Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms
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Identification and analysis of the acetylated status of poplar proteins reveals analogous N-terminal protein processing mechanisms with other eukaryotesAn unusual peptide deformylase features in the human mitochondrial N-terminal methionine excision pathwayHuman mitochondrial peptide deformylase, a new anticancer target of actinonin-based antibioticsThe metalloendopeptidase nardilysin (NRDc) is potently inhibited by heparin-binding epidermal growth factor-like growth factor (HB-EGF)The two authentic methionine aminopeptidase genes are differentially expressed in Bacillus subtilis.N-terminal modifications of cellular proteins: The enzymes involved, their substrate specificities and biological effectsTrapping conformational states along ligand-binding dynamics of peptide deformylase: the impact of induced fit on enzyme catalysisStructural variation and inhibitor binding in polypeptide deformylase from four different bacterial speciesStructure and Activity of Human Mitochondrial Peptide Deformylase, a Novel Cancer TargetUnderstanding the highly efficient catalysis of prokaryotic peptide deformylases by shedding light on the determinants specifying the low activity of the human counterpartYeast methionine aminopeptidase type 1 is ribosome-associated and requires its N-terminal zinc finger domain for normal function in vivo.Eukaryotic peptide deformylases. Nuclear-encoded and chloroplast-targeted enzymes in ArabidopsisSorting signals, N-terminal modifications and abundance of the chloroplast proteomeThe biological functions of Naa10 - From amino-terminal acetylation to human diseaseGeneration of Artificial N-end Rule Substrate Proteins In Vivo and In Vitro.High-throughput identification of inhibitors of human mitochondrial peptide deformylase.N-myristoylation regulates the SnRK1 pathway in Arabidopsis.Target of rapamycin regulates development and ribosomal RNA expression through kinase domain in Arabidopsis.System for expression of microsporidian methionine amino peptidase type 2 (MetAP2) in the yeast Saccharomyces cerevisiaeCell and plastid division are coordinated through the prereplication factor AtCDT1Ligand-induced changes in the structure and dynamics of Escherichia coli peptide deformylaseMegadalton complexes in the chloroplast stroma of Arabidopsis thaliana characterized by size exclusion chromatography, mass spectrometry, and hierarchical clusteringMethionine aminopeptidase 2 is a new target for the metastasis-associated protein, S100A4.Expression of Escherichia coli methionyl-tRNA formyltransferase in Saccharomyces cerevisiae leads to formylation of the cytoplasmic initiator tRNA and possibly to initiation of protein synthesis with formylmethionine.Identification of protein stability determinants in chloroplastsExploration of the core metabolism of symbiotic bacteria.Peptide deformylase: a target for novel antibiotics?Control of protein life-span by N-terminal methionine excisionThe crystal structure of mitochondrial (Type 1A) peptide deformylase provides clear guidelines for the design of inhibitors specific for the bacterial forms.Impact of the N-terminal amino acid on targeted protein degradation.Overexpression of peptide deformylase in breast, colon, and lung cancers.Identification of crucial amino acids of bacterial Peptide deformylases affecting enzymatic activity in response to oxidative stressNovel agents for the treatment of resistant Gram-positive infections.Peptide deformylase inhibitors as potent antimycobacterial agents.An N-terminal formyl methionine on COX 1 is required for the assembly of cytochrome c oxidase.Genome-wide identification and in silico analysis of poplar peptide deformylases.Structure-Based Drug Design of Small Molecule Peptide Deformylase Inhibitors to Treat Cancer.The plastid-derived organelle of protozoan human parasites as a target of established and emerging drugs.Zinc is the metal cofactor of Borrelia burgdorferi peptide deformylase.Delineation of alternative conformational states in Escherichia coli peptide deformylase via thermodynamic studies for the binding of actinonin.
P2860
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P2860
Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms
description
2000 nî lūn-bûn
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2000 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
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
@wuu
name
Identification of eukaryotic p ...... protein processing mechanisms
@ast
Identification of eukaryotic p ...... protein processing mechanisms
@en
Identification of eukaryotic p ...... protein processing mechanisms
@nl
type
label
Identification of eukaryotic p ...... protein processing mechanisms
@ast
Identification of eukaryotic p ...... protein processing mechanisms
@en
Identification of eukaryotic p ...... protein processing mechanisms
@nl
prefLabel
Identification of eukaryotic p ...... protein processing mechanisms
@ast
Identification of eukaryotic p ...... protein processing mechanisms
@en
Identification of eukaryotic p ...... protein processing mechanisms
@nl
P2093
P2860
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Identification of eukaryotic p ...... protein processing mechanisms
@en
P2093
P2860
P304
P3181
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10.1093/EMBOJ/19.21.5916
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P577
2000-11-01T00:00:00Z