Self-association of the Escherichia coli transcription activator MalT in the presence of maltotriose and ATP
about
X-ray structure of MalY from Escherichia coli: a pyridoxal 5′-phosphate-dependent enzyme acting as a modulator in mal gene expressionSynergistic transcription activation: a dual role for CRP in the activation of an Escherichia coli promoter depending on MalT and CRPRoles of glucitol in the GutR-mediated transcription activation process in Bacillus subtilis: tight binding of GutR to tis binding site.A complex signaling module governs the activity of MalT, the prototype of an emerging transactivator familyExposure to Glycolytic Carbon Sources Reveals a Novel Layer of Regulation for the MalT Regulon.ABC transporter architecture and regulatory roles of accessory domains.The N terminus of the Escherichia coli transcription activator MalT is the domain of interaction with MalY.Structural model of MalK, the ABC subunit of the maltose transporter of Escherichia coli: implications for mal gene regulation, inducer exclusion, and subunit assembly.How 'arm-twisting' by the inducer triggers activation of the MalT transcription factor, a typical signal transduction ATPase with numerous domains (STAND).A dual role for the inducer in signalling by MalT, a signal transduction ATPase with numerous domains (STAND).A new mechanism for the control of a prokaryotic transcriptional regulator: antagonistic binding of positive and negative effectors.MalK, the ATP-binding cassette component of the Escherichia coli maltodextrin transporter, inhibits the transcriptional activator malt by antagonizing inducer binding.A conserved inverted repeat, the LipR box, mediates transcriptional activation of the Streptomyces exfoliatus lipase gene by LipR, a member of the STAND class of P-loop nucleoside triphosphatases.Conserved motifs involved in ATP hydrolysis by MalT, a signal transduction ATPase with numerous domains from Escherichia coli.Roles of cell division control factor SdiA: recognition of quorum sensing signals and modulation of transcription regulation targets.Single-target regulators form a minor group of transcription factors in Escherichia coli K-12.
P2860
Q27621601-9DCF19A1-3BC4-4501-B351-29931B743ACBQ28140010-A7A3A58A-0893-47AE-962D-01174F51B22AQ31705697-6F5EC252-3A14-40E5-920E-E6EF608C45A6Q34605744-672E2A35-D8CA-4D78-A1F9-E0BFEE0C7F49Q35179640-1E7DD771-8C34-4FFF-B107-964120276E69Q36352495-CC9EF5C4-6A66-4FF4-9907-91C22A7D8BB6Q38289389-95690E9F-2682-43FE-B771-4CB181179ACDQ38294699-E7843177-E509-4E84-91EE-D647D2F36BE7Q38300654-816827A3-89F4-4C6E-A0C7-0C868949238FQ38311861-253EFEE4-D4F5-42CE-9C0A-030842A0A784Q38315049-632B226A-F690-4663-914D-E8AD66B743F3Q38340379-92C36591-F514-4882-9A17-3163DF2B20BEQ39109604-1C5AA986-943C-48EB-B594-3BBF2ED2570EQ41955530-13E7DFBC-9589-4500-8F5C-27F2ED38B023Q46916976-0A95AAD5-EFFD-46D7-8DFB-DB61AD946A93Q54208178-3C1BD943-DEEA-4521-9137-ECF61BBF7A40
P2860
Self-association of the Escherichia coli transcription activator MalT in the presence of maltotriose and ATP
description
1999 nî lūn-bûn
@nan
1999 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Self-association of the Escher ...... resence of maltotriose and ATP
@ast
Self-association of the Escher ...... resence of maltotriose and ATP
@en
Self-association of the Escher ...... resence of maltotriose and ATP
@nl
type
label
Self-association of the Escher ...... resence of maltotriose and ATP
@ast
Self-association of the Escher ...... resence of maltotriose and ATP
@en
Self-association of the Escher ...... resence of maltotriose and ATP
@nl
prefLabel
Self-association of the Escher ...... resence of maltotriose and ATP
@ast
Self-association of the Escher ...... resence of maltotriose and ATP
@en
Self-association of the Escher ...... resence of maltotriose and ATP
@nl
P2860
P356
P1476
Self-association of the Escher ...... resence of maltotriose and ATP
@en
P2093
P2860
P304
P356
10.1074/JBC.274.47.33220
P407
P577
1999-11-19T00:00:00Z