Solution structure of human P1*P2 heterodimer provides insights into the role of eukaryotic stalk in recruiting the ribosome-inactivating protein trichosanthin to the ribosome

Solution structure of human P1*P2 heterodimer provides insights into the role of eukaryotic stalk in recruiting the ribosome-inactivating protein trichosanthin to the ribosome

Item
http://www.wikidata.org/entity/Q27679227
Do the A subunits contribute to the differences in the toxicity of Shiga toxin 1 and Shiga toxin 2?Structures and Ribosomal Interaction of Ribosome-Inactivating ProteinsFunctional divergence between the two P1-P2 stalk dimers on the ribosome in their interaction with ricin A chainHuman ribosomal P1-P2 heterodimer represents an optimal docking site for ricin A chain with a prominent role for P1 C-terminus.Arginine residues on the opposite side of the active site stimulate the catalysis of ribosome depurination by ricin A chain by interacting with the P-protein stalkCrystal 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.Ricin uses arginine 235 as an anchor residue to bind to P-proteins of the ribosomal stalk.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.Molten globule nature of Plasmodium falciparum P2 homo-tetramer.The C-terminal helix of ribosomal P stalk recognizes a hydrophobic groove of elongation factor 2 in a novel fashion.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.Functional Assays for Measuring the Catalytic Activity of Ribosome Inactivating Proteins.Structural and Functional Investigation and Pharmacological Mechanism of Trichosanthin, a Type 1 Ribosome-Inactivating ProteinPeptide Mimics of the Ribosomal P Stalk Inhibit the Activity of Ricin A Chain by Preventing Ribosome Binding
P2860

Solution structure of human P1*P2 heterodimer provides insights into the role of eukaryotic stalk in recruiting the ribosome-inactivating protein trichosanthin to the ribosome

Item
http://www.wikidata.org/entity/Q27679227
description
2013 nî lūn-bûn
@nan
2013 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Solution structure of human P1 ...... trichosanthin to the ribosome
@ast
Solution structure of human P1 ...... trichosanthin to the ribosome
@en
Solution structure of human P1 ...... trichosanthin to the ribosome
@nl
type
label
Solution structure of human P1 ...... trichosanthin to the ribosome
@ast
Solution structure of human P1 ...... trichosanthin to the ribosome
@en
Solution structure of human P1 ...... trichosanthin to the ribosome
@nl
prefLabel
Solution structure of human P1 ...... trichosanthin to the ribosome
@ast
Solution structure of human P1 ...... trichosanthin to the ribosome
@en
Solution structure of human P1 ...... trichosanthin to the ribosome
@nl
P1433
P1476
P2093
P2860
P304
P31
P3181
P356
P407
P433
P478
P50
P577
P5875
P698
P921
P932
P3181
P356
P1433
P1476
Solution structure of human P1 ...... trichosanthin to the ribosome
@en
P2093
P2860
P304
P31
P3181
P356
P407
P433
P478
P50
P577
P5875
P698
P921
P932