Glycobiology of immune responses
Unlike their protein "roommates" and their nucleic acid "cousins," carbohydrates remain an enigmatic arm of biology. The central reason for the difficulty in fully understanding how carbohydrate structure and biological function are tied is the nontemplate nature of their synthes...
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00778923_v1253_n1_p1_Rabinovich http://hdl.handle.net/20.500.12110/paper_00778923_v1253_n1_p1_Rabinovich |
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paper:paper_00778923_v1253_n1_p1_Rabinovich2023-06-08T15:07:31Z Glycobiology of immune responses C-type lectins Galectins Glycans Glycobiology Glycoimmunology Lectins Siglecs binding protein carbohydrate galectin glycan glycan binding protein glycoprotein lectin lipid major histocompatibility antigen class 2 nucleic acid nucleotide binding oligomerization domain like receptor unclassified drug autoimmunity chronic inflammation glycobiology human Human immunodeficiency virus immune response immune system innate immunity nonhuman pathogenesis protein expression review tumor immunity Unlike their protein "roommates" and their nucleic acid "cousins," carbohydrates remain an enigmatic arm of biology. The central reason for the difficulty in fully understanding how carbohydrate structure and biological function are tied is the nontemplate nature of their synthesis and the resulting heterogeneity. The goal of this collection of expert reviews is to highlight what is known about how carbohydrates and their binding partners-the microbial (non-self), tumor (altered-self), and host (self)-cooperate within the immune system, while also identifying areas of opportunity to those willing to take up the challenge of understanding more about how carbohydrates influence immune responses. In the end, these reviews will serve as specific examples of how carbohydrates are as integral to biology as are proteins, nucleic acids, and lipids. Here, we attempt to summarize general concepts on glycans and glycan-binding proteins (mainly C-type lectins, siglecs, and galectins) and their contributions to the biology of immune responses in physiologic and pathologic settings. © 2012 New York Academy of Sciences. 2012 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00778923_v1253_n1_p1_Rabinovich http://hdl.handle.net/20.500.12110/paper_00778923_v1253_n1_p1_Rabinovich |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
C-type lectins Galectins Glycans Glycobiology Glycoimmunology Lectins Siglecs binding protein carbohydrate galectin glycan glycan binding protein glycoprotein lectin lipid major histocompatibility antigen class 2 nucleic acid nucleotide binding oligomerization domain like receptor unclassified drug autoimmunity chronic inflammation glycobiology human Human immunodeficiency virus immune response immune system innate immunity nonhuman pathogenesis protein expression review tumor immunity |
spellingShingle |
C-type lectins Galectins Glycans Glycobiology Glycoimmunology Lectins Siglecs binding protein carbohydrate galectin glycan glycan binding protein glycoprotein lectin lipid major histocompatibility antigen class 2 nucleic acid nucleotide binding oligomerization domain like receptor unclassified drug autoimmunity chronic inflammation glycobiology human Human immunodeficiency virus immune response immune system innate immunity nonhuman pathogenesis protein expression review tumor immunity Glycobiology of immune responses |
topic_facet |
C-type lectins Galectins Glycans Glycobiology Glycoimmunology Lectins Siglecs binding protein carbohydrate galectin glycan glycan binding protein glycoprotein lectin lipid major histocompatibility antigen class 2 nucleic acid nucleotide binding oligomerization domain like receptor unclassified drug autoimmunity chronic inflammation glycobiology human Human immunodeficiency virus immune response immune system innate immunity nonhuman pathogenesis protein expression review tumor immunity |
description |
Unlike their protein "roommates" and their nucleic acid "cousins," carbohydrates remain an enigmatic arm of biology. The central reason for the difficulty in fully understanding how carbohydrate structure and biological function are tied is the nontemplate nature of their synthesis and the resulting heterogeneity. The goal of this collection of expert reviews is to highlight what is known about how carbohydrates and their binding partners-the microbial (non-self), tumor (altered-self), and host (self)-cooperate within the immune system, while also identifying areas of opportunity to those willing to take up the challenge of understanding more about how carbohydrates influence immune responses. In the end, these reviews will serve as specific examples of how carbohydrates are as integral to biology as are proteins, nucleic acids, and lipids. Here, we attempt to summarize general concepts on glycans and glycan-binding proteins (mainly C-type lectins, siglecs, and galectins) and their contributions to the biology of immune responses in physiologic and pathologic settings. © 2012 New York Academy of Sciences. |
title |
Glycobiology of immune responses |
title_short |
Glycobiology of immune responses |
title_full |
Glycobiology of immune responses |
title_fullStr |
Glycobiology of immune responses |
title_full_unstemmed |
Glycobiology of immune responses |
title_sort |
glycobiology of immune responses |
publishDate |
2012 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00778923_v1253_n1_p1_Rabinovich http://hdl.handle.net/20.500.12110/paper_00778923_v1253_n1_p1_Rabinovich |
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1768544771375104000 |