Disease relevance of ECs4884

• The C-terminal Domain of the Escherichia coli WaaJ Glycosyltransferase Is Important for Catalytic Activity and Membrane Association [1].
• The membrane domain of a bacteriophage assembly protein. Membrane insertion and growth inhibition [2].
• Cloning and expression of the filamentous bacteriophage Pf1 major coat protein gene in Escherichia coli. Membrane protein processing and virus assembly [3].
• Changes in chemical structure and function in Escherichia coli cell membranes caused by freeze-thawing. II. Membrane lipid state and response of cells to dehydration [4].
• The MePNet (Membrane Protein Network) was established to overexpress a large number of GPCRs in three major expression systems, based on Escherichia coli, Pichia pastoris and Semliki Forest virus (SFV) vectors [5].

High impact information on ECs4884

• Biosynthesis of membrane-derived oligosaccharides. Membrane-bound glucosyltransferase system from Escherichia coli requires polyprenyl phosphate [6].
• 1) Oxidative phosphorylation was markedly impaired in vivo 2) Membrane ATPase and ATP-driven proton-pumping activities were decreased markedly [7].
• 3. Membrane vesicles prepared from an AraE+,AraF+ strain accumulated the sugar, energized most efficiently by the respiratory substrates ascorbate + phenazine methosulphate [8].
• Functional Characterization and Membrane Topology of Escherichia coli WecA, a Sugar-Phosphate Transferase Initiating the Biosynthesis of Enterobacterial Common Antigen and O-Antigen Lipopolysaccharide [9].
• We have previously reported that rat parotid gland basolateral plasma membrane vesicles (BLMV) have a relatively high affinity Ca2+ transport pathway and an unsaturable Ca2+ flux component (Lockwich et al., 1994. J. Membrane Biol. 141:289-296) [10].

Chemical compound and disease context of ECs4884

• 1. Membrane vesicles of Escherichia coli K-12 CS7, a strain gentically derepressed for glutamate permease, maintain low aspartate transport activity, like that of prep [11].

Biological context of ECs4884

• Nature of radiation and chemically induced lesions and role of cellular mechanisms in cell survival and mutagenesis. I. Membrane and cellular repair [12].

Anatomical context of ECs4884

• 1. Membrane-bound polysomes synthesize proteins which are exported from the cell [13].

Analytical, diagnostic and therapeutic context of ECs4884

• (ii) Membrane filtration confirmed that mrACBP bound to anionic phospholipid-rich SUV but only weakly interacted with neutral SUV or large unilamellar vesicles (LUV), regardless of charge [14].
• For these last activities, French press breakage (see section on Membrane Preparations) of bacteria prior to immobilization was necessary [15].

References