The highly refined solution structure of the cytotoxic ribonuclease alpha-sarcin reveals the structural requirements for substrate recognition and ribonucleolytic activity
about
Molecular dynamics simulations of sarcin-ricin rRNA motif.Solution structure and dynamics of ribonuclease SaX-ray structure of two crystalline forms of a streptomycete ribonuclease with cytotoxic activityMicrobial ribonucleases (RNases): production and application potential.Cleavage of the sarcin-ricin loop of 23S rRNA differentially affects EF-G and EF-Tu bindingTyr-48, a conserved residue in ribotoxins, is involved in the RNA-degrading activity of alpha-sarcin.Fungal ribotoxins: molecular dissection of a family of natural killers.A deimmunised form of the ribotoxin, α-sarcin, lacking CD4+ T cell epitopes and its use as an immunotoxin warhead.Isosteric and nonisosteric base pairs in RNA motifs: molecular dynamics and bioinformatics study of the sarcin-ricin internal loop.Involvement of the amino-terminal beta-hairpin of the Aspergillus ribotoxins on the interaction with membranes and nonspecific ribonuclease activity.Hirsutellin A: A Paradigmatic Example of the Insecticidal Function of Fungal Ribotoxins.Fungal proteinaceous compounds with multiple biological activities.Conditional protein splicing of α-sarcin in live cells.Fungal Ribotoxins: A Review of Potential Biotechnological Applications.Effect of mutations in VP5 hydrophobic loops on rotavirus cell entryLeucine 145 of the ribotoxin alpha-sarcin plays a key role for determining the specificity of the ribosome-inactivating activity of the protein.NMR structure of the noncytotoxic alpha-sarcin mutant Delta(7-22): the importance of the native conformation of peripheral loops for activity.Cytotoxic mechanism of the ribotoxin alpha-sarcin. Induction of cell death via apoptosis.Arginine 121 is a crucial residue for the specific cytotoxic activity of the ribotoxin alpha-sarcin.Tautomeric state of alpha-sarcin histidines. Ndelta tautomers are a common feature in the active site of extracellular microbial ribonucleases.Conserved asparagine residue 54 of alpha-sarcin plays a role in protein stability and enzyme activity.The insecticidal protein hirsutellin A from the mite fungal pathogen Hirsutella thompsonii is a ribotoxin.Deletion of the NH2-terminal beta-hairpin of the ribotoxin alpha-sarcin produces a nontoxic but active ribonuclease.
P2860
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P2860
The highly refined solution structure of the cytotoxic ribonuclease alpha-sarcin reveals the structural requirements for substrate recognition and ribonucleolytic activity
description
2000 nî lūn-bûn
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2000 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունիսին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
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name
The highly refined solution st ...... n and ribonucleolytic activity
@ast
The highly refined solution st ...... n and ribonucleolytic activity
@en
The highly refined solution st ...... n and ribonucleolytic activity
@nl
type
label
The highly refined solution st ...... n and ribonucleolytic activity
@ast
The highly refined solution st ...... n and ribonucleolytic activity
@en
The highly refined solution st ...... n and ribonucleolytic activity
@nl
prefLabel
The highly refined solution st ...... n and ribonucleolytic activity
@ast
The highly refined solution st ...... n and ribonucleolytic activity
@en
The highly refined solution st ...... n and ribonucleolytic activity
@nl
P2093
P50
P3181
P356
P1476
The highly refined solution st ...... n and ribonucleolytic activity
@en
P2093
A Martínez del Pozo
J G Gavilanes
J M Pérez-Cañadillas
P304
P3181
P356
10.1006/JMBI.2000.3813
P407
P577
2000-06-16T00:00:00Z