S-Ribosylhomocysteinase (LuxS) is a mononuclear iron protein.
about
Quorum quenching revisited--from signal decays to signalling confusionStructures of Metal-Substituted Human Histone Deacetylase 8 Provide Mechanistic Inferences on Biological Function,A Strategy for Antagonizing Quorum SensingProduction of FAME biodiesel in E. coli by direct methylation with an insect enzymeFunctional correlation of bacterial LuxS with their quaternary associations: interface analysis of the structure networks.On-off Bodipy chemosensor for recognition of iron(III) ion based on the inner filter effect and its applications in cellular and bacterial imaging.2D proteome analysis initiates new insights on the Salmonella Typhimurium LuxS proteinElucidation of the conformational free energy landscape in H.pylori LuxS and its implications to catalysisIdentification of a key amino acid of LuxS involved in AI-2 production in Campylobacter jejuniActive site metal ion in UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) switches between Fe(II) and Zn(II) depending on cellular conditions.The Staphylococcus aureus autoinducer-2 synthase LuxS is regulated by Ser/Thr phosphorylation.Exposure to static magnetic field stimulates quorum sensing circuit in luminescent Vibrio strains of the Harveyi clade.Messing with bacterial quorum sensingA stochastic model of Escherichia coli AI-2 quorum signal circuit reveals alternative synthesis pathways.Transition state analogue inhibitors of human methylthioadenosine phosphorylase and bacterial methylthioadenosine/S-adenosylhomocysteine nucleosidase incorporating acyclic ribooxacarbenium ion mimicsThiol reactive probes and chemosensors.S-Ribosylhomocysteine analogues with the carbon-5 and sulfur atoms replaced by a vinyl or (fluoro)vinyl unit.Look who's talking: communication and quorum sensing in the bacterial world.Probing the catalytic mechanism of S-ribosylhomocysteinase (LuxS) with catalytic intermediates and substrate analogues.Attenuation of Edwardsiella tarda virulence by small peptides that interfere with LuxS/autoinducer type 2 quorum sensing.AI-2-mediated signalling in bacteria.LuxS and quorum-sensing in Campylobacter.Small molecule inhibitors of AI-2 signaling in bacteria: state-of-the-art and future perspectives for anti-quorum sensing agents.Multi-scale computational enzymology: enhancing our understanding of enzymatic catalysis.Inhibition of LuxS by S-ribosylhomocysteine analogues containing a [4-aza]ribose ring.Cell-to-Cell Signaling in Escherichia coli and Salmonella.The Metal Drives the Chemistry: Dual Functions of Acireductone Dioxygenase.Deep sequencing of Porphyromonas gingivalis and comparative transcriptome analysis of a LuxS mutant.Structural and thermodynamic characterization of metal binding in Vps29 from Entamoeba histolytica: Implication in retromer function.Activation of Escherichia coli UDP-3-O-[(R)-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase by Fe2+ yields a more efficient enzyme with altered ligand affinity.Kinetics and thermodynamics of metal-binding to histone deacetylase 8.The activity and cofactor preferences of N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB) change depending on environmental conditions.Inhibition of S-ribosylhomocysteinase (LuxS) by substrate analogues modified at the ribosyl C-3 position.Assessment of the roles of LuxS, S-ribosyl homocysteine, and autoinducer 2 in cell attachment during biofilm formation by Listeria monocytogenes EGD-e.S-Ribosylhomocysteine analogs containing a [4-thio]ribose ring.Zinc is required to ensure the expression of flagella and the ability to form biofilms in Salmonella enterica sv Typhimurium.O2 -independent demethylation of trimethylamine N-oxide by Tdm of Methylocella silvestris.
P2860
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P2860
S-Ribosylhomocysteinase (LuxS) is a mononuclear iron protein.
description
2003 nî lūn-bûn
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2003 թուականի Ապրիլին հրատարակուած գիտական յօդուած
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2003 թվականի ապրիլին հրատարակված գիտական հոդված
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2003年の論文
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2003年学术文章
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2003年学术文章
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2003年学术文章
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2003年学术文章
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2003年学术文章
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2003年學術文章
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name
S-Ribosylhomocysteinase (LuxS) is a mononuclear iron protein.
@ast
S-Ribosylhomocysteinase (LuxS) is a mononuclear iron protein.
@en
S-Ribosylhomocysteinase
@nl
type
label
S-Ribosylhomocysteinase (LuxS) is a mononuclear iron protein.
@ast
S-Ribosylhomocysteinase (LuxS) is a mononuclear iron protein.
@en
S-Ribosylhomocysteinase
@nl
prefLabel
S-Ribosylhomocysteinase (LuxS) is a mononuclear iron protein.
@ast
S-Ribosylhomocysteinase (LuxS) is a mononuclear iron protein.
@en
S-Ribosylhomocysteinase
@nl
P2093
P356
P1433
P1476
S-Ribosylhomocysteinase (LuxS) is a mononuclear iron protein.
@en
P2093
Anne-Sophie Wavreille
Eric Dizin
Junguk Park
P304
P356
10.1021/BI034289J
P407
P577
2003-04-01T00:00:00Z