Dynamic polar sequestration of excess MurG may regulate enzymatic function.
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Large-scale filament formation inhibits the activity of CTP synthetaseA retrospective: use of Escherichia coli as a vehicle to study phospholipid synthesis and functionRegulated shift from helical to polar localization of Listeria monocytogenes cell wall-anchored proteins.A new suite of tnaA mutants suggests that Escherichia coli tryptophanase is regulated by intracellular sequestration and by occlusion of its active siteAnalysis of the Spore Membrane Proteome in Clostridium perfringens Implicates Cyanophycin in Spore Assembly.Discovery of a cardiolipin synthase utilizing phosphatidylethanolamine and phosphatidylglycerol as substrates.A Spatial Control for Correct Timing of Gene Expression during the Escherichia coli Cell Cycle.Spatial Organization of Cell Wall-Anchored Proteins at the Surface of Gram-Positive Bacteria.Why do bacteria divide?The general phosphotransferase system proteins localize to sites of strong negative curvature in bacterial cells.The GTPase function of YvcJ and its subcellular relocalization are dependent on growth conditions in Bacillus subtilis.Phenotypic Heterogeneity in Sugar Utilization by E. coli Is Generated by Stochastic Dispersal of the General PTS Protein EI from Polar Clusters.Revisiting the cell biology of the acyl-ACP:phosphate transacylase PlsX suggests that the phospholipid synthesis and cell division machineries are not coupled in Bacillus subtilis.Isolation and identification of new inner membrane-associated proteins that localize to cell poles in Escherichia coli.
P2860
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P2860
Dynamic polar sequestration of excess MurG may regulate enzymatic function.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Dynamic polar sequestration of excess MurG may regulate enzymatic function.
@en
Dynamic polar sequestration of excess MurG may regulate enzymatic function.
@nl
type
label
Dynamic polar sequestration of excess MurG may regulate enzymatic function.
@en
Dynamic polar sequestration of excess MurG may regulate enzymatic function.
@nl
prefLabel
Dynamic polar sequestration of excess MurG may regulate enzymatic function.
@en
Dynamic polar sequestration of excess MurG may regulate enzymatic function.
@nl
P2860
P356
P1476
Dynamic polar sequestration of excess MurG may regulate enzymatic function.
@en
P2093
Allison M Michaelis
Zemer Gitai
P2860
P304
P356
10.1128/JB.00676-10
P577
2010-07-19T00:00:00Z