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Heterologous Aggregates Promote De Novo Prion Appearance via More than One Mechanism

https://doi.org/10.1371/journal.pgen.1004814

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae.

inferredcites →https://doi.org/10.1002/j.1460-2075.1996.tb00675.xopenalex-snapshot

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

inferredcites →https://doi.org/10.1002/yea.1504openalex-snapshot

Bimolecular fluorescence complementation analysis system for in vivo detection of protein–protein interaction in Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1002/yea.320040302openalex-snapshot

The ψ factor of yeast: A problem in inheritance

inferredcites →https://doi.org/10.1002/yea.320111609openalex-snapshot

[PSI] and [URE3] as yeast prions

inferredcites →https://doi.org/10.1007/bf00351802openalex-snapshot

Multicopy SUP35 gene induces de-novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1007/bf02778003openalex-snapshot

Spontaneous generation of infectious nucleating amyloids in the transmissible and nontransmissible cerebral amyloidoses

inferredcites →https://doi.org/10.1007/s004390050204openalex-snapshot

Genetic basis of Creutzfeldt-Jakob disease in the United Kingdom: a systematic analysis of predisposing mutations and allelic variation in the PRNP gene

inferredcites →https://doi.org/10.1016/0021-9975(73)90024-8openalex-snapshot

Scrapie in mice

inferredcites →https://doi.org/10.1016/0092-8674(93)90585-eopenalex-snapshot

A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes

inferredcites →https://doi.org/10.1016/j.bbrc.2013.10.147openalex-snapshot

The interaction of Hsp104 with yeast prion Sup35 as analyzed by fluorescence cross-correlation spectroscopy

inferredcites →https://doi.org/10.1016/j.cell.2009.02.044openalex-snapshot

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

inferredcites →https://doi.org/10.1016/j.cell.2012.04.017openalex-snapshot

Cell-free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers within Hydrogels

inferredcites →https://doi.org/10.1016/j.cell.2013.05.057openalex-snapshot

Distinct α-Synuclein Strains Differentially Promote Tau Inclusions in Neurons

inferredcites →https://doi.org/10.1016/j.jmb.2009.04.063openalex-snapshot

Ssa1 Overexpression and [PIN+] Variants Cure [PSI+] by Dilution of Aggregates

inferredcites →https://doi.org/10.1016/j.jmb.2010.06.053openalex-snapshot

Structural Similarity between the Prion Domain of HET-s and a Homologue Can Explain Amyloid Cross-Seeding in Spite of Limited Sequence Identity

inferredcites →https://doi.org/10.1016/j.jmb.2013.06.006openalex-snapshot

Exploring the Basis of [PIN+] Variant Differences in [PSI+] Induction

inferredcites →https://doi.org/10.1016/j.jns.2006.07.009openalex-snapshot

Preventing familial ALS: A clinical trial may be feasible but is an efficacy trial warranted?

inferredcites →https://doi.org/10.1016/j.jsb.2012.05.002openalex-snapshot

Chaperone networks in protein disaggregation and prion propagation

inferredcites →https://doi.org/10.1016/j.molcel.2011.07.001openalex-snapshot

Prion Induction by the Short-Lived, Stress-Induced Protein Lsb2 Is Regulated by Ubiquitination and Association with the Actin Cytoskeleton

inferredcites →https://doi.org/10.1016/j.semcdb.2011.03.003openalex-snapshot

Newly identified prions in budding yeast, and their possible functions

inferredcites →https://doi.org/10.1016/s0021-9258(17)36755-8openalex-snapshot

STV1 gene encodes functional homologue of 95-kDa yeast vacuolar H(+)-ATPase subunit Vph1p.

inferredcites →https://doi.org/10.1016/s0076-6879(97)83025-xopenalex-snapshot

Use of conditional promoters for expression of heterologous proteins in Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1016/s0092-8674(00)80264-0openalex-snapshot

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

inferredcites →https://doi.org/10.1016/s0092-8674(00)81467-1openalex-snapshot

A Critical Role for Amino-Terminal Glutamine/Asparagine Repeats in the Formation and Propagation of a Yeast Prion

inferredcites →https://doi.org/10.1016/s0092-8674(01)00427-5openalex-snapshot

Prions Affect the Appearance of Other Prions

inferredcites →https://doi.org/10.1016/s0092-8674(01)00440-8openalex-snapshot

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

inferredcites →https://doi.org/10.1016/s0960-9822(00)00802-2openalex-snapshot

Chaperones that cure yeast artificial [PSI+] and their prion-specific effects

inferredcites →https://doi.org/10.1016/s1097-2765(00)80412-8openalex-snapshot

Rnq1

inferredcites →https://doi.org/10.1016/s1534-5807(02)00118-1openalex-snapshot

The Utility of Prions

inferredcites →https://doi.org/10.1017/s0016672300020140openalex-snapshot

Reversion analysis of [psi−] mutations inSaccharomyces cerevisiae

inferredcites →https://doi.org/10.1038/383685a0openalex-snapshot

Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD

inferredcites →https://doi.org/10.1038/42166openalex-snapshot

α-Synuclein in Lewy bodies

inferredcites →https://doi.org/10.1038/hdy.1965.65openalex-snapshot

Ψ, A cytoplasmic suppressor of super-suppressor in yeast

inferredcites →https://doi.org/10.1038/nature02026openalex-snapshot

Global analysis of protein localization in budding yeast

inferredcites →https://doi.org/10.1038/nature03679openalex-snapshot

Structural insights into a yeast prion illuminate nucleation and strain diversity

inferredcites →https://doi.org/10.1038/nature07195openalex-snapshot

Misfolded proteins partition between two distinct quality control compartments

inferredcites →https://doi.org/10.1038/ncb1843openalex-snapshot

The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion

inferredcites →https://doi.org/10.1038/ncb2838openalex-snapshot

Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress

inferredcites →https://doi.org/10.1038/ng.112openalex-snapshot

Newly identified prion linked to the chromatin-remodeling factor Swi1 in Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1038/nm0798-755openalex-snapshot

Alpha synuclein in neurodegenerative disorders: Murderer or accomplice?

inferredcites →https://doi.org/10.1038/nprot.2006.201openalex-snapshot

Design and implementation of bimolecular fluorescence complementation (BiFC) assays for the visualization of protein interactions in living cells

inferredcites →https://doi.org/10.1038/sj.emboj.7601811openalex-snapshot

J‐protein co‐chaperone Sis1 required for generation of [RNQ +] seeds necessary for prion propagation

inferredcites →https://doi.org/10.1046/j.1365-2958.2001.02224.xopenalex-snapshot

The relationship between visible intracellular aggregates that appear after overexpression of Sup35 and the yeast prion‐like elements [PSI + ] and [PIN + ]

inferredcites →https://doi.org/10.1056/nejm198403083101021openalex-snapshot

Some Speculations about Prions, Amyloid, and Alzheimer's Disease

inferredcites →https://doi.org/10.1056/nejm199609263351310openalex-snapshot

New Diagnostic Tests for Prion Diseases

inferredcites →https://doi.org/10.1073/pnas.0404968101openalex-snapshot

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

inferredcites →https://doi.org/10.1073/pnas.0509386103openalex-snapshot

Aβ and tau form soluble complexes that may promote self aggregation of both into the insoluble forms observed in Alzheimer’s disease

inferredcites →https://doi.org/10.1073/pnas.0802082105openalex-snapshot

A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity

inferredcites →https://doi.org/10.1073/pnas.0802593105openalex-snapshot

Chaperone-dependent amyloid assembly protects cells from prion toxicity

inferredcites →https://doi.org/10.1073/pnas.1003895107openalex-snapshot

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

inferredcites →https://doi.org/10.1073/pnas.1005949107openalex-snapshot

Non-Mendelian determinant [ ISP + ] in yeast is a nuclear-residing prion form of the global transcriptional regulator Sfp1

inferredcites →https://doi.org/10.1073/pnas.1211976109openalex-snapshot

Heritable yeast prions have a highly organized three-dimensional architecture with interfiber structures

inferredcites →https://doi.org/10.1073/pnas.152330699openalex-snapshot

Interactions among prions and prion “strains” in yeast

inferredcites →https://doi.org/10.1073/pnas.252652099openalex-snapshot

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

inferredcites →https://doi.org/10.1073/pnas.85.11.4051openalex-snapshot

Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau.

inferredcites →https://doi.org/10.1073/pnas.95.23.13363openalex-snapshot

Prions

inferredcites →https://doi.org/10.1073/pnas.95.5.2400openalex-snapshot

Overexpression of the SUP45 gene encoding a Sup35p-binding protein inhibits the induction of the de novo appearance of the [PSI + ] prion

inferredcites →https://doi.org/10.1073/pnas.97.1.240openalex-snapshot

Guanidine hydrochloride blocks a critical step in the propagation of the prion-like determinant [ PSI + ] of Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1074/jbc.274.3.1181openalex-snapshot

The Yeast [PSI+] Prion: Making Sense of Nonsense

inferredcites →https://doi.org/10.1074/jbc.m110.125039openalex-snapshot

Interaction with Polyglutamine Aggregates Reveals a Q/N-rich Domain in TDP-43

inferredcites →https://doi.org/10.1074/jbc.m111.302869openalex-snapshot

Insight into Molecular Basis of Curing of [PSI+] Prion by Overexpression of 104-kDa Heat Shock Protein (Hsp104)

inferredcites →https://doi.org/10.1074/jbc.m307996200openalex-snapshot

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

inferredcites →https://doi.org/10.1074/jbc.m311300200openalex-snapshot

Seeding Specificity in Amyloid Growth Induced by Heterologous Fibrils

inferredcites →https://doi.org/10.1074/jbc.m410150200openalex-snapshot

Nonsense Suppression in Yeast Cells Overproducing Sup35 (eRF3) Is Caused by Its Non-heritable Amyloids

inferredcites →https://doi.org/10.1074/jbc.m609269200openalex-snapshot

Visualization of Aggregation of the Rnq1 Prion Domain and Cross-seeding Interactions with Sup35NM

inferredcites →https://doi.org/10.1074/jbc.m609597200openalex-snapshot

Effects of Ubiquitin System Alterations on the Formation and Loss of a Yeast Prion

inferredcites →https://doi.org/10.1083/jcb.128.5.779openalex-snapshot

A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast.

inferredcites →https://doi.org/10.1083/jcb.201106037openalex-snapshot

Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1083/jcb.201201074openalex-snapshot

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

inferredcites →https://doi.org/10.1091/mbc.e08-01-0078openalex-snapshot

Variant-specific [PSI+] Infection Is Transmitted by Sup35 Polymers within [PSI+] Aggregates with Heterogeneous Protein Composition

inferredcites →https://doi.org/10.1091/mbc.e09-11-0927openalex-snapshot

Analyzing the Birth and Propagation of Two Distinct Prions, [PSI+] and [Het-s]y, in Yeast

inferredcites →https://doi.org/10.1093/emboj/19.9.1942openalex-snapshot

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

inferredcites →https://doi.org/10.1093/genetics/137.3.671openalex-snapshot

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

inferredcites →https://doi.org/10.1093/genetics/144.4.1375openalex-snapshot

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

inferredcites →https://doi.org/10.1093/genetics/147.2.507openalex-snapshot

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

inferredcites →https://doi.org/10.1093/genetics/156.2.559openalex-snapshot

A Role for Cytosolic Hsp70 in Yeast [PSI+] Prion Propagation and [PSI+] as a Cellular Stress

inferredcites →https://doi.org/10.1093/genetics/160.1.25openalex-snapshot

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

inferredcites →https://doi.org/10.1093/genetics/163.2.495openalex-snapshot

Saccharomyces cerevisiae Hsp70 Mutations Affect [PSI+] Prion Propagation and Cell Growth Differently and Implicate Hsp40 and Tetratricopeptide Repeat Cochaperones in Impairment of [PSI+]

inferredcites →https://doi.org/10.1093/genetics/165.1.23openalex-snapshot

Analysis of the Generation and Segregation of Propagons: Entities That Propagate the [PSI+] Prion in Yeast

inferredcites →https://doi.org/10.1093/nar/22.25.5767openalex-snapshot

Regulatable promoters of Saccharomyces cerevisiae: comparison of transcriptional activity and their use for heterologous expression

inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a021406openalex-snapshot

Dimerization Characteristics of the 94-kDa Glucose-Regulated Protein

inferredcites →https://doi.org/10.1097/00019052-200008000-00006openalex-snapshot

Recent advances in amyotrophic lateral sclerosis

inferredcites →https://doi.org/10.1101/087969693.41.305openalex-snapshot

7 Prions of Yeast and Filamentous Fungi: [URE3], [ PSI + ], [ PIN + ], and [Het-s]

inferredcites →https://doi.org/10.1110/ps.04707004openalex-snapshot

Observation of sequence specificity in the seeding of protein amyloid fibrils

inferredcites →https://doi.org/10.1111/j.1365-2958.1993.tb01159.xopenalex-snapshot

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

inferredcites →https://doi.org/10.1111/j.1365-2958.2008.06135.xopenalex-snapshot

Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation

inferredcites →https://doi.org/10.1111/j.1471-4159.2012.07847.xopenalex-snapshot

Cross‐seeding effects of amyloid β‐protein and α‐synuclein

inferredcites →https://doi.org/10.1111/j.1749-6632.1982.tb26849.xopenalex-snapshot

Alzheimer's Disease and Transmissible Virus Dementia (Creutzfeldt‐Jakob Disease)

inferredcites →https://doi.org/10.1111/mmi.12716openalex-snapshot

Prion‐promoted phosphorylation of heterologous amyloid is coupled with ubiquitin‐proteasome system inhibition and toxicity

inferredcites →https://doi.org/10.1126/science.1062097openalex-snapshot

Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils

inferredcites →https://doi.org/10.1126/science.1098007openalex-snapshot

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

inferredcites →https://doi.org/10.1126/science.1131864openalex-snapshot

Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host

inferredcites →https://doi.org/10.1126/science.1134108openalex-snapshot

Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

inferredcites →https://doi.org/10.1126/science.1154584openalex-snapshot

TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis

inferredcites →https://doi.org/10.1126/science.1165942openalex-snapshot

Mutations in FUS, an RNA Processing Protein, Cause Familial Amyotrophic Lateral Sclerosis Type 6

inferredcites →https://doi.org/10.1126/science.1166066openalex-snapshot

Mutations in the FUS/TLS Gene on Chromosome 16 Cause Familial Amyotrophic Lateral Sclerosis

inferredcites →https://doi.org/10.1126/science.1219491openalex-snapshot

A Yeast Prion, Mod5, Promotes Acquired Drug Resistance and Cell Survival Under Environmental Stress

inferredcites →https://doi.org/10.1126/science.273.5275.622openalex-snapshot

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

inferredcites →https://doi.org/10.1126/science.289.5483.1317openalex-snapshot

Nucleated Conformational Conversion and the Replication of Conformational Information by a Prion Determinant

inferredcites →https://doi.org/10.1126/science.6801762openalex-snapshot

Novel Proteinaceous Infectious Particles Cause Scrapie

inferredcites →https://doi.org/10.1126/science.7754373openalex-snapshot

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

inferredcites →https://doi.org/10.1126/science.7909170openalex-snapshot

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

inferredcites →https://doi.org/10.1128/ec.00353-08openalex-snapshot

Increased [ PSI + ] Appearance by Fusion of Rnq1 with the Prion Domain of Sup35 in Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1128/ec.4.2.289-297.2005openalex-snapshot

Role for Hsp70 Chaperone in Saccharomyces cerevisiae Prion Seed Replication

inferredcites →https://doi.org/10.1128/jvi.68.12.7859-7868.1994openalex-snapshot

Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy

inferredcites →https://doi.org/10.1128/mcb.00875-12openalex-snapshot

Regulation of Chaperone Effects on a Yeast Prion by Cochaperone Sgt2

inferredcites →https://doi.org/10.1128/mcb.16.8.4378openalex-snapshot

Functional Interaction of Cytosolic hsp70 and a DnaJ-Related Protein, Ydj1p, in Protein Translocation In Vivo

inferredcites →https://doi.org/10.1128/mcb.19.12.8103openalex-snapshot

Evidence for a Protein Mutator in Yeast: Role of the Hsp70-Related Chaperone Ssb in Formation, Stability, and Toxicity of the [PSI] Prion

inferredcites →https://doi.org/10.1128/mcb.19.2.1325openalex-snapshot

Antagonistic Interactions between Yeast Chaperones Hsp104 and Hsp70 in Prion Curing

inferredcites →https://doi.org/10.1128/mcb.21.20.7035-7046.2001openalex-snapshot

Induction of Distinct [ URE3 ] Yeast Prion Strains

inferredcites →https://doi.org/10.1128/mcb.22.11.3590-3598.2002openalex-snapshot

Antagonistic Interactions between Yeast [ PSI + ] and [ URE3 ] Prions and Curing of [ URE3 ] by Hsp70 Protein Chaperone Ssa1p but Not by Ssa2p

inferredcites →https://doi.org/10.1128/mcb.24.9.3928-3937.2004openalex-snapshot

Propagation of Saccharomyces cerevisiae [ PSI + ] Prion Is Impaired by Factors That Regulate Hsp70 Substrate Binding

inferredcites →https://doi.org/10.1128/mcb.26.2.617-629.2006openalex-snapshot

Modulation of Prion Formation, Aggregation, and Toxicity by the Actin Cytoskeleton in Yeast

inferredcites →https://doi.org/10.1139/o09-118openalex-snapshot

Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagationThis paper is one of a selection of papers published in this special issue entitled 8th International Conference on AAA Proteins and has undergone the Journal's usual peer review process.

inferredcites →https://doi.org/10.1159/000337230openalex-snapshot

Amyloid Oligomers Exacerbate Tau Pathology in a Mouse Model of Tauopathy

inferredcites →https://doi.org/10.1242/jcs.051672openalex-snapshot

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

inferredcites →https://doi.org/10.1371/journal.pbio.0050024openalex-snapshot

Hsp104-Dependent Remodeling of Prion Complexes Mediates Protein-Only Inheritance

inferredcites →https://doi.org/10.1371/journal.pbio.0060294openalex-snapshot

Prion Switching in Response to Environmental Stress

inferredcites →https://doi.org/10.1371/journal.pgen.1001386openalex-snapshot

Prion Formation and Polyglutamine Aggregation Are Controlled by Two Classes of Genes

inferredcites →https://doi.org/10.1371/journal.pgen.1003236openalex-snapshot

Heterologous Gln/Asn-Rich Proteins Impede the Propagation of Yeast Prions by Altering Chaperone Availability

inferredcites →https://doi.org/10.1371/journal.pone.0079582openalex-snapshot

Spontaneous Variants of the [RNQ+] Prion in Yeast Demonstrate the Extensive Conformational Diversity Possible with Prion Proteins

inferredcites →https://doi.org/10.1523/jneurosci.0783-09.2009openalex-snapshot

Cross-Seeding Fibrillation of Q/N-Rich Proteins Offers New Pathomechanism of Polyglutamine Diseases

inferredcites →https://doi.org/10.1523/jneurosci.3088-11.2011openalex-snapshot

Soluble Aβ Seeds Are Potent Inducers of Cerebral β-Amyloid Deposition

inferredcites →https://doi.org/10.1534/genetics.104.037168openalex-snapshot

Hsp70 Chaperones as Modulators of Prion Life Cycle

inferredcites →https://doi.org/10.1534/genetics.109.110213openalex-snapshot

The Spontaneous Appearance Rate of the Yeast Prion [PSI+] and Its Implications for the Evolution of the Evolvability Properties of the [PSI+] System

inferredcites →https://doi.org/10.1534/genetics.111.127779openalex-snapshot

Molecular Chaperone Hsp104 Can Promote Yeast Prion Generation

inferredcites →https://doi.org/10.1534/genetics.111.137760openalex-snapshot

Prions in Yeast

inferredcites →https://doi.org/10.2174/092986609788490078openalex-snapshot

Hsp104 and Prion Propagation

inferredcites →https://doi.org/10.4161/pri.1.2.4440openalex-snapshot

Characterization of Proteins Associated with Polyglutamine Aggregates

inferredcites →https://doi.org/10.4161/pri.1.3.4837openalex-snapshot

Prion-Prion Interactions

inferredcites →https://doi.org/10.4161/pri.26021openalex-snapshot

The story of stolen chaperones

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.5177180openalex-extracted

Adaptive Variation in Mutagenesis Driven by Protein Self-Assembly

inferred← citeshttps://doi.org/10.1002/prot.26282openalex-snapshot

The non‐prion SUP35 preexists in large chaperone‐containing molecular complexes

inferred← citeshttps://doi.org/10.1007/s00294-017-0736-1openalex-snapshot

Toxicity and infectivity: insights from de novo prion formation

inferred← citeshttps://doi.org/10.1016/b978-0-08-102850-6.00004-8openalex-snapshot

Novel protein and peptide nanofibrous structures via supramolecular co-assembly

inferred← citeshttps://doi.org/10.1016/bs.adgen.2020.01.002openalex-snapshot

Application of yeast to studying amyloid and prion diseases

inferred← citeshttps://doi.org/10.1016/j.cell.2026.05.018openalex-snapshot

Prion-based protein self-assembly tunes mutagenesis to enable rapid adaptation

inferred← citeshttps://doi.org/10.1016/j.isci.2020.102000openalex-snapshot

Tumor suppressor protein p53 expressed in yeast can remain diffuse, form a prion, or form unstable liquid-like droplets

inferred← citeshttps://doi.org/10.1016/j.molcel.2018.06.016openalex-snapshot

Quantifying Nucleation In Vivo Reveals the Physical Basis of Prion-like Phase Behavior

inferred← citeshttps://doi.org/10.1016/j.semcdb.2015.08.016openalex-snapshot

Yeast prions: Paramutation at the protein level?

inferred← citeshttps://doi.org/10.1016/j.semcdb.2019.07.007openalex-snapshot

Protein-based inheritance

inferred← citeshttps://doi.org/10.1038/s41594-020-0416-6openalex-snapshot

Nucleation seed size determines amyloid clearance and establishes a barrier to prion appearance in yeast

inferred← citeshttps://doi.org/10.1038/s41598-017-00135-6openalex-snapshot

De novo [PSI +] prion formation involves multiple pathways to form infectious oligomers

inferred← citeshttps://doi.org/10.1038/s41598-017-05829-5openalex-snapshot

Heterologous prion-forming proteins interact to cross-seed aggregation in Saccharomyces cerevisiae

inferred← citeshttps://doi.org/10.1080/19336896.2015.1065372openalex-snapshot

Sup35 methionine oxidation is a trigger forde novo[PSI+] prion formation

inferred← citeshttps://doi.org/10.1080/19336896.2016.1176659openalex-snapshot

Wild type huntingtin toxicity in yeast: Implications for the role of amyloid cross-seeding in polyQ diseases

inferred← citeshttps://doi.org/10.1080/19336896.2016.1204060openalex-snapshot

Strain conformation controls the specificity of cross-species prion transmission in the yeast model

inferred← citeshttps://doi.org/10.1080/19336896.2016.1234574openalex-snapshot

The small heat shock protein Hsp31 cooperates with Hsp104 to modulate Sup35 prion aggregation

inferred← citeshttps://doi.org/10.1080/19336896.2017.1344806openalex-snapshot

The effects of glutamine/asparagine content on aggregation and heterologous prion induction by yeast prion-like domains

inferred← citeshttps://doi.org/10.1091/mbc.e15-08-0548openalex-snapshot

Autophagy protects against de novo formation of the [PSI+] prion in yeast

inferred← citeshttps://doi.org/10.1093/femsyr/foy026openalex-snapshot

[PIN+]ing down the mechanism of prion appearance

inferred← citeshttps://doi.org/10.1101/145060openalex-snapshot

Actin impacts the late stages of prion formation and prion propagation

inferred← citeshttps://doi.org/10.1111/mmi.14329openalex-snapshot

Growth phase‐dependent changes in the size and infectivity of SDS‐resistant Sup35p assemblies associated with the [PSI+] prion in yeast

inferred← citeshttps://doi.org/10.1111/mmi.14515openalex-snapshot

Glucose availability dictates the export of the soluble and prion forms of Sup35p via periplasmic or extracellular vesicles

inferred← citeshttps://doi.org/10.1111/tra.12344openalex-snapshot

Actin, Membrane Trafficking and the Control of Prion Induction, Propagation and Transmission in Yeast

inferred← citeshttps://doi.org/10.1128/aem.01703-24openalex-snapshot

Effects of Sup35 overexpression on the formation, morphology, and physiological functions of intracellular Sup35 assemblies

inferred← citeshttps://doi.org/10.1134/s0006297917100078openalex-snapshot

Distinct mechanisms of phenotypic effects of inactivation and prionization of Swi1 protein in Saccharomyces cerevisiae

inferred← citeshttps://doi.org/10.1371/journal.pgen.1006708openalex-snapshot

Disrupting the cortical actin cytoskeleton points to two distinct mechanisms of yeast [PSI+] prion formation

inferred← citeshttps://doi.org/10.1371/journal.pgen.1011194openalex-snapshot

Sequestrase chaperones protect against oxidative stress-induced protein aggregation and [PSI+] prion formation

inferred← citeshttps://doi.org/10.3389/fnmol.2018.00075openalex-snapshot

Q-Rich Yeast Prion [PSI+] Accelerates Aggregation of Transthyretin, a Non-Q-Rich Human Protein

inferred← citeshttps://doi.org/10.3390/antiox12020401openalex-snapshot

Methionine Sulfoxide Reductases Suppress the Formation of the [PSI+] Prion and Protein Aggregation in Yeast

inferred← citeshttps://doi.org/10.3390/biology11121688openalex-snapshot

Processing of Fluorescent Proteins May Prevent Detection of Prion Particles in [PSI+] Cells

inferred← citeshttps://doi.org/10.3390/ijms19082292openalex-snapshot

Protein Co-Aggregation Related to Amyloids: Methods of Investigation, Diversity, and Classification

inferred← citeshttps://doi.org/10.3390/ijms22010090openalex-snapshot

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

inferred← citeshttps://doi.org/10.3390/ijms22041542openalex-snapshot

Dangerous Stops: Nonsense Mutations Can Dramatically Increase Frequency of Prion Conversion

inferred← citeshttps://doi.org/10.3390/v14071581openalex-snapshot

Implications of the Actin Cytoskeleton on the Multi-Step Process of [PSI+] Prion Formation

inferred← citeshttps://doi.org/10.3390/v14081635openalex-snapshot

Beyond Amyloid Fibers: Accumulation, Biological Relevance, and Regulation of Higher-Order Prion Architectures

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