Mutation processes at the protein level: is Lamarck back?
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THE EVOLUTION OF THE EVOLVABILITY PROPERTIES OF THE YEAST PRION [PSI + ]A scientific revolution? The prion anomaly may challenge the central dogma of molecular biologyLike father like son. A fresh review of the inheritance of acquired characteristicsYeast prions: protein aggregation is not enoughFine-tuning of translation termination efficiency in Saccharomyces cerevisiae involves two factors in close proximity to the exit tunnel of the ribosome.Challenges for the Modern Science in its Descend Towards Nano ScaleTightly regulated and heritable division control in single bacterial cells.A novel mutant of the Sup35 protein of Saccharomyces cerevisiae defective in translation termination and in GTPase activity still supports cell viability.Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities.Genetic interactions between [PSI+] and nonstop mRNA decay affect phenotypic variationLuminidependens (LD) is an Arabidopsis protein with prion behavior.Yeast prion protein derivative defective in aggregate shearing and production of new 'seeds'Mouse GSPT2, but not GSPT1, can substitute for yeast eRF3 in vivo.Poly(A)-binding protein acts in translation termination via eukaryotic release factor 3 interaction and does not influence [PSI(+)] propagation.Does the central dogma still stand?Microbiome, holobiont and the net of life.Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]Evolutionary capacitance may be favored by natural selection.A small, glutamine-free domain propagates the [SWI(+)] prion in budding yeast.Prions in yeast.An overview of transmissible spongiform encephalopathies.Diversify or die: generation of diversity in response to stress.Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1The elongation of yeast prion fibers involves separable steps of association and conversion.Stress and prions: lessons from the yeast model.Propagation of the [PIN+] prion by fragments of Rnq1 fused to GFPChaperone effects on prion and nonprion aggregates.Biological roles of prion domains.Hsp104 and prion propagation.Physiological and environmental control of yeast prions.Prion: disease or relief?Mechanism of prion loss after Hsp104 inactivation in yeast.Strains of [PSI(+)] are distinguished by their efficiencies of prion-mediated conformational conversionModulation of prion formation, aggregation, and toxicity by the actin cytoskeleton in yeast.Prion-dependent lethality of sup45 mutants in Saccharomyces cerevisiae.Pleiotropic effects of Ubp6 loss on drug sensitivities and yeast prion are due to depletion of the free ubiquitin pool.Screening for amyloid proteins in the yeast proteome.Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model.Allelic variants of hereditary prions: The bimodularity principle.
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P2860
Mutation processes at the protein level: is Lamarck back?
description
2001 nî lūn-bûn
@nan
2001 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի մարտին 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
Mutation processes at the protein level: is Lamarck back?
@ast
Mutation processes at the protein level: is Lamarck back?
@en
Mutation processes at the protein level: is Lamarck back?
@nl
type
label
Mutation processes at the protein level: is Lamarck back?
@ast
Mutation processes at the protein level: is Lamarck back?
@en
Mutation processes at the protein level: is Lamarck back?
@nl
prefLabel
Mutation processes at the protein level: is Lamarck back?
@ast
Mutation processes at the protein level: is Lamarck back?
@en
Mutation processes at the protein level: is Lamarck back?
@nl
P1433
P1476
Mutation processes at the protein level: is Lamarck back?
@en
P2093
Y O Chernoff
P356
10.1016/S1383-5742(00)00060-0
P407
P577
2001-03-01T00:00:00Z