Enzyme Molecular Mechanism as a Starting Point to Design New Inhibitors: A Theoretical Study of O-GlcNAcase-Reference-Cited by-同舟云学术

Enzyme Molecular Mechanism as a Starting Point to Design New Inhibitors: A Theoretical Study of O-GlcNAcase

Published:2011-05-04 Issue:20 Volume:115 Page:6764-6775
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Lameira Jerônimo¹,Alves Cláudio Nahum¹,Tuñón Iñaki²,Martí Sergio³,Moliner Vicent³

Affiliation:

1. Laboratório de Planejamento e Desenvolvimento de Fármacos, Instituto de Ciências Exatas e Naturais, Universidade Federal do Pará, CP 11101, 66075-110 Belém, PA, Brazil

2. Departament de Química Física, Universitat de València, 46100 Burjassot, València, Spain

3. Departament de Química Física i Analítica, Universitat Jaume I, 12071 Castellón, Spain

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp202079e

Reference69 articles.

1. Mechanistic insights into glycosidase chemistry

2. Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc.

3. Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol.

4. Glycosylation of Nucleocytoplasmic Proteins: Signal Transduction and O-GlcNAc

5. O-GlcNAc modification of nucleocytoplasmic proteins and diabetes

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