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 5,221

Protein folding and misfolding

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

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

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

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

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 2,209

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 2,107

Why are ?natively unfolded? proteins unstructured under physiologic conditions?

Uversky, V. N., Gillespie, J. R., & Fink, A. L. (2000) · Proteins Structure Function and Bioinformatics · doi:10.1002/1097-0134(20001115)41:3 · Cited by 2,097

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

AN UNSOLVED PROBLEM OF BIOLOGY

(1953) · The Medical Journal of Australia · doi:10.5694/j.1326-5377.1953.tb84985.x · Cited by 1,806

Shaping the learning curve: epigenetic dynamics in neural plasticity

Bronfman, Z. Z., Ginsburg, S., & Jablonka, E. (2014) · Frontiers in Integrative Neuroscience · doi:10.3389/fnint.2014.00055 · Cited by 24

Purification of Hsp104, a Protein Disaggregase

Sweeny, E. A., DeSantis, M. E., & Shorter, J. (2011) · Journal of Visualized Experiments · doi:10.3791/3190 · Cited by 23

Induction of ligand-specific PrPCsignaling in human neuronal cells

Arsenault, R. J., Li, Y., Potter, A. A., Griebel, P. J., KUSALIK, A. J., & Napper, S. (2012) · Prion · doi:10.4161/pri.21914 · Cited by 23

Alcohol oxidase (AOX1) from Pichia pastoris is a novel inhibitor of prion propagation and a potential ATPase

Zhang, H., Loovers, H. M., Xu, L., Wang, M., Rowling, P. J. E., Itzhaki, L. S., Gong, W., Zhou, J., Jones, G. W., & Perrett, S. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06557.x · Cited by 23

Protein misfolding in Dictyostelium: Using a freak of nature to gain insight into a universal problem

Malinovska, L., & Alberti, S. (2015) · Prion · doi:10.1080/19336896.2015.1099799 · Cited by 23

Epigenetics of Filamentous Fungi

Smith, K., Phatale, P. A., Bredeweg, E., Connolly, L., Pomraning, K., & Freitag, M. (2012) · Wiley-VCH eBooks · doi:10.1002/3527600906.mcb.201100035 · Cited by 24

In planta expression of human polyQ-expanded huntingtin fragment reveals mechanisms to prevent disease-related protein aggregation

Llamas, E., Koyuncu, S., Lee, H. J., Wehrmann, M., Gutiérrez-García, R., Dunken, N., Charura, N., Torres‐Montilla, S., Schlimgen, E., Mandel, A. M., et al. (2023) · Nature Aging · doi:10.1038/s43587-023-00502-1 · Cited by 22

Genetic Basis of Hidden Phenotypic Variation Revealed by Increased Translational Readthrough in Yeast

Torabi, N., & Kruglyak, L. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002546 · Cited by 22

Variants in SUP45 and TRM10 Underlie Natural Variation in Translation Termination Efficiency in Saccharomyces cerevisiae

Torabi, N., & Kruglyak, L. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002211 · Cited by 22

Manipulating the Prion Protein Gene Sequence and Expression Levels with CRISPR/Cas9

Kaczmarczyk, L., Mende, Y., Zevnik, B., & Jackson, W. S. (2016) · PLoS ONE · doi:10.1371/journal.pone.0154604 · Cited by 22

The prion-like nature of amyotrophic lateral sclerosis

McAlary, L., Yerbury, J. J., & Cashman, N. R. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.07.002 · Cited by 21

Prion-like proteins as epigenetic devices of stress adaptation

Oamen, H. P., Lau, Y., & Caudron, F. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.112262 · Cited by 21

A prion accelerates proliferation at the expense of lifespan

Garcia, D. M., Campbell, E., Jakobson, C. M., Tsuchiya, M., (23811802), E. A. S., DiNardo, A. L., Kaeberlein, M. R., & Jarosz, D. F. (2021) · eLife · doi:10.7554/elife.60917 · Cited by 25

Polyglutamine misfolding in yeast: Toxic and protective aggregation

Duennwald, M. L. (2011) · Prion · doi:10.4161/pri.18071 · Cited by 22

Protein homeostasis in neurons and its pathological alterations

Malgaroli, A., Vallar, L., & Zimarino, V. (2006) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2006.05.009 · Cited by 22

A Small, Glutamine-Free Domain Propagates the [SWI+] Prion in Budding Yeast

Crow, E. T., Du, Z., & Li, L. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05338-11 · Cited by 21

The developmental construction of heredity

Jablonka, E. (2007) · Developmental Psychobiology · doi:10.1002/dev.20260 · Cited by 21

Temperature Dependence of the Aggregation Kinetics of Sup35 and Ure2p Yeast Prions

Sabaté, R., Villar‐Piqué, A., Espargaró, A., & Ventura, S. (2011) · Biomacromolecules · doi:10.1021/bm201527m · Cited by 20

Countering amyloid polymorphism and drug resistance with minimal drug cocktails

Duennwald, M. L., & Shorter, J. (2010) · Prion · doi:10.4161/pri.4.4.13597 · Cited by 20

MED15 prion-like domain forms a coiled-coil responsible for its amyloid conversion and propagation

Batlle, C., Calvo, I., Iglesias, V., Lynch, C. J., Gil-García, M., Serrano, M., & Ventura, S. (2021) · Communications Biology · doi:10.1038/s42003-021-01930-8 · Cited by 20

Nanoimaging for prion related diseases

Krasnoslobodtsev, A. V., Portillo, A. M., Deckert‐Gaudig, T., Deckert, V., & Lyubchenko, Y. L. (2010) · Prion · doi:10.4161/pri.4.4.13125 · Cited by 20

Prion protein as a mediator of synaptic transmission

Steinert, J. R. (2015) · Communicative & Integrative Biology · doi:10.1080/19420889.2015.1063753 · Cited by 20

Cryo-EM structures of functional and pathological amyloid ribonucleoprotein assemblies

García‐Pardo, J., & Ventura, S. (2023) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2023.10.005 · Cited by 19

Aggregation of Human S100A8 and S100A9 Amyloidogenic Proteins Perturbs Proteostasis in a Yeast Model

Eremenko, E., Ben‐Zvi, A., Morozova‐Roche, L. A., & Raveh, D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0058218 · Cited by 19

Genetically engineered protein nanowires: unique features in site-specific functionalization and multi-dimensional self-assembly

Maeda, Y., & Matsui, H. (2012) · Soft Matter · doi:10.1039/c2sm25352f · Cited by 19

More than just trash bins? Potential roles for extracellular vesicles in the vertical and horizontal transmission of yeast prions

Kabani, M., & Melki, R. (2015) · Current Genetics · doi:10.1007/s00294-015-0534-6 · Cited by 19

Nanoscale Fluorescence Imaging of Single Amyloid Fibrils

Dalal, V., Bhattacharya, M., Narang, D., Sharma, P. K., & Mukhopadhyay, S. (2012) · The Journal of Physical Chemistry Letters · doi:10.1021/jz300687f · Cited by 19

Amyloid fibrils embodying distinctive yeast prion phenotypes exhibit diverse morphologies

Ghosh, R., Dong, J., Wall, J., & Frederick, K. K. (2018) · FEMS Yeast Research · doi:10.1093/femsyr/foy059 · Cited by 19

Microbial Prions: Dawn of a New Era

Levkovich, S. A., Rencus‐Lazar, S., Gazit, E., & Bar‐Yosef, D. L. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.12.006 · Cited by 19

Single-particle tracking of quantum dot-conjugated prion proteins inside yeast cells

Tsuji, T., Kawai‐Noma, S., Pack, C., Terajima, H., Yajima, J., Nishizaka, T., Kinjo, M., & Taguchi, H. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.01.083 · Cited by 19

Drosophila GAGA factor polyglutamine domains exhibit prion-like behavior

Tariq, M., Wegrzyn, R. D., Anwar, S., Bukau, B., & Paro, R. (2013) · BMC Genomics · doi:10.1186/1471-2164-14-374 · Cited by 19

The [URE3] Prion in Candida

Edskes, H. K., & Wickner, R. B. (2013) · Eukaryotic Cell · doi:10.1128/ec.00015-13 · Cited by 18

Recent advances in nanofibrous assemblies based on β‐sheet‐forming peptides for biomedical applications

Waku, T., & Tanaka, N. (2016) · Polymer International · doi:10.1002/pi.5195 · Cited by 18

Mass Determination of Entire Amyloid Fibrils by Using Mass Spectrometry

Doussineau, T., Mathevon, C., Altamura, L., Vendrely, C., Dugourd, P., Forge, V., & Antoine, R. (2015) · Angewandte Chemie · doi:10.1002/ange.201508995 · Cited by 18

Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria

Macedo, B., Sant’Anna, R., Navarro, S., Cordeiro, Y., & Ventura, S. (2015) · Microbial Cell Factories · doi:10.1186/s12934-015-0361-y · Cited by 18

Automated, Microscopic Measurement of Fibrinaloid Microclots and Their Degradation by Nattokinase, the Main Natto Protease

Grixti, J. M., Theron, C. W., Salcedo-Sora, J. E., Pretorius, E., & Kell, D. B. (2024) · Journal of Experimental and Clinical Application of Chinese Medicine · doi:10.62767/jecacm504.6557 · Cited by 17

Cross‐Talk Between the Octarepeat Domain and the Fifth Binding Site of Prion Protein Driven by the Interaction of Copper(II) with the N‐terminus

Natale, G. D., Turi, I., Pappalardo, G., Sóvágó, I., & Rizzarelli, E. (2015) · Chemistry - A European Journal · doi:10.1002/chem.201405502 · Cited by 17

Alternatively folded proteins with unexpected beneficial functions

Min, S., Meehan, J., Sullivan, L. M., Harte, N. P., Xie, Y., Davey, G. P., Svanborg, C., Brodkorb, A., & Mok, K. H. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120029 · Cited by 17

Prion protein/protein interactions: fusion with yeast Sup35p‐NM modulates cytosolic PrP aggregation in mammalian cells

Nussbaum-Krammer, C. I., Suhre, M. H., Kremmer, E., Diemer, C., Hess, S., Schätzl, H. M., Scheibel, T., & Vorberg, I. M. (2007) · The FASEB Journal · doi:10.1096/fj.07-8733com · Cited by 17

DNA methylation by three Type I restriction modification systems of Escherichia coli does not influence gene regulation of the host bacterium

Mehershahi, K. S., & Chen, S. L. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab530 · Cited by 16

Radically Different Amyloid Conformations Dictate the Seeding Specificity of a Chimeric Sup35 Prion

Foo, C. K., Ohhashi, Y., Kelly, M. J. S., Tanaka, M., & Weissman, J. S. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.02.025 · Cited by 16

Yeast as a Platform to Explore Polyglutamine Toxicity and Aggregation

Duennwald, M. L. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-438-8_11 · Cited by 16

Amyloids in Site-Specific Autoimmune Reactions and Inflammatory Responses

Huang, Y., Hong, X., Shen, J. X., Geng, L.-J., Pan, Y.-H., Ling, W., & Zhao, H. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02980 · Cited by 16

Using palladium nanoparticle-decorated lysozyme amyloid fibrils to catalyze the reduction of methylene blue

Wang, Y.-C., Lai, Y.-R., Wu, J. W., Wang, S. S. ‐., & Lin, K. (2021) · Journal of the Taiwan Institute of Chemical Engineers · doi:10.1016/j.jtice.2020.12.030 · Cited by 16

A novel neurobehavioral framework of the effects of positive early postnatal experience on incentive and consummatory reward sensitivity

Fu, Y., & Depue, R. A. (2019) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2019.09.026 · Cited by 18

Protein Microgels from Amyloid Fibril Networks

Roode, L. W. Y., Shimanovich, U., Wu, S., Perrett, S., & Knowles, T. P. J. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-9791-2_7 · Cited by 16

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

Dupré, J., & O’Malley, M. A. (2013) · History, philosophy and theory of the life sciences · doi:10.1007/978-94-007-2445-7_13 · Cited by 16

Self-organized computation in the far-from-equilibrium cell

England, J. L. (2022) · Biophysics Reviews · doi:10.1063/5.0103151 · Cited by 15

Dicer and Hsp104 Function in a Negative Feedback Loop to Confer Robustness to Environmental Stress

Oberti, D., Biasini, A., Kirschmann, M., Genoud, C., Stunnenberg, R., Shimada, Y., & Bühler, M. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.12.006 · Cited by 16

Phased Fiber Growth in a Peptide Conjugate: Aggregation and Disaggregation Studies

Ghosh, S., & Verma, S. K. (2007) · The Journal of Physical Chemistry B · doi:10.1021/jp066546a · Cited by 15

Suppression of Polyglutamine Toxicity by the Yeast Sup35 Prion Domain in Drosophila

Li, L.-B., Xu, K., & Bonini, N. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705211200 · Cited by 15

A prolonged chronological lifespan is an unexpected benefit of the [PSI+] prion in yeast

Wang, K., Melki, R., & Kabani, M. (2017) · PLoS ONE · doi:10.1371/journal.pone.0184905 · Cited by 15

Molecular Mechanisms for the Initiation and Maintenance of Long-Term Memory Storage

Puthanveettil, S. V., & Kandel, E. R. (2010) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-16602-0_13 · Cited by 15

RNA Reigns in Neurons

Tiedge, H. (2005) · Neuron · doi:10.1016/j.neuron.2005.09.002 · Cited by 15

Repeats are one of the main characteristics of RNA-binding proteins with prion-like domains

Galzitskaya, O. V. (2015) · Molecular BioSystems · doi:10.1039/c5mb00273g · Cited by 15

Environment-transformable sequence–structure relationship: a general mechanism for proteotoxicity

Song, J. (2017) · Biophysical Reviews · doi:10.1007/s12551-017-0369-0 · Cited by 13

A comparative approach to the principal mechanisms of different memory systems

Rensing, L., Koch, M., & Becker, A. (2009) · Die Naturwissenschaften · doi:10.1007/s00114-009-0591-0 · Cited by 13

Plasmid Segregation: A New Class of Cytoskeletal Proteins Emerges

Gitai, Z. (2006) · Current Biology · doi:10.1016/j.cub.2006.02.007 · Cited by 13

Monitoring polyglutamine toxicity in yeast

Duennwald, M. L. (2010) · Methods · doi:10.1016/j.ymeth.2010.12.001 · Cited by 13

Prion protein insertional mutations increase aggregation propensity but not fiber stability

Kalastavadi, T., & True, H. L. (2008) · BMC Biochemistry · doi:10.1186/1471-2091-9-7 · Cited by 13

Proteolysis suppresses spontaneous prion generation in yeast

Okamoto, A., Hosoda, N., Tanaka, A., Newnam, G. P., Chernoff, Y. O., & Hoshino, S.-I. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.811323 · Cited by 12

Growth-Regulated Hsp70 Phosphorylation Regulates Stress Responses and Prion Maintenance

Kao, C.-H., Ryu, S. W., Kim, M. J., Wen, X., Wimalarathne, O., & Paull, T. T. (2020) · Molecular and Cellular Biology · doi:10.1128/mcb.00628-19 · Cited by 12

Why death and aging ? All memories are imperfect

Miller, W. B., Baluška, F., Reber, A. S., & Slijepčević, P. (2024) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2024.02.001 · Cited by 12

Use of yeast as a system to study amyloid toxicity

Summers, D. W., & Cyr, D. (2010) · Methods · doi:10.1016/j.ymeth.2010.11.007 · Cited by 12

Disease Transmission by Misfolded Prion-Protein Isoforms, Prion-Like Amyloids, Functional Amyloids and the Central Dogma

Daus, M. L. (2016) · Biology · doi:10.3390/biology5010002 · Cited by 12

Impact of the [GAR+] Prion on Fermentation and Bacterial Community Composition withSaccharomyces cerevisiaeUCD932

Walker, G. A., Hjelmeland, A. K., Bokulich, N. A., Mills, D. A., Ebeler, S. E., & Bisson, L. F. (2016) · American Journal of Enology and Viticulture · doi:10.5344/ajev.2016.15092 · Cited by 12

Anti-prion and α-Synuclein Aggregation Inhibitory Sterols from the Sponge Lamellodysidea cf. chlorea

Jennings, L. K., Prebble, D. W., Xu, M., Ekins, M., Munn, A. L., Mellick, G. D., & Carroll, A. R. (2020) · Journal of Natural Products · doi:10.1021/acs.jnatprod.0c01168 · Cited by 12

Molecular Determinants of Liquid Demixing and Amyloidogenesis in Human CPEB3Preprint

de Mingo, D. R., López-García, P., Hervás, R., Laurents, D. V., & Carrión‐Vázquez, M. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.02.129783 · Cited by 12

Structural insights into functional regulation of the human CPEB3 prion by an amyloid-forming segment

Flores, M. D., Sawaya, M. R., Boyer, D. R., Zink, S., Tovmasyan, S., Saucedo, A., Richards, L. S., Zee, C.-T., Cardenas, J., Fioriti, L., et al. (2025) · Structure · doi:10.1016/j.str.2025.05.007 · Cited by 11

Impact of N-glycosylation site variants during human PrP aggregation and fibril nucleation

Mishra, R., Elgland, M., Begum, A., Fyrner, T., Konradsson, P., Nyström, S., & Hammarström, P. (2019) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.03.010 · Cited by 11

Self-replicating protein conformations and information transfer: The adaptive β-sheet model

Maury, C. P. J. (2008) · Bioscience hypotheses · doi:10.1016/j.bihy.2008.02.010 · Cited by 11

Prion–like Proteins in Plants: Key Regulators of Development and Environmental Adaptation via Phase Separation

Wu, P., & Li, Y. (2024) · Plants · doi:10.3390/plants13182666 · Cited by 11

Prion Protein Signaling in the Nervous System—A Review and Perspective

Liebert, A. D., Bicknell, B. T., & Adams, R. D. (2014) · Signal Transduction Insights · doi:10.4137/sti.s12319 · Cited by 11

A Fluorescent Mutant of the NM Domain of the Yeast Prion Sup35 Provides Insight into Fibril Formation and Stability

Palhano, F. L., Rocha, C. B., Bernardino, A. J. M., Weissmüller, G., Masuda, C. A., Montero-Lomelı́, M., Gomes, A. M., Chien, P., Fernandes, P. M. B., & Foguel, D. (2009) · Biochemistry · doi:10.1021/bi9000276 · Cited by 10

The Role of the Prion Protein in the Molecular Basis for Synaptic Plasticity and Nervous System Development

Encalada, S. E., Moya, K. L., Lehmann, S., & Zahn, R. (2007) · Journal of Molecular Neuroscience · doi:10.1007/s12031-007-0011-x · Cited by 10

In Search of Darwin's Imaginary Gemmules

Liu, Y. (2018) · Advances in genetics · doi:10.1016/bs.adgen.2018.05.004 · Cited by 9

Biomimetic and bioinspired design of collective systems

Schmickl, T., Crailsheim, K., Deneubourg, J., & Halloy, J. (2011) · VU Research Portal · doi:10.4032/9789814364119 · Cited by 9

Patterns of [PSI+] aggregation allow insights into cellular organization of yeast prion aggregates

Tyedmers, J. (2012) · Prion · doi:10.4161/pri.18986 · Cited by 9

Yeast prions, mammalian amyloidoses, and the problem of proteomic networks

Galkin, A. P., Mironova, L. N., Zhouravleva, G. A., & Inge-Vechtomov, S. G. (2006) · Russian Journal of Genetics · doi:10.1134/s1022795406110135 · Cited by 9

Epigenetics Connects the Genome to Its Environment

Bressan, R. A., Zhu, J., Oosten, M. J. V., Maggio, A., Bohnert, H. J., & Chinnusamy, V. (2014) · Wiley eBooks · doi:10.1002/9781118916865.ch03 · Cited by 9

Bend or break: how biochemically versatile molecules enable metabolic division of labor in clonal microbial communities

Varahan, S., & Laxman, S. (2021) · Genetics · doi:10.1093/genetics/iyab109 · Cited by 8

Les prions

Crozet, C., & Lehmann, S. (2007) · médecine/sciences · doi:10.1051/medsci/200723121148 · Cited by 8

Probing the drivers of Staphylococcus aureus biofilm protein amyloidogenesis and disrupting biofilms with engineered protein disaggregases

Howard, M. K., Miller, K. R., Sohn, B. S., Ryan, J. J., Xu, A., & Jackrel, M. E. (2023) · mBio · doi:10.1128/mbio.00587-23 · Cited by 8

Effects of Pulsed Electric Fields on Yeast with Prions and the Structure of Amyloid Fibrils

Jurgelevičiūtė, J., Bičkovas, N., Sakalauskas, A., Novickij, V., Smirnovas, V., & Lastauskienė, E. (2021) · Applied Sciences · doi:10.3390/app11062684 · Cited by 7

Sycosterol A, an α-Synuclein Inhibitory Sterol from the Australian Ascidian Sycozoa cerebriformis

Prebble, D. W., Xu, M., Mellick, G. D., & Carroll, A. R. (2021) · Journal of Natural Products · doi:10.1021/acs.jnatprod.1c00768 · Cited by 7

Nucleotide-Dependent Control of Internal Strains in Ring-Shaped AAA+ Motors

Hwang, W., & Lang, M. J. (2012) · Cellular and Molecular Bioengineering · doi:10.1007/s12195-012-0264-5 · Cited by 7

[KIL-d] Protein Element Confers Antiviral Activity via Catastrophic Viral Mutagenesis

Suzuki, G., Weissman, J. S., & Tanaka, M. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.10.020 · Cited by 7

Advances in AFM Imaging Applications for Characterizing the Biophysical Properties of Amyloid Fibrils

Lee, W., Lee, H., Lee, G., & Yoon, D. S. (2016) · InTech eBooks · doi:10.5772/63316 · Cited by 7

Cytoplasmic inheritance of parent–offspring cell structure in the clonal diatomCyclotella meneghiniana

Shirokawa, Y., & Shimada, M. (2016) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.2016.1632 · Cited by 7

Prions: Roles in Development and Adaptive Evolution

Dixson, J. D., & Azad, R. K. (2020) · Journal of Molecular Evolution · doi:10.1007/s00239-020-09944-2 · Cited by 7

The role of non-genetic information in evolutionary frameworks

Moran, K. L., Shlyakhtina, Y., & Portal, M. M. (2021) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2021.1908949 · Cited by 7

Fleeting Amyloid-like Forms of Rim4 Ensure Meiotic Fidelity

Ford, A. F., & Shorter, J. (2015) · Cell · doi:10.1016/j.cell.2015.09.049 · Cited by 7

Yeast prion [PSI] lowers the levels of mitochondrial prohibitins

Sikora, J. W., Towpik, J., Graczyk, D., Kistowski, M., Rubel, T., Poznański, J. T., Langridge, J., Hughes, C. J., Dadlez, M., & Boguta, M. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2009.08.003 · Cited by 7

The Sixth Sense-Emotional Contagion; Review of Biophysical Mechanisms Influencing Information Transfer in Groups

McDonnell, A. (2014) · Journal of Behavioral and Brain Science · doi:10.4236/jbbs.2014.47035 · Cited by 6

Population Genetic Structure: Where, What, and Why?

Ragauskas, A., Maziliauskaitė, E., Prakas, P., & Butkauskas, D. (2025) · Diversity · doi:10.3390/d17080584 · Cited by 6

Geophagy, Rare Earth Elements and Geochemical Endemics

Panichev, A. M., Golokhvast, K. S., Baranovskaya, N. V., & Strepetov, D. A. (2025) · Geosciences · doi:10.3390/geosciences15110428 · Cited by 6

Downshifting Yeast Dominance: Cell Physiology and Phospholipid Composition Are Altered With Establishment of the [GAR+] Prion in Saccharomyces cerevisiae

Walker, G. A., Henderson, C. M., Luong, P., Block, D. E., & Bisson, L. F. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.02011 · Cited by 6

Michler’s hydrol blue elucidates structural differences in prion strains

Xiao, Y., Rocha, S., Kitts, C. C., Reymer, A., Beke‐Somfai, T., Frederick, K. K., & Nordén, B. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2001732117 · Cited by 6

The role of tandem repeats in bacterial functional amyloids

Nowakowska, A. W., Wojciechowski, J. W., Szulc, N., & Kotulska, M. (2023) · Journal of Structural Biology · doi:10.1016/j.jsb.2023.108002 · Cited by 6

Toward an Understanding of the Dynamic Interdependence of Genes and Environment in the Regulation of Phenotype

Weaver, I. C. G. (2011) · Springer eBooks · doi:10.1007/978-3-642-17426-1_11 · Cited by 6

Prions: an evolutionary perspective.

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

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

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