| scholarly article | Q13442814 |
| P50 | author | Justin K Hines | Q89700501 |
| P2093 | author name string | Sarah C Miller | |
| Andrea N Killian | |||
| P2860 | cites work | Variant-specific and reciprocal Hsp40 functions in Hsp104-mediated prion elimination. | Q54464289 |
| Forms and abundance of chaperone proteins influence yeast prion variant competition | Q90738305 | ||
| Anti-prion systems in yeast | Q91312189 | ||
| Function, evolution, and structure of J-domain proteins | Q93383323 | ||
| Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae | Q24533260 | ||
| Prion strains and amyloid polymorphism influence phenotypic variation | Q26827209 | ||
| Yeast prions: structure, biology, and prion-handling systems | Q27007482 | ||
| Hsp104-dependent remodeling of prion complexes mediates protein-only inheritance | Q27334853 | ||
| Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates | Q27929853 | ||
| Curing of the [URE3] prion by Btn2p, a Batten disease-related protein | Q27930078 | ||
| The translation machinery and 70 kd heat shock protein cooperate in protein synthesis | Q27931744 | ||
| Complex interactions among members of an essential subfamily of hsp70 genes in Saccharomyces cerevisiae | Q27933205 | ||
| Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions | Q27933549 | ||
| Prions affect the appearance of other prions: the story of [PIN(+)]. | Q27937880 | ||
| Dissection of Swa2p/auxilin domain requirements for cochaperoning Hsp70 clathrin-uncoating activity in vivo | Q27938386 | ||
| Sequential duplications of an ancient member of the DnaJ-family expanded the functional chaperone network in the eukaryotic cytosol. | Q27939634 | ||
| The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104. | Q44688356 | ||
| Hsp104 disaggregase at normal levels cures many [PSI+] prion variants in a process promoted by Sti1p, Hsp90, and Sis1p | Q45141428 | ||
| The physical basis of how prion conformations determine strain phenotypes | Q46092862 | ||
| Broadening the functionality of a J-protein/Hsp70 molecular chaperone system | Q46652361 | ||
| Prion variant maintained only at high levels of the Hsp104 disaggregase | Q46819506 | ||
| Curing of [PSI+] by Hsp104 overexpression: clues to solving the puzzle | Q47331963 | ||
| Chaperones that cure yeast artificial [PSI+] and their prion-specific effects | Q47850007 | ||
| Differential effects of chaperones on yeast prions: CURrent view. | Q47950900 | ||
| To CURe or not to CURe? Differential effects of the chaperone sorting factor Cur1 on yeast prions are mediated by the chaperone Sis1. | Q48247555 | ||
| Chaperone functional specificity promotes yeast prion diversity. | Q48309474 | ||
| Hsp70 at the membrane: driving protein translocation | Q49272509 | ||
| Molecular evolution of the HSP70 multigene family | Q27940113 | ||
| Protein disaggregation mediated by heat-shock protein Hsp104. | Q27940314 | ||
| Spontaneous variants of the [RNQ+] prion in yeast demonstrate the extensive conformational diversity possible with prion proteins | Q28534632 | ||
| The HSP70 chaperone machinery: J proteins as drivers of functional specificity | Q29616140 | ||
| HSP90 at the hub of protein homeostasis: emerging mechanistic insights | Q29616824 | ||
| Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+] | Q29619693 | ||
| Ssb1 chaperone is a [PSI+] prion-curing factor | Q30992350 | ||
| Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing | Q33368981 | ||
| Biology and genetics of prions causing neurodegeneration | Q33567229 | ||
| Influence of prion variant and yeast strain variation on prion-molecular chaperone requirements | Q33575503 | ||
| Distinct prion strains are defined by amyloid core structure and chaperone binding site dynamics. | Q33649008 | ||
| Heat shock protein 104 (Hsp104)-mediated curing of [PSI+] yeast prions depends on both [PSI+] conformation and the properties of the Hsp104 homologs | Q33737701 | ||
| Evolutionary Conservation and Emerging Functional Diversity of the Cytosolic Hsp70:J Protein Chaperone Network of Arabidopsis thaliana | Q33807686 | ||
| [SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity | Q33838230 | ||
| Normal levels of the antiprion proteins Btn2 and Cur1 cure most newly formed [URE3] prion variants | Q33854246 | ||
| In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104 | Q33874246 | ||
| Prion generation in vitro: amyloid of Ure2p is infectious | Q33947121 | ||
| Myopathy-causing mutations in an HSP40 chaperone disrupt processing of specific client conformers. | Q33947263 | ||
| Evidence for a protein mutator in yeast: role of the Hsp70-related chaperone ssb in formation, stability, and toxicity of the [PSI] prion | Q33960587 | ||
| Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104. | Q33963759 | ||
| Induction of distinct [URE3] yeast prion strains | Q34012527 | ||
| Low activity of select Hsp104 mutants is sufficient to propagate unstable prion variants | Q34051189 | ||
| Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance | Q34098129 | ||
| The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner | Q34125006 | ||
| Hsp40s specify functions of Hsp104 and Hsp90 protein chaperone machines | Q34350913 | ||
| Interactions among prions and prion "strains" in yeast | Q34443841 | ||
| Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+] | Q34572502 | ||
| A role for cytosolic hsp70 in yeast [PSI(+)] prion propagation and [PSI(+)] as a cellular stress. | Q34610589 | ||
| Destabilizing interactions among [PSI(+)] and [PIN(+)] yeast prion variants. | Q34619382 | ||
| Suicidal [PSI+] is a lethal yeast prion | Q34750018 | ||
| The most infectious prion protein particles. | Q34805737 | ||
| Destabilization and recovery of a yeast prion after mild heat shock. | Q34985224 | ||
| Prion diseases of yeast: amyloid structure and biology | Q35053520 | ||
| Molecular chaperone Hsp104 can promote yeast prion generation | Q35065489 | ||
| Functional diversification of hsp40: distinct j-protein functional requirements for two prions allow for chaperone-dependent prion selection | Q35212560 | ||
| Functions of yeast Hsp40 chaperone Sis1p dispensable for prion propagation but important for prion curing and protection from prion toxicity. | Q35222751 | ||
| Continuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes. | Q35539802 | ||
| The sensitive [SWI (+)] prion: new perspectives on yeast prion diversity | Q35578773 | ||
| Network of general and specialty J protein chaperones of the yeast cytosol | Q35758703 | ||
| Hsp90-Associated Immunophilin Homolog Cpr7 Is Required for the Mitotic Stability of [URE3] Prion in Saccharomyces cerevisiae | Q35810283 | ||
| Nucleotide exchange factors for Hsp70s are required for [URE3] prion propagation in Saccharomyces cerevisiae | Q35810636 | ||
| Molecular pathogenesis of sporadic prion diseases in man. | Q36005158 | ||
| Hsp40 function in yeast prion propagation: Amyloid diversity necessitates chaperone functional complexity | Q36147550 | ||
| The ribosome-associated complex antagonizes prion formation in yeast | Q36147694 | ||
| Prions in yeast | Q36154362 | ||
| The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion | Q36287669 | ||
| Swa2, the yeast homolog of mammalian auxilin, is specifically required for the propagation of the prion variant [URE3-1]. | Q36399121 | ||
| Structural variants of yeast prions show conformer-specific requirements for chaperone activity. | Q36498591 | ||
| Human J-protein DnaJB6b Cures a Subset of Saccharomyces cerevisiae Prions and Selectively Blocks Assembly of Structurally Related Amyloids | Q36594690 | ||
| Prions of fungi: inherited structures and biological roles | Q36647771 | ||
| Specificity of the J-protein Sis1 in the propagation of 3 yeast prions | Q36954907 | ||
| Prion variants and species barriers among Saccharomyces Ure2 proteins | Q37117028 | ||
| Guanidine hydrochloride blocks a critical step in the propagation of the prion-like determinant [PSI(+)] of Saccharomyces cerevisiae. | Q37148653 | ||
| Influence of Hsp70s and their regulators on yeast prion propagation | Q37266700 | ||
| Design and construction of diverse mammalian prion strains | Q37453512 | ||
| Structure and function of the molecular chaperone Hsp104 from yeast | Q37600791 | ||
| The amyloid state of proteins in human diseases | Q37994283 | ||
| Prion-specific Hsp40 function: The role of the auxilin homolog Swa2. | Q38748751 | ||
| Extensive diversity of prion strains is defined by differential chaperone interactions and distinct amyloidogenic regions. | Q39385432 | ||
| The life of [PSI]. | Q39399957 | ||
| The role of Sis1 in the maintenance of the [RNQ+] prion | Q39645207 | ||
| Yeast and Fungal Prions: Amyloid-Handling Systems, Amyloid Structure, and Prion Biology | Q39968510 | ||
| Feedback control of prion formation and propagation by the ribosome-associated chaperone complex | Q41558446 | ||
| Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104. | Q41597556 | ||
| The structural basis of yeast prion strain variants | Q41792123 | ||
| Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae. | Q41815189 | ||
| Chaperone proteins select and maintain [PIN+] prion conformations in Saccharomyces cerevisiae | Q41879808 | ||
| Regulation of the Hsp104 middle domain activity is critical for yeast prion propagation. | Q41888807 | ||
| Agents that cause a high frequency of genetic change from [psi+] to [psi-] in Saccharomyces cerevisiae | Q42048419 | ||
| The [PSI+] prion of Saccharomyces cerevisiae can be propagated by an Hsp104 orthologue from Candida albicans | Q42176668 | ||
| Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation | Q42264565 | ||
| Ssa1 overexpression and [PIN(+)] variants cure [PSI(+)] by dilution of aggregates | Q42547259 | ||
| Hsp70/Hsp90 co-chaperones are required for efficient Hsp104-mediated elimination of the yeast [PSI(+)] prion but not for prion propagation | Q43219189 | ||
| Conformational variations in an infectious protein determine prion strain differences | Q44187524 | ||
| P275 | copyright license | Creative Commons Attribution 4.0 International | Q20007257 |
| P6216 | copyright status | copyrighted | Q50423863 |
| P433 | issue | 4 | |
| P577 | publication date | 2019-04-16 | |
| P1433 | published in | Viruses | Q7935305 |
| P1476 | title | Impact of Amyloid Polymorphism on Prion-Chaperone Interactions in Yeast | |
| P478 | volume | 11 |
Search more.