Initial characterization of the nascent polypeptide-associated complex in yeast. - Wikidata - wikimedia - TriplyDB

Initial characterization of the nascent polypeptide-associated complex in yeast.

Initial characterization of the nascent polypeptide-associated complex in yeast.

http://www.wikidata.org/entity/Q27930105

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The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides Computational verification of protein-protein interactions by orthologous co-expression Ccr4-Not complex: the control freak of eukaryotic cells Crystal structures of NAC domains of human nascent polypeptide-associated complex (NAC) and its αNAC subunit OM14 is a mitochondrial receptor for cytosolic ribosomes that supports co-translational import into mitochondria.The yeast Ccr4-Not complex controls ubiquitination of the nascent-associated polypeptide (NAC-EGD) complex.The nascent polypeptide-associated complex (NAC) of yeast functions in the targeting process of ribosomes to the ER membrane.The synthetic genetic network around PKC1 identifies novel modulators and components of protein kinase C signaling in Saccharomyces cerevisiae RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin.L25 functions as a conserved ribosomal docking site shared by nascent chain-associated complex and signal-recognition particle.The alpha and beta subunit of the nascent polypeptide-associated complex have distinct functions Covert genetic selections to optimize phenotypes.Hierarchical functional specificity of cytosolic heat shock protein 70 (Hsp70) nucleotide exchange factors in yeast.A dual function for chaperones SSB-RAC and the NAC nascent polypeptide-associated complex on ribosomes Defining the specificity of cotranslationally acting chaperones by systematic analysis of mRNAs associated with ribosome-nascent chain complexes.Dual binding mode of the nascent polypeptide-associated complex reveals a novel universal adapter site on the ribosome.NAC functions as a modulator of SRP during the early steps of protein targeting to the endoplasmic reticulum.The nascent polypeptide-associated complex is a key regulator of proteostasis.A conserved motif is prerequisite for the interaction of NAC with ribosomal protein L23 and nascent chains.Inhibition of a basal transcription factor 3-like gene Osj10gBTF3 in rice results in significant plant miniaturization and typical pollen abortion.Association of protein biogenesis factors at the yeast ribosomal tunnel exit is affected by the translational status and nascent polypeptide sequence.Comparative analysis indicates regulatory neofunctionalization of yeast duplicates.Functional Dissection of the Nascent Polypeptide-Associated Complex in Saccharomyces cerevisiae Chaperone-assisted folding of newly synthesized proteins in the cytosol.Development stage-specific proteomic profiling uncovers small, lineage specific proteins most abundant in the Aspergillus Fumigatus conidial proteome.Nascent polypeptide-associated complex stimulates protein import into yeast mitochondria.Ribosome association and stability of the nascent polypeptide-associated complex is dependent upon its own ubiquitination.Access to ribosomal protein Rpl25p by the signal recognition particle is required for efficient cotranslational translocation.The African swine fever virus protein j4R binds to the alpha chain of nascent polypeptide-associated complex.TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes Analysis of the interplay of protein biogenesis factors at the ribosome exit site reveals new role for NAC.Transgenic tobacco plants constitutively expressing peanut BTF3 exhibit increased growth and tolerance to abiotic stresses.The yeast ubiquitin ligase Rsp5 downregulates the alpha subunit of nascent polypeptide-associated complex Egd2 under stress conditions.Role for ribosome-associated complex and stress-seventy subfamily B (RAC-Ssb) in integral membrane protein translation.αβ'-NAC cooperates with Sam37 to mediate early stages of mitochondrial protein import.OST1-mediated BTF3L phosphorylation positively regulates CBFs during plant cold responses.The crystal structure of archaeal nascent polypeptide-associated complex (NAC) reveals a unique fold and the presence of a ubiquitin-associated domain.The nascent polypeptide-associated complex (NAC) promotes interaction of ribosomes with the mitochondrial surface in vivo

P2860

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P2860

Initial characterization of the nascent polypeptide-associated complex in yeast.

http://www.wikidata.org/entity/Q27930105

description

1999 nî lūn-bûn

@nan

1999 թուականի Մարտին հրատարակուած գիտական յօդուած

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1999 թվականի մարտին հրատարակված գիտական հոդված

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1999年の論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年论文

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name

Initial characterization of the nascent polypeptide-associated complex in yeast.

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Initial characterization of the nascent polypeptide-associated complex in yeast.

@en

Initial characterization of the nascent polypeptide-associated complex in yeast.

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type

label

Initial characterization of the nascent polypeptide-associated complex in yeast.

@ast

Initial characterization of the nascent polypeptide-associated complex in yeast.

@en

Initial characterization of the nascent polypeptide-associated complex in yeast.

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altLabel

Initial characterization of the nascent polypeptide-associated complex in yeast

@en

prefLabel

Initial characterization of the nascent polypeptide-associated complex in yeast.

@ast

Initial characterization of the nascent polypeptide-associated complex in yeast.

@en

Initial characterization of the nascent polypeptide-associated complex in yeast.

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(SICI)1097-0061(19990330)15:5%3C397::AID-YEA384%3E3.0.CO;2-U

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Initial characterization of the nascent polypeptide-associated complex in yeast.

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B Reimann

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B Wiedmann

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E Hartmann

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P2860

Binding of signal recognition particle gives ribosome/nascent chain complexes a competitive advantage in endoplasmic reticulum membrane interaction.

Signal recognition particle-dependent targeting of ribosomes to the rough endoplasmic reticulum in the absence and presence of the nascent polypeptide-associated complex.

The EGD1 product, a yeast homolog of human BTF3, may be involved in GAL4 DNA binding.

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397-407

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10.1002/(SICI)1097-0061(19990330)15:5<397::AID-YEA384>3.0.CO;2-U

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