Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/s0041-1345(00)02120-5 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Structural insights into the inhibition mechanism of glucosidase inhibitors toward kojibiose hydrolase belonging to glycoside hydrolase family 65.
Biosci Biotechnol Biochem
December 2024
Department of Bioscience, Graduate School of Science and Technology, Shizuoka University, Shizuoka, Japan.
Glycoside hydrolase family 65 (GH65) includes glycoside hydrolases active on various α-glucosides. We previously demonstrated that the GH65 enzyme from Flavobacterium johnsoniae (FjGH65A) is a kojibiose hydrolase and determined its 3-dimensional structure. In this study, the effects of glucosidase inhibitors on FjGH65A and their complex structures were analyzed to elucidate their inhibition mechanism.
View Article and Find Full Text PDFThe effects of Castanospermine, an oligosaccharide processing inhibitor, on mononuclear/endothelial cell binding and the expression of cell adhesion molecules.
Transpl Immunol
August 2012
Newcastle Transplant Unit, Division of Surgery, John Hunter Hospital, New Lambton, Australia.
Introduction: In this study we aimed to determine whether Castanospermine, a transplant immunosuppressive agent, impaired mononuclear/endothelial cell binding and expression of their cell adhesion molecules.
Methods: The binding of human umbilical vein endothelial cells with peripheral blood mononuclear cells was measured by a binding assay using Chromium 51 label; the membrane expression of cell adhesion molecules was measured by flow cytometry expressed as mean fluorescence intensity ratios.
Results: Castanospermine decreased mononuclear/endothelial cell binding if and only if both cell types were treated with Castanospermine: this impairment occurred if endothelial cells were treated with a range of doses of Castanospermine and mononuclear cells were treated with a constant dose of Castanospermine (p<0.
Studies on α-glucosidase inhibitors development: magic molecules for the treatment of carbohydrate mediated diseases.
Mini Rev Med Chem
July 2012
REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, 687, Rua do Campo Alegre, 4169-007 Porto, Portugal.
α-Glucosidase (EC 3.2.1.
View Article and Find Full Text PDFComparison and characterization of α-amylase inducers in Aspergillus nidulans based on nuclear localization of AmyR.
Appl Microbiol Biotechnol
June 2012
Department of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Nagoya-shi, Aichi 464-8601, Japan.
AmyR, a fungal transcriptional activator responsible for induction of amylolytic genes in Aspergillus nidulans, localizes to the nucleus in response to the physiological inducer isomaltose. Maltose, kojibiose, and D: -glucose were also found to trigger the nuclear localization of GFP-AmyR. Isomaltose- and kojibiose-triggered nuclear localization was not inhibited by the glucosidase inhibitor, castanospermine, while maltose-triggered localization was inhibited.
View Article and Find Full Text PDFNovel method for chase analysis of oligosaccharide metabolic error caused by xenobiotics.
Anal Biochem
October 2010
Japan Chemical Innovation Institute, Chiyoda-ku, Tokyo 101-0051, Japan.
Saccharide primers, such as dodecyl beta-lactoside (Lac-C12), are unique artificial precursors of glycolipid synthesis. In culture media supplemented with saccharide primers, they are taken up by the cells in the culture media and glycosylated by cellular glycosyltransferases in the Golgi apparatus to form pseudo-glycolipids. In this study, we examine the effects of various xenobiotics on glycolipid synthesis by implementing a novel method to analyze pseudo-glycolipids, mainly gangliosides, produced by ONS-76 medulloblastoma cells in a culture medium containing various xenobiotics.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!