Prions as adaptive conduits of memory and inheritance

Novel Proteinaceous Infectious Particles Cause Scrapie

Prusiner, S. B. (1982) · Science · doi:10.1126/science.6801762 · Cited by 5,121 · see citing works

Protein folding and misfolding

Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791 · see citing works

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064 · see citing works

Functional Discovery via a Compendium of Expression Profiles

Hughes, T. R., Marton, M. J., Jones, A. R., Roberts, C. J., Stoughton, R. B., Armour, C. D., Bennett, H. A., Coffey, E. M., Dai, H. A., He, Y. D., et al. (2000) · Cell · doi:10.1016/s0092-8674(00)00015-5 · Cited by 2,534 · see citing works

Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins.

Pan, K. M., Baldwin, M. A., Nguyen, J. T., Gasset, M., Serban, A. V., Groth, D., Mehlhorn, I., Huang, Z., Fletterick, R. J., & Cohen, F. E. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.10962 · Cited by 2,281 · see citing works

Impairment of the Ubiquitin-Proteasome System by Protein Aggregation

Bence, N., Sampat, R. M., & Kopito, R. R. (2001) · Science · doi:10.1126/science.292.5521.1552 · Cited by 2,192 · see citing works

Mice devoid of PrP are resistant to scrapie

Büeler, H., Aguzzi, A., Sailer, A. W., Greiner, R., Autenried, P., Aguet, M., & Weissmann, C. (1993) · Cell · doi:10.1016/0092-8674(93)90360-3 · Cited by 2,098 · see citing works

The molecular basis of CaMKII function in synaptic and behavioural memory

Lisman, J., Schulman, H., & Cline, H. (2002) · Nature Reviews Neuroscience · doi:10.1038/nrn753 · Cited by 1,860 · see citing works

AN UNSOLVED PROBLEM OF BIOLOGY

(1953) · The Medical Journal of Australia · doi:10.5694/j.1326-5377.1953.tb84985.x · Cited by 1,805 · see citing works

Sequencing and comparison of yeast species to identify genes and regulatory elements

Kellis, M., Patterson, N. J., Endrizzi, M. G., Birren, B. W., & Lander, E. S. (2003) · Nature · doi:10.1038/nature01644 · Cited by 1,731 · see citing works

Emergent Properties of Networks of Biological Signaling Pathways

Bhalla, U. S., & Iyengar, R. (1999) · Science · doi:10.1126/science.283.5400.381 · Cited by 1,686 · see citing works

Hsp104, Hsp70, and Hsp40

Glover, J. R., & Lindquist, S. L. (1998) · Cell · doi:10.1016/s0092-8674(00)81223-4 · Cited by 1,361 · see citing works

Role of Escherichia coli Curli Operons in Directing Amyloid Fiber Formation

Chapman, M., Robinson, L. S., Pinkner, J., Roth, R., Heuser, J., Hammar, M., Normark, S., & Hultgren, S. (2002) · Science · doi:10.1126/science.1067484 · Cited by 1,282 · see citing works

Eight prion strains have PrPSc molecules with different conformations

Safar, J., Wille, H., Itri, V., Groth, D., Serban, H., Torchia, M., Cohen, F. E., & Prusiner, S. B. (1998) · Nature Medicine · doi:10.1038/2654 · Cited by 1,244 · see citing works

[URE3] as an Altered URE2 Protein: Evidence for a Prion Analog in Saccharomyces cerevisiae

Wickner, R. B. (1994) · Science · doi:10.1126/science.7909170 · Cited by 1,216 · see citing works

Nature of the Scrapie Agent: Self-replication and Scrapie

Griffith, J. S. (1967) · Nature · doi:10.1038/2151043a0 · Cited by 1,161 · see citing works

Evolvability

Kirschner, M., & Gerhart, J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.15.8420 · Cited by 1,129 · see citing works

Interference by Huntingtin and Atrophin-1 with CBP-Mediated Transcription Leading to Cellular Toxicity

Nucifora, F. C., Sasaki, M., Peters, M. F., Huang, H., Cooper, J. K., Yamada, M., Takahashi, H., Tsuji, S., Troncoso, J. C., Dawson, V. L., et al. (2001) · Science · doi:10.1126/science.1056784 · Cited by 1,095 · see citing works

Epigenetic Regulation of Cellular Memory by the Polycomb and Trithorax Group Proteins

Ringrose, L., & Paro, R. (2004) · Annual Review of Genetics · doi:10.1146/annurev.genet.38.072902.091907 · Cited by 1,077 · see citing works

Scrapie prions aggregate to form amyloid-like birefringent rods

Prusiner, S. B., McKinley, M. P., Bowman, K. A., Bolton, D. C., Bendheim, P. E., Groth, D., & Glenner, G. G. (1983) · Cell · doi:10.1016/0092-8674(83)90168-x · Cited by 1,043 · see citing works

Role of the Chaperone Protein Hsp104 in Propagation of the Yeast Prion-Like Factor [ psi + ]

Chernoff, Y. O., Lindquist, S. L., Ono, B., Inge-Vechtomov, S. G., & Liebman, S. W. (1995) · Science · doi:10.1126/science.7754373 · Cited by 1,030 · see citing works

Synthetic Mammalian Prions

Legname, G., Baskakov, I. V., Nguyen, H.-O. B., Riesner, D., Cohen, F. E., DeArmond, S. J., & Prusiner, S. B. (2004) · Science · doi:10.1126/science.1100195 · Cited by 1,022 · see citing works

Conformational constraints for amyloid fibrillation: the importance of being unfolded

Uversky, V. N., & Fink, A. L. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2003.12.008 · Cited by 1,012 · see citing works

Stress Granule Assembly Is Mediated by Prion-like Aggregation of TIA-1

Farny, N. G., Kedersha, N., Ayodele, M. O., Shen, L., Stoecklin, G., Dember, L. M., & Anderson, P. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-08-0715 · Cited by 1,000 · see citing works

Nucleated conformational conversion and the replication of conformational information by a prion determinant.

Serio, T., Cashikar, A., Kowal, A., Sawicki, G., Moslehi, J., Serpell, L., Arnsdorf, M., & Lindquist, S. (2000) · Science · doi:10.1126/science.289.5483.1317 · Cited by 988 · see citing works

THE POPULATION GENETICS OF ADAPTATION: THE DISTRIBUTION OF FACTORS FIXED DURING ADAPTIVE EVOLUTION

Orr, H. A. (1998) · Evolution · doi:10.1111/j.1558-5646.1998.tb01823.x · Cited by 895 · see citing works

Protein disaggregation mediated by heat-shock protein Hspl04

Parsell, D. A., Kowal, A. S., Singer, M. A., & Lindquist, S. L. (1994) · Nature · doi:10.1038/372475a0 · Cited by 864 · see citing works

Normal host prion protein necessary for scrapie-induced neurotoxicity

Brandner, S., Isenmann, S., Raeber, A. J., Fischer, M., Sailer, A. W., Kobayashi, Y., Marino, S., Weissmann, C., & Aguzzi, A. (1996) · Nature · doi:10.1038/379339a0 · Cited by 813 · see citing works

In Vitro Generation of Infectious Scrapie Prions

Castilla, J., Saá, P., Hetz, C. A., & Soto, C. A. (2005) · Cell · doi:10.1016/j.cell.2005.02.011 · Cited by 790 · see citing works

Depleting Neuronal PrP in Prion Infection Prevents Disease and Reverses Spongiosis

Mallucci, G. R., Dickinson, A., Linehan, J. M., Klöhn, P., Brandner, S., & Collinge, J. (2003) · Science · doi:10.1126/science.1090187 · Cited by 772 · see citing works

Conformational variations in an infectious protein determine prion strain differences

Tanaka, M., Chien, P., Naber, N. I., Cooke, R., & Weissman, J. S. (2004) · Nature · doi:10.1038/nature02392 · Cited by 770 · see citing works

Conducting nanowires built by controlled self-assembly of amyloid fibers and selective metal deposition

Scheibel, T., Parthasarathy, R., Sawicki, G. J., Lin, X., Jaeger, H. M., & Lindquist, S. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0431081100 · Cited by 718 · see citing works

RNAi suppresses polyglutamine-induced neurodegeneration in a model of spinocerebellar ataxia

Xia, H., Mao, Q.-W., Eliason, S., Harper, S., Martins, I. H., Orr, H., Paulson, H., Yang, L., Kotin, R., & Davidson, B. (2004) · Nature Medicine · doi:10.1038/nm1076 · Cited by 689 · see citing works

Does the Agent of Scrapie Replicate without Nucleic Acid ?

Alper, T., Cramp, W. A., Haig, D. A., & Clarke, M. (1967) · Nature · doi:10.1038/214764a0 · Cited by 683 · see citing works

A self-replicating peptide

Lee, D. H., Granja, J. R., Martinez, J. A., Severin, K., & Ghadiri, M. R. (1996) · Nature · doi:10.1038/382525a0 · Cited by 677 · see citing works

A yeast prion provides a mechanism for genetic variation and phenotypic diversity

True, H. L., & Lindquist, S. L. (2000) · Nature · doi:10.1038/35035005 · Cited by 672 · see citing works

Prion biology and diseases.

Prusiner, S. B. (1991) · PubMed · Cited by 641 · see citing works

Support for the Prion Hypothesis for Inheritance of a Phenotypic Trait in Yeast

Patino, M. M., Liu, J., Glover, J. R., & Lindquist, S. L. (1996) · Science · doi:10.1126/science.273.5275.622 · Cited by 612 · see citing works

Translational control by CPEB: a means to the end

Méndez, R., & Richter, J. D. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35080081 · Cited by 609 · see citing works

The SWI/SNF complex — chromatin and cancer

Roberts, C. W. M., & Orkin, S. H. (2004) · Nature reviews. Cancer · doi:10.1038/nrc1273 · Cited by 603 · see citing works

Self-Seeded Fibers Formed by Sup35, the Protein Determinant of [PSI+], a Heritable Prion-like Factor of S. cerevisiae

Glover, J. R., Kowal, A. S., Schirmer, E. C., Patino, M. M., Liu, J., & Lindquist, S. L. (1997) · Cell · doi:10.1016/s0092-8674(00)80264-0 · Cited by 591 · see citing works

An mRNA Surveillance Mechanism That Eliminates Transcripts Lacking Termination Codons

Frischmeyer, P. A., van Hoof, A., O’Donnell, K. A., Guerrerio, A. L., Parker, R., & Dietz, H. C. (2002) · Science · doi:10.1126/science.1067338 · Cited by 590 · see citing works

Conformational diversity and protein evolution – a 60-year-old hypothesis revisited

James, L. C., & Tawfik, D. S. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00135-x · Cited by 579 · see citing works

A Neuronal Isoform of the Aplysia CPEB Has Prion-Like Properties

Si, K., Lindquist, S. L., & Kandel, E. R. (2003) · Cell · doi:10.1016/s0092-8674(03)01020-1 · Cited by 565 · see citing works

Prions Affect the Appearance of Other Prions

Derkatch, I. L., Bradley, M. E., Hong, J. Y., & Liebman, S. W. (2001) · Cell · doi:10.1016/s0092-8674(01)00427-5 · Cited by 561 · see citing works

Genesis and Variability of [PSI] Prion Factors in Saccharomyces cerevisiae

Derkatch, I. L., Chernoff, Y. O., Kushnirov, V. V., Inge-Vechtomov, S. G., & Liebman, S. W. (1996) · Genetics · doi:10.1093/genetics/144.4.1375 · Cited by 527 · see citing works

Evolutionary capacitance as a general feature of complex gene networks

Bergman, A., & Siegal, M. L. (2003) · Nature · doi:10.1038/nature01765 · Cited by 520 · see citing works

Mechanism of Prion Propagation: Amyloid Growth Occurs by Monomer Addition

Collins, S. R., Douglass, A. D., Vale, R. D., & Weissman, J. S. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020321 · Cited by 514 · see citing works

Ψ, A cytoplasmic suppressor of super-suppressor in yeast

Cox, B. S. (1965) · Heredity · doi:10.1038/hdy.1965.65 · Cited by 506 · see citing works

Propagation of the yeast prion‐like [psi+] determinant is mediated by oligomerization of the SUP35‐encoded polypeptide chain release factor.

Paushkin, S. V., Kushnirov, V. V., Smirnov, V. N., & Ter‐Avanesyan, M. D. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00675.x · Cited by 502 · see citing works

Rnq1

Sondheimer, N. J., & Lindquist, S. L. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80412-8 · Cited by 494 · see citing works

The product of the yeast UPF1 gene is required for rapid turnover of mRNAs containing a premature translational termination codon.Preprint

Leeds, P., Peltz, S. W., Jacobson, A., & Culbertson, M. R. (1991) · Genes & Development · doi:10.1101/gad.5.12a.2303 · Cited by 491 · see citing works

Positive autoregulation of the myogenic determination gene MyoD1

Thayer, M. J., Tapscott, S. J., Davis, R. L., Wright, W. E., Lassar, A. B., & Weintraub, H. M. (1989) · Cell · doi:10.1016/0092-8674(89)90838-6 · Cited by 471 · see citing works

Hsp104 Catalyzes Formation and Elimination of Self-Replicating Sup35 Prion Conformers

Shorter, J., & Lindquist, S. L. (2004) · Science · doi:10.1126/science.1098007 · Cited by 464 · see citing works

A census of glutamine/asparagine-rich regions: Implications for their conserved function and the prediction of novel prions

Michelitsch, M. D., & Weissman, J. S. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.22.11910 · Cited by 463 · see citing works

Protein-only transmission of three yeast prion strains

King, C., & Díaz-Avalos, R. (2004) · Nature · doi:10.1038/nature02391 · Cited by 460 · see citing works

The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog

Coustou, V., Deleu, C., Saupe, S. J., & Bégueret, J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9773 · Cited by 456 · see citing works

Genetic and Environmental Factors Affecting the de novo Appearance of the [PSI + ] Prion in Saccharomyces cerevisiae

Derkatch, I. L., Bradley, M. E., Zhou, P., Chernoff, Y. O., & Liebman, S. W. (1997) · Genetics · doi:10.1093/genetics/147.2.507 · Cited by 451 · see citing works

Yeast [PSI+] Prion Aggregates Are Formed by Small Sup35 Polymers Fragmented by Hsp104

Kryndushkin, D. S., Alexandrov, I. M., Ter‐Avanesyan, M. D., & Kushnirov, V. V. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307996200 · Cited by 446 · see citing works

Pathway Complexity of Prion Protein Assembly into Amyloid

Baskakov, I. V., Legname, G., Baldwin, M. A., Prusiner, S. B., & Cohen, F. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111402200 · Cited by 438 · see citing works

A Neuronal Isoform of CPEB Regulates Local Protein Synthesis and Stabilizes Synapse-Specific Long-Term Facilitation in Aplysia

Si, K., Giustetto, M., Etkin, A., Hsu, R., Janisiewicz, A. M., Miniaci, M. C., Kim, J., Zhu, H., & Kandel, E. R. (2003) · Cell · doi:10.1016/s0092-8674(03)01021-3 · Cited by 432 · see citing works

Eukaryotic Proteasomes Cannot Digest Polyglutamine Sequences and Release Them during Degradation of Polyglutamine-Containing Proteins

Venkatraman, P., Wetzel, R. B., Tanaka, M., Nukina, N., & Goldberg, A. L. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00151-0 · Cited by 424 · see citing works

Whole-genome expression analysis of <i>snf/swi</i> mutants of <i>Saccharomyces</i> <i>cerevisiae</i>

Sudarsanam, P., Iyer, V. R., Brown, P. O., & Winston, F. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.7.3364 · Cited by 389 · see citing works

The SUP35 omnipotent suppressor gene is involved in the maintenance of the non-Mendelian determinant [psi+] in the yeast Saccharomyces cerevisiae.

Ter‐Avanesyan, M. D., Dagkesamanskaya, A. R., Kushnirov, V. V., & Smirnov, V. N. (1994) · Genetics · doi:10.1093/genetics/137.3.671 · Cited by 386 · see citing works

siRNA relieves chronic neuropathic pain

Dorn, G. (2004) · Nucleic Acids Research · doi:10.1093/nar/gnh044 · Cited by 380 · see citing works

Prion-Inducing Domain of Yeast Ure2p and Protease Resistance of Ure2p in Prion-Containing Cells

Masison, D. C., & Wickner, R. B. (1995) · Science · doi:10.1126/science.270.5233.93 · Cited by 351 · see citing works

Late-associativity, synaptic tagging, and the role of dopamine during LTP and LTD

Sajikumar, S. (2004) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2004.03.003 · Cited by 341 · see citing works

Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits

True, H. L., Berlin, I., & Lindquist, S. L. (2004) · Nature · doi:10.1038/nature02885 · Cited by 331 · see citing works

Emerging Principles of Conformation-Based Prion Inheritance

Chien, P., Weissman, J. S., & DePace, A. H. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161837 · Cited by 326 · see citing works

De novo amyloid proteins from designed combinatorial libraries

West, M. W., Wang, W., Patterson, J., Mancias, J. D., Beasley, J. R., & Hecht, M. H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11211 · Cited by 321 · see citing works

Non-Mendelian Mutation Allowing Ureidosuccinic Acid Uptake in Yeast

Lacroute, F. (1971) · Journal of Bacteriology · doi:10.1128/jb.106.2.519-522.1971 · Cited by 317 · see citing works

The mec-3 gene of Caenorhabditis elegans requires its own product for maintained expression and is expressed in three neuronal cell types.Preprint

Way, J. C., & Chalfie, M. (1989) · Genes & Development · doi:10.1101/gad.3.12a.1823 · Cited by 317 · see citing works

A chiroselective peptide replicator

Saghatelian, A., Yokobayashi, Y., Soltani, K., & Ghadiri, M. R. (2001) · Nature · doi:10.1038/35057238 · Cited by 310 · see citing works

Multiple Gln/Asn-Rich Prion Domains Confer Susceptibility to Induction of the Yeast [PSI] Prion

Osherovich, L. Z., & Weissman, J. S. (2001) · Cell · doi:10.1016/s0092-8674(01)00440-8 · Cited by 309 · see citing works

Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis

Berson, J. F., Theos, A. C., Harper, D. C., Tenza, D., Raposo, G., & Marks, M. S. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302072 · Cited by 288 · see citing works

Deletion analysis of the SUP35 gene of the yeast Saccharomyces cerevisiae reveals two non‐overlapping functional regions in the encoded protein

Ter‐Avanesyan, M. D., Kushnirov, V. V., Dagkesamanskaya, A. R., Didichenko, S. A., Chernoff, Y. O., Inge-Vechtomov, S. G., & Smirnov, V. N. (1993) · Molecular Microbiology · doi:10.1111/j.1365-2958.1993.tb01159.x · Cited by 284 · see citing works

Amyloid aggregates of the HET-s prion protein are infectious

Maddelein, M., Reis, S. D., Duvezin‐Caubet, S., Salin, B., & Saupe, S. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.072199199 · Cited by 281 · see citing works

Transmissibility of systemic amyloidosis by a prion-like mechanism

Lundmark, K., Westermark, G. T., Nyström, S. N., Murphy, C. L., Solomon, A., & Westermark, P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092205999 · Cited by 278 · see citing works

Prion Domain Initiation of Amyloid Formation in Vitro from Native Ure2p

Taylor, K. L., Cheng, N., Williams, R. W., Steven, A. C., & Wickner, R. B. (1999) · Science · doi:10.1126/science.283.5406.1339 · Cited by 277 · see citing works

The Persistence of Long-Term Memory

Bailey, C. H., Kandel, E. R., & Si, K. (2004) · Neuron · doi:10.1016/j.neuron.2004.09.017 · Cited by 277 · see citing works

Emergence of symbiosis in peptide self-replication through a hypercyclic network

Lee, D. H., Severin, K., Yokobayashi, Y., & Ghadiri, M. R. (1997) · Nature · doi:10.1038/37569 · Cited by 265 · see citing works

[URE3] Prion Propagation in Saccharomyces cerevisiae : Requirement for Chaperone Hsp104 and Curing by Overexpressed Chaperone Ydj1p

Moriyama, H., Edskes, H. K., & Wickner, R. B. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.23.8916-8922.2000 · Cited by 265 · see citing works

Molecular Basis of a Yeast Prion Species Barrier

Santoso, A., Chien, P., Osherovich, L. Z., & Weissman, J. S. (2000) · Cell · doi:10.1016/s0092-8674(00)81565-2 · Cited by 264 · see citing works

Prion Protein Devoid of the Octapeptide Repeat Region Restores Susceptibility to Scrapie in PrP Knockout Mice

Flechsig, E., Shmerling, D., Hegyi, I., Raeber, A. J., Fischer, M., Cozzio, A., von Mering, C., Aguzzi, A., & Weissmann, C. (2000) · Neuron · doi:10.1016/s0896-6273(00)00046-5 · Cited by 257 · see citing works

Under cover: causes, effects and implications of Hsp90‐mediated genetic capacitance

Sangster, T. A., Lindquist, S., & Queitsch, C. (2004) · BioEssays · doi:10.1002/bies.20020 · Cited by 251 · see citing works

Interactions among prions and prion “strains” in yeast

Bradley, M. E., Edskes, H. K., Hong, J. Y., Wickner, R. B., & Liebman, S. W. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.152330699 · Cited by 245 · see citing works

Quantifying the kinetic parameters of prion replication

Masel, J., Jansen, V. A. A., & Nowak, M. A. (1999) · Biophysical Chemistry · doi:10.1016/s0301-4622(99)00016-2 · Cited by 244 · see citing works

Evolvability is a selectable trait

Earl, D. J., & Deem, M. W. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404656101 · Cited by 240 · see citing works

Prions as Protein-Based Genetic Elements

Uptain, S. M., & Lindquist, S. L. (2002) · Annual Review of Microbiology · doi:10.1146/annurev.micro.56.013002.100603 · Cited by 238 · see citing works

The elimination of the yeast [ PSI + ] prion by guanidine hydrochloride is the result of Hsp104 inactivation

Ferreira, P. C., Ness, F., Edwards, S. R., Cox, B. S., & Tuite, M. F. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02478.x · Cited by 237 · see citing works

Positioning of follicular dendritic cells within the spleen controls prion neuroinvasion

Prinz, M., Heikenwälder, M. F., Junt, T., Schwarz, P., Glatzel, M., Heppner, F. L., Fu, Y., Lipp, M., & Aguzzi, A. (2003) · Nature · doi:10.1038/nature02072 · Cited by 217 · see citing works

Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion‐mediated mechanism

Eaglestone, S., Cox, B. S., & Tuite, M. F. (1999) · The EMBO Journal · doi:10.1093/emboj/18.7.1974 · Cited by 215 · see citing works

Domain organization and structure–function relationship of the HET‐s prion protein of Podospora anserina

Balguerie, A., Reis, S. D., Ritter, C., Chaignepain, S., Salin, B., Forge, V., Bathany, K., Lascu, I., Schmitter, J., Riek, R., et al. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg213 · Cited by 213 · see citing works

The SAM domain of polyhomeotic forms a helical polymer.

Kim, C. A., Gingery, M., Pilpa, R. M., & Bowie, J. U. (2002) · PubMed · doi:10.1038/nsb802 · Cited by 209 · see citing works

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

Derkatch, I. L., Uptain, S. M., Outeiro, T. F., Krishnan, R., Lindquist, S. L., & Liebman, S. W. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404968101 · Cited by 206 · see citing works

Oligopeptide-repeat expansions modulate ‘protein-only’ inheritance in yeast

Liu, J., & Lindquist, S. L. (1999) · Nature · doi:10.1038/23048 · Cited by 194 · see citing works

Two previously undescribed members of the mouse CPEB family of genes and their inducible expression in the principal cell layers of the hippocampus

Theis, M., Si, K., & Kandel, E. R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1133424100 · Cited by 194 · see citing works

The role of Sis1 in the maintenance of the [RNQ+] prion

Sondheimer, N., Lopez, N., Craig, E. A., & Lindquist, S. L. (2001) · The EMBO Journal · doi:10.1093/emboj/20.10.2435 · Cited by 194 · see citing works

Strain-specified characteristics of mouse synthetic prions

Legname, G., Nguyen, H.-O. B., Baskakov, I. V., Cohen, F. E., DeArmond, S. J., & Prusiner, S. B. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409079102 · Cited by 194 · see citing works

Evolutionary conservation of prion‐forming abilities of the yeast Sup35 protein

Chernoff, Y. O., Galkin, A. P., Lewitin, E., Chernova, T. A., Newnam, G. P., & Belenkiy, S. M. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01761.x · Cited by 193 · see citing works

Mechanism of Prion Loss after Hsp104 Inactivation in Yeast

Wegrzyn, R. D., Bapat, K., Newnam, G. P., Zink, A. D., & Chernoff, Y. O. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.14.4656-4669.2001 · Cited by 191 · see citing works

Dependence and independence of [PSI+] and [PIN+]: a two‐prion system in yeast?

Derkatch, I. L., Bradley, M. E., Masse, S. V. L., Zadorsky, S. P., Polozkov, G. V., Inge-Vechtomov, S. G., & Liebman, S. W. (2000) · The EMBO Journal · doi:10.1093/emboj/19.9.1942 · Cited by 184 · see citing works

Dissection and Design of Yeast Prions

Osherovich, L. Z., Cox, B. S., Tuite, M. F., & Weissman, J. S. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020086 · Cited by 183 · see citing works

Scrambled Prion Domains Form Prions and Amyloid

Ross, E. D., Baxa, U., & Wickner, R. B. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.16.7206-7213.2004 · Cited by 183 · see citing works

Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor‐1 mutants

Hattendorf, D. A., & Lindquist, S. L. (2002) · The EMBO Journal · doi:10.1093/emboj/21.1.12 · Cited by 179 · see citing works

Creating a Protein-Based Element of Inheritance

Li, L., & Lindquist, S. L. (2000) · Science · doi:10.1126/science.287.5453.661 · Cited by 177 · see citing works

Mechanism of Cross-Species Prion Transmission

Tanaka, M., Chien, P., Yonekura, K., & Weissman, J. S. (2005) · Cell · doi:10.1016/j.cell.2005.03.008 · Cited by 177 · see citing works

Evidence for and against the transmissibility of Alzheimer disease

Goudsmit, J., Morrow, C. H., Asher, D. M., Yanagihara, R. T., Masters, C. L., Gibbs, C. J., & Gajdusek, D. C. (1980) · Neurology · doi:10.1212/wnl.30.9.945 · Cited by 165 · see citing works

Mechanism of inactivation on prion conversion of the Saccharomyces cerevisiae Ure2 protein

Baxa, U., Speransky, V. V., Steven, A. C., & Wickner, R. B. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.082097899 · Cited by 159 · see citing works

Mad Cows Meet Psi-chotic Yeast: The Expansion of the Prion Hypothesis

Lindquist, S. L. (1997) · Cell · doi:10.1016/s0092-8674(00)80231-7 · Cited by 159 · see citing works

The Hydrophobin EAS Is Largely Unstructured in Solution and Functions by Forming Amyloid-Like Structures

Mackay, J. P., Matthews, J. M., Winefield, R. D., Mackay, L. G., Haverkamp, R., & Templeton, M. D. (2001) · Structure · doi:10.1016/s0969-2126(00)00559-1 · Cited by 152 · see citing works

Induction of Distinct [ URE3 ] Yeast Prion Strains

Schlumpberger, M., Prusiner, S. B., & Herskowitz, I. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.20.7035-7046.2001 · Cited by 151 · see citing works

Induction of β(A4)-amyloid in primates by injection of Alzheimer’s disease brain homogenate

Baker, H. F., Ridley, R. M., Duchen, L. W., Crow, T. J., & Bruton, C. J. (1994) · Molecular Neurobiology · doi:10.1007/bf02778005 · Cited by 149 · see citing works

Changes in the middle region of Sup35 profoundly alter the nature of epigenetic inheritance for the yeast prion [ PSI + ]

Liu, J., Sondheimer, N. J., & Lindquist, S. L. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252652099 · Cited by 140 · see citing works

Strains of [PSI+] are distinguished by their efficiencies of prion‐mediated conformational conversion

Uptain, S. M., Sawicki, G. J., Caughey, B. W., & Lindquist, S. L. (2001) · The EMBO Journal · doi:10.1093/emboj/20.22.6236 · Cited by 138 · see citing works

The Prion Curing Agent Guanidinium Chloride Specifically Inhibits ATP Hydrolysis by Hsp104

Grimminger, V., Richter, K., Imhof, A., Büchner, J., & Walter, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312403200 · Cited by 133 · see citing works

A synthetic peptide initiates Gerstmann-Sträussler-Scheinker (GSS) disease in transgenic mice

Kaneko, K., Ball, H. L., Wille, H., Zhang, H., Groth, D., Torchia, M., Tremblay, P. J., Safar, J., Prusiner, S. B., DeArmond, S. J., et al. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3386 · Cited by 133 · see citing works

A method to assess compositional bias in biological sequences and its application to prion-like glutamine/asparagine-rich domains in eukaryotic proteomes

Harrison, P. M., & Gerstein, M. (2003) · Genome biology · doi:10.1186/gb-2003-4-6-r40 · Cited by 130 · see citing works

Improvement of Nitrogen Assimilation and Fermentation Kinetics under Enological Conditions by Derepression of Alternative Nitrogen-Assimilatory Pathways in an IndustrialSaccharomyces cerevisiaeStrain

Salmon, J., & Barre, P. (1998) · Applied and Environmental Microbiology · doi:10.1128/aem.64.10.3831-3837.1998 · Cited by 128 · see citing works

Heritable activity: a prion that propagates by covalent autoactivationPreprint

Roberts, B. T., & Wickner, R. B. (2003) · Genes & Development · doi:10.1101/gad.1115803 · Cited by 126 · see citing works

Origins and kinetic consequences of diversity in Sup35 yeast prion fibers

DePace, A. H., & Weissman, J. S. (2002) · Nature Structural Biology · doi:10.1038/nsb786 · Cited by 119 · see citing works

Specificity of Class II Hsp40 Sis1 in Maintenance of Yeast Prion [RNQ+]

Lopez, N., Aron, R., & Craig, E. A. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-09-0593 · Cited by 118 · see citing works

Yeast [PSI+] “Prions” that Are Crosstransmissible and Susceptible beyond a Species Barrier through a Quasi-Prion State

Nakayashiki, T., Ebihara, K., Bannai, H., & Nakamura, Y. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00259-3 · Cited by 113 · see citing works

Tissue-Type Plasminogen Activator Is a Multiligand Cross-β Structure Receptor

Kranenburg, O., Bouma, B., Kroon-Batenburg, L. M. J., Reijerkerk, A., Wu, Y., Voest, E. E., & Gebbink, M. F. B. G. (2002) · Current Biology · doi:10.1016/s0960-9822(02)01224-1 · Cited by 110 · see citing works

Translational readthrough of the PDE2 stop codon modulates cAMP levels in Saccharomyces cerevisiae

Namy, O., Duchâteau-Nguyen, G., & Rousset, J. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02770.x · Cited by 109 · see citing works

A small reservoir of disabled ORFs in the yeast genome and its implications for the dynamics of proteome evolution

Harrison, P. M., Kumar, A., Lan, N., Echols, N., Snyder, M. P., & Gerstein, M. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5343 · Cited by 104 · see citing works

Sexual transmission of the [Het-s] prion leads to meiotic drive in Podospora anserina

Dalstra, H. J. P., Swart, K., Debets, A. J. M., Saupe, S. J., & Hoekstra, R. F. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1030058100 · Cited by 103 · see citing works

The GATA Transcription Factors GLN3 and GAT1 Link TOR to Salt Stress in Saccharomyces cerevisiae

Crespo, J. L., Daicho, K., Ushimaru, T., & Hall, M. N. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103601200 · Cited by 97 · see citing works

Separation of Scrapie Prion Infectivity from PrP Amyloid Polymers

Wille, H., Zhang, G.-F., Baldwin, M. A., Cohen, F. E., & Prusiner, S. B. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0343 · Cited by 94 · see citing works

Specificity of Prion Assembly in Vivo

Bagriantsev, S. N., & Liebman, S. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410611200 · Cited by 93 · see citing works

Derepression by Depolymerization

Qiao, F., Song, H., Kim, C. A., Sawaya, M. R., Hunter, J. B., Gingery, M., Rebay, I., Courey, A. J., & Bowie, J. U. (2004) · Cell · doi:10.1016/j.cell.2004.07.010 · Cited by 92 · see citing works

Prion protein gene polymorphisms in Saccharomyces cerevisiae

Resende, C. G., Outeiro, T. F., Sands, L., Lindquist, S. L., & Tuite, M. F. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03608.x · Cited by 88 · see citing works

Novel Non-Mendelian Determinant Involved in the Control of Translation Accuracy in Saccharomyces cerevisiae

Volkov, K. V., Aksenova, A. Y., Soom, M. J., Osipov, K. V., Svitin, A., Kurischko, C., Shkundina, I. S., Ter‐Avanesyan, M. D., Inge-Vechtomov, S. G., & Mironova, L. N. (2002) · Genetics · doi:10.1093/genetics/160.1.25 · Cited by 86 · see citing works

Hsp104 Binds to Yeast Sup35 Prion Fiber but Needs Other Factor(s) to Sever It

Inoue, Y., Taguchi, H., Kishimoto, A., & Yoshida, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408159200 · Cited by 83 · see citing works

Destabilizing Interactions Among [PSI +] and [PIN +] Yeast Prion Variants

Bradley, M. E., & Liebman, S. W. (2003) · Genetics · doi:10.1093/genetics/165.4.1675 · Cited by 83 · see citing works

Internal initiation drives the synthesis of Ure2 protein lacking the prion domain and affects [URE3] propagation in yeast cells

Komar, A. A., Lesnik, T., Cullin, C., Merrick, W. C., Trachsel, H., & Altmann, M. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg103 · Cited by 78 · see citing works

THE EVOLUTION OF THE EVOLVABILITY PROPERTIES OF THE YEAST PRION [PSI+]

Masel, J., & Bergman, A. (2003) · Evolution · doi:10.1111/j.0014-3820.2003.tb00358.x · Cited by 78 · see citing works

Protein-only inheritance in yeast: something to get [PSI+]-ched about

Serio, T. R., Lindquist, S. L., & Lindquist, S. L. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(99)01711-0 · Cited by 77 · see citing works

Prion Filament Networks in [Ure3] Cells of Saccharomyces cerevisiae

Speransky, V. V., Taylor, K. L., Edskes, H. K., Wickner, R. B., & Steven, A. C. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.6.1327 · Cited by 77 · see citing works

Nonsense-mediated decay mutants do not affect programmed −1 frameshifting

Bidou, L., Stahl, G., Hatin, I., Namy, O., Rousset, J., & Farabaugh, P. J. (2000) · RNA · doi:10.1017/s1355838200000443 · Cited by 77 · see citing works

Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding

Hattendorf, D. A., & Lindquist, S. L. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.261693199 · Cited by 66 · see citing works

Evolving evolvability

Partridge, L., & Barton, N. (2000) · Nature · doi:10.1038/35035173 · Cited by 61 · see citing works

Propagation of a Novel Cytoplasmic, Infectious and Deleterious Determinant Is Controlled by Translational Accuracy in Podospora anserina

Silar, P., Haedens, V., Rossignol, M., & Lalucque, H. (1999) · Genetics · doi:10.1093/genetics/151.1.87 · Cited by 58 · see citing works

Molecular Population Genetics and Evolution of a Prion-like Protein in Saccharomyces cerevisiae

Jensen, M. A., True, H. L., Chernoff, Y. O., & Lindquist, S. L. (2001) · Genetics · doi:10.1093/genetics/159.2.527 · Cited by 58 · see citing works

Conservation of the Prion Properties of Ure2p through Evolution

Baudin‐Baillieu, A., Fernandez‐Bellot, E., Reine, F., Coissac, É., & Cullin, C. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-01-0007 · Cited by 55 · see citing works

Induction of Protein Conformational Change in Mouse Senile Amyloidosis

Xing, Y., Nakamura, A., Korenaga, T., Guo, Z., Yao, J., Fu, X., Matsushita, T., Kogishi, K., Hosokawa, M., Kametani, F., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111570200 · Cited by 51 · see citing works

Evolution: The evolvability enigma

Brookfield, J. F. Y. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00041-0 · Cited by 48 · see citing works

The mechanisms of [URE3] prion elimination demonstrate that large aggregates of Ure2p are dead‐end products

Ripaud, L., Maillet, L., & Cullin, C. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg488 · Cited by 40 · see citing works

Analysis of yeast prion aggregates with amyloid-staining compound in vivo.

Kimura, Y., Koitabashi, S., & Fujita, T. (2003) · Cell Structure and Function · doi:10.1247/csf.28.187 · Cited by 37 · see citing works

A Transforming Principle

Fink, G. R. (2005) · Cell · doi:10.1016/j.cell.2005.01.004 · Cited by 33 · see citing works

GLUCOSAMINE RESISTANCE IN YEAST. I. A PRELIMINARY GENETIC ANALYSIS

Ball, A. J. S., Wong, D., & Elliott, J. (1976) · Genetics · doi:10.1093/genetics/84.2.311 · Cited by 32 · see citing works

Glucosamine resistance in yeast

Kunz, B. A., & Ball, A. J. S. (1977) · Molecular and General Genetics MGG · doi:10.1007/bf00264732 · Cited by 30 · see citing works

Navigating the ClpB channel to solution

Shorter, J., & Lindquist, S. L. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb0105-4 · Cited by 27 · see citing works

From Microbes to Prions

Zou, W., & Gambetti, P. L. (2005) · Cell · doi:10.1016/j.cell.2005.04.002 · Cited by 25 · see citing works

Do antiangiogenic protein fragments have amyloid properties?

Gebbink, M. F. B. G., Voest, E. E., & Reijerkerk, A. (2004) · Blood · doi:10.1182/blood-2004-02-0433 · Cited by 24 · see citing works

A non-chromosomal factor allows viability ofSchizosaccharomyces pombelacking the essential chaperone calnexin

Collin, P. J. L., Beauregard, P. B., Elagöz, A., & Rokeach, L. A. (2004) · Journal of Cell Science · doi:10.1242/jcs.00943 · Cited by 19 · see citing works

The [KIL-d] Cytoplasmic Genetic Element of Yeast Results in Epigenetic Regulation of Viral M Double-Stranded RNA Gene Expression

Tallóczy, Z., Menon, S., Neigeborn, L., & Leibowitz, M. J. (1998) · Genetics · doi:10.1093/genetics/150.1.21 · Cited by 17 · see citing works

Structural consequences of an amino acid deletion in the B1 domain of protein G

O’Neil, K. T., Bach, A., & DeGrado, W. F. (2000) · Proteins Structure Function and Bioinformatics · doi:10.1002/1097-0134(20001115)41:3 · Cited by 11 · see citing works

. . . but yeast prion offers clues about evolution

Lindquist, S. L. (2000) · Nature · doi:10.1038/35040758 · Cited by 7 · see citing works

Prion proof in progress

Edskes, H. K., & Wickner, R. B. (2004) · Nature · doi:10.1038/430977a · Cited by 7 · see citing works

Transgenerational Epigenetic Inheritance: Prevalence, Mechanisms, and Implications for the Study of Heredity and Evolution

Jablonka, E., & Raz, G. (2009) · The Quarterly Review of Biology · doi:10.1086/598822 · Cited by 1,659 · see citing works

Epigenetics and the biological definition of gene×environment interactions

Meaney, M. J. (2010) · Child Development · doi:10.1111/j.1467-8624.2009.01381.x · Cited by 1,239 · see citing works

Sex-specific, male-line transgenerational responses in humans

The ALSPAC Study Team, Pembrey, M. E., Bygren, L. O., Kaati, G., Edvinsson, S., Northstone, K., Sjöström, M., & Golding, J. (2006) · European Journal of Human Genetics · doi:10.1038/sj.ejhg.5201538 · Cited by 1,150 · see citing works

Functional amyloid – from bacteria to humans

Fowler, D. M., Koulov, A. V., Balch, W. E., & Kelly, J. W. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.03.003 · Cited by 1,052 · see citing works

Evolution, the Extended Synthesis

Pigliucci, M., & Müller, G. (2010) · The MIT Press eBooks · doi:10.7551/mitpress/9780262513678.001.0001 · Cited by 966 · see citing works

A Systematic Survey Identifies Prions and Illuminates Sequence Features of Prionogenic Proteins

Alberti, S., Halfmann, R., King, O. D., Kapila, A., & Lindquist, S. L. (2009) · Cell · doi:10.1016/j.cell.2009.02.044 · Cited by 957 · see citing works

Epigenetic and chromatin-based mechanisms in environmental stress adaptation and stress memory in plants

Lämke, J., & Bäurle, I. (2017) · Genome biology · doi:10.1186/s13059-017-1263-6 · Cited by 914 · see citing works

Stress granules as crucibles of ALS pathogenesis

Li, Y. R., King, O. D., Shorter, J., & Gitler, A. D. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201302044 · Cited by 913 · see citing works

TDP-43 Is Intrinsically Aggregation-prone, and Amyotrophic Lateral Sclerosis-linked Mutations Accelerate Aggregation and Increase Toxicity

Johnson, B. S., Snead, D., Lee, J. J., McCaffery, J. M., Shorter, J., & Gitler, A. D. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.010264 · Cited by 790 · see citing works

Nanomechanics of functional and pathological amyloid materials

Knowles, T. P. J., & Buehler, M. J. (2011) · Nature Nanotechnology · doi:10.1038/nnano.2011.102 · Cited by 782 · see citing works

Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis

Prasad, A., Bharathi, V., Sivalingam, V., Girdhar, A., & Patel, B. K. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00025 · Cited by 770 · see citing works

The molecular language of membraneless organelles

Gomes, E., & Shorter, J. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.tm118.001192 · Cited by 763 · see citing works

Cell-free Formation of RNA Granules: Bound RNAs Identify Features and Components of Cellular Assemblies

Han, T. W., Kato, M., Xie, S., Wu, L. C., Mirzaei, H., Pei, J., Chen, M., Xie, Y., Allen, J. D., Xiao, G., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.016 · Cited by 758 · see citing works

The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease

King, O. D., Gitler, A. D., & Shorter, J. (2012) · Brain Research · doi:10.1016/j.brainres.2012.01.016 · Cited by 637 · see citing works

Epigenetic Gene Regulation in the Bacterial World

Casadesús, J., & Low, D. A. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00016-06 · Cited by 635 · see citing works

Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders

Jucker, M., & Walker, L. C. (2011) · Annals of Neurology · doi:10.1002/ana.22615 · Cited by 622 · see citing works

Amyloid Fibrils as Building Blocks for Natural and Artificial Functional Materials

Knowles, T. P. J., & Mezzenga, R. (2016) · Advanced Materials · doi:10.1002/adma.201505961 · Cited by 590 · see citing works

The physical basis of how prion conformations determine strain phenotypes

Tanaka, M., Collins, S. R., Toyama, B. H., & Weissman, J. S. (2006) · Nature · doi:10.1038/nature04922 · Cited by 589 · see citing works

Decoding the Epigenetic Language of Neuronal Plasticity

Borrelli, E., Nestler, E. J., Allis, C. D., & Sassone‐Corsi, P. (2008) · Neuron · doi:10.1016/j.neuron.2008.10.012 · Cited by 529 · see citing works

Prions: Protein Aggregation and Infectious Diseases

Aguzzi, A., & Calella, A. M. (2009) · Physiological Reviews · doi:10.1152/physrev.00006.2009 · Cited by 502 · see citing works

Transgenerational response to nutrition, early life circumstances and longevity

Kaati, G., Bygren, L. O., Pembrey, M., & Sjöström, M. (2007) · European Journal of Human Genetics · doi:10.1038/sj.ejhg.5201832 · Cited by 500 · see citing works

Structural insights into a yeast prion illuminate nucleation and strain diversity

Krishnan, R., & Lindquist, S. L. (2005) · Nature · doi:10.1038/nature03679 · Cited by 470 · see citing works

Molecular Determinants and Genetic Modifiers of Aggregation and Toxicity for the ALS Disease Protein FUS/TLS

Sun, Z., Diaz, Z., Fang, X., Hart, M. P., Chesi, A., Shorter, J., & Gitler, A. D. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000614 · Cited by 448 · see citing works

The human connectome: Origins and challenges

Sporns, O. (2013) · NeuroImage · doi:10.1016/j.neuroimage.2013.03.023 · Cited by 434 · see citing works

Folding versus aggregation: Polypeptide conformations on competing pathways

Jahn, T. R., & Radford, S. E. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.05.015 · Cited by 428 · see citing works

RNA-binding proteins with prion-like domains in health and disease

Harrison, A. F., & Shorter, J. (2017) · Biochemical Journal · doi:10.1042/bcj20160499 · Cited by 415 · see citing works

Aplysia CPEB Can Form Prion-like Multimers in Sensory Neurons that Contribute to Long-Term Facilitation

Si, K., Choi, Y., White‐Grindley, E., Majumdar, A., & Kandel, E. R. (2010) · Cell · doi:10.1016/j.cell.2010.01.008 · Cited by 385 · see citing works

Fidelity at the Molecular Level: Lessons from Protein Synthesis

Zaher, H. S., & Green, R. (2009) · Cell · doi:10.1016/j.cell.2009.01.036 · Cited by 381 · see citing works

Protein homeostasis and aging in neurodegeneration

Douglas, P. M., & Dillin, A. G. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201005144 · Cited by 372 · see citing works

The Seeds of Neurodegeneration: Prion-like Spreading in ALS

Polymenidou, M., & Cleveland, D. W. (2011) · Cell · doi:10.1016/j.cell.2011.10.011 · Cited by 370 · see citing works

The Mammalian Disaggregase Machinery: Hsp110 Synergizes with Hsp70 and Hsp40 to Catalyze Protein Disaggregation and Reactivation in a Cell-Free System

Shorter, J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026319 · Cited by 340 · see citing works

Functional AmyloidsPreprint

Otzen, D. E., & Riek, R. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033860 · Cited by 332 · see citing works

Insights into prion strains and neurotoxicity

Aguzzi, A., Heikenwälder, M. F., & Polymenidou, M. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2204 · Cited by 327 · see citing works

Varieties of Living Things: Life at the Intersection of Lineage and Metabolism

Dupré, J., & O’Malley, M. A. (2009) · Philosophy and Theory in Biology · doi:10.3998/ptb.6959004.0001.003 · Cited by 323 · see citing works

FUS and TDP-43 Phases in Health and Disease

Portz, B., Lee, B. L., & Shorter, J. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.12.005 · Cited by 323 · see citing works

A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures

Mukhopadhyay, S., Krishnan, R., Lemke, E. A., Lindquist, S. L., & Deniz, A. A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611503104 · Cited by 316 · see citing works

Transgenerational epigenetic inheritance: how important is it?

Grossniklaus, U., Kelly, W. G., Ferguson‐Smith, A. C., Pembrey, M. E., & Lindquist, S. L. (2013) · Nature Reviews Genetics · doi:10.1038/nrg3435 · Cited by 301 · see citing works

A Diversity of Assembly Mechanisms of a Generic Amyloid Fold

Eichner, T., & Radford, S. E. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.05.012 · Cited by 293 · see citing works

Prion-like disorders: blurring the divide between transmissibility and infectivity

Cushman-Nick, M., Johnson, B. S., King, O. D., Gitler, A. D., & Shorter, J. (2010) · Journal of Cell Science · doi:10.1242/jcs.051672 · Cited by 288 · see citing works

Transgenerational developmental programming

Aiken, C., & Ozanne, S. E. (2013) · Human Reproduction Update · doi:10.1093/humupd/dmt043 · Cited by 283 · see citing works

Hsp104 and ClpB: protein disaggregating machines

Doyle, S. M., & Wickner, S. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2008.09.010 · Cited by 283 · see citing works

Prion Switching in Response to Environmental Stress

Tyedmers, J., Madariaga, M. L. L., & Lindquist, S. L. (2008) · PLoS Biology · doi:10.1371/journal.pbio.0060294 · Cited by 270 · see citing works

Molecular mechanisms for protein-encoded inheritance

Wiltzius, J. J. W., Landau, M., Nelson, R. A., Sawaya, M. R., Apostol, M. I., Goldschmidt, L., Soriaga, A. B., Cascio, D., Rajashankar, K. R., & Eisenberg, D. S. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1643 · Cited by 260 · see citing works

Protein rescue from aggregates by powerful molecular chaperone machines

Doyle, S. M., Genest, O., & Wickner, S. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3660 · Cited by 250 · see citing works

The cellular prion protein mediates neurotoxic signalling of β‐sheet‐rich conformers independent of prion replication

Resenberger, U. K., Harmeier, A., Woerner, A. C., Goodman, J. L., Müller, V., Krishnan, R., Vabulas, R. M., Kretzschmar, H. A., Lindquist, S. L., Hartl, F. U., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.86 · Cited by 244 · see citing works

Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates

Malinovska, L., Kroschwald, S., Munder, M. C., Richter, D., & Alberti, S. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-03-0194 · Cited by 221 · see citing works

Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity

Nekooki-Machida, Y., Kurosawa, M., Nukina, N., Ito, K., Oda, T., & Tanaka, M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812083106 · Cited by 218 · see citing works

Conceptual Evolution of Cell Signaling

Nair, A., Chauhan, P. S., Saha, B., & Kubatzky, K. F. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20133292 · Cited by 218 · see citing works

Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation

Winkler, J., Tyedmers, J., Bukau, B., & Mogk, A. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201201074 · Cited by 216 · see citing works

Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative disease

March, Z. M., King, O. D., & Shorter, J. (2016) · Brain Research · doi:10.1016/j.brainres.2016.02.037 · Cited by 215 · see citing works

Prion-like low-complexity sequences: Key regulators of protein solubility and phase behavior

Franzmann, T. M., & Alberti, S. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.tm118.001190 · Cited by 215 · see citing works

Intrinsically Disordered Proteins Drive Emergence and Inheritance of Biological Traits

Chakrabortee, S., Byers, J. S., Jones, S. K., Garcia, D. M., Bhullar, B., Chang, A., She, R., Lee, L. R., Fremin, B. J., Lindquist, S. L., et al. (2016) · Cell · doi:10.1016/j.cell.2016.09.017 · Cited by 205 · see citing works

Destruction or Potentiation of Different Prions Catalyzed by Similar Hsp104 Remodeling Activities

Shorter, J., & Lindquist, S. L. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.05.042 · Cited by 198 · see citing works

In Vitro Polymerization of a Functional Escherichia coli Amyloid Protein

Wang, X., Smith, D. R., Jones, J. W. M., & Chapman, M. R. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609228200 · Cited by 193 · see citing works

Hsp104 antagonizes α-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease

Bianco, C. L., Shorter, J., Régulier, E., Lashuel, H. A., Iwatsubo, T., Lindquist, S. L., & Aebischer, P. (2008) · Journal of Clinical Investigation · doi:10.1172/jci35781 · Cited by 189 · see citing works

Cryo-EM structure of a neuronal functional amyloid implicated in memory persistence in Drosophila

Hervás, R., Rau, M., Park, Y., Zhang, W., Murzin, A. G., Fitzpatrick, J. A. J., Scheres, S. H. W., & Si, K. (2020) · Science · doi:10.1126/science.aba3526 · Cited by 189 · see citing works

Protein disorder, prion propensities, and self-organizing macromolecular collectives

Malinovska, L., Kroschwald, S., & Alberti, S. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2013.01.003 · Cited by 185 · see citing works

Amyloid-based nanosensors and nanodevices

Hauser, C. A. E., Maurer‐Stroh, S., & Martins, I. C. (2014) · Chemical Society Reviews · doi:10.1039/c4cs00082j · Cited by 185 · see citing works

Luminidependens (LD) is an Arabidopsis protein with prion behavior

Chakrabortee, S., Kayatekin, C., Newby, G. A., Mendillo, M. L., Lancaster, A. K., & Lindquist, S. L. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1604478113 · Cited by 184 · see citing works

Chromatin‐based mechanisms of temperature memory in plants

Friedrich, T., Faivre, L., Bäurle, I., & Schubert, D. (2019) · Plant, Cell &amp; Environment · doi:10.1111/pce.13373 · Cited by 182 · see citing works

Amyloid assembly and disassembly

Chuang, E., Hori, A. M., Hesketh, C. D., & Shorter, J. (2018) · Journal of Cell Science · doi:10.1242/jcs.189928 · Cited by 182 · see citing works

Protein Homeostasis and the Phenotypic Manifestation of Genetic Diversity: Principles and Mechanisms

Jarosz, D. F., Taipale, M., & Lindquist, S. (2010) · Annual Review of Genetics · doi:10.1146/annurev.genet.40.110405.090412 · Cited by 179 · see citing works

Solid-State NMR Study of Amyloid Nanocrystals and Fibrils Formed by the Peptide GNNQQNY from Yeast Prion Protein Sup35p

van der Wel, P. C. A., Lewandowski, J. R., & Griffin, R. G. (2007) · Journal of the American Chemical Society · doi:10.1021/ja068633m · Cited by 179 · see citing works

Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions

Shorter, J., & Lindquist, S. L. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.194 · Cited by 178 · see citing works

Small Heat Shock Proteins Potentiate Amyloid Dissolution by Protein Disaggregases from Yeast and Humans

Duennwald, M. L., Echeverria, A., & Shorter, J. (2012) · PLoS Biology · doi:10.1371/journal.pbio.1001346 · Cited by 178 · see citing works

Suicidal [ PSI + ] is a lethal yeast prion

McGlinchey, R. P., Kryndushkin, D. S., & Wickner, R. B. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102762108 · Cited by 177 · see citing works

Protein misfolding and disease: from the test tube to the organism

Luheshi, L. M., Crowther, D. C., & Dobson, C. M. (2008) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2008.02.011 · Cited by 174 · see citing works

Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregation

Mogk, A., Kummer, E., & Bukau, B. (2015) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2015.00022 · Cited by 173 · see citing works

Operational Plasticity Enables Hsp104 to Disaggregate Diverse Amyloid and Nonamyloid Clients

DeSantis, M. E., Leung, E. H., Sweeny, E. A., Jackrel, M. E., Cushman-Nick, M., Neuhaus‐Follini, A., Vashist, S., Sochor, M., Knight, M. N., & Shorter, J. (2012) · Cell · doi:10.1016/j.cell.2012.09.038 · Cited by 173 · see citing works

Soft inheritance: challenging the modern synthesis

Jablonka, E., & Lamb, M. J. (2008) · Genetics and Molecular Biology · doi:10.1590/s1415-47572008000300001 · Cited by 173 · see citing works

Higher-order organization of biomolecular condensates

Fare, C. M., Villani, A., Drake, L. E., & Shorter, J. (2021) · Open Biology · doi:10.1098/rsob.210137 · Cited by 170 · see citing works

The sour side of neurodegenerative disorders: the effects of protein glycation

Miranda, H. V., & Outeiro, T. F. (2009) · The Journal of Pathology · doi:10.1002/path.2682 · Cited by 168 · see citing works

Chaperone-dependent amyloid assembly protects cells from prion toxicity

Douglas, P. M., Treusch, S., Ren, H.-Y., Halfmann, R., Duennwald, M. L., Lindquist, S. L., & Cyr, D. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802593105 · Cited by 168 · see citing works

The role of advanced glycation end products in various types of neurodegenerative disease: a therapeutic approach

Salahuddin, P., Rabbani, G., & Khan, R. H. (2014) · Cellular & Molecular Biology Letters · doi:10.2478/s11658-014-0205-5 · Cited by 167 · see citing works

A heritable switch in carbon source utilization driven by an unusual yeast prionPreprint

Brown, J. C. S., & Lindquist, S. L. (2009) · Genes & Development · doi:10.1101/gad.1839109 · Cited by 166 · see citing works

Prions, protein homeostasis, and phenotypic diversity

Halfmann, R., Alberti, S., & Lindquist, S. L. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.12.003 · Cited by 164 · see citing works

RNA-binding proteins with prion-like domains in ALS and FTLD-U

Gitler, A. D., & Shorter, J. (2011) · Prion · doi:10.4161/pri.5.3.17230 · Cited by 161 · see citing works

Amyloidogenesis of Tau protein

Niżyński, B., Dzwolak, W., & Nieznański, K. (2017) · Protein Science · doi:10.1002/pro.3275 · Cited by 157 · see citing works

Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity

Doyle, S. M., Shorter, J., Žółkiewski, M., Hoskins, J. R., Lindquist, S. L., & Wickner, S. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1198 · Cited by 156 · see citing works

Autocatalysis: Kinetics, Mechanisms and Design

Hanopolskyi, A. I., Smaliak, V. A., Novichkov, A. I., & Semenov, S. N. (2020) · ChemSystemsChem · doi:10.1002/syst.202000026 · Cited by 156 · see citing works

A network of protein interactions determines polyglutamine toxicity

Duennwald, M. L., Jagadish, S., Giorgini, F., Muchowski, P. J., & Lindquist, S. L. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604548103 · Cited by 151 · see citing works

Cross-Kingdom Chemical Communication Drives a Heritable, Mutually Beneficial Prion-Based Transformation of Metabolism

Jarosz, D. F., Brown, J. C. S., Walker, G. A., Datta, M. S., Ung, W. L., Lancaster, A. K., Rotem, A., Chang, A., Newby, G. A., Weitz, D. A., et al. (2014) · Cell · doi:10.1016/j.cell.2014.07.025 · Cited by 146 · see citing works

The TDP‐43 N‐terminal domain structure at high resolution

Mompeán, M., Romano, V. C., Pantoja‐Uceda, D., Stuani, C., Baralle, F. E., Buratti, E., & Laurents, D. V. (2016) · FEBS Journal · doi:10.1111/febs.13651 · Cited by 146 · see citing works

Human Pat1b Connects Deadenylation with mRNA Decapping and Controls the Assembly of Processing Bodies

Ozgur, S., Chekulaeva, M., & Stoecklin, G. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00429-10 · Cited by 143 · see citing works

Protein Microgels from Amyloid Fibril Networks

Shimanovich, U., Efimov, I., Mason, T. G., Flagmeier, P., Buell, A. K., Gedanken, A., Linse, S. S., Åkerfeldt, K. S., Dobson, C. M., Weitz, D. A., et al. (2014) · ACS Nano · doi:10.1021/nn504869d · Cited by 142 · see citing works

Prion recognition elements govern nucleation, strain specificity and species barriers

Tessier, P. M., & Lindquist, S. L. (2007) · Nature · doi:10.1038/nature05848 · Cited by 137 · see citing works

New Insights into Prion Structure and Toxicity

Harris, D. A., & True, H. L. (2006) · Neuron · doi:10.1016/j.neuron.2006.04.020 · Cited by 137 · see citing works

The Molecular Basis of Functional Bacterial Amyloid Polymerization and Nucleation

Wang, X., Hammer, N. D., & Chapman, M. R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800466200 · Cited by 135 · see citing works

Amyloid deposits: Protection against toxic protein species?

Treusch, S., Cyr, D., & Lindquist, S. L. (2009) · Cell Cycle · doi:10.4161/cc.8.11.8503 · Cited by 134 · see citing works

The role of copper ions in pathophysiology and fluorescent sensors for the detection thereof

Verwilst, P., Sunwoo, K., & Kim, J. S. (2015) · Chemical Communications · doi:10.1039/c4cc10366a · Cited by 130 · see citing works

Conserved features of intermediates in amyloid assembly determine their benign or toxic states

Krishnan, R., Goodman, J. L., Mukhopadhyay, S., Pacheco, C. D., Lemke, E. A., Deniz, A. A., & Lindquist, S. L. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1209527109 · Cited by 130 · see citing works

Protein Denaturation and Aggregation

Meredith, S. C. (2006) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1363.030 · Cited by 129 · see citing works

Observation of Highly Flexible Residues in Amyloid Fibrils of the HET-s Prion

Siemer, A. B., Arnold, A. A., Ritter, C., Westfeld, T., Ernst, M., Riek, R., & Meier, B. H. (2006) · Journal of the American Chemical Society · doi:10.1021/ja063639x · Cited by 127 · see citing works

The CPEB3 Protein Is a Functional Prion that Interacts with the Actin Cytoskeleton

Stephan, J. S., Fioriti, L., Lamba, N., Colnaghi, L., Karl, K. A., Derkatch, I. L., & Kandel, E. R. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.04.060 · Cited by 126 · see citing works

Chaperone networks in protein disaggregation and prion propagation

Winkler, J., Tyedmers, J., Bukau, B., & Mogk, A. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.05.002 · Cited by 126 · see citing works

Epigenetic Contribution to Covariance Between Relatives

Tal, O., Kisdi, É., & Jablonka, E. (2010) · Genetics · doi:10.1534/genetics.109.112466 · Cited by 125 · see citing works

The emerging concept of functional amyloid

Maury, C. P. J. (2009) · Journal of Internal Medicine · doi:10.1111/j.1365-2796.2008.02068.x · Cited by 124 · see citing works

An Evolutionarily Conserved Prion-like Element Converts Wild Fungi from Metabolic Specialists to Generalists

Jarosz, D. F., Lancaster, A. K., Brown, J. C. S., & Lindquist, S. L. (2014) · Cell · doi:10.1016/j.cell.2014.07.024 · Cited by 124 · see citing works

Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentation

Tyedmers, J., Treusch, S., Dong, J., McCaffery, J. M., Bevis, B. J., & Lindquist, S. L. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003895107 · Cited by 120 · see citing works

Maintenance of abiotic stress memory in plants: Lessons learned from heat acclimation

Charng, Y., Mitra, S., & Yu, S.-J. (2022) · The Plant Cell · doi:10.1093/plcell/koac313 · Cited by 119 · see citing works

Prions: an evolutionary perspective.

Ogayar, A., & Sánchez‐Pérez, M. (1998) · PubMed · Cited by 16 · see citing works

The shape of things to come: structural insights into how prion proteins encipher heritable information

Telling, G. C. (2022) · Nature Communications · doi:10.1038/s41467-022-31460-8 · Cited by 19 · see citing works

Prion-induced heritable states in Caenorhabditis elegansPreprint

Ilbay, O., Zabinsky, R. A., Lozanoski, T. M., Jarosz, D. F., & Fire, A. Z. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.27.753494

Prions and Memory

Ewert, J.-P. (2013) · Springer eBooks · doi:10.1007/978-1-4020-8265-8_200153

Herencia y memoria: ¿un nuevo rol para los priones?

Gualdrón, A. J., & Ávila, V. Á. (2008) · Medunab