The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex.
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A novel human NatA Nalpha-terminal acetyltransferase complex: hNaa16p-hNaa10p (hNat2-hArd1)The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complexKnockdown of human N alpha-terminal acetyltransferase complex C leads to p53-dependent apoptosis and aberrant human Arl8b localizationThe chaperone-like protein HYPK acts together with NatA in cotranslational N-terminal acetylation and prevention of Huntingtin aggregationThe yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptidesThe cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome systemPrefoldin-nascent chain complexes in the folding of cytoskeletal proteinsMicroarray analysis of orthologous genes: conservation of the translational machinery across species at the sequence and expression levelLong-oligomer microarray profiling in Neurospora crassa reveals the transcriptional program underlying biochemical and physiological events of conidial germination.A functional chaperone triad on the yeast ribosomeThe Hsp70 homolog Ssb is essential for glucose sensing via the SNF1 kinase networkSti1 is a novel activator of the Ssa proteins.Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1pFine-tuning of translation termination efficiency in Saccharomyces cerevisiae involves two factors in close proximity to the exit tunnel of the ribosome.A lysine-rich region within fungal BAG domain-containing proteins mediates a novel association with ribosomes.A ribosome-anchored chaperone network that facilitates eukaryotic ribosome biogenesisZuotin, a ribosome-associated DnaJ molecular chaperoneHyperactive forms of the Pdr1p transcription factor fail to respond to positive regulation by the hsp70 protein Pdr13p.The yeast hsp70 homologue Ssa is required for translation and interacts with Sis1 and Pab1 on translating ribosomes.Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins.Novel G-protein complex whose requirement is linked to the translational status of the cell.Posttranscriptional control of gene expression in yeast.The ribosome-bound chaperones RAC and Ssb1/2p are required for accurate translation in Saccharomyces cerevisiae.Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC systemA nuclear export signal prevents Saccharomyces cerevisiae Hsp70 Ssb1p from stimulating nuclear localization signal-directed nuclear transport.RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin.The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone.The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains.Pathways of chaperone-mediated protein folding in the cytosolHsp110 is required for spindle length control.Molecular cloning and characterization of the Candida albicans UBI3 gene coding for a ubiquitin-hybrid protein.Identification and characterization of a drug-sensitive strain enables puromycin-based translational assays in Saccharomyces cerevisiae.A dual function for chaperones SSB-RAC and the NAC nascent polypeptide-associated complex on ribosomesDivergent functional properties of the ribosome-associated molecular chaperone Ssb compared with other Hsp70s.The glycine-phenylalanine-rich region determines the specificity of the yeast Hsp40 Sis1.Evidence for a protein mutator in yeast: role of the Hsp70-related chaperone ssb in formation, stability, and toxicity of the [PSI] prion.The in vivo function of the ribosome-associated Hsp70, Ssz1, does not require its putative peptide-binding domain.Maturation of steroid receptors: an example of functional cooperation among molecular chaperones and their associated proteinsHsp90 interacts specifically with viral RNA and differentially regulates replication initiation of Bamboo mosaic virus and associated satellite RNANovel protein phosphatases in yeast.
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P2860
The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex.
description
1998 nî lūn-bûn
@nan
1998 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
name
The molecular chaperone Ssb fr ...... ibosome-nascent chain complex.
@ast
The molecular chaperone Ssb fr ...... ibosome-nascent chain complex.
@en
The molecular chaperone Ssb fr ...... ibosome-nascent chain complex.
@nl
type
label
The molecular chaperone Ssb fr ...... ibosome-nascent chain complex.
@ast
The molecular chaperone Ssb fr ...... ibosome-nascent chain complex.
@en
The molecular chaperone Ssb fr ...... ibosome-nascent chain complex.
@nl
prefLabel
The molecular chaperone Ssb fr ...... ibosome-nascent chain complex.
@ast
The molecular chaperone Ssb fr ...... ibosome-nascent chain complex.
@en
The molecular chaperone Ssb fr ...... ibosome-nascent chain complex.
@nl
P2093
P2860
P3181
P356
P1433
P1476
The molecular chaperone Ssb fr ...... ibosome-nascent chain complex.
@en
P2093
B A Schilke
M Wiedmann
N Lopez-Hoyo
P Lopez-Buesa
T Ziegelhoffer
W A Walter
P2860
P304
P3181
P356
10.1093/EMBOJ/17.14.3981
P407
P577
1998-07-15T00:00:00Z