Expression of egasyn-esterase in mammalian cells. Sequestration in the endoplasmic reticulum and complexation with beta-glucuronidase.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference24 articles.
1. Identity of esterase-22 and egasyn, the protein which complexes with microsomal β-glucuronidase
2. An accessory protein identical to mouse egasyn is complexed with rat microsomal beta-glucuronidase and is identical to rat esterase-3.
3. Selective inhibition of rat liver carboxylesterases by various organophosphorus diesters in vivo and in vitro
4. Specificity of purified monoacylglycerol lipase, palmitoyl-CoA hydrolase, palmitoyl-carnitine hydrolase, and nonspecific carboxylesterase from rat liver microsomes
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1. Lipolytic and esterolytic activity-based profiling of murine liver;PROTEOMICS;2008-09
2. Keynote review: Mammalian carboxylesterases: From drug targets to protein therapeutics;Drug Discovery Today;2005-03
3. Posttranslational Regulation of Acid Sphingomyelinase in Niemann-Pick Type C1 Fibroblasts and Free Cholesterol-enriched Chinese Hamster Ovary Cells;Journal of Biological Chemistry;2000-12
4. Human Egasyn Binds β-Glucuronidase but neither the Esterase Active Site of Egasyn nor the C Terminus of β-Glucuronidase Is Involved in Their Interaction;Archives of Biochemistry and Biophysics;1999-12
5. Identification of a C-reactive Protein Binding Site in Two Hepatic Carboxylesterases Capable of Retaining C-reactive Protein within the Endoplasmic Reticulum;Journal of Biological Chemistry;1996-09
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