Probing the catalytic mechanism of S-ribosylhomocysteinase (LuxS) with catalytic intermediates and substrate analogues.
about
The Vibrio cholerae quorum-sensing autoinducer CAI-1: analysis of the biosynthetic enzyme CqsA2D 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 catalysisScreening of Actinobacillus pleuropneumoniae LuxS inhibitors.Exposure to static magnetic field stimulates quorum sensing circuit in luminescent Vibrio strains of the Harveyi clade.A RubisCO-like protein links SAM metabolism with isoprenoid biosynthesis."Clicking" on the lights to reveal bacterial social networking.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.Substituted lactam and cyclic azahemiacetals modulate Pseudomonas aeruginosa quorum sensing.Inhibition of LuxS by S-ribosylhomocysteine analogues containing a [4-aza]ribose ring.S-Ribosylhomocysteine Analogues Modified at the Ribosyl C-4 Position.A naturally occurring brominated furanone covalently modifies and inactivates LuxS.Reduction of sugar lactones to hemiacetals with lithium triethylborohydride.Inhibition of S-ribosylhomocysteinase (LuxS) by substrate analogues modified at the ribosyl C-3 position.Interspecies bacterial communication as a target for therapy in otitis media.S-Ribosylhomocysteine analogs containing a [4-thio]ribose ring.Biofilm formation, host-cell adherence, and virulence genes regulation of Streptococcus suis in response to autoinducer-2 signaling.Overexpression of luxS cannot increase autoinducer-2 production, only affect the growth and biofilm formation in Streptococcus suis.
P2860
Q27657840-BE41CE80-23C3-4F08-807F-5F280D575171Q33503418-F4B2E46A-06C1-493E-BF40-2CAAD1E9D0D3Q33655522-A2504EBA-1F59-40E2-ADF9-3E057FDC7F83Q34762300-219A90FA-6F76-45A2-BC68-3FD5C4104917Q35194012-AA2FAD92-8476-41AA-96EE-CC3273D7B9EBQ36331187-4423642D-0E7C-45F7-9E1B-45CAB9FA91E0Q37977411-3D4D142B-B287-48C2-9602-275ABD626CE9Q38133222-755E6F41-74E0-47A2-9384-03F0B0DB0A4EQ38175308-E313DC1B-D23E-4D2F-AAFE-BFC1ECB0EA4CQ38381664-260A216B-627F-4E03-AE20-88BF2D6A6854Q38382554-69B4D651-0B69-4B55-8B00-855BA5446ABEQ41833897-0A21B029-656F-45E3-889E-C83D3B238556Q42049118-398C7456-2D00-4C0F-9B03-BFE6DBEF80BEQ42376517-C751AFB8-33B8-4698-A137-8E13B7F8C1A0Q42588530-9458E1E8-0EA5-4485-AD0E-4599724C694BQ42748256-1A92FC35-1419-4DED-ACAA-1BED625D7C6CQ43223907-A3045457-00F9-43E9-9A4F-38F7AE9C9582Q54230391-CC8E0741-8DE2-425F-A654-39A55651AD97Q54232344-C79210C6-E7A2-4355-A500-F48F6EF14FAA
P2860
Probing the catalytic mechanism of S-ribosylhomocysteinase (LuxS) with catalytic intermediates and substrate analogues.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on January 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Probing the catalytic mechanis ...... iates and substrate analogues.
@en
Probing the catalytic mechanism of S-ribosylhomocysteinase
@nl
type
label
Probing the catalytic mechanis ...... iates and substrate analogues.
@en
Probing the catalytic mechanism of S-ribosylhomocysteinase
@nl
prefLabel
Probing the catalytic mechanis ...... iates and substrate analogues.
@en
Probing the catalytic mechanism of S-ribosylhomocysteinase
@nl
P2093
P2860
P356
P1476
Probing the catalytic mechanis ...... iates and substrate analogues.
@en
P2093
Adam J Sobczak
Bhaskar Gopishetty
Charles E Bell
Rakhi Rajan
Stanislaw F Wnuk
P2860
P304
P356
10.1021/JA808206W
P407
P577
2009-01-01T00:00:00Z