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O-GlcNAcylation: The Sweet Side of the Cancer

O-GlcNAcylation is an O-linked β-N-acetylglucosamine (O-GlcNAc) moiety linked to the serine or threonine residues in proteins. O-GlcNAcylation is a dynamic post-translational modification involved in a wide range of biological processes and diseases such as cancer. This modification can increase and...

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Autores principales: de Queiroz, Rafaela Muniz, Carvalho, Érika, Dias, Wagner Barbosa
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4042083/
https://www.ncbi.nlm.nih.gov/pubmed/24918087
http://dx.doi.org/10.3389/fonc.2014.00132
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author de Queiroz, Rafaela Muniz
Carvalho, Érika
Dias, Wagner Barbosa
author_facet de Queiroz, Rafaela Muniz
Carvalho, Érika
Dias, Wagner Barbosa
author_sort de Queiroz, Rafaela Muniz
collection PubMed
description O-GlcNAcylation is an O-linked β-N-acetylglucosamine (O-GlcNAc) moiety linked to the serine or threonine residues in proteins. O-GlcNAcylation is a dynamic post-translational modification involved in a wide range of biological processes and diseases such as cancer. This modification can increase and decrease the activity of enzymes as well as interfere with protein stability and interaction. The modulatory capacity of O-GlcNAcylation, as well as protein phosphorylation, is of paramount importance in the regulation of metabolism and intracellular signaling of tumor cells. Thus, understanding the regulation of O-GlcNAcylation in tumor cells and their difference compared to non-tumor cells may elucidate new mechanisms related to tumor generation and development, could provide a new marker to diagnosis and prognosis in patients with cancer and indicate a new target to cancer chemotherapy.
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spelling pubmed-40420832014-06-10 O-GlcNAcylation: The Sweet Side of the Cancer de Queiroz, Rafaela Muniz Carvalho, Érika Dias, Wagner Barbosa Front Oncol Oncology O-GlcNAcylation is an O-linked β-N-acetylglucosamine (O-GlcNAc) moiety linked to the serine or threonine residues in proteins. O-GlcNAcylation is a dynamic post-translational modification involved in a wide range of biological processes and diseases such as cancer. This modification can increase and decrease the activity of enzymes as well as interfere with protein stability and interaction. The modulatory capacity of O-GlcNAcylation, as well as protein phosphorylation, is of paramount importance in the regulation of metabolism and intracellular signaling of tumor cells. Thus, understanding the regulation of O-GlcNAcylation in tumor cells and their difference compared to non-tumor cells may elucidate new mechanisms related to tumor generation and development, could provide a new marker to diagnosis and prognosis in patients with cancer and indicate a new target to cancer chemotherapy. Frontiers Media S.A. 2014-06-03 /pmc/articles/PMC4042083/ /pubmed/24918087 http://dx.doi.org/10.3389/fonc.2014.00132 Text en Copyright © 2014 de Queiroz, Carvalho and Dias. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Oncology
de Queiroz, Rafaela Muniz
Carvalho, Érika
Dias, Wagner Barbosa
O-GlcNAcylation: The Sweet Side of the Cancer
title O-GlcNAcylation: The Sweet Side of the Cancer
title_full O-GlcNAcylation: The Sweet Side of the Cancer
title_fullStr O-GlcNAcylation: The Sweet Side of the Cancer
title_full_unstemmed O-GlcNAcylation: The Sweet Side of the Cancer
title_short O-GlcNAcylation: The Sweet Side of the Cancer
title_sort o-glcnacylation: the sweet side of the cancer
topic Oncology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4042083/
https://www.ncbi.nlm.nih.gov/pubmed/24918087
http://dx.doi.org/10.3389/fonc.2014.00132
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