Michelle Ogava Igual

Universidade de São Paulo (USP). Faculdade de Ciências Farmacêuticas de Ribeirão Preto (FCFRP) (Institutional affiliation from the last research proposal)
Birthplace: Brazil

Abstract
The O-GlcNAcylation or O-GlcNAc modification is regulated by two importante enzimes, a glycosyltransferase, known as O-GlcNAc transferase (OGT) and a hydrolase, O-GlcNAcase (OGA). Several studies have shown the importance of O-GlcNAcylation in essential cellular process and its correlation with type 2 diabetes, Alzheimer Disease and cancer. Many inhibitors have been described so far. Howe…
Design, synthesis and biological evaluation of novel selective inhibitors of the hydrolase O-GlcNAcase (OGA), BP.MS
Abstract
The glycosylation of nuclear and cytoplasmic proteins with one unit of N-acetylglucosamine covalently bond at serine and threonine residues via O-²-Glyosidic linkage is known as O-GlcNAc modification. Two enzymes are involved in this process: a glycosyltransferase, referred to as O-GlcNAc transferase (OGT), which transfers molecules of N-acetylglucosamine, via Uridine 5'-diphosphate-acety…
Synthesis of bioisosteres of N-acetyl-glucosamine as potential inhibitors of O-GlcNAcase hydrolase, BP.IC
Phytochemical study of Vernonia polyanthes Less (Asteraceae), BP.IC

Source:Lattes Curriculum

CV Lattes

3 / 3	Completed scholarships in Brazil

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Abstract

Abstract