The gene, ialA, associated with the invasion of human erythrocytes by Bartonella bacilliformis, designates a nudix hydrolase active on dinucleoside 5'-polyphosphates.
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The diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe and Saccharomyces cerevisiae are homologues of the human diphosphoinositol polyphosphate phosphohydrolase. Overlapping substrate specificities in a MutT-type proteinSite-directed mutagenesis of diphosphoinositol polyphosphate phosphohydrolase, a dual specificity NUDT enzyme that attacks diadenosine polyphosphates and diphosphoinositol polyphosphatesIntruders below the radar: molecular pathogenesis of Bartonella sppStudies on the ADP-ribose pyrophosphatase subfamily of the nudix hydrolases and tentative identification of trgB, a gene associated with tellurite resistance.Cloning and characterization of a new member of the Nudix hydrolases from human and mouseCharacterization of active-site residues in diadenosine tetraphosphate hydrolase from Lupinus angustifoliusIdentification of Escherichia coli K1 genes contributing to human brain microvascular endothelial cell invasion by differential fluorescence induction.Orf135 from Escherichia coli Is a Nudix hydrolase specific for CTP, dCTP, and 5-methyl-dCTP.The pnhA gene of Pasteurella multocida encodes a dinucleoside oligophosphate pyrophosphatase member of the Nudix hydrolase superfamily.Establishing a direct role for the Bartonella bacilliformis invasion-associated locus B (IalB) protein in human erythrocyte parasitism.Legionella pneumophila NudA Is a Nudix hydrolase and virulence factor.Immune aspects of Bartonella.RppH-dependent pyrophosphohydrolysis of mRNAs is regulated by direct interaction with DapF in Escherichia coli.Genome sequence of a nephritogenic and highly transformable M49 strain of Streptococcus pyogenesInvA protein is a Nudix hydrolase required for infection by pathogenic Leptospira in cell lines and animals.Gene ytkD of Bacillus subtilis encodes an atypical nucleoside triphosphatase member of the Nudix hydrolase superfamily.Persistence of Bartonella spp. stealth pathogens: from subclinical infections to vasoproliferative tumor formation.Bartonella Species, an Emerging Cause of Blood-Culture-Negative Endocarditis.Aae, an autotransporter involved in adhesion of Actinobacillus actinomycetemcomitans to epithelial cells.AtNUDT7, a negative regulator of basal immunity in Arabidopsis, modulates two distinct defense response pathways and is involved in maintaining redox homeostasis.Enzymatic characteristics of an ApaH-like phosphatase, PrpA, and a diadenosine tetraphosphate hydrolase, ApaH, from Myxococcus xanthus.Gene expression and phenotypic traits of Aggregatibacter actinomycetemcomitans in response to environmental changes.Analysis of the catalytic and binding residues of the diadenosine tetraphosphate pyrophosphohydrolase from Caenorhabditis elegans by site-directed mutagenesis.The NudA protein in the gastric pathogen Helicobacter pylori is an ubiquitous and constitutively expressed dinucleoside polyphosphate hydrolase.Purification of a plant nucleotide pyrophosphatase as a protein that interferes with nitrate reductase and glutamine synthetase assays.Regulation of dinucleoside polyphosphate pools by the YgdP and ApaH hydrolases is essential for the ability of Salmonella enterica serovar typhimurium to invade cultured mammalian cells.A new subfamily of the Nudix hydrolase superfamily active on 5-methyl-UTP (ribo-TTP) and UTP.Analysis of genotypic variation in genes associated with virulence in Aggregatibacter actinomycetemcomitans clinical isolates.The 26 Nudix hydrolases of Bacillus cereus, a close relative of Bacillus anthracis.Galleria mellonella as an infection model to investigate virulence of Vibrio parahaemolyticus.Three new Nudix hydrolases from Escherichia coli.Cloning and characterization of the first member of the Nudix family from Arabidopsis thaliana.The Rickettsia prowazekii invasion gene homolog (invA) encodes a Nudix hydrolase active on adenosine (5')-pentaphospho-(5')-adenosine.
P2860
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P2860
The gene, ialA, associated with the invasion of human erythrocytes by Bartonella bacilliformis, designates a nudix hydrolase active on dinucleoside 5'-polyphosphates.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh-hant
name
The gene, ialA, associated wit ...... inucleoside 5'-polyphosphates.
@en
The gene, ialA, associated wit ...... inucleoside 5'-polyphosphates.
@nl
type
label
The gene, ialA, associated wit ...... inucleoside 5'-polyphosphates.
@en
The gene, ialA, associated wit ...... inucleoside 5'-polyphosphates.
@nl
prefLabel
The gene, ialA, associated wit ...... inucleoside 5'-polyphosphates.
@en
The gene, ialA, associated wit ...... inucleoside 5'-polyphosphates.
@nl
P2860
P356
P1476
The gene, ialA, associated wit ...... inucleoside 5'-polyphosphates.
@en
P2093
Bessman MJ
Conyers GB
P2860
P304
P356
10.1074/JBC.274.3.1203
P407
P577
1999-01-01T00:00:00Z