screening for amyloid aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis. Journal of Visualized Experiments : Jove. PMID 19066511 DOI: 10.3791/838 |
0.742 |
|
| 2008 |
Lindquist S. Using yeast to understand protein folding diseases: An interview with Susan Lindquist Dmm Disease Models and Mechanisms. 1: 17-19. PMID 19048046 DOI: 10.1242/dmm.000810 |
0.31 |
|
| 2008 |
Duennwald ML, Lindquist S. Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity. Genes & Development. 22: 3308-19. PMID 19015277 DOI: 10.1101/Gad.1673408 |
0.736 |
|
| 2008 |
Shorter J, Lindquist S. Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions Embo Journal. 27: 2712-2724. PMID 18833196 DOI: 10.1038/Emboj.2008.194 |
0.582 |
|
| 2008 |
Chen D, Steele AD, Hutter G, Bruno J, Govindarajan A, Easlon E, Lin SJ, Aguzzi A, Lindquist S, Guarente L. The role of calorie restriction and SIRT1 in prion-mediated neurodegeneration. Experimental Gerontology. 43: 1086-93. PMID 18799131 DOI: 10.1016/J.Exger.2008.08.050 |
0.528 |
|
| 2008 |
Steele AD, Hutter G, Jackson WS, Heppner FL, Borkowski AW, King OD, Raymond GJ, Aguzzi A, Lindquist S. Heat shock factor 1 regulates lifespan as distinct from disease onset in prion disease. Proceedings of the National Academy of Sciences of the United States of America. 105: 13626-31. PMID 18757733 DOI: 10.1073/Pnas.0806319105 |
0.753 |
|
| 2008 |
Lo Bianco C, Shorter J, Régulier E, Lashuel H, Iwatsubo T, Lindquist S, Aebischer P. Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease. The Journal of Clinical Investigation. 118: 3087-97. PMID 18704197 DOI: 10.1172/Jci35781 |
0.575 |
|
| 2008 |
Wang H, Duennwald ML, Roberts BE, Rozeboom LM, Zhang YL, Steele AD, Krishnan R, Su LJ, Griffin D, Mukhopadhyay S, Hennessy EJ, Weigele P, Blanchard BJ, King J, Deniz AA, ... ... Lindquist S, et al. Direct and selective elimination of specific prions and amyloids by 4,5-dianilinophthalimide and analogs. Proceedings of the National Academy of Sciences of the United States of America. 105: 7159-64. PMID 18480256 DOI: 10.1073/Pnas.0801934105 |
0.798 |
|
| 2008 |
Douglas PM, Treusch S, Ren HY, Halfmann R, Duennwald ML, Lindquist S, Cyr DM. Chaperone-dependent amyloid assembly protects cells from prion toxicity. Proceedings of the National Academy of Sciences of the United States of America. 105: 7206-11. PMID 18480252 DOI: 10.1073/Pnas.0802593105 |
0.829 |
|
| 2008 |
Johnson BS, McCaffery JM, Lindquist S, Gitler AD. A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity. Proceedings of the National Academy of Sciences of the United States of America. 105: 6439-44. PMID 18434538 DOI: 10.1073/Pnas.0802082105 |
0.668 |
|
| 2008 |
Fleming J, Outeiro TF, Slack M, Lindquist SL, Bulawa CE. Detection of compounds that rescue Rab1-synuclein toxicity. Methods in Enzymology. 439: 339-51. PMID 18374176 DOI: 10.1016/S0076-6879(07)00425-9 |
0.562 |
|
| 2008 |
Sadlish H, Rampelt H, Shorter J, Wegrzyn RD, Andréasson C, Lindquist S, Bukau B. Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities. Plos One. 3: e1763. PMID 18335038 DOI: 10.1371/Journal.Pone.0001763 |
0.596 |
|
| 2008 |
Sangster TA, Salathia N, Undurraga S, Milo R, Schellenberg K, Lindquist S, Queitsch C. HSP90 affects the expression of genetic variation and developmental stability in quantitative traits. Proceedings of the National Academy of Sciences of the United States of America. 105: 2963-8. PMID 18287065 DOI: 10.1073/Pnas.0712200105 |
0.794 |
|
| 2008 |
Sangster TA, Salathia N, Lee HN, Watanabe E, Schellenberg K, Morneau K, Wang H, Undurraga S, Queitsch C, Lindquist S. HSP90-buffered genetic variation is common in Arabidopsis thaliana. Proceedings of the National Academy of Sciences of the United States of America. 105: 2969-74. PMID 18287064 DOI: 10.1073/Pnas.0712210105 |
0.811 |
|
| 2008 |
Gitler AD, Bevis BJ, Shorter J, Strathearn KE, Hamamichi S, Su LJ, Caldwell KA, Caldwell GA, Rochet JC, McCaffery JM, Barlowe C, Lindquist S. The Parkinson's disease protein alpha-synuclein disrupts cellular Rab homeostasis. Proceedings of the National Academy of Sciences of the United States of America. 105: 145-50. PMID 18162536 DOI: 10.1073/Pnas.0710685105 |
0.666 |
|
| 2008 |
Halfmann R, Lindquist S. Screening for amyloid aggregation by semi-denaturing detergent-agarose gel electrophoresis Journal of Visualized Experiments. DOI: 10.3791/838 |
0.67 |
|
| 2008 |
Allendoerfer KL, Julie Su L, Lindquist S. Yeast Cells as a Discovery Platform for Parkinson's Disease and other Protein Misfolding Diseases Parkinson's Disease. 505-536. DOI: 10.1016/B978-0-12-374028-1.00038-5 |
0.797 |
|
| 2007 |
Steele AD, Hetz C, Yi CH, Jackson WS, Borkowski AW, Yuan J, Wollmann RH, Lindquist S. Prion pathogenesis is independent of caspase-12. Prion. 1: 243-7. PMID 19164919 DOI: 10.4161/Pri.1.4.5551 |
0.747 |
|
| 2007 |
Steele AD, Lindquist S, Aguzzi A. The prion protein knockout mouse: a phenotype under challenge. Prion. 1: 83-93. PMID 19164918 DOI: 10.4161/Pri.1.2.4346 |
0.551 |
|
| 2007 |
Wendler P, Shorter J, Plisson C, Cashikar AG, Lindquist S, Saibil HR. Atypical AAA+ Subunit Packing Creates an Expanded Cavity for Disaggregation by the Protein-Remodeling Factor Hsp104 Cell. 131: 1366-1377. PMID 18160044 DOI: 10.1016/J.Cell.2007.10.047 |
0.592 |
|
| 2007 |
Jackson WS, Lindquist S. Illuminating aggregate heterogeneity in neurodegenerative disease. Nature Methods. 4: 1000-1. PMID 18049468 DOI: 10.1038/Nmeth1207-1000 |
0.683 |
|
| 2007 |
Steele AD, King OD, Jackson WS, Hetz CA, Borkowski AW, Thielen P, Wollmann R, Lindquist S. Diminishing apoptosis by deletion of Bax or overexpression of Bcl-2 does not protect against infectious prion toxicity in vivo. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 27: 13022-7. PMID 18032675 DOI: 10.1523/Jneurosci.3290-07.2007 |
0.751 |
|
| 2007 |
Hess S, Lindquist SL, Scheibel T. Alternative assembly pathways of the amyloidogenic yeast prion determinant Sup35-NM. Embo Reports. 8: 1196-201. PMID 17975557 DOI: 10.1038/Sj.Embor.7401096 |
0.563 |
|
| 2007 |
Dong J, Bloom JD, Goncharov V, Chattopadhyay M, Millhauser GL, Lynn DG, Scheibel T, Lindquist S. Probing the role of PrP repeats in conformational conversion and amyloid assembly of chimeric yeast prions. The Journal of Biological Chemistry. 282: 34204-12. PMID 17893150 DOI: 10.1074/Jbc.M704952200 |
0.631 |
|
| 2007 |
Dai C, Whitesell L, Rogers AB, Lindquist S. Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis. Cell. 130: 1005-18. PMID 17889646 DOI: 10.1016/J.Cell.2007.07.020 |
0.32 |
|
| 2007 |
Sangster TA, Bahrami A, Wilczek A, Watanabe E, Schellenberg K, McLellan C, Kelley A, Kong SW, Queitsch C, Lindquist S. Phenotypic diversity and altered environmental plasticity in Arabidopsis thaliana with reduced Hsp90 levels. Plos One. 2: e648. PMID 17653275 DOI: 10.1371/Journal.Pone.0000648 |
0.804 |
|
| 2007 |
Alberti S, Gitler AD, Lindquist S. A suite of Gateway cloning vectors for high-throughput genetic analysis in Saccharomyces cerevisiae. Yeast (Chichester, England). 24: 913-9. PMID 17583893 DOI: 10.1002/Yea.1502 |
0.603 |
|
| 2007 |
Tessier PM, Lindquist S. Prion recognition elements govern nucleation, strain specificity and species barriers. Nature. 447: 556-61. PMID 17495929 DOI: 10.1038/Nature05848 |
0.306 |
|
| 2007 |
Mukhopadhyay S, Krishnan R, Lemke EA, Lindquist S, Deniz AA. A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures. Proceedings of the National Academy of Sciences of the United States of America. 104: 2649-54. PMID 17299036 DOI: 10.1073/Pnas.0611503104 |
0.346 |
|
| 2007 |
Steele AD, Jackson WS, King OD, Lindquist S. The power of automated high-resolution behavior analysis revealed by its application to mouse models of Huntington's and prion diseases. Proceedings of the National Academy of Sciences of the United States of America. 104: 1983-8. PMID 17261803 DOI: 10.1073/Pnas.0610779104 |
0.729 |
|
| 2007 |
Doyle SM, Shorter J, Zolkiewski M, Hoskins JR, Lindquist S, Wickner S. Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity Nature Structural and Molecular Biology. 14: 114-122. PMID 17259993 DOI: 10.1038/Nsmb1198 |
0.59 |
|
| 2006 |
Cowen LE, Carpenter AE, Matangkasombut O, Fink GR, Lindquist S. Genetic architecture of Hsp90-dependent drug resistance. Eukaryotic Cell. 5: 2184-8. PMID 17056742 DOI: 10.1128/Ec.00274-06 |
0.6 |
|
| 2006 |
Ehrnhoefer DE, Duennwald M, Markovic P, Wacker JL, Engemann S, Roark M, Legleiter J, Marsh JL, Thompson LM, Lindquist S, Muchowski PJ, Wanker EE. Green tea (-)-epigallocatechin-gallate modulates early events in huntingtin misfolding and reduces toxicity in Huntington's disease models. Human Molecular Genetics. 15: 2743-51. PMID 16893904 DOI: 10.1093/Hmg/Ddl210 |
0.736 |
|
| 2006 |
Shorter J, Lindquist S. Destruction or Potentiation of Different Prions Catalyzed by Similar Hsp104 Remodeling Activities Molecular Cell. 23: 425-438. PMID 16885031 DOI: 10.1016/J.Molcel.2006.05.042 |
0.625 |
|
| 2006 |
Duennwald ML, Jagadish S, Muchowski PJ, Lindquist S. Flanking sequences profoundly alter polyglutamine toxicity in yeast. Proceedings of the National Academy of Sciences of the United States of America. 103: 11045-50. PMID 16832050 DOI: 10.1073/Pnas.0604547103 |
0.807 |
|
| 2006 |
Duennwald ML, Jagadish S, Giorgini F, Muchowski PJ, Lindquist S. A network of protein interactions determines polyglutamine toxicity. Proceedings of the National Academy of Sciences of the United States of America. 103: 11051-6. PMID 16832049 DOI: 10.1073/Pnas.0604548103 |
0.817 |
|
| 2006 |
Cooper AA, Gitler AD, Cashikar A, Haynes CM, Hill KJ, Bhullar B, Liu K, Xu K, Strathearn KE, Liu F, Cao S, Caldwell KA, Caldwell GA, Marsischky G, Kolodner RD, ... ... Lindquist S, et al. Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models. Science (New York, N.Y.). 313: 324-8. PMID 16794039 DOI: 10.1126/Science.1129462 |
0.695 |
|
| 2006 |
Steele AD, Emsley JG, Ozdinler PH, Lindquist S, Macklis JD. Prion protein (PrPc) positively regulates neural precursor proliferation during developmental and adult mammalian neurogenesis. Proceedings of the National Academy of Sciences of the United States of America. 103: 3416-21. PMID 16492732 DOI: 10.1073/Pnas.0511290103 |
0.497 |
|
| 2006 |
Zhang CC, Steele AD, Lindquist S, Lodish HF. Prion protein is expressed on long-term repopulating hematopoietic stem cells and is important for their self-renewal. Proceedings of the National Academy of Sciences of the United States of America. 103: 2184-9. PMID 16467153 DOI: 10.1073/Pnas.0510577103 |
0.591 |
|
| 2005 |
Homann OR, Cai H, Becker JM, Lindquist SL. Harnessing natural diversity to probe metabolic pathways. Plos Genetics. 1: e80. PMID 16429164 DOI: 10.1371/Journal.Pgen.0010080 |
0.764 |
|
| 2005 |
Chen D, Steele AD, Lindquist S, Guarente L. Increase in activity during calorie restriction requires Sirt1. Science (New York, N.Y.). 310: 1641. PMID 16339438 DOI: 10.1126/Science.1118357 |
0.484 |
|
| 2005 |
Cowen LE, Lindquist S. Hsp90 potentiates the rapid evolution of new traits: drug resistance in diverse fungi. Science (New York, N.Y.). 309: 2185-9. PMID 16195452 DOI: 10.1126/Science.1118370 |
0.606 |
|
| 2005 |
Whitesell L, Lindquist SL. HSP90 and the chaperoning of cancer. Nature Reviews. Cancer. 5: 761-72. PMID 16175177 DOI: 10.1038/nrc1716 |
0.426 |
|
| 2005 |
Krishnan R, Lindquist SL. Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature. 435: 765-72. PMID 15944694 DOI: 10.1038/nature03679 |
0.4 |
|
| 2005 |
Shorter J, Lindquist S. Prions as adaptive conduits of memory and inheritance Nature Reviews Genetics. 6: 435-450. PMID 15931169 DOI: 10.1038/Nrg1616 |
0.544 |
|
| 2005 |
Cashikar AG, Duennwald M, Lindquist SL. A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104. The Journal of Biological Chemistry. 280: 23869-75. PMID 15845535 DOI: 10.1074/Jbc.M502854200 |
0.75 |
|
| 2005 |
Shorter J, Lindquist S. Navigating the CIpB channel to solution Nature Structural and Molecular Biology. 12: 4-6. PMID 15689967 DOI: 10.1038/Nsmb0105-4 |
0.566 |
|
| 2004 |
Colby DW, Chu Y, Cassady JP, Duennwald M, Zazulak H, Webster JM, Messer A, Lindquist S, Ingram VM, Wittrup KD. Potent inhibition of huntingtin aggregation and cytotoxicity by a disulfide bond-free single-domain intracellular antibody. Proceedings of the National Academy of Sciences of the United States of America. 101: 17616-21. PMID 15598740 DOI: 10.1073/Pnas.0408134101 |
0.711 |
|
| 2004 |
Derkatch IL, Uptain SM, Outeiro TF, Krishnan R, Lindquist SL, Liebman SW. Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro. Proceedings of the National Academy of Sciences of the United States of America. 101: 12934-9. PMID 15326312 DOI: 10.1073/Pnas.0404968101 |
0.591 |
|
| 2004 |
True HL, Berlin I, Lindquist SL. Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits. Nature. 431: 184-7. PMID 15311209 DOI: 10.1038/Nature02885 |
0.351 |
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| 2004 |
Shorter J, Lindquist S. Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers Science. 304: 1793-1797. PMID 15155912 DOI: 10.1126/Science.1098007 |
0.589 |
|
| 2004 |
Rochet JC, Outeiro TF, Conway KA, Ding TT, Volles MJ, Lashuel HA, Bieganski RM, Lindquist SL, Lansbury PT. Interactions among alpha-synuclein, dopamine, and biomembranes: some clues for understanding neurodegeneration in Parkinson's disease. Journal of Molecular Neuroscience : Mn. 23: 23-34. PMID 15126689 DOI: 10.1385/Jmn:23:1-2:023 |
0.522 |
|
| 2004 |
Sangster TA, Lindquist S, Queitsch C. Under cover: causes, effects and implications of Hsp90-mediated genetic capacitance. Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology. 26: 348-62. PMID 15057933 DOI: 10.1002/Bies.20020 |
0.821 |
|
| 2004 |
Scheibel T, Bloom J, Lindquist SL. The elongation of yeast prion fibers involves separable steps of association and conversion. Proceedings of the National Academy of Sciences of the United States of America. 101: 2287-92. PMID 14983002 DOI: 10.1073/Pnas.0308754101 |
0.563 |
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| 2004 |
Schirmer EC, Homann OR, Kowal AS, Lindquist S. Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region. Molecular Biology of the Cell. 15: 2061-72. PMID 14978213 DOI: 10.1091/Mbc.E02-08-0502 |
0.81 |
|
| 2003 |
Si K, Lindquist S, Kandel ER. A neuronal isoform of the aplysia CPEB has prion-like properties. Cell. 115: 879-91. PMID 14697205 DOI: 10.1016/S0092-8674(03)01020-1 |
0.397 |
|
| 2003 |
Outeiro TF, Lindquist S. Yeast cells provide insight into alpha-synuclein biology and pathobiology. Science (New York, N.Y.). 302: 1772-5. PMID 14657500 DOI: 10.1126/Science.1090439 |
0.52 |
|
| 2003 |
Willingham S, Outeiro TF, DeVit MJ, Lindquist SL, Muchowski PJ. Yeast genes that enhance the toxicity of a mutant huntingtin fragment or alpha-synuclein. Science (New York, N.Y.). 302: 1769-72. PMID 14657499 DOI: 10.1126/Science.1090389 |
0.548 |
|
| 2003 |
Resende CG, Outeiro TF, Sands L, Lindquist S, Tuite MF. Prion protein gene polymorphisms in Saccharomyces cerevisiae. Molecular Microbiology. 49: 1005-17. PMID 12890024 DOI: 10.1046/j.1365-2958.2003.03608.x |
0.488 |
|
| 2003 |
Sangster TA, Queitsch C, Lindquist S. Hsp90 and chromatin: where is the link? Cell Cycle (Georgetown, Tex.). 2: 166-8. PMID 12734413 |
0.784 |
|
| 2003 |
Scheibel T, Parthasarathy R, Sawicki G, Lin XM, Jaeger H, Lindquist SL. Conducting nanowires built by controlled self-assembly of amyloid fibers and selective metal deposition. Proceedings of the National Academy of Sciences of the United States of America. 100: 4527-32. PMID 12672964 DOI: 10.1073/Pnas.0431081100 |
0.545 |
|
| 2003 |
Sangster TA, Queitsch C, Lindquist S. Hsp90 and chromatin: where is the link? Cell Cycle. 2: 165-167. DOI: 10.4161/Cc.2.3.400 |
0.784 |
|
| 2002 |
Lindquist SL, Henikoff S. Self-perpetuating structural states in biology, disease, and genetics. Proceedings of the National Academy of Sciences of the United States of America. 99: 16377. PMID 12475994 DOI: 10.1073/pnas.212504699 |
0.599 |
|
| 2002 |
Liu JJ, Sondheimer N, Lindquist SL. Changes in the middle region of Sup35 profoundly alter the nature of epigenetic inheritance for the yeast prion [PSI+]. Proceedings of the National Academy of Sciences of the United States of America. 99: 16446-53. PMID 12461168 DOI: 10.1073/Pnas.252652099 |
0.739 |
|
| 2002 |
Ma J, Wollmann R, Lindquist S. Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science. 298: 1781-1785. PMID 12386337 DOI: 10.1126/Science.1073725 |
0.378 |
|
| 2002 |
Ma J, Lindquist S. Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol. Science. 298: 1785-1788. PMID 12386336 DOI: 10.1126/Science.1073619 |
0.35 |
|
| 2002 |
Uptain SM, Lindquist S. Prions as protein-based genetic elements. Annual Review of Microbiology. 56: 703-41. PMID 12142498 DOI: 10.1146/ANNUREV.MICRO.56.013002.100603 |
0.438 |
|
| 2002 |
Chernoff YO, Uptain SM, Lindquist SL. Analysis of prion factors in yeast. Methods in Enzymology. 351: 499-538. PMID 12073366 DOI: 10.1016/S0076-6879(02)51867-X |
0.406 |
|
| 2002 |
Queitsch C, Sangster TA, Lindquist S. Hsp90 as a capacitor of phenotypic variation. Nature. 417: 618-24. PMID 12050657 DOI: 10.1038/Nature749 |
0.806 |
|
| 2002 |
Cashikar AG, Schirmer EC, Hattendorf DA, Glover JR, Ramakrishnan MS, Ware DM, Lindquist SL. Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein. Molecular Cell. 9: 751-60. PMID 11983167 DOI: 10.1016/S1097-2765(02)00499-9 |
0.784 |
|
| 2002 |
Hattendorf DA, Lindquist SL. Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding. Proceedings of the National Academy of Sciences of the United States of America. 99: 2732-7. PMID 11867765 DOI: 10.1073/Pnas.261693199 |
0.783 |
|
| 2002 |
Hattendorf DA, Lindquist SL. Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants. The Embo Journal. 21: 12-21. PMID 11782421 DOI: 10.1093/emboj/21.1.12 |
0.795 |
|
| 2001 |
Serio TR, Lindquist SL. The yeast prion [PSI+]: molecular insights and functional consequences. Advances in Protein Chemistry. 59: 391-412. PMID 11868278 DOI: 10.1016/S0065-3233(01)59012-9 |
0.747 |
|
| 2001 |
Clos J, Klaholz L, Kroemer M, Krobitsch S, Lindquist S. Heat shock protein 100 and the amastigote stage-specific A2 proteins of Leishmania donovani Medical Microbiology and Immunology. 190: 47-50. PMID 11770109 DOI: 10.1007/S004300100078 |
0.412 |
|
| 2001 |
Ma J, Lindquist S. Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation Proceedings of the National Academy of Sciences of the United States of America. 98: 14955-14960. PMID 11742063 DOI: 10.1073/Pnas.011578098 |
0.388 |
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| 2001 |
Uptain SM, Sawicki GJ, Caughey B, Lindquist S. Strains of [PSI(+)] are distinguished by their efficiencies of prion-mediated conformational conversion. The Embo Journal. 20: 6236-45. PMID 11707395 DOI: 10.1093/emboj/20.22.6236 |
0.388 |
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| 2001 |
Scheibel T, Lindquist SL. The role of conformational flexibility in prion propagation and maintenance for Sup35p. Nature Structural Biology. 8: 958-62. PMID 11685242 DOI: 10.1038/Nsb1101-958 |
0.578 |
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| 2001 |
Serio TR, Cashikar AG, Kowal AS, Sawicki GJ, Lindquist SL. Self-perpetuating changes in Sup35 protein conformation as a mechanism of heredity in yeast. Biochemical Society Symposium. 35-43. PMID 11573346 DOI: 10.1042/Bst028A050C |
0.743 |
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| 2001 |
Serio TR, Lindquist SL. [PSI+], SUP35, and chaperones. Advances in Protein Chemistry. 57: 335-66. PMID 11447696 DOI: 10.1016/S0065-3233(01)57027-8 |
0.757 |
|
| 2001 |
Sondheimer N, Lopez N, Craig EA, Lindquist S. The role of Sis1 in the maintenance of the [RNQ+] prion Embo Journal. 20: 2435-2442. PMID 11350932 DOI: 10.1093/Emboj/20.10.2435 |
0.681 |
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| 2001 |
Scheibel T, Kowal AS, Bloom JD, Lindquist SL. Bidirectional amyloid fiber growth for a yeast prion determinant. Current Biology : Cb. 11: 366-9. PMID 11267875 DOI: 10.1016/S0960-9822(01)00099-9 |
0.563 |
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| 2001 |
Lindquist S, Krobitsch S, Li L, Sondheimer N, Peto H, Dobson CM, Perutz MF, Pepys M, Goldberg ME. Investigating protein conformation-based inheritance and disease in yeast Philosophical Transactions of the Royal Society B: Biological Sciences. 356: 169-176. PMID 11260797 DOI: 10.1098/Rstb.2000.0762 |
0.717 |
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| 2001 |
Schirmer EC, Ware DM, Queitsch C, Kowal AS, Lindquist SL. Subunit interactions influence the biochemical and biological properties of Hsp104. Proceedings of the National Academy of Sciences of the United States of America. 98: 914-9. PMID 11158570 DOI: 10.1073/Pnas.98.3.914 |
0.77 |
|
| 2000 |
Lindquist S. But yeast prion offers clues about evolution. Nature. 408: 17-18. PMID 11081485 DOI: 10.1038/35040758 |
0.342 |
|
| 2000 |
True HL, Lindquist SL. A yeast prion provides a mechanism for genetic variation and phenotypic diversity. Nature. 407: 477-83. PMID 11028992 DOI: 10.1038/35035005 |
0.343 |
|
| 2000 |
Serio TR, Cashikar AG, Kowal AS, Sawicki GJ, Moslehi JJ, Serpell L, Arnsdorf MF, Lindquist SL. Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science (New York, N.Y.). 289: 1317-21. PMID 10958771 DOI: 10.1126/Science.289.5483.1317 |
0.745 |
|
| 2000 |
Satyal SH, Schmidt E, Kitagawa K, Sondheimer N, Lindquist S, Kramer JM, Morimoto RI. Polyglutamine aggregates alter protein folding homeostasis in Caenorhabditis elegans. Proceedings of the National Academy of Sciences of the United States of America. 97: 5750-5. PMID 10811890 DOI: 10.1073/Pnas.100107297 |
0.77 |
|
| 2000 |
Queitsch C, Hong SW, Vierling E, Lindquist S. Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis. The Plant Cell. 12: 479-92. PMID 10760238 DOI: 10.1105/Tpc.12.4.479 |
0.665 |
|
| 2000 |
Sondheimer N, Lindquist S. Rnq1: An Epigenetic Modifier of Protein Function in Yeast Molecular Cell. 5: 163-172. PMID 10678178 DOI: 10.1016/S1097-2765(00)80412-8 |
0.706 |
|
| 2000 |
Krobitsch S, Lindquist S. Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins Proceedings of the National Academy of Sciences of the United States of America. 97: 1589-1594. PMID 10677504 DOI: 10.1073/Pnas.97.4.1589 |
0.377 |
|
| 2000 |
Serio TR, Lindquist SL. Protein-only inheritance in yeast: something to get [PSI+]-ched about. Trends in Cell Biology. 10: 98-105. PMID 10675903 DOI: 10.1016/S0962-8924(99)01711-0 |
0.761 |
|
| 2000 |
Li L, Lindquist S. Creating a Protein-Based Element of Inheritance Science. 287: 661-664. PMID 10650001 DOI: 10.1126/Science.287.5453.661 |
0.416 |
|
| 2000 |
Lindquist SL, Krobitsch S, Li L, Sondheimer N, True H. New Mechanisms of Inheritance Based on Self-perpetuating Changes in Protein Conformation Biochemical Society Transactions. 28. DOI: 10.1042/Bst028A137A |
0.648 |
|
| 2000 |
Kowal AS, Scheibel T, Lindquist SL. Observation of Amyloid-Like Fibers of the Sup35 Protein from Saccharomyces Cerevisiae Microscopy and Microanalysis. 6: 664-665. DOI: 10.1017/S1431927600035819 |
0.545 |
|
| 2000 |
Lindquist S, Liu J. Expanding the prion model for the yeast [PSI+] element: Response Trends in Microbiology. 8: 3. DOI: 10.1016/S0966-842X(99)01652-2 |
0.613 |
|
| 1999 |
Serio TR, Lindquist SL. [PSI+]: an epigenetic modulator of translation termination efficiency. Annual Review of Cell and Developmental Biology. 15: 661-703. PMID 10611975 DOI: 10.1146/Annurev.Cellbio.15.1.661 |
0.748 |
|
| 1999 |
Scheibel T, Weikl T, Rimerman R, Smith D, Lindquist S, Buchner J. Contribution of N- and C-terminal domains to the function of Hsp90 in Saccharomyces cerevisiae. Molecular Microbiology. 34: 701-13. PMID 10564510 DOI: 10.1046/J.1365-2958.1999.01632.X |
0.681 |
|
| 1999 |
Serio TR, Cashikar AG, Moslehi JJ, Kowal AS, Lindquist SL. Yeast prion [psi +] and its determinant, Sup35p. Methods in Enzymology. 309: 649-73. PMID 10507053 DOI: 10.1016/S0076-6879(99)09043-6 |
0.751 |
|
| 1999 |
Liu J, Lindquist S. Oligopeptide-repeat expansions modulate ‘protein-only’ inheritance in yeast Nature. 400: 573-576. PMID 10448860 DOI: 10.1038/23048 |
0.581 |
|
| 1999 |
Zhou P, Derkatch IL, Uptain SM, Patino MM, Lindquist S, Liebman SW. The yeast non-Mendelian factor [ETA+] is a variant of [PSI+], a prion-like form of release factor eRF3. The Embo Journal. 18: 1182-91. PMID 10064585 DOI: 10.1093/Emboj/18.5.1182 |
0.362 |
|
| 1999 |
Nathan DF, Vos MH, Lindquist S. Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation. Proceedings of the National Academy of Sciences of the United States of America. 96: 1409-1414. PMID 9990037 DOI: 10.1073/Pnas.96.4.1409 |
0.429 |
|
| 1999 |
Newnam GP, Wegrzyn RD, Lindquist SL, Chernoff YO. Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing. Molecular and Cellular Biology. 19: 1325-33. PMID 9891066 DOI: 10.1128/Mcb.19.2.1325 |
0.43 |
|
| 1999 |
Xu Y, Singer MA, Lindquist S. Maturation of the tyrosine kinase c-src as a kinase and as a substrate depends on the molecular chaperone Hsp90. Proceedings of the National Academy of Sciences of the United States of America. 96: 109-14. PMID 9874780 DOI: 10.1073/pnas.96.1.109 |
0.378 |
|
| 1998 |
Rutherford SL, Lindquist S. Hsp90 as a capacitor for morphological evolution Nature. 396: 336-342. PMID 9845070 DOI: 10.1038/24550 |
0.426 |
|
| 1998 |
Singer MA, Lindquist S. Thermotolerance in Saccharomyces cerevisiae: the Yin and Yang of trehalose. Trends in Biotechnology. 16: 460-8. PMID 9830154 DOI: 10.1016/S0167-7799(98)01251-7 |
0.412 |
|
| 1998 |
Lindquist S, DebBurman SK, Glover JR, Kowal AS, Liu JJ, Schirmer EC, Serio TR. Amyloid fibres of Sup35 support a prion-like mechanism of inheritance in yeast. Biochemical Society Transactions. 26: 486-90. PMID 9765901 DOI: 10.1042/Bst0260486 |
0.773 |
|
| 1998 |
Glover JR, Lindquist S. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell. 94: 73-82. PMID 9674429 DOI: 10.1016/S0092-8674(00)81223-4 |
0.682 |
|
| 1998 |
Singer MA, Lindquist S. Multiple effects of trehalose on protein folding in vitro and in vivo. Molecular Cell. 1: 639-48. PMID 9660948 DOI: 10.1016/S1097-2765(00)80064-7 |
0.43 |
|
| 1998 |
Schirmer EC, Queitsch C, Kowal AS, Parsell DA, Lindquist S. The ATPase activity of Hsp104, effects of environmental conditions and mutations. The Journal of Biological Chemistry. 273: 15546-52. PMID 9624144 DOI: 10.1074/Jbc.273.25.15546 |
0.763 |
|
| 1998 |
Duina AA, Marsh JA, Kurtz RB, Chang HC, Lindquist S, Gaber RF. The peptidyl-prolyl isomerase domain of the CyP-40 cyclophilin homolog Cpr7 is not required to support growth or glucocorticoid receptor activity in Saccharomyces cerevisiae. The Journal of Biological Chemistry. 273: 10819-22. PMID 9556552 DOI: 10.1074/Jbc.273.18.10819 |
0.342 |
|
| 1998 |
Schirmer EC, Lindquist S. Purification And Properties Of Hsp104 From Yeast Methods in Enzymology. 290: 430-444. PMID 9534180 DOI: 10.1016/S0076-6879(98)90036-2 |
0.696 |
|
| 1997 |
DebBurman SK, Raymond GJ, Caughey B, Lindquist S. Chaperone-supervised conversion of prion protein to its protease-resistant form. Proceedings of the National Academy of Sciences of the United States of America. 94: 13938-43. PMID 9391131 DOI: 10.1073/pnas.94.25.13938 |
0.435 |
|
| 1997 |
Schirmer EC, Lindquist S. Interactions of the chaperone Hsp104 with yeast Sup35 and mammalian PrP Proceedings of the National Academy of Sciences of the United States of America. 94: 13932-13937. PMID 9391130 DOI: 10.1073/Pnas.94.25.13932 |
0.683 |
|
| 1997 |
Nathan DF, Vos MH, Lindquist S. In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone Proceedings of the National Academy of Sciences of the United States of America. 94: 12949-12956. PMID 9371781 DOI: 10.1073/Pnas.94.24.12949 |
0.472 |
|
| 1997 |
Golic MM, Rong YS, Petersen RB, Lindquist SL, Golic KG. FLP-mediated DNA mobilization to specific target sites in Drosophila chromosomes. Nucleic Acids Research. 25: 3665-71. PMID 9278488 DOI: 10.1093/Nar/25.18.3665 |
0.703 |
|
| 1997 |
Kimura Y, Rutherford SL, Miyata Y, Yahara I, Freeman BC, Yue L, Morimoto RI, Lindquist S. Cdc37 is a molecular chaperone with specific functions in signal transduction. Genes & Development. 11: 1775-85. PMID 9242486 DOI: 10.1101/Gad.11.14.1775 |
0.568 |
|
| 1997 |
Glover JR, Kowal AS, Schirmer EC, Patino MM, Liu JJ, Lindquist S. Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell. 89: 811-9. PMID 9182769 DOI: 10.1016/S0092-8674(00)80264-0 |
0.776 |
|
| 1997 |
Lindquist S. Mad Cows Meet Psi-chotic Yeast: The Expansion of the Prion Hypothesis Cell. 89: 495-498. PMID 9160741 DOI: 10.1016/S0092-8674(00)80231-7 |
0.376 |
|
| 1997 |
Chang HC, Nathan DF, Lindquist S. In vivo analysis of the Hsp90 cochaperone Sti1 (p60). Molecular and Cellular Biology. 17: 318-25. PMID 8972212 DOI: 10.1128/MCB.17.1.318 |
0.428 |
|
| 1996 |
Tuite MF, Lindquist SL. Maintenance and inheritance of yeast prions. Trends in Genetics : Tig. 12: 467-71. PMID 8973157 DOI: 10.1016/0168-9525(96)10045-7 |
0.456 |
|
| 1996 |
Duina AA, Chang HC, Marsh JA, Lindquist S, Gaber RF. A cyclophilin function in Hsp90-dependent signal transduction. Science (New York, N.Y.). 274: 1713-5. PMID 8939862 DOI: 10.1126/science.274.5293.1713 |
0.365 |
|
| 1996 |
Patino MM, Liu JJ, Glover JR, Lindquist S. Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science (New York, N.Y.). 273: 622-6. PMID 8662547 DOI: 10.1126/Science.273.5275.622 |
0.738 |
|
| 1996 |
Lindquist S, Kim G. Heat-shock protein 104 expression is sufficient for thermotolerance in yeast. Proceedings of the National Academy of Sciences of the United States of America. 93: 5301-5306. PMID 8643570 DOI: 10.1073/Pnas.93.11.5301 |
0.359 |
|
| 1996 |
Schirmer EC, Glover JR, Singer MA, Lindquist S. HSP100/Clp proteins: a common mechanism explains diverse functions Trends in Biochemical Sciences. 21: 289-296. DOI: 10.1016/S0968-0004(96)10038-4 |
0.435 |
|
| 1995 |
Nathan DF, Lindquist S. Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase. Molecular and Cellular Biology. 15: 3917-3925. PMID 7791797 DOI: 10.1128/Mcb.15.7.3917 |
0.418 |
|
| 1995 |
Vogel JL, Parsell DA, Lindquist S. Heat-shock proteins Hsp104 and Hsp70 reactivate mRNA splicing after heat inactivation Current Biology. 5: 306-317. PMID 7780741 DOI: 10.1016/S0960-9822(95)00061-3 |
0.393 |
|
| 1995 |
Kimura Y, Yahara I, Lindquist S. Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways Science. 268: 1362-1365. PMID 7761857 DOI: 10.1126/Science.7761857 |
0.403 |
|
| 1995 |
Chernoff YO, Lindquist SL, Ono B, Inge-Vechtomov SG, Liebman SW. Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science (New York, N.Y.). 268: 880-4. PMID 7754373 DOI: 10.1126/Science.7754373 |
0.462 |
|
| 1995 |
Welte MA, Duncan I, Lindquist S. The basis for a heat-induced developmental defect: defining crucial lesions. Genes & Development. 9: 2240-50. PMID 7557378 DOI: 10.1101/Gad.9.18.2240 |
0.604 |
|
| 1994 |
Parsell DA, Kowal AS, Singer MA, Lindquist S. Protein disaggregation mediated by heat-shock protein Hsp104. Nature. 372: 475-8. PMID 7984243 DOI: 10.1038/372475a0 |
0.423 |
|
| 1994 |
Schirmer EC, Lindquist S, Vierling E. An Arabidopsis heat shock protein complements a thermotolerance defect in yeast Plant Cell. 6: 1899-1909. PMID 7866032 DOI: 10.1105/Tpc.6.12.1899 |
0.67 |
|
| 1994 |
Dellavalle RP, Petersen R, Lindquist S. Preferential deadenylation of Hsp70 mRNA plays a key role in regulating Hsp70 expression in Drosophila melanogaster Molecular and Cellular Biology. 14: 3646-3659. PMID 7515148 DOI: 10.1128/mcb.14.6.3646-3659.1994 |
0.305 |
|
| 1994 |
Parsell DA, Lindquist S. 18 Heat Shock Proteins and Stress Tolerance Cold Spring Harbor Monograph Archive. 26: 457-494. DOI: 10.1101/087969427.26.457 |
0.353 |
|
| 1993 |
Welte MA, Tetrault JM, Dellavalle RP, Lindquist SL. A new method for manipulating transgenes: engineering heat tolerance in a complex, multicellular organism. Current Biology : Cb. 3: 842-53. PMID 15335817 DOI: 10.1016/0960-9822(93)90218-D |
0.627 |
|
| 1993 |
Sanchez Y, Parsell DA, Taulien J, Vogel JL, Craig EA, Lindquist S. Genetic evidence for a functional relationship between Hsp104 and Hsp70 Journal of Bacteriology. 175: 6484-6491. PMID 8407824 DOI: 10.1128/Jb.175.20.6484-6491.1993 |
0.432 |
|
| 1993 |
Parsell DA, Lindquist S. The Function of Heat-Shock Proteins in Stress Tolerance: Degradation and Reactivation of Damaged Proteins Annual Review of Genetics. 27: 437-496. PMID 8122909 DOI: 10.1146/Annurev.Ge.27.120193.002253 |
0.366 |
|
| 1993 |
Parsell DA, Taulien J, Lindquist SL. The role of heat-shock proteins in thermotolerance Philosophical Transactions of the Royal Society B. 339: 279-286. PMID 8098532 DOI: 10.1098/Rstb.1993.0026 |
0.454 |
|
| 1993 |
Xu Y, Lindquist S. Heat-shock protein hsp90 governs the activity of pp60v-src kinase. Proceedings of the National Academy of Sciences of the United States of America. 90: 7074-8. PMID 7688470 DOI: 10.1073/pnas.90.15.7074 |
0.36 |
|
| 1992 |
Feder JH, Rossi JM, Solomon J, Solomon N, Lindquist S. The consequences of expressing hsp70 in Drosophila cells at normal temperatures. Genes & Development. 6: 1402-13. PMID 1644286 DOI: 10.1101/Gad.6.8.1402 |
0.37 |
|
| 1992 |
Lindquist S. Heat-shock proteins and stress tolerance in microorganisms. Current Opinion in Genetics & Development. 2: 748-755. PMID 1458023 DOI: 10.1016/S0959-437X(05)80135-2 |
0.354 |
|
| 1992 |
Lindquist S. Heat-shock proteins and stress tolerance in microorganisms Current Biology. 2: 584. DOI: 10.1016/0960-9822(92)90156-5 |
0.338 |
|
| 1992 |
Sanchez Y, Taulien J, Borkovich KA, Lindquist S. Hsp104 is required for tolerance to many forms of stress. The Embo Journal. 11: 2357-2364. DOI: 10.1002/J.1460-2075.1992.Tb05295.X |
0.393 |
|
| 1991 |
Susek RE, Lindquist S. Transcriptional derepression of the Saccharomyces cerevisiae HSP26 gene during heat shock. Molecular and Cellular Biology. 10: 6362-73. PMID 2123293 DOI: 10.1128/MCB.10.12.6362 |
0.352 |
|
| 1991 |
Welsh N, Welsh M, Lindquist S, Eizirik DL, Bendtzen K, Sandler S. Interleukin-1 beta increases the biosynthesis of the heat shock protein hsp70 and selectively decreases the biosynthesis of five proteins in rat pancreatic islets. Autoimmunity. 9: 33-40. PMID 1669845 DOI: 10.3109/08916939108997121 |
0.33 |
|
| 1990 |
Picard D, Khursheed B, Garabedian MJ, Fortin MG, Lindquist S, Yamamoto KR. Reduced levels of hsp90 compromise steroid receptor action in vivo. Nature. 348: 166-8. PMID 2234079 DOI: 10.1038/348166A0 |
0.338 |
|
| 1990 |
Sanchez Y, Lindquist SL. HSP104 required for induced thermotolerance. Science (New York, N.Y.). 248: 1112-5. PMID 2188365 DOI: 10.1126/Science.2188365 |
0.347 |
|
| 1990 |
Yost HJ, Petersen RB, Lindquist S. 16 Posttranscriptional Regulation of Heat Shock Protein Synthesis in Drosophila Cold Spring Harbor Monograph Archive. 19: 379-409. DOI: 10.1101/087969337.19.379 |
0.627 |
|
| 1989 |
Lindquist S, Craig EA. The heat-shock proteins. Annual Review of Genetics. 22: 631-77. PMID 2853609 DOI: 10.1146/Annurev.Ge.22.120188.003215 |
0.307 |
|
| 1989 |
Susek RE, Lindquist SL. hsp26 of Saccharomyces cerevisiae is related to the superfamily of small heat shock proteins but is without a demonstrable function. Molecular and Cellular Biology. 9: 5265-71. PMID 2689876 DOI: 10.1128/Mcb.9.11.5265 |
0.407 |
|
| 1989 |
Borkovich KA, Farrelly FW, Finkelstein DB, Taulien J, Lindquist S. hsp82 Is an essential protein that is required in higher concentrations for growth of cells at higher temperatures Molecular and Cellular Biology. 9: 3919-3930. PMID 2674684 DOI: 10.1128/Mcb.9.9.3919 |
0.41 |
|
| 1989 |
Rossi JM, Lindquist S. The intracellular location of yeast heat-shock protein 26 varies with metabolism Journal of Cell Biology. 108: 425-439. PMID 2645298 DOI: 10.1083/Jcb.108.2.425 |
0.398 |
|
| 1989 |
Petersen RB, Lindquist S. Regulation of HSP70 synthesis by messenger RNA degradation. Cell Regulation. 1: 135-49. PMID 2519613 DOI: 10.1091/Mbc.1.1.135 |
0.313 |
|
| 1989 |
Golic KG, Lindquist S. The FLP recombinase of yeast catalyzes site-specific recombination in the Drosophila genome. Cell. 59: 499-509. PMID 2509077 DOI: 10.1016/0092-8674(89)90033-0 |
0.666 |
|
| 1988 |
Petersen R, Lindquist S. The Drosophila hsp70 message is rapidly degraded at normal temperatures and stabilized by heat shock Gene. 72: 161-168. PMID 3243430 DOI: 10.1016/0378-1119(88)90138-2 |
0.355 |
|
| 1986 |
Petko L, Lindquist S. Hsp26 is not required for growth at high temperatures, nor for thermotolerance, spore development, or germination. Cell. 45: 885-894. PMID 3518952 DOI: 10.1016/0092-8674(86)90563-5 |
0.342 |
|
| 1986 |
Kurtz S, Rossi J, Petko L, Lindquist S. An ancient developmental induction: heat-shock proteins induced in sporulation and oogenesis. Science. 231: 1154-1157. PMID 3511530 DOI: 10.1126/Science.3511530 |
0.367 |
|
| 1986 |
Lindquist S. The Heat-Shock Response Annual Review of Biochemistry. 55: 1151-1191. PMID 2427013 DOI: 10.1146/Annurev.Bi.55.070186.005443 |
0.302 |
|
| 1986 |
Yost HJ, Lindquist S. RNA splicing is interrupted by heat shock and is rescued by heat shock protein synthesis. Cell. 45: 185-93. PMID 2421918 DOI: 10.1016/0092-8674(86)90382-X |
0.59 |
|
| 1986 |
McGarry TJ, Lindquist S. Inhibition of heat shock protein synthesis by heat-inducible antisense RNA Proceedings of the National Academy of Sciences of the United States of America. 83: 399-403. PMID 2417242 DOI: 10.1073/Pnas.83.2.399 |
0.354 |
|
| 1985 |
McGarry TJ, Lindquist S. The preferential translation of Drosophila hsp70 mRNA requires sequences in the untranslated leader Cell. 42: 903-911. PMID 4053186 DOI: 10.1016/0092-8674(85)90286-7 |
0.318 |
|
| 1984 |
Velazquez JM, Lindquist S. hsp70: nuclear concentration during environmental stress and cytoplasmic storage during recovery. Cell. 36: 655-62. PMID 6421488 DOI: 10.1016/0092-8674(84)90345-3 |
0.366 |
|
| 1984 |
Kurtz S, Lindquist S. Changing patterns of gene expression during sporulation in yeast Proceedings of the National Academy of Sciences of the United States of America. 81: 7323-7327. PMID 6390434 DOI: 10.1073/Pnas.81.23.7323 |
0.328 |
|
| 1984 |
Pelham H, Lewis M, Lindquist SL. Expression of a Drosophila heat shock protein in mammalian cells: transient association with nucleoli after heat shock. Philosophical Transactions of the Royal Society B. 307: 301-307. PMID 6151701 DOI: 10.1098/Rstb.1984.0131 |
0.39 |
|
| 1983 |
Velazquez JM, Sonoda S, Bugaisky G, Lindquist S. Is the major Drosophila heat shock protein present in cells that have not been heat shocked? The Journal of Cell Biology. 96: 286-90. PMID 6826649 DOI: 10.1083/Jcb.96.1.286 |
0.387 |
|
| 1982 |
Didomenico BJ, Bugaisky GE, Lindquist S. The heat shock response is self-regulated at both the transcriptional and posttranscriptional levels Cell. 31: 593-603. PMID 7159929 DOI: 10.1016/0092-8674(82)90315-4 |
0.381 |
|
| 1982 |
DiDomenico BJ, Bugaisky GE, Lindquist S. Heat shock and recovery are mediated by different translational mechanisms Proceedings of the National Academy of Sciences of the United States of America. 79: 6181-6185. PMID 6815647 DOI: 10.1073/Pnas.79.20.6181 |
0.353 |
|
| 1981 |
Lindquist S. Regulation of protein synthesis during heat shock Nature. 293: 311-314. PMID 6792546 DOI: 10.1038/293311A0 |
0.385 |
|
| 1980 |
Lindquist S. Varying patterns of protein synthesis in Drosophila during heat shock: Implications for regulation Developmental Biology. 77: 463-479. PMID 7399133 DOI: 10.1016/0012-1606(80)90488-1 |
0.358 |
|
| 1980 |
Velazquez JM, DiDomenico BJ, Lindquist S. Intracellular localization of heat shock proteins in Drosophila. Cell. 20: 679-89. PMID 6774811 DOI: 10.1016/0092-8674(80)90314-1 |
0.4 |
|
| 1980 |
Lindquist S. Translational efficiency of heat-induced messages in Drosophila melanogaster cells. Journal of Molecular Biology. 137: 151-158. PMID 6768893 DOI: 10.1016/0022-2836(80)90322-8 |
0.375 |
|
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