The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p
about
Moonlighting proteins in yeastsAlterations in the Ure2 αCap domain elicit different GATA factor responses to rapamycin treatment and nitrogen limitationGln3p nuclear localization and interaction with Ure2p in Saccharomyces cerevisiaeA model for Ure2p prion filaments and other amyloids: the parallel superpleated beta-structureIdentification of a small molecule that modifies MglA/SspA interaction and impairs intramacrophage survival of Francisella tularensisParallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p.Yeast prions assembly and propagation: contributions of the prion and non-prion moieties and the nature of assemblies.Amyloid-like aggregates of the yeast prion protein ure2 enter vertebrate cells by specific endocytotic pathways and induce apoptosis.The core of Ure2p prion fibrils is formed by the N-terminal segment in a parallel cross-β structure: evidence from solid-state NMR.Mechanism of inactivation on prion conversion of the Saccharomyces cerevisiae Ure2 protein.The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitroPrions: En route from structural models to structures.Characterization of an Nmr homolog that modulates GATA factor-mediated nitrogen metabolite repression in Cryptococcus neoformans.Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein.Prion domain of yeast Ure2 protein adopts a completely disordered structure: a solid-support EPR studyThe relationship of prions and translationThe [URE3] prion is not conserved among Saccharomyces speciesIn Sup35p filaments (the [PSI+] prion), the globular C-terminal domains are widely offset from the amyloid fibril backboneNetwork-dosage compensation topologies as recurrent network motifs in natural gene networksUre2, a prion precursor with homology to glutathione S-transferase, protects Saccharomyces cerevisiae cells from heavy metal ion and oxidant toxicity.Hierarchical organization in the amyloid core of yeast prion protein Ure2.Self-Assembly of Amyloid Fibrils That Display Active Enzymes.Molecular chaperones and the assembly of the prion Ure2p in vitro.Ure2p function is enhanced by its prion domain in Saccharomyces cerevisiae.Prions in yeast.Insights into the architecture of the Ure2p yeast protein assemblies from helical twisted fibrilsHuman J-protein DnaJB6b Cures a Subset of Saccharomyces cerevisiae Prions and Selectively Blocks Assembly of Structurally Related Amyloids.Scrambled prion domains form prions and amyloid.Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2Recent advances in nitrogen regulation: a comparison between Saccharomyces cerevisiae and filamentous fungiDisulfide bond formation significantly accelerates the assembly of Ure2p fibrils because of the proximity of a potential amyloid stretch.Synthetic lipid vesicles recruit native-like aggregates and affect the aggregation process of the prion Ure2p: insights on vesicle permeabilization and charge selectivity.Conservation of the prion properties of Ure2p through evolution.In vivo specificity of Ure2 protection from heavy metal ion and oxidative cellular damage in Saccharomyces cerevisiae.Direct observation of oligomerization by single molecule fluorescence reveals a multi-step aggregation mechanism for the yeast prion protein Ure2.Three distinct-type glutathione S-transferases from Escherichia coli important for defense against oxidative stress.Heavy metal sensitivities of gene deletion strains for ITT1 and RPS1A connect their activities to the expression of URE2, a key gene involved in metal detoxification in yeast
P2860
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P2860
The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p
description
2001 nî lūn-bûn
@nan
2001 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2001年の論文
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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
name
The crystal structure of the n ...... the yeast prion protein Ure2p
@ast
The crystal structure of the n ...... the yeast prion protein Ure2p
@en
The crystal structure of the n ...... the yeast prion protein Ure2p
@nl
type
label
The crystal structure of the n ...... the yeast prion protein Ure2p
@ast
The crystal structure of the n ...... the yeast prion protein Ure2p
@en
The crystal structure of the n ...... the yeast prion protein Ure2p
@nl
prefLabel
The crystal structure of the n ...... the yeast prion protein Ure2p
@ast
The crystal structure of the n ...... the yeast prion protein Ure2p
@en
The crystal structure of the n ...... the yeast prion protein Ure2p
@nl
P2093
P2860
P921
P356
P1476
The crystal structure of the n ...... the yeast prion protein Ure2p
@en
P2093
P2860
P304
P356
10.1073/PNAS.98.4.1459
P407
P50
P577
2001-02-13T00:00:00Z