about
Structure-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active siteX-ray sequence and crystal structure of luffaculin 1, a novel type 1 ribosome-inactivating proteinCrystal structure of PD-L1, a ribosome inactivating protein from Phytolacca dioica L. leaves with the property to induce DNA cleavageTransition state analogues in structures of ricin and saporin ribosome-inactivating proteinsStructures of the ribosome-inactivating protein from barley seeds reveal a unique activation mechanismFirst structural evidence of sequestration of mRNA cap structures by type 1 ribosome inactivating protein from Momordica balsaminaStructures and Ribosomal Interaction of Ribosome-Inactivating ProteinsRibosome-Inactivating Proteins from Plants: A Historical OverviewIsolation, characterization, sequencing and crystal structure of charybdin, a type 1 ribosome-inactivating protein from Charybdis maritima agg.Identification of small-molecule inhibitors of ricin and shiga toxin using a cell-based high-throughput screenIdentification of new classes of ricin toxin inhibitors by virtual screening.Llama-derived single domain antibodies specific for Abrus agglutinin.Maize ribosome-inactivating protein uses Lys158-lys161 to interact with ribosomal protein P2 and the strength of interaction is correlated to the biological activities.Linking Single Domain Antibodies that Recognize Different Epitopes on the Same Target.A two-step binding model proposed for the electrostatic interactions of ricin a chain with ribosomes.Crystal Structure of Ribosome-Inactivating Protein Ricin A Chain in Complex with the C-Terminal Peptide of the Ribosomal Stalk Protein P2.Ricin uses arginine 235 as an anchor residue to bind to P-proteins of the ribosomal stalk.Structure-based design of ricin inhibitors.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 RolesBiological activities of the antiviral protein BE27 from sugar beet (Beta vulgaris L.).A Long Journey to the Cytosol
P2860
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P2860
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
The structure of ribosome inactivating proteins.
@ast
The structure of ribosome inactivating proteins.
@en
type
label
The structure of ribosome inactivating proteins.
@ast
The structure of ribosome inactivating proteins.
@en
prefLabel
The structure of ribosome inactivating proteins.
@ast
The structure of ribosome inactivating proteins.
@en
P356
P1476
The structure of ribosome inactivating proteins.
@en
P2093
Arthur F Monzingo
Jon D Robertus
P304
P356
10.2174/1389557043403837
P577
2004-06-01T00:00:00Z