Functions of cell surface galectin-glycoprotein lattices
- Autores
- Rabinovich, Gabriel Adrián; Toscano, Marta Alicia; Jackson, Shawn S.; Vasta, Gerardo R.
- Año de publicación
- 2007
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Programmed remodeling of cell surface glycans by the sequential action of specific glycosyltransferases can control biological processes by generating or masking ligands for endogenous lectins. Galectins, a family of animal lectins with affinity for beta-galactosides, can form multivalent complexes with cell surface glycoconjugates and deliver a variety of intracellular signals to modulate cell activation, differentiation, and survival. Recent efforts involving genetic or biochemical manipulation of O-glycosylation and N-glycosylation pathways, as well as blockade of the synthesis of endogenous galectins, have illuminated essential roles for galectin-glycoprotein lattices in the control of biological processes including receptor turnover and endocytosis, host-pathogen interactions, and immune cell activation and homeostasis.
Fil: Rabinovich, Gabriel Adrián. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Toscano, Marta Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
Fil: Jackson, Shawn S.. University of Maryland; Estados Unidos
Fil: Vasta, Gerardo R.. University of Maryland; Estados Unidos - Materia
-
GALECTINS
B-LYMPHOCYTES
INMUNITY
CELL MEMBRANE - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/26257
Ver los metadatos del registro completo
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Functions of cell surface galectin-glycoprotein latticesRabinovich, Gabriel AdriánToscano, Marta AliciaJackson, Shawn S.Vasta, Gerardo R.GALECTINSB-LYMPHOCYTESINMUNITYCELL MEMBRANEhttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3https://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3Programmed remodeling of cell surface glycans by the sequential action of specific glycosyltransferases can control biological processes by generating or masking ligands for endogenous lectins. Galectins, a family of animal lectins with affinity for beta-galactosides, can form multivalent complexes with cell surface glycoconjugates and deliver a variety of intracellular signals to modulate cell activation, differentiation, and survival. Recent efforts involving genetic or biochemical manipulation of O-glycosylation and N-glycosylation pathways, as well as blockade of the synthesis of endogenous galectins, have illuminated essential roles for galectin-glycoprotein lattices in the control of biological processes including receptor turnover and endocytosis, host-pathogen interactions, and immune cell activation and homeostasis.Fil: Rabinovich, Gabriel Adrián. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Toscano, Marta Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; ArgentinaFil: Jackson, Shawn S.. University of Maryland; Estados UnidosFil: Vasta, Gerardo R.. University of Maryland; Estados UnidosElsevier2007-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/26257Rabinovich, Gabriel Adrián; Toscano, Marta Alicia; Jackson, Shawn S.; Vasta, Gerardo R.; Functions of cell surface galectin-glycoprotein lattices; Elsevier; Current Opinion In Structural Biology; 17; 5; 10-2007; 513-5200959-440X1879-033XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0959440X07001303info:eu-repo/semantics/altIdentifier/doi/10.1016/j.sbi.2007.09.002info:eu-repo/semantics/altIdentifier/pmid/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2100406/info:eu-repo/semantics/altIdentifier/pmid/17950594info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:00:12Zoai:ri.conicet.gov.ar:11336/26257instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:00:12.763CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Functions of cell surface galectin-glycoprotein lattices |
title |
Functions of cell surface galectin-glycoprotein lattices |
spellingShingle |
Functions of cell surface galectin-glycoprotein lattices Rabinovich, Gabriel Adrián GALECTINS B-LYMPHOCYTES INMUNITY CELL MEMBRANE |
title_short |
Functions of cell surface galectin-glycoprotein lattices |
title_full |
Functions of cell surface galectin-glycoprotein lattices |
title_fullStr |
Functions of cell surface galectin-glycoprotein lattices |
title_full_unstemmed |
Functions of cell surface galectin-glycoprotein lattices |
title_sort |
Functions of cell surface galectin-glycoprotein lattices |
dc.creator.none.fl_str_mv |
Rabinovich, Gabriel Adrián Toscano, Marta Alicia Jackson, Shawn S. Vasta, Gerardo R. |
author |
Rabinovich, Gabriel Adrián |
author_facet |
Rabinovich, Gabriel Adrián Toscano, Marta Alicia Jackson, Shawn S. Vasta, Gerardo R. |
author_role |
author |
author2 |
Toscano, Marta Alicia Jackson, Shawn S. Vasta, Gerardo R. |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
GALECTINS B-LYMPHOCYTES INMUNITY CELL MEMBRANE |
topic |
GALECTINS B-LYMPHOCYTES INMUNITY CELL MEMBRANE |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/3.1 https://purl.org/becyt/ford/3 https://purl.org/becyt/ford/3.1 https://purl.org/becyt/ford/3 |
dc.description.none.fl_txt_mv |
Programmed remodeling of cell surface glycans by the sequential action of specific glycosyltransferases can control biological processes by generating or masking ligands for endogenous lectins. Galectins, a family of animal lectins with affinity for beta-galactosides, can form multivalent complexes with cell surface glycoconjugates and deliver a variety of intracellular signals to modulate cell activation, differentiation, and survival. Recent efforts involving genetic or biochemical manipulation of O-glycosylation and N-glycosylation pathways, as well as blockade of the synthesis of endogenous galectins, have illuminated essential roles for galectin-glycoprotein lattices in the control of biological processes including receptor turnover and endocytosis, host-pathogen interactions, and immune cell activation and homeostasis. Fil: Rabinovich, Gabriel Adrián. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina Fil: Toscano, Marta Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina Fil: Jackson, Shawn S.. University of Maryland; Estados Unidos Fil: Vasta, Gerardo R.. University of Maryland; Estados Unidos |
description |
Programmed remodeling of cell surface glycans by the sequential action of specific glycosyltransferases can control biological processes by generating or masking ligands for endogenous lectins. Galectins, a family of animal lectins with affinity for beta-galactosides, can form multivalent complexes with cell surface glycoconjugates and deliver a variety of intracellular signals to modulate cell activation, differentiation, and survival. Recent efforts involving genetic or biochemical manipulation of O-glycosylation and N-glycosylation pathways, as well as blockade of the synthesis of endogenous galectins, have illuminated essential roles for galectin-glycoprotein lattices in the control of biological processes including receptor turnover and endocytosis, host-pathogen interactions, and immune cell activation and homeostasis. |
publishDate |
2007 |
dc.date.none.fl_str_mv |
2007-10 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/26257 Rabinovich, Gabriel Adrián; Toscano, Marta Alicia; Jackson, Shawn S.; Vasta, Gerardo R.; Functions of cell surface galectin-glycoprotein lattices; Elsevier; Current Opinion In Structural Biology; 17; 5; 10-2007; 513-520 0959-440X 1879-033X CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/26257 |
identifier_str_mv |
Rabinovich, Gabriel Adrián; Toscano, Marta Alicia; Jackson, Shawn S.; Vasta, Gerardo R.; Functions of cell surface galectin-glycoprotein lattices; Elsevier; Current Opinion In Structural Biology; 17; 5; 10-2007; 513-520 0959-440X 1879-033X CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0959440X07001303 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.sbi.2007.09.002 info:eu-repo/semantics/altIdentifier/pmid/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2100406/ info:eu-repo/semantics/altIdentifier/pmid/17950594 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
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application/pdf application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier |
publisher.none.fl_str_mv |
Elsevier |
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reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) |
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CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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13.070432 |