Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure
about
In vivo formation of allosteric aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains: implications for protein folding and assemblyCharacterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1Genetic and sequence analysis of an 8.7-kilobase Pseudomonas denitrificans fragment carrying eight genes involved in transformation of precorrin-2 to cobyrinic acidEukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymesExtent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acidThe anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidaseComparative proteogenomics: combining mass spectrometry and comparative genomics to analyze multiple genomesMolecular recognition of angiogenesis inhibitors fumagillin and ovalicin by methionine aminopeptidase 2Whole proteome analysis of post-translational modifications: applications of mass-spectrometry for proteogenomic annotationMethionine aminopeptidase gene of Escherichia coli is essential for cell growthDetection of low-level promoter activity within open reading frame sequences of Escherichia coli.The two authentic methionine aminopeptidase genes are differentially expressed in Bacillus subtilis.Highly expressed proteins have an increased frequency of alanine in the second amino acid position.Effect of foreign N-terminal residues on the conformational stability of human lysozymeThe structure and the characteristic DNA binding property of the C-terminal domain of the RNA polymerase alpha subunit from Thermus thermophilusInteractions of Streptomyces griseus aminopeptidase with amino acid reaction products and their implications toward a catalytic mechanismCharacterization of a thiamin diphosphate-dependent phenylpyruvate decarboxylase from Saccharomyces cerevisiae.Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases.Yeast methionine aminopeptidase type 1 is ribosome-associated and requires its N-terminal zinc finger domain for normal function in vivo.Characterization of a novel enantioselective halohydrin hydrogen-halide-lyasePeptide methionine sulfoxide reductase from Escherichia coli and Mycobacterium tuberculosis protects bacteria against oxidative damage from reactive nitrogen intermediatesExpression and characterization of two functional methionine aminopeptidases from Mycobacterium tuberculosis H37RvFollow the leader: preference for specific amino acids directly following the initial methionine in proteins of different organismsThe NMR solution structure and function of RPA3313: a putative ribosomal transport protein from Rhodopseudomonas palustris.Direct genetic selection of two classes of R17/MS2 coat proteins with altered capsid assembly properties and expanded RNA-binding activities.The unique functional role of the C-HS hydrogen bond in the substrate specificity and enzyme catalysis of type 1 methionine aminopeptidase.Analysis of the matrix-assisted laser desorption ionization-time of flight mass spectrum of Staphylococcus aureus identifies mutations that allow differentiation of the main clonal lineagesActivation, proteolytic processing, and peptide specificity of recombinant cardosin A.Identification and characterization of a homologue of the pro-inflammatory cytokine Macrophage Migration Inhibitory Factor in the tick, Amblyomma americanum.Development and validation of a whole-cell inhibition assay for bacterial methionine aminopeptidase by surface-enhanced laser desorption ionization-time of flight mass spectrometryClpS is an essential component of the N-end rule pathway in Escherichia coli.RecA-mediated cleavage activates UmuD for mutagenesis: mechanistic relationship between transcriptional derepression and posttranslational activationProtein N-terminal processing: substrate specificity of Escherichia coli and human methionine aminopeptidases.Amino acid residues involved in the functional integrity of Escherichia coli methionine aminopeptidase.MarA, SoxS and Rob of Escherichia coli - Global regulators of multidrug resistance, virulence and stress response.Amino-terminal extension present in the methionine aminopeptidase type 1c of Mycobacterium tuberculosis is indispensible for its activity.The bacteriophage P1 HumD protein is a functional homolog of the prokaryotic UmuD'-like proteins and facilitates SOS mutagenesis in Escherichia coliExperimental annotation of post-translational features and translated coding regions in the pathogen Salmonella TyphimuriumNalpha -terminal acetylation of eukaryotic proteins.C-terminal extension of truncated recombinant proteins in Escherichia coli with a 10Sa RNA decapeptide.
P2860
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P2860
Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure
description
1987 nî lūn-bûn
@nan
1987 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
name
Processing of the initiation m ...... ptidase and its gene structure
@ast
Processing of the initiation m ...... ptidase and its gene structure
@en
Processing of the initiation m ...... ptidase and its gene structure
@nl
type
label
Processing of the initiation m ...... ptidase and its gene structure
@ast
Processing of the initiation m ...... ptidase and its gene structure
@en
Processing of the initiation m ...... ptidase and its gene structure
@nl
prefLabel
Processing of the initiation m ...... ptidase and its gene structure
@ast
Processing of the initiation m ...... ptidase and its gene structure
@en
Processing of the initiation m ...... ptidase and its gene structure
@nl
P2093
P2860
P1476
Processing of the initiation m ...... ptidase and its gene structure
@en
P2093
P2860
P304
P356
10.1128/JB.169.2.751-757.1987
P407
P577
1987-02-01T00:00:00Z