The crystal structure of archaeal nascent polypeptide-associated complex (NAC) reveals a unique fold and the presence of a ubiquitin-associated domain.
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Proteomic Analysis of Interaction between a Plant Virus and Its Vector Insect Reveals New Functions of Hemipteran Cuticular ProteinCcr4-Not complex: the control freak of eukaryotic cellsThe Not4 RING E3 Ligase: A Relevant Player in Cotranslational Quality ControlCrystal structures of NAC domains of human nascent polypeptide-associated complex (NAC) and its αNAC subunitThe yeast Ccr4-Not complex controls ubiquitination of the nascent-associated polypeptide (NAC-EGD) complex.L25 functions as a conserved ribosomal docking site shared by nascent chain-associated complex and signal-recognition particle.Specific targeting of proteins to outer envelope membranes of endosymbiotic organelles, chloroplasts, and mitochondriaRotational restriction of nascent peptides as an essential element of co-translational protein folding: possible molecular players and structural consequences.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.A conserved motif is prerequisite for the interaction of NAC with ribosomal protein L23 and nascent chains.Functional Dissection of the Nascent Polypeptide-Associated Complex in Saccharomyces cerevisiaeRibosome association and stability of the nascent polypeptide-associated complex is dependent upon its own ubiquitination.Exploring the roles of basal transcription factor 3 in eukaryotic growth and development.Intrinsic indicators for specimen degradation.alphaNAC depletion as an initiator of ER stress-induced apoptosis in hypoxia.Analysis of the interplay of protein biogenesis factors at the ribosome exit site reveals new role for NAC.Shape evolution with temperature of a thermotolerant protein (PeaT1) in solution detected by small angle X-ray scattering.αβ'-NAC cooperates with Sam37 to mediate early stages of mitochondrial protein import.Conformational flexibility within the nascent polypeptide-associated complex enables its interactions with structurally diverse client proteins.Cytosolic targeting factor AKR2A captures chloroplast outer membrane-localized client proteins at the ribosome during translation.
P2860
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P2860
The crystal structure of archaeal nascent polypeptide-associated complex (NAC) reveals a unique fold and the presence of a ubiquitin-associated domain.
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2005 nî lūn-bûn
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2005年の論文
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2005年学术文章
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2005年学术文章
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2005年学术文章
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2005年學術文章
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name
The crystal structure of archa ...... a ubiquitin-associated domain.
@en
The crystal structure of archaeal nascent polypeptide-associated complex
@nl
type
label
The crystal structure of archa ...... a ubiquitin-associated domain.
@en
The crystal structure of archaeal nascent polypeptide-associated complex
@nl
prefLabel
The crystal structure of archa ...... a ubiquitin-associated domain.
@en
The crystal structure of archaeal nascent polypeptide-associated complex
@nl
P2093
P2860
P356
P1476
The crystal structure of archa ...... a ubiquitin-associated domain.
@en
P2093
Birgitta Beatrix
Markus Pech
Thomas Spreter
P2860
P304
15849-15854
P356
10.1074/JBC.M500160200
P407
P577
2005-01-22T00:00:00Z