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.

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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

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The emerging dynamic view of proteins: Protein plasticity in allostery, evolution and self-assembly

Bastolla, U., Porto, M., & Roman, H. E. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2013.03.016 · Cited by 6

From past to future: suppressor mutations in yeast genes encoding translation termination factors

Trubitsina, N. P., Zemlyanko, O. M., Moskalenko, S. E., & Zhouravleva, G. A. (2019) · Biological Communications · doi:10.21638/spbu03.2019.202 · Cited by 6

Memory of plants: present understanding

Garai, S., & Sopory, S. K. (2022) · The Nucleus · doi:10.1007/s13237-022-00399-y · Cited by 6

PLETHORA-WOX5 interaction and subnuclear localisation control Arabidopsis root stem cell maintenancePreprint

Burkart, R. C., Strotmann, V. I., Kirschner, G. K., Akinci, A., Czempik, L., Dolata, A., Maizel, A., Weidtkamp‐Peters, S., & Stahl, Y. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/818187 · Cited by 6

Origin of life: β‐sheet amyloid conformers as the primordial functional polymers on the early Earth and their role in the emergence of complex dynamic networks

Maury, C. P. J. (2025) · FEBS Letters · doi:10.1002/1873-3468.70112 · Cited by 7

TDP ‐43 proteinopathies and neurodegeneration: insights from Caenorhabditis elegans models

Pir, G. J., Buddenkotte, J., Alam, M. A., Own, A. M., Eck, R. J., Kraemer, B. C., Mandelkow�, E., & Steinhoff, M. S. (2025) · FEBS Journal · doi:10.1111/febs.70239 · Cited by 5

Intrinsically Disordered Compositional Bias in Proteins: Sequence Traits, Region Clustering, and Generation of Hypothetical Functional Associations

Harrison, P. M. (2024) · Bioinformatics and Biology Insights · doi:10.1177/11779322241287485 · Cited by 5

Amyloids Go Genomic: Insights Regarding the Sequence Determinants of Prion Formation from Genome‐Wide Studies

Lashuel, H. A., & Pappu, R. V. (2009) · ChemBioChem · doi:10.1002/cbic.200900373 · Cited by 5

Toxicity of Protein and DNA-AGEs in Neurodegenerative Diseases (NDDs) with Decisive Approaches to Stop the Deadly Consequences

Akhter, F., Akhter, A., & Ahmad, S. (2017) · Environmental science and engineering · doi:10.1007/978-3-319-46248-6_5 · Cited by 5

Case for an RNA–prion world: a hypothesis based on conformational diversity

Singh, P. P., & Banerji, A. (2011) · Journal of Biological Physics · doi:10.1007/s10867-011-9219-7 · Cited by 5

Amyloids in solid-state nuclear magnetic resonance: potential causes of the usually low resolution

Sabaté, R., Espargaró, A., Busquets, M. A., & Estelrich, J. (2015) · International Journal of Nanomedicine · doi:10.2147/ijn.s89385 · Cited by 5

SPECIAL ISSUE: ABSTRACTS FROM THE 2008 ISSOL MEETING

Orange, F., Westall, F., Disnar, J.-R., Prieur, D., Gautret, P., Romancer, M. L., & Défarge, C. (2009) · Origins of Life and Evolution of Biospheres · doi:10.1007/s11084-009-9164-7 · Cited by 5

Two Faces of Evil: Cancer and Neurodegeneration

Curran, T., & Christen, Y. (2010) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-16602-0 · Cited by 5

Protein Aggregation Disorders

Outeiro, T. F., McLean, P. J., & Hyman, B. T. (2007) · Elsevier eBooks · doi:10.1016/b978-012088592-3/50012-8 · Cited by 5

What makes a good prion?

Saupe, S. J., & Supattapone, S. (2006) · EMBO Reports · doi:10.1038/sj.embor.7400642 · Cited by 5

The Epigenetics of Neural Learning

Bronfman, Z. Z., Ginsburg, S., & Jablonka, E. (2016) · Wiley eBooks · doi:10.1002/9781118650813.ch7 · Cited by 6

Chloroplast protein import determines plant proteostasis and retrograde signalingPreprint

Llamas, E., Koyuncu, S., Lee, H. J., Gutiérrez-García, R., Dunken, N., Charura, N., Torres‐Montilla, S., Schlimgen, E., Pulido, P., Rodríguez-Concepción, M., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.19.484971 · Cited by 5

Saccharomyces cerevisiae as a Model for Studying Human Neurodegenerative Disorders: Viral Capsid Protein Expression

Bayandina, S. V., & Mukha, D. V. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242417213 · Cited by 7

Site-specific structural analysis of a yeast prion strain with species-specific seeding activity

Marcelino, A. M. C., Bhattacharya, M., Anselmo, A. C., & Tessier, P. M. (2011) · Prion · doi:10.4161/pri.5.3.16694 · Cited by 4

“Centric” and “Excluding” Conceptions of Biological Inheritance

Müller, G. A. (2024) · Advances in Historical Studies · doi:10.4236/ahs.2024.132007 · Cited by 4

New insights into the molecular mechanism of amyloid formation from cysteine scanning

Fei, L., & Perrett, S. (2010) · Prion · doi:10.4161/pri.4.1.10670 · Cited by 4

Aggregation-Prone Proteins Modulate Huntingtin Inclusion Body Formation in Yeast

Kantcheva, R., Mason, R. P., & Giorgini, F. (2014) · PLoS Currents · doi:10.1371/currents.hd.501008f3051342c9a5c0cd0f3a5bf3a4 · Cited by 4

Amyloid‐Like Fibrils: Origin, Structure, Properties, and Potential Technological Applications

Taboada, P., Barbosa, S., Juárez, J., Alatorre‐Meda, M., & Mosquera, V. (2013) · Wiley eBooks · doi:10.1002/9781118523063.ch12 · Cited by 4

Epigenetic regulation of genome integrity by a prion-based mechanismPreprint

Byers, J. S., Garcia, D. M., & Jarosz, D. F. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/152512 · Cited by 4

Patterny: A Troupe of Decipherment Helpers for Intrinsic Disorder, Low Complexity and Compositional Bias in Proteins

Harrison, P. M. (2025) · Biomolecules · doi:10.3390/biom15091332 · Cited by 3

Cellular toxicity of scrapie prions in prion diseases; a biochemical and molecular overview

Esmaili, M., & Eldeeb, M. A. (2022) · Molecular Biology Reports · doi:10.1007/s11033-022-07806-2 · Cited by 3

The prion-like effect and prion-like protein targeting strategy in amyotrophic lateral sclerosis

Wenzhi, Y., Xiangyi, L., & Dongsheng, F. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e34963 · Cited by 3

Amyloid-Like Peptide Aggregates

Kokotidou, C., Tamamis, P., & Mitraki, A. (2020) · Royal Society of Chemistry eBooks · doi:10.1039/9781839161148-00217 · Cited by 3

Extracellular Vesicles-Encapsulated Yeast Prions and What They Can Tell Us about the Physical Nature of Propagons

Kabani, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010090 · Cited by 3

Modeling Amyloid Aggregation Kinetics: A Case Study with Sup35NM

Sharma, A., McDonald, M. A., Rose, H. B., Chernoff, Y. O., Behrens, S. H., & Bommarius, A. S. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c11250 · Cited by 3

Come together now: Dynamic body-formation of key regulators integrates environmental cues in plant development

Burkart, R. C., Eljebbawi, A., & Stahl, Y. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2022.1052107 · Cited by 3

From the Modern Synthesis to the Inclusive Evolutionary Synthesis: An Einsteinian Revolution in Evolution

Danchin, É. (2023) · Synthese Library/Synthese library · doi:10.1007/978-3-031-33358-3_18 · Cited by 3

Conserved functions of prion candidates suggest a primeval role of protein self‐templating

Zajkowski, T., Lee, M., Sharma, S., Vallota‐Eastman, A., Kuska, M. I., Malczewska, M., & Rothschild, L. J. (2023) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26558 · Cited by 3

Do prions aggregate in response to electrical stimulation and does this play a role in long-term memory?

Concepción, G. P., & PADLAN, E. A. (2008) · Bioscience hypotheses · doi:10.1016/j.bihy.2008.10.003 · Cited by 3

Review: The Prion and its Potentiality

Dipendra Raj, P., eya, Acharya, N. K., & Hong, S. (2010) · Rowan Digitals Works (Rowan University) · Cited by 3

Advantages of Self-assembled Supramolecular Polymers Toward Biological Applications

Halperin‐Sternfeld, M., Ghosh, M., & Adler‐Abramovich, L. (2017) · Springer eBooks · doi:10.1007/978-981-10-6059-5_2 · Cited by 3

Origins and challenges

Gifford, F., & Rodríguez, A. M. (2011) · Cited by 3

The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid

Peña‐Díaz, S., Jiang, Y., Zhang, Z., Daugberg, A. O. H., Ferreira, P., Hernández, M. L., Mittal, C., Ramos, M. J., Pedersen, J. S., Dueholm, M. S., et al. (2025) · Advanced Science · doi:10.1002/advs.202517090 · Cited by 2

High-throughput screening approach identifies substrate-selective Hsp104 variants that counter amyloid seeding with diminished off-target effects

Ryan, J. J., Miller, K. R., Puri, A., Sprunger, M. L., Bochantine, M. M., Lopez, A., Chen, S., Bao, A., Ling, C., Xu, A., et al. (2026) · Molecular Cell · doi:10.1016/j.molcel.2026.04.015 · Cited by 2

A “poly-matter network” conception of biological inheritance

Müller, G. A., & Müller, T. D. (2024) · Genetica · doi:10.1007/s10709-024-00216-1 · Cited by 2

Prion-ViT: Prions-Inspired Vision Transformers for Temperature Prediction with Specklegrams

Sebastian, A., Pragna, R., Rajagopal, S., & Mani, M. (2025) · Lecture notes in networks and systems · doi:10.1007/978-981-96-8687-2_10 · Cited by 2

The Role of Cells in Encoding and Storing Information: A Narrative Review of Cellular Memory

Flores, A. I., & Liester, M. B. (2024) · Cureus · doi:10.7759/cureus.73063 · Cited by 3

The Transformation Experiment of Frederick Griffith I: Its Narrowing and Potential for the Creation of Novel Microorganisms

Müller, G. A. (2025) · Bioengineering · doi:10.3390/bioengineering12030324 · Cited by 2

The Role of Functional Prions in the Persistence of Memory Storage

Kandel, E. R., Derkatch, I. L., & Pavlopoulos, E. (2013) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-35491-5_11 · Cited by 2

A Prion-Mediated Mechanism for Memory Proposed in Drosophila

Li, W., & Dubnau, J. (2012) · Neuron · doi:10.1016/j.neuron.2012.10.001 · Cited by 2

An evolutionarily conserved mechanism for presynaptic trapping

Fernandez, F., Torres, V. I., & Zamorano, P. L. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0343-5 · Cited by 2

Rethinking the Origin of Chronic Diseases

Shoja, M. M., Tubbs, R. S., Ghaffari, A., Loukas, M., & Agutter, P. S. (2012) · BioScience · doi:10.1525/bio.2012.62.5.8 · Cited by 2

High-throughput Screening for Protein-based Inheritance in S. cerevisiae

Byers, J. S., & Jarosz, D. F. (2017) · Journal of Visualized Experiments · doi:10.3791/56069 · Cited by 2

Insoluble Cellular Prion Protein

Zou, W.-Q. (2012) · Springer eBooks · doi:10.1007/978-1-4614-5305-5_5 · Cited by 2

Amyloid fibrils are nanoparticles that target lysosomes.

Jakhria, T. (2014) · UPT. Syiah Kuala University Library (Syiah Kuala University) · Cited by 2

Plant Prionome maps reveal specific roles of prion-like proteins in stress and memoryPreprint

Garai, S., Citu, Pandey, J., Singla-Pareek, S. L., Sopory, S. K., Kaur, C., & Yadav, G. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.25.311993 · Cited by 2

Breaking β-sheets in FUS prion-like domain preserves phase separation and function but prevents aggregation and toxicityPreprint

Wake, N., Alcalde, J., Jutzi, D., Bajaj, A., Kour, S., Barai, M., Weng, S.-L., Cummings, S. R., Zheng, T., Anderson, E. N., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.17.706410 · Cited by 2

Transgenerational Plant Immunity in Plant Disease Management

Rashid, M. M., Bajpai, R., Teli, B., Sarkar, A., & Sarma, B. K. (2020) · Springer eBooks · doi:10.1007/978-981-15-6275-4_21 · Cited by 1

A Prion‐Like Domain in EBV EBNA1 Promotes Phase Separation and Enables SRRM1 Splicing

Zhang, X., Li, Z., Zheng, R., Xiang, Z., Wang, J., Liu, C., Wu, Y., Wen, Y., Ou, C., Fan, S., et al. (2025) · Advanced Science · doi:10.1002/advs.202501977 · Cited by 1

Tdrd6a and Tdrd6b are required together for germ plasm formation

Consorte, A., Michowicz, J., Carey, F., Möckel, M. M., Sherif, Y. E., Wittkopp, N., & Ketting, R. F. (2026) · Development · doi:10.1242/dev.204545 · Cited by 1

Cystine oligomers successfully attached to peptide cysteine-rich fibrils

Bortolini, C., & Dong, M. (2016) · Frontiers of Chemical Science and Engineering · doi:10.1007/s11705-016-1554-6 · Cited by 1

Molecular Mechanisms Encoding Strains of Prions and Prion-Like Misfolded Proteins

Hromádková, L., Siddiqi, M. K., Liu, H., & Safar, J. (2023) · Springer eBooks · doi:10.1007/978-3-031-20565-1_7 · Cited by 1

Glycosylphosphatidylinositol-anchored proteins as non-DNA matter of inheritance: from molecular to cell to philosophical biology

Müller, G. A. (2024) · Academia molecular biology and genomics. · doi:10.20935/acadmolbiogen7401 · Cited by 1

Novel Perspectives on Protein Structure Prediction

Berger, B., & Waldispühl, J. (2010) · Springer eBooks · doi:10.1007/978-0-387-09760-2_9 · Cited by 1

Clearance of yeast prions by misfolded multi-transmembrane proteins

Arai, C., Kurahashi, H., Ishiwata, M., Oishi, K., & Nakamura, Y. (2013) · Biochimie · doi:10.1016/j.biochi.2013.01.009 · Cited by 1

Clearance of yeast eRF-3 prion [PSI+] by amyloid enlargement due to the imbalance between chaperone Ssa1 and cochaperone Sgt2

Arai, C., Kurahashi, H., Pack, C., Sako, Y., & Nakamura, Y. (2013) · Translation · doi:10.4161/trla.26574 · Cited by 1

Strategies for Inhibiting Protein Aggregation: Therapeutic Approaches to Protein-Aggregation Diseases

Lanning, J. D., & Meredith, S. C. (2011) · Springer eBooks · doi:10.1007/978-94-007-2774-8_14 · Cited by 1

Nanoscale Optical Imaging of Protein Amyloids

Mukhopadhyay, S., Dalal, V., & Arya, S. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-394431-3.00037-7 · Cited by 1

Response and Cytoprotective Mechanisms Against Proteotoxic Stress in Yeast and Fungi

Kimata, Y., Nguyen, T. M. P., & Kohno, K. (2018) · Springer eBooks · doi:10.1007/978-3-030-00683-9_5 · Cited by 1

Amyotrophic Lateral Sclerosis

Osafo, N., Obiri, D. D., Yeboah, K. O., & Minkah, P. A. B. (2018) · Advances in medical diagnosis, treatment, and care (AMDTC) book series · doi:10.4018/978-1-5225-5282-6.ch015 · Cited by 1

Multi-Scale Mathematical Modeling of Prion Aggregate Dynamics and Phenotypes in Yeast Colonies

Banwarth-Kuhn, M., & Sindi, S. (2020) · IntechOpen eBooks · doi:10.5772/intechopen.88575 · Cited by 2

Role of CPEB-Family Proteins in Memory

Si, K. (2020) · Oxford University Press eBooks · doi:10.1093/oxfordhb/9780190686307.013.11 · Cited by 1

Varieties of Living ThingsLife at the Intersection of Lineage and Metabolism1

O’Malley, M. A. (2012) · Oxford University Press eBooks · doi:10.1093/acprof:oso/9780199691982.003.0013 · Cited by 1

A complexa interação epigenética na predisposição à dependência de drogas: uma revisão sistemática da literatura

Ferreira, A. P., Nichele, C. D. S. T., dos Santos, J. B., & Cruz-Hernández, M. J. (2022) · Research Society and Development · doi:10.33448/rsd-v11i7.30216 · Cited by 1

Insoluble Cellular Prion Protein and Other Neurodegeneration-Related Protein Aggregates in the Brain of Asymptomatic Individuals

Zou, W. (2023) · Springer eBooks · doi:10.1007/978-3-031-20565-1_4 · Cited by 1

Amyloid Remodeling by Hsp104

Shorter, J. (2011) · Wiley eBooks · doi:10.1002/9781118063903.ch7 · Cited by 1

Polarization transfer dynamics in multi-spin systems using the DREAM scheme

Westfeld, T. (2010) · Repository for Publications and Research Data (ETH Zurich) · doi:10.3929/ethz-a-006410379 · Cited by 1

Crystalline, membrane-embedded, and fibrillar proteins investigated by solid-state NMR spectroscopy

Schneider, R. (2009) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-2601 · Cited by 1

Author response: A common bacterial metabolite elicits prion-based bypass of glucose repression

Garcia, D. M., Dietrich, D. K., Clardy, J., & Jarosz, D. F. (2016) · eLife · doi:10.7554/elife.17978.016 · Cited by 1

Prion-like proteins reveal crosstalk between Stress and Memory pathways in PlantsPreprint

Garai, S., Citu, Singla-Pareek, S. L., Sopory, S. K., Kaur, C., & Yadav, G. (2021) · Research Square · doi:10.21203/rs.3.rs-201763/v1 · Cited by 1

Prions

Bodemer, W. (2009) · Elsevier eBooks · doi:10.1016/b978-012373944-5.00200-5 · Cited by 1

Amyloid Formation

MacPhee, C. E. (2012) · Springer eBooks · doi:10.1007/978-3-642-16712-6_180 · Cited by 1

Germplasm stability in zebrafish requires maternal Tdrd6a and Tdrd6cPreprint

Consorte, A., Sherif, Y. E., Kielisch, F., Wittkopp, N., & Ketting, R. F. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.04.615777 · Cited by 1

Characterization of the curli nucleator CsgB

Hammer, N. D. (2009) · Deep Blue (University of Michigan)

Unraveling Molecular Mechanisms and Structures of Self‐Perpetuating Prions

Tessier, P. M., & Lindquist, S. L. (2010) · Wiley eBooks · doi:10.1002/9780470572702.ch8

Генотип-средовое взаимодействие: молекулярно-генетический подход к изучению волевого контроля в период беременности

Чистякова, Н. В., & Сергиенко, Е. А. (2012) · Российский психологический журнал · doi:10.21702/rpj.2012.4.3

Molecular basis of gene dosage sensitivity

Chen, J. (2009) · Rice Research Repository (Rice University)

Prions as Epigenetic Regulators of Phenotype in Fungi

Naeimi, W. R., & Tuite, M. F. (2012) · Wiley-VCH eBooks · doi:10.1002/3527600906.mcb.201100029

Analysis Of CPEB Family Protein Member CPEB4 Function In Mammalian Neurons: A Dissertation

Kan, K. (2008) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/k2p5-k961

Chaperone‐Dependent Amyloid Assembly and Prion Toxicity

Summers, D. W., Wolfe, K. J., & Cyr, D. (2011) · Wiley eBooks · doi:10.1002/9781118063903.ch8

Self‐Replication in Chemistry and Biology

Holliger, P., & Loakes, D. (2009) · Wiley eBooks · doi:10.1002/9780470437988.ch13

Mechanism of yeast prion portein aggregation and strain formation

Kalastavadi, T. (2010) · Open Scholarship Institutional Repository (Washington University in St. Louis) · doi:10.7936/k7930r5d

(GAR + ): A Novel Type of Prion Involved in Glucose Signaling and Environmental Sensing in S. cerevisiae

Brown, J. C. S. (2008)

Le phénomène Prion, différents aspects d'un nouveau concept en biologie

Moudjou, M., & Ermonval, M. (2010) · HAL · doi:10.1684/vir.2010.0313

Characterization of the Prion Protein in Relation to Normal Cellular Function and in Disease

Wik, L. (2012) · Epsilon Open Archive (Sveriges lantbruksuniversitet biblioteket (Swedish University of Agricultural Sciences))

Development and application of genus-specific peptide arrays for kinome analysis

Arsenault, R. J. (2011) · HARVEST (University of Saskatchewan)

Формирование ценностного отношения старших школьников в карачаевской семье

Биджиев, А. С.-М. (2009) · Российский психологический журнал · doi:10.21702/rpj.2009.1.9

Yeast Prions Are Pathogenic, In-Register Parallel Amyloids

Wickner, R. B., Edskes, H. K., Bateman, D. A., Kelly, A. C., & Gorkovskiy, A. (2012) · Springer eBooks · doi:10.1007/978-1-4614-5305-5_16

Epigenetics of Psychiatric Diseases

Weaver, I. C. G., & Petronis, A. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.00097-0

Elucidating the Interaction between the Molecular Chaperone Hsp104 and the Yeast Prion Sup35

Helsen, C. W. (2012) · TSpace (University of Toronto)

Functional characterization of Shadoo, a PrP-like protein with neuroprotective activity

Haass, C. (2011)

Fibrillar Structures of Yeast Prion Sup35 In Vivo

Taguchi, H., & Kawai‐Noma, S. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-394431-3.00025-0

Transmissible Spongiform Encephalopathies: Slow Infections of the Nervous System

Asher, D. M. (2008) · Elsevier eBooks · doi:10.1016/b978-0-7020-3468-8.50056-0

Yeast Cells as a Discovery Platform for Parkinson's Disease and other Protein Misfolding Diseases

Allendoerfer, K. L., Su, L. J., & Lindquist, S. L. (2008) · Elsevier eBooks · doi:10.1016/b978-0-12-374028-1.00038-5

Performing Collective Tasks with Flagellated Bacteria Acting as Natural and Hybrid Microrobots

Martel, S. M. (2013) · doi:10.1201/b14908-27

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