Solution structure of the dimerization domain of the eukaryotic stalk P1/P2 complex reveals the structural organization of eukaryotic stalk complex

Solution structure of the dimerization domain of the eukaryotic stalk P1/P2 complex reveals the structural organization of eukaryotic stalk complex

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http://www.wikidata.org/entity/Q24298826
Solution structure of human P1*P2 heterodimer provides insights into the role of eukaryotic stalk in recruiting the ribosome-inactivating protein trichosanthin to the ribosomePhosphorylation of initiation factor eIF2 in response to stress conditions is mediated by acidic ribosomal P1/P2 proteins in Saccharomyces cerevisiae.Human ribosomal P1-P2 heterodimer represents an optimal docking site for ricin A chain with a prominent role for P1 C-terminus.Targeting ricin to the ribosome.Crystal Structure of Ribosome-Inactivating Protein Ricin A Chain in Complex with the C-Terminal Peptide of the Ribosomal Stalk Protein P2.Structural insights into the interaction of the ribosomal P stalk protein P2 with a type II ribosome-inactivating protein ricin.Structures of eukaryotic ribosomal stalk proteins and its complex with trichosanthin, and their implications in recruiting ribosome-inactivating proteins to the ribosomes.Molecular insights into the interaction of the ribosomal stalk protein with elongation factor 1α.Molecular dissection of the silkworm ribosomal stalk complex: the role of multiple copies of the stalk proteins.Carboxy terminal modifications of the P0 protein reveal alternative mechanisms of nuclear ribosomal stalk assembly.Molten globule nature of Plasmodium falciparum P2 homo-tetramer.Multiplication of Ribosomal P-Stalk Proteins Contributes to the Fidelity of Translation.The C-terminal helix of ribosomal P stalk recognizes a hydrophobic groove of elongation factor 2 in a novel fashion.The acidic ribosomal protein P2 from Euplotes octocarinatus is phosphorylated at its N-terminal domain.Functional role of the C-terminal tail of the archaeal ribosomal stalk in recruitment of two elongation factors to the sarcin/ricin loop of 23S rRNA.Structural and Functional Investigation and Pharmacological Mechanism of Trichosanthin, a Type 1 Ribosome-Inactivating Protein
P2860

Solution structure of the dimerization domain of the eukaryotic stalk P1/P2 complex reveals the structural organization of eukaryotic stalk complex

Item
http://www.wikidata.org/entity/Q24298826
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2012 nî lūn-bûn
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2012 թուականի Ապրիլին հրատարակուած գիտական յօդուած
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2012 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2012年の論文
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2012年論文
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2012年論文
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2012年論文
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2012年論文
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2012年論文
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2012年论文
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name
Solution structure of the dime ...... on of eukaryotic stalk complex
@ast
Solution structure of the dime ...... on of eukaryotic stalk complex
@en
Solution structure of the dime ...... on of eukaryotic stalk complex
@en-gb
Solution structure of the dime ...... on of eukaryotic stalk complex
@nl
type
label
Solution structure of the dime ...... on of eukaryotic stalk complex
@ast
Solution structure of the dime ...... on of eukaryotic stalk complex
@en
Solution structure of the dime ...... on of eukaryotic stalk complex
@en-gb
Solution structure of the dime ...... on of eukaryotic stalk complex
@nl
prefLabel
Solution structure of the dime ...... on of eukaryotic stalk complex
@ast
Solution structure of the dime ...... on of eukaryotic stalk complex
@en
Solution structure of the dime ...... on of eukaryotic stalk complex
@en-gb
Solution structure of the dime ...... on of eukaryotic stalk complex
@nl
P1433
P1476
P2093
P2860
P304
P31
P3181
P356
P407
P433
P478
P50
P577
P5875
P698
P932
P3181
P356
P1433
P1476
Solution structure of the dime ...... on of eukaryotic stalk complex
@en
P2093
P2860
P304
P31
P3181
P356
P407
P433
P478
P50
P577
P5875
P698
P932