The catalytic subunit of shiga-like toxin 1 interacts with ribosomal stalk proteins and is inhibited by their conserved C-terminal domain.
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The C-terminal fragment of the ribosomal P protein complexed to trichosanthin reveals the interaction between the ribosome-inactivating protein and the ribosomeRibosome-inactivating proteins: from plant defense to tumor attackDo the A subunits contribute to the differences in the toxicity of Shiga toxin 1 and Shiga toxin 2?Shiga Toxin (Stx) Classification, Structure, and FunctionActivation of cell stress response pathways by Shiga toxinsSolution structure of the dimerization domain of ribosomal protein P2 provides insights for the structural organization of eukaryotic stalkSolution structure of human P1*P2 heterodimer provides insights into the role of eukaryotic stalk in recruiting the ribosome-inactivating protein trichosanthin to the ribosomeStructures and Ribosomal Interaction of Ribosome-Inactivating ProteinsPokeweed antiviral protein: its cytotoxicity mechanism and applications in plant disease resistanceThe 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 HolotoxinsInduction of apoptosis by Shiga toxins.Engineered toxins "zymoxins" are activated by the HCV NS3 protease by removal of an inhibitory protein domain.Functional 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.Interaction of ricin and Shiga toxins with ribosomesCharged and hydrophobic surfaces on the a chain of shiga-like toxin 1 recognize the C-terminal domain of ribosomal stalk proteinsPentameric organization of the ribosomal stalk accelerates recruitment of ricin a chain to the ribosome for depurination.Maize ribosome-inactivating protein uses Lys158-lys161 to interact with ribosomal protein P2 and the strength of interaction is correlated to the biological activities.Identification of amino acids critical for the cytotoxicity of Shiga toxin 1 and 2 in Saccharomyces cerevisiae.Shiga toxin 1 is more dependent on the P proteins of the ribosomal stalk for depurination activity than Shiga toxin 2Disruption of the ribosomal P complex leads to stress-induced autophagy.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.The ribosomal stalk is required for ribosome binding, depurination of the rRNA and cytotoxicity of ricin A chain in Saccharomyces cerevisiaeAB5 Preassembly Is Not Required for Shiga Toxin Activity.Structural insights into the neutralization mechanism of monoclonal antibody 6C2 against ricin.A two-step binding model proposed for the electrostatic interactions of ricin a chain with ribosomes.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.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.The interactions of human neutrophils with shiga toxins and related plant toxins: danger or safety?Structures of eukaryotic ribosomal stalk proteins and its complex with trichosanthin, and their implications in recruiting ribosome-inactivating proteins to the ribosomes.Shiga toxins: from structure and mechanism to applications.Toxicity of ricin A chain is reduced in mammalian cells by inhibiting its interaction with the ribosome.The carcinoembryonic antigen IgV-like N domain plays a critical role in the implantation of metastatic tumor cells.Extensive Evolution of Cereal Ribosome-Inactivating Proteins Translates into Unique Structural Features, Activation Mechanisms, and Physiological RolesRegulation of cytokine and chemokine expression by the ribotoxic stress response elicited by Shiga toxin type 1 in human macrophage-like THP-1 cells
P2860
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P2860
The catalytic subunit of shiga-like toxin 1 interacts with ribosomal stalk proteins and is inhibited by their conserved C-terminal domain.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh
2008年學術文章
@zh-hant
name
The catalytic subunit of shiga ...... r conserved C-terminal domain.
@en
The catalytic subunit of shiga ...... r conserved C-terminal domain.
@nl
type
label
The catalytic subunit of shiga ...... r conserved C-terminal domain.
@en
The catalytic subunit of shiga ...... r conserved C-terminal domain.
@nl
prefLabel
The catalytic subunit of shiga ...... r conserved C-terminal domain.
@en
The catalytic subunit of shiga ...... r conserved C-terminal domain.
@nl
P2093
P1476
The catalytic subunit of shiga ...... r conserved C-terminal domain.
@en
P2093
Andrew J McCluskey
Brian Raught
Eleonora Bolewska-Pedyczak
Gregory M K Poon
Jean Gariépy
Stanley M Jeram
Tharan Srikumar
P304
P356
10.1016/J.JMB.2008.02.014
P407
P577
2008-02-15T00:00:00Z