Oligopeptide repeats in the yeast protein Sup35p stabilize intermolecular prion interactions.
about
Complex adaptations can drive the evolution of the capacitor [PSI], even with realistic rates of yeast sexThe role of the N-terminal oligopeptide repeats of the yeast Sup35 prion protein in propagation and transmission of prion variantsThe strength of selection against the yeast prion [PSI+]Melanosomes--dark organelles enlighten endosomal membrane transportAmyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structureDissection and design of yeast prionsPotential roles for prions and protein-only inheritance in cancerYeast prions and human prion-like proteins: sequence features and prediction methodsThe [RNQ+] prion: a model of both functional and pathological amyloidProbing the role of structural features of mouse PrP in yeast by expression as Sup35-PrP fusionsOverlapping functions of argonaute proteins in patterning and morphogenesis of Drosophila embryosSplice variants of perlucin from Haliotis laevigata modulate the crystallisation of CaCO3Natural variation of the amino-terminal glutamine-rich domain in Drosophila argonaute2 is not associated with developmental defectsProtRepeatsDB: a database of amino acid repeats in genomes.Prion protein insertional mutations increase aggregation propensity but not fiber stability.Distinct type of transmission barrier revealed by study of multiple prion determinants of Rnq1.Effect of domestication on the spread of the [PIN+] prion in Saccharomyces cerevisiae.Primary sequence independence for prion formation[PSI+] maintenance is dependent on the composition, not primary sequence, of the oligopeptide repeat domain.Yeast prion protein derivative defective in aggregate shearing and production of new 'seeds'Poly(A)-binding protein acts in translation termination via eukaryotic release factor 3 interaction and does not influence [PSI(+)] propagation.Structural insights into a yeast prion illuminate nucleation and strain diversityConserved roles of the prion protein domains on subcellular localization and cell-cell adhesionDistinct amino acid compositional requirements for formation and maintenance of the [PSI⁺] prion in yeast.Increasing prion propensity by hydrophobic insertion.Propagation of yeast prions.Insight into molecular basis of curing of [PSI+] prion by overexpression of 104-kDa heat shock protein (Hsp104).Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI+].Generating new prions by targeted mutation or segment duplication.The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization.Prion protein repeat expansion results in increased aggregation and reveals phenotypic variability.Prions in yeast.Distinct Prion Domain Sequences Ensure Efficient Amyloid Propagation by Promoting Chaperone Binding or Processing In Vivo.Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein compositionPropagation of the [PIN+] prion by fragments of Rnq1 fused to GFPInsights into intragenic and extragenic effectors of prion propagation using chimeric prion proteins.Prion stability.The genetic control of the formation and propagation of the [PSI+] prion of yeast.N-terminal domains elicit formation of functional Pmel17 amyloid fibrilsA novel splice variant of Pmel17 expressed by human melanocytes and melanoma cells lacking some of the internal repeats.
P2860
Q21563345-E9A5D063-DCB5-4948-8A4A-F09EE68E2126Q24545846-BEF0DD76-F04C-4D4A-8839-5024324E07DFQ24645062-104A0FDA-A2C9-481F-B7FF-FD724617454DQ24647195-5ECF0FD1-4E13-4CCA-BC4D-EB1FD3C73F1DQ24676369-72ACC6F3-A9D9-4539-8328-CA5630577E7AQ24801750-2F57E165-5364-4819-9590-EC61E2084837Q26825056-16CE8B59-794A-4D8F-ADED-1672F00111BDQ26863334-F038F427-C73D-43E5-BEB5-9B9A9301EFF9Q27008442-11008E06-E243-4248-91CC-603808EC276EQ27022544-A08E1C06-C8F0-43CF-9BA6-C5FD119E7E4EQ27315245-A4ECEB3C-7CC6-4166-B0D8-998E6CCDB6B2Q28538777-D0F13F00-C9C3-47A2-9F01-D40E3A9CE15EQ28744151-F94F7B0D-E850-46C2-B03A-1B77131B7285Q33249306-95D9AA0E-D445-454F-BEC0-E222D2B59921Q33325657-4B4D0BE0-7F45-4700-87D5-78F41986ACF0Q33527001-EF7EC7F1-4B88-4FC0-9DEC-659FF7D0CEAAQ33895003-5D4B2720-9021-4A53-BDF3-585FD56FC163Q33943998-7FB44BD5-D18B-496D-8E23-87F524AAF27FQ33961634-C828AC12-E0D5-4BD7-B17D-52027C180A6CQ34085020-14F0C577-EEC7-4F20-80FE-4A314428CAF8Q34278926-02B53A69-D80A-41F7-8F99-04525C2EDD4EQ34425023-C345919D-A8FE-45B3-B8C5-EA4FA8824FF5Q34922583-2EEB12F0-5793-495A-B41C-150B735300D7Q35069582-9821216E-3C65-4AA5-AD54-E99841D494BEQ35106999-DAA9C4EE-4844-42A1-B98E-7BAD0E974C64Q35587875-7878D49E-1F61-4237-9717-14580923137BQ35643775-686F4B80-DB18-4826-80BF-EE1659BD5DD3Q35852028-5B3845F5-C962-40CA-A8B1-C56F0C79ABF7Q35865739-9671AB09-7839-4BF1-B03C-C48D07C2BCF8Q35927987-34786A98-3018-4B2F-849B-FDA213CEE53BQ35950108-411BBF29-853F-4653-A541-329BA3088F95Q36154362-C548467D-2B48-4FC5-BE2D-75290FA20316Q36182814-6F68E157-F571-4701-B49A-D538B1A4D490Q36678054-7D6F4A8A-BD71-4B4D-BDDB-118D6A98E073Q37004185-54840877-A79B-46E1-BC5E-A13997842039Q37355539-AFCBD1A6-95DB-4327-90A7-68B176E2BA45Q37375804-A53F24CE-0225-411E-B6A9-01393CB73AFDQ37375844-556E0C42-BA3B-48BF-B180-AC555812A9A2Q37467613-FB7D03E5-C086-4E78-A981-C0CEFD608E7FQ37476322-4BBA5A23-2B3D-4D95-84BA-165C8E4D2B5C
P2860
Oligopeptide repeats in the yeast protein Sup35p stabilize intermolecular prion interactions.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
2001年论文
@zh
2001年论文
@zh-cn
name
Oligopeptide repeats in the ye ...... rmolecular prion interactions.
@en
Oligopeptide repeats in the ye ...... rmolecular prion interactions.
@nl
type
label
Oligopeptide repeats in the ye ...... rmolecular prion interactions.
@en
Oligopeptide repeats in the ye ...... rmolecular prion interactions.
@nl
prefLabel
Oligopeptide repeats in the ye ...... rmolecular prion interactions.
@en
Oligopeptide repeats in the ye ...... rmolecular prion interactions.
@nl
P2093
P2860
P356
P1433
P1476
Oligopeptide repeats in the ye ...... rmolecular prion interactions.
@en
P2093
P2860
P304
P356
10.1093/EMBOJ/20.9.2111
P407
P577
2001-05-01T00:00:00Z