Alanine-scanning mutagenesis of the predicted rRNA-binding domain of ErmC' redefines the substrate-binding site and suggests a model for protein-RNA interactions.
about
Substrate binding analysis of the 23S rRNA methyltransferase RrmJInsights into the structure, function and evolution of the radical-SAM 23S rRNA methyltransferase Cfr that confers antibiotic resistance in bacteriaSubstrate specificity and properties of the Escherichia coli 16S rRNA methyltransferase, RsmEFunctional specialization of domains tandemly duplicated within 16S rRNA methyltransferase RsmCStructural Basis for Binding of RNA and Cofactor by a KsgA MethyltransferaseStructural basis for S-adenosylmethionine binding and methyltransferase activity by mitochondrial transcription factor B1The carboxyl-terminal extension of yeast tRNA m5C methyltransferase enhances the catalytic efficiency of the amino-terminal domain.Molecular basis of intrinsic macrolide resistance in the Mycobacterium tuberculosis complexMethyltransferase Erm(37) slips on rRNA to confer atypical resistance in Mycobacterium tuberculosis.Sequence and structural evolution of the KsgA/Dim1 methyltransferase familyMinimal substrate features for Erm methyltransferases defined by using a combinatorial oligonucleotide library.Fast and sensitive alignment of microbial whole genome sequencing reads to large sequence datasets on a desktop PC: application to metagenomic datasets and pathogen identification.Critical residues for cofactor binding and catalytic activity in the aminoglycoside resistance methyltransferase Sgm.Speculative strategies for new antibacterials: all roads should not lead to Rome.A novel hybrid SCCmec-mecC region in Staphylococcus sciuri.Substrate Recognition and Modification by a Pathogen-Associated Aminoglycoside Resistance 16S rRNA Methyltransferase.Drosophila mitochondrial transcription factor B1 modulates mitochondrial translation but not transcription or DNA copy number in Schneider cells.A knowledge-based potential function predicts the specificity and relative binding energy of RNA-binding proteins.Bioinformatics Tools and Benchmarks for Computational Docking and 3D Structure Prediction of RNA-Protein Complexes
P2860
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P2860
Alanine-scanning mutagenesis of the predicted rRNA-binding domain of ErmC' redefines the substrate-binding site and suggests a model for protein-RNA interactions.
description
2003 nî lūn-bûn
@nan
2003 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Alanine-scanning mutagenesis o ...... for protein-RNA interactions.
@ast
Alanine-scanning mutagenesis o ...... for protein-RNA interactions.
@en
Alanine-scanning mutagenesis o ...... for protein-RNA interactions.
@nl
type
label
Alanine-scanning mutagenesis o ...... for protein-RNA interactions.
@ast
Alanine-scanning mutagenesis o ...... for protein-RNA interactions.
@en
Alanine-scanning mutagenesis o ...... for protein-RNA interactions.
@nl
prefLabel
Alanine-scanning mutagenesis o ...... for protein-RNA interactions.
@ast
Alanine-scanning mutagenesis o ...... for protein-RNA interactions.
@en
Alanine-scanning mutagenesis o ...... for protein-RNA interactions.
@nl
P2093
P2860
P356
P1476
Alanine-scanning mutagenesis o ...... for protein-RNA interactions.
@en
P2093
Gordana Maravić
Marcin Feder
Mirna Flögel
Sándor Pongor
P2860
P304
P356
10.1093/NAR/GKG666
P407
P577
2003-08-01T00:00:00Z