| Yeast Prion Protein Sup35 Initiates alpha-Synuclein Pathology in Parkinson's Disease. | Yeast Prion Protein Sup35 Initiates α-Synuclein Pathology in Parkinson's Disease.
Wang Y, Li H, Song N, Xie J. | 07/18/2024 |
| Gene Expression Analysis of Yeast Strains with a Nonsense Mutation in the eRF3-Coding Gene Highlights Possible Mechanisms of Adaptation. | Gene Expression Analysis of Yeast Strains with a Nonsense Mutation in the eRF3-Coding Gene Highlights Possible Mechanisms of Adaptation.
Maksiutenko EM, Barbitoff YA, Danilov LG, Matveenko AG, Zemlyanko OM, Efremova EP, Moskalenko SE, Zhouravleva GA., Free PMC Article | 07/17/2024 |
| The yeast prion protein Sup35 initiates alpha-synuclein pathology in mouse models of Parkinson's disease. | The yeast prion protein Sup35 initiates α-synuclein pathology in mouse models of Parkinson's disease.
Meng L, Liu C, Li Y, Chen G, Xiong M, Yu T, Pan L, Zhang X, Zhou L, Guo T, Yuan X, Liu C, Zhang Z, Zhang Z., Free PMC Article | 11/4/2023 |
| Substoichiometric Hsp104 regulates the genesis and persistence of self-replicable amyloid seeds of Sup35 prion domain. | Substoichiometric Hsp104 regulates the genesis and persistence of self-replicable amyloid seeds of Sup35 prion domain.
Mahapatra S, Sarbahi A, Madhu P, Swasthi HM, Sharma A, Singh P, Mukhopadhyay S., Free PMC Article | 09/17/2022 |
| Yeast J-protein Sis1 prevents prion toxicity by moderating depletion of prion protein. | Yeast J-protein Sis1 prevents prion toxicity by moderating depletion of prion protein.
Kumar J, Reidy M, Masison DC., Free PMC Article | 03/26/2022 |
| Gene Amplification as a Mechanism of Yeast Adaptation to Nonsense Mutations in Release Factor Genes. | Gene Amplification as a Mechanism of Yeast Adaptation to Nonsense Mutations in Release Factor Genes.
Maksiutenko EM, Barbitoff YA, Matveenko AG, Moskalenko SE, Zhouravleva GA., Free PMC Article | 02/12/2022 |
| Mechanisms that ensure speed and fidelity in eukaryotic translation termination. | Mechanisms that ensure speed and fidelity in eukaryotic translation termination.
Lawson MR, Lessen LN, Wang J, Prabhakar A, Corsepius NC, Green R, Puglisi JD., Free PMC Article | 08/28/2021 |
| Clustering and Fibril Formation during GNNQQNY Aggregation: A Molecular Dynamics Study. | Clustering and Fibril Formation during GNNQQNY Aggregation: A Molecular Dynamics Study.
Szała-Mendyk B, Molski A., Free PMC Article | 06/26/2021 |
| Aggregation and Prion-Inducing Properties of the G-Protein Gamma Subunit Ste18 are Regulated by Membrane Association. | Aggregation and Prion-Inducing Properties of the G-Protein Gamma Subunit Ste18 are Regulated by Membrane Association.
Chernova TA, Yang Z, Karpova TS, Shanks JR, Shcherbik N, Wilkinson KD, Chernoff YO., Free PMC Article | 02/27/2021 |
| Nucleation seed size determines amyloid clearance and establishes a barrier to prion appearance in yeast. | Nucleation seed size determines amyloid clearance and establishes a barrier to prion appearance in yeast.
Villali J, Dark J, Brechtel TM, Pei F, Sindi SS, Serio TR., Free PMC Article | 10/31/2020 |
| Short disordered protein segment regulates cross-species transmission of a yeast prion. | Short disordered protein segment regulates cross-species transmission of a yeast prion.
Shida T, Kamatari YO, Yoda T, Yamaguchi Y, Feig M, Ohhashi Y, Sugita Y, Kuwata K, Tanaka M. | 10/10/2020 |
| Using high-speed atomic force microscopy (HS-AFM), we directly visualized the prion determinant domain (Sup35NM) and the formation of its oligomers and fibrils at subsecond and submolecular resolutions. | Dynamics of oligomer and amyloid fibril formation by yeast prion Sup35 observed by high-speed atomic force microscopy.
Konno H, Watanabe-Nakayama T, Uchihashi T, Okuda M, Zhu L, Kodera N, Kikuchi Y, Ando T, Taguchi H., Free PMC Article | 07/18/2020 |
| The dramatic changes in the size and amounts of SDS-resistant Sup35p that occur during growth do not correlate with the infectious titer. | Growth phase-dependent changes in the size and infectivity of SDS-resistant Sup35p assemblies associated with the [PSI(+) ] prion in yeast.
Wang K, Melki R, Kabani M. | 05/23/2020 |
| Defects in the Dbp5-guided eRF1 delivery lead to premature contact and premature dissociation of eRF1 and eRF3 from the ribosome and to subsequent stop codon readthrough. Thus, the stepwise Dbp5-controlled termination complex assembly is essential for regular translation termination events | Translation termination depends on the sequential ribosomal entry of eRF1 and eRF3.
Beißel C, Neumann B, Uhse S, Hampe I, Karki P, Krebber H., Free PMC Article | 11/30/2019 |
| In all [PSI+] variants the Sup35 amino acid residues 2-32 were fully resistant and the region up to residue 72 was partially resistant to proteinase K digestion. Sup35 prion cores can be composed of up to four elements. | Yeast Sup35 Prion Structure: Two Types, Four Parts, Many Variants.
Dergalev AA, Alexandrov AI, Ivannikov RI, Ter-Avanesyan MD, Kushnirov VV., Free PMC Article | 11/16/2019 |
| Data show that parts of the Sup35NMp excluded from the fibril core can form a wide "coat". | Sup35NMp morphology evaluation on Au, Si, formvar and mica surfaces using AFM, SEM and TEM.
Sokolov PA, Bondarev SA, Belousov MV, Zhouravleva GA, Kasyanenko NA. | 10/12/2019 |
| The authors show that when [PSI(+) ] variants VK and VL co-infect a dividing host, only one prevails in the end and the host genetic background is involved in winner selection. | Forms and abundance of chaperone proteins influence yeast prion variant competition.
Yu CI, King CY. | 08/3/2019 |
| Data show no evidence to support that SUP35 protein (PSI (+) prion protein) induces chromosomal instability (CIN). | The [PSI (+)] yeast prion does not wildly affect proteome composition whereas selective pressure exerted on [PSI (+)] cells can promote aneuploidy.
Chan PHW, Lee L, Kim E, Hui T, Stoynov N, Nassar R, Moksa M, Cameron DM, Hirst M, Gsponer J, Mayor T., Free PMC Article | 03/30/2019 |
| amyloidogenic proteins promote prion nucleation in yeast | Mammalian amyloidogenic proteins promote prion nucleation in yeast.
Chandramowlishwaran P, Sun M, Casey KL, Romanyuk AV, Grizel AV, Sopova JV, Rubel AA, Nussbaum-Krammer C, Vorberg IM, Chernoff YO., Free PMC Article | 01/12/2019 |
| The role of SUP35 in protein folding in the ribosome and prion propagation | Protein Folding Activity of the Ribosome is involved in Yeast Prion Propagation.
Blondel M, Soubigou F, Evrard J, Nguyen PH, Hasin N, Chédin S, Gillet R, Contesse MA, Friocourt G, Stahl G, Jones GW, Voisset C., Free PMC Article | 05/19/2018 |
| With the use of both segmental and specific isotopic labeling schemes in combination with dynamic nuclear polarization (DNP) NMR, the study examined an amyloid form of Sup35NM that does not have a parallel in-register structure. | Combining DNP NMR with segmental and specific labeling to study a yeast prion protein strain that is not parallel in-register.
Frederick KK, Michaelis VK, Caporini MA, Andreas LB, Debelouchina GT, Griffin RG, Lindquist S., Free PMC Article | 05/12/2018 |
| In stressed conditions, Sup35 formed protective gels via pH-regulated liquid-like phase separation followed by gelation. | Phase separation of a yeast prion protein promotes cellular fitness.
Franzmann TM, Jahnel M, Pozniakovsky A, Mahamid J, Holehouse AS, Nüske E, Richter D, Baumeister W, Grill SW, Pappu RV, Hyman AA, Alberti S. | 04/14/2018 |
| proteolytic cleavage of Sup35 suppresses spontaneous de novo generation of the [PSI(+)] prion. | Proteolysis suppresses spontaneous prion generation in yeast.
Okamoto A, Hosoda N, Tanaka A, Newnam GP, Chernoff YO, Hoshino SI., Free PMC Article | 01/6/2018 |
| Hsp31 can modulate prion status in cooperation with Hsp104 because it inhibits Sup35 aggregate formation and potentiates [PSI(+)] prion curing upon overexpression of Hsp104 | The small heat shock protein Hsp31 cooperates with Hsp104 to modulate Sup35 prion aggregation.
Aslam K, Tsai CJ, Hazbun TR., Free PMC Article | 11/11/2017 |
| results show that the presence of Rnq1p in the cell significantly decreases the loss of [PSI;(+)] prion, which is caused by a double mutation in SUP35 (Q61K, Q62K substitutions in the Sup35 protein). | [Rnq1 protein protects [PSI^(+)] prion from effect of the PNM mutation].
Bondarev SA, Likholetova DV, Belousov MV, Zhouravleva GA. | 08/19/2017 |