Charged and hydrophobic surfaces on the a chain of shiga-like toxin 1 recognize the C-terminal domain of ribosomal stalk proteins
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Do the A subunits contribute to the differences in the toxicity of Shiga toxin 1 and Shiga toxin 2?Shiga Toxin (Stx) Classification, Structure, and FunctionSelection of recombinant anti-SH3 domain antibodies by high-throughput phage display.The A1 Subunit of Shiga Toxin 2 Has Higher Affinity for Ribosomes and Higher Catalytic Activity than the A1 Subunit of Shiga Toxin 1.Differences in Ribosome Binding and Sarcin/Ricin Loop Depurination by Shiga and Ricin HolotoxinsHuman ribosomal P1-P2 heterodimer represents an optimal docking site for ricin A chain with a prominent role for P1 C-terminus.Maize ribosome-inactivating protein uses Lys158-lys161 to interact with ribosomal protein P2 and the strength of interaction is correlated to the biological activities.The P1/P2 proteins of the human ribosomal stalk are required for ribosome binding and depurination by ricin in human cellsTargeting ricin to the ribosome.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.Conserved Arginines at the P-Protein Stalk Binding Site and the Active Site Are Critical for Ribosome Interactions of Shiga Toxins but Do Not Contribute to Differences in the Affinity of the A1 Subunits for the Ribosome.Ricin uses arginine 235 as an anchor residue to bind to P-proteins of the ribosomal stalk.Facing glycosphingolipid-Shiga toxin interaction: dire straits for endothelial cells of the human vasculature.Structures of eukaryotic ribosomal stalk proteins and its complex with trichosanthin, and their implications in recruiting ribosome-inactivating proteins to the ribosomes.Toxicity of ricin A chain is reduced in mammalian cells by inhibiting its interaction with the ribosome.Extensive Evolution of Cereal Ribosome-Inactivating Proteins Translates into Unique Structural Features, Activation Mechanisms, and Physiological RolesStructural 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
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P2860
Charged and hydrophobic surfaces on the a chain of shiga-like toxin 1 recognize the C-terminal domain of ribosomal stalk proteins
description
2012 nî lūn-bûn
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2012 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2012年の論文
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2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
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name
Charged and hydrophobic surfac ...... in of ribosomal stalk proteins
@ast
Charged and hydrophobic surfac ...... in of ribosomal stalk proteins
@en
Charged and hydrophobic surfac ...... in of ribosomal stalk proteins
@nl
type
label
Charged and hydrophobic surfac ...... in of ribosomal stalk proteins
@ast
Charged and hydrophobic surfac ...... in of ribosomal stalk proteins
@en
Charged and hydrophobic surfac ...... in of ribosomal stalk proteins
@nl
prefLabel
Charged and hydrophobic surfac ...... in of ribosomal stalk proteins
@ast
Charged and hydrophobic surfac ...... in of ribosomal stalk proteins
@en
Charged and hydrophobic surfac ...... in of ribosomal stalk proteins
@nl
P2093
P2860
P1433
P1476
Charged and hydrophobic surfac ...... in of ribosomal stalk proteins
@en
P2093
Andrew J McCluskey
Eleonora Bolewska-Pedyczak
Jean Gariépy
Nick Jarvik
Sachdev S Sidhu
P2860
P304
P356
10.1371/JOURNAL.PONE.0031191
P407
P577
2012-02-15T00:00:00Z