Aim for the readers! Bromodomains as new targets against Chagas` disease

Autores
Alonso, Victoria Lucia; Tavernelli, Luis Emilio; Pezza, Alejandro; Cribb, Pamela; Ritagliati, Carla; Serra, Esteban Carlos
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Bromodomains recognize and bind acetyl-lysine residues present in histone and non-histone proteins in a specific manner. Inthe last decade they have raised as attractive target for drug discovery because the miss-regulation of human bromodomains was discovered tobe involved in the development of a large spectrum of diseases..However, targeting eukaryotic pathogens bromodomains continues to bealmost unexplored. We and others have reported the essentiality of diverse bromodomain-containing proteins in protozoa, offering a newopportunity for the development of antiparasitic drugs, especially for Trypansoma cruzi, the causative agent of Chagas? disease. Mammalianbromodomains were classified in eight groups based on sequence similarity but parasitic bromodomains are very divergent proteins and ishard to assign them to any of these groups, suggesting that selective inhibitors can be obtained. In this review we describe the importance oflysine acetylation and bromodomains in T. cruzi as well as the current knowledge on mammalian bromodomains. Also, we summarize themyriad of small-molecules under study to treat different pathologies and which of them have been tested in trypanosomatids and otherprotozoa. All the information available led us to propose that T. cruzi bromodomains should be considered as important potential targetsand the search for small-molecules to inhibit them should be empowered.
Fil: Alonso, Victoria Lucia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Tavernelli, Luis Emilio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Pezza, Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Cribb, Pamela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Ritagliati, Carla. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Serra, Esteban Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Materia
BROMODOMAINS
ACETYLATION
TRYPANOSOMA CRUZI
BROMODOMAIN INHIBITORS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/92615
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Aim for the readers! Bromodomains as new targets against Chagas` diseaseAlonso, Victoria LuciaTavernelli, Luis EmilioPezza, AlejandroCribb, PamelaRitagliati, CarlaSerra, Esteban CarlosBROMODOMAINSACETYLATIONTRYPANOSOMA CRUZIBROMODOMAIN INHIBITORShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Bromodomains recognize and bind acetyl-lysine residues present in histone and non-histone proteins in a specific manner. Inthe last decade they have raised as attractive target for drug discovery because the miss-regulation of human bromodomains was discovered tobe involved in the development of a large spectrum of diseases..However, targeting eukaryotic pathogens bromodomains continues to bealmost unexplored. We and others have reported the essentiality of diverse bromodomain-containing proteins in protozoa, offering a newopportunity for the development of antiparasitic drugs, especially for Trypansoma cruzi, the causative agent of Chagas? disease. Mammalianbromodomains were classified in eight groups based on sequence similarity but parasitic bromodomains are very divergent proteins and ishard to assign them to any of these groups, suggesting that selective inhibitors can be obtained. In this review we describe the importance oflysine acetylation and bromodomains in T. cruzi as well as the current knowledge on mammalian bromodomains. Also, we summarize themyriad of small-molecules under study to treat different pathologies and which of them have been tested in trypanosomatids and otherprotozoa. All the information available led us to propose that T. cruzi bromodomains should be considered as important potential targetsand the search for small-molecules to inhibit them should be empowered.Fil: Alonso, Victoria Lucia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Tavernelli, Luis Emilio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Pezza, Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Cribb, Pamela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Ritagliati, Carla. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Serra, Esteban Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaBentham Science Publishers2018-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/92615Alonso, Victoria Lucia; Tavernelli, Luis Emilio; Pezza, Alejandro; Cribb, Pamela; Ritagliati, Carla; et al.; Aim for the readers! Bromodomains as new targets against Chagas` disease; Bentham Science Publishers; Current Medicinal Chemistry; 25; 36; 10-2018; 1-170929-8673CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.eurekaselect.com/166814/articleinfo:eu-repo/semantics/altIdentifier/doi/10.2174/0929867325666181031132007info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:46:13Zoai:ri.conicet.gov.ar:11336/92615instacron: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:34982025-09-03 09:46:14.238CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Aim for the readers! Bromodomains as new targets against Chagas` disease
title Aim for the readers! Bromodomains as new targets against Chagas` disease
spellingShingle Aim for the readers! Bromodomains as new targets against Chagas` disease
Alonso, Victoria Lucia
BROMODOMAINS
ACETYLATION
TRYPANOSOMA CRUZI
BROMODOMAIN INHIBITORS
title_short Aim for the readers! Bromodomains as new targets against Chagas` disease
title_full Aim for the readers! Bromodomains as new targets against Chagas` disease
title_fullStr Aim for the readers! Bromodomains as new targets against Chagas` disease
title_full_unstemmed Aim for the readers! Bromodomains as new targets against Chagas` disease
title_sort Aim for the readers! Bromodomains as new targets against Chagas` disease
dc.creator.none.fl_str_mv Alonso, Victoria Lucia
Tavernelli, Luis Emilio
Pezza, Alejandro
Cribb, Pamela
Ritagliati, Carla
Serra, Esteban Carlos
author Alonso, Victoria Lucia
author_facet Alonso, Victoria Lucia
Tavernelli, Luis Emilio
Pezza, Alejandro
Cribb, Pamela
Ritagliati, Carla
Serra, Esteban Carlos
author_role author
author2 Tavernelli, Luis Emilio
Pezza, Alejandro
Cribb, Pamela
Ritagliati, Carla
Serra, Esteban Carlos
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv BROMODOMAINS
ACETYLATION
TRYPANOSOMA CRUZI
BROMODOMAIN INHIBITORS
topic BROMODOMAINS
ACETYLATION
TRYPANOSOMA CRUZI
BROMODOMAIN INHIBITORS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Bromodomains recognize and bind acetyl-lysine residues present in histone and non-histone proteins in a specific manner. Inthe last decade they have raised as attractive target for drug discovery because the miss-regulation of human bromodomains was discovered tobe involved in the development of a large spectrum of diseases..However, targeting eukaryotic pathogens bromodomains continues to bealmost unexplored. We and others have reported the essentiality of diverse bromodomain-containing proteins in protozoa, offering a newopportunity for the development of antiparasitic drugs, especially for Trypansoma cruzi, the causative agent of Chagas? disease. Mammalianbromodomains were classified in eight groups based on sequence similarity but parasitic bromodomains are very divergent proteins and ishard to assign them to any of these groups, suggesting that selective inhibitors can be obtained. In this review we describe the importance oflysine acetylation and bromodomains in T. cruzi as well as the current knowledge on mammalian bromodomains. Also, we summarize themyriad of small-molecules under study to treat different pathologies and which of them have been tested in trypanosomatids and otherprotozoa. All the information available led us to propose that T. cruzi bromodomains should be considered as important potential targetsand the search for small-molecules to inhibit them should be empowered.
Fil: Alonso, Victoria Lucia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Tavernelli, Luis Emilio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Pezza, Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Cribb, Pamela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Ritagliati, Carla. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Serra, Esteban Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
description Bromodomains recognize and bind acetyl-lysine residues present in histone and non-histone proteins in a specific manner. Inthe last decade they have raised as attractive target for drug discovery because the miss-regulation of human bromodomains was discovered tobe involved in the development of a large spectrum of diseases..However, targeting eukaryotic pathogens bromodomains continues to bealmost unexplored. We and others have reported the essentiality of diverse bromodomain-containing proteins in protozoa, offering a newopportunity for the development of antiparasitic drugs, especially for Trypansoma cruzi, the causative agent of Chagas? disease. Mammalianbromodomains were classified in eight groups based on sequence similarity but parasitic bromodomains are very divergent proteins and ishard to assign them to any of these groups, suggesting that selective inhibitors can be obtained. In this review we describe the importance oflysine acetylation and bromodomains in T. cruzi as well as the current knowledge on mammalian bromodomains. Also, we summarize themyriad of small-molecules under study to treat different pathologies and which of them have been tested in trypanosomatids and otherprotozoa. All the information available led us to propose that T. cruzi bromodomains should be considered as important potential targetsand the search for small-molecules to inhibit them should be empowered.
publishDate 2018
dc.date.none.fl_str_mv 2018-10
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/11336/92615
Alonso, Victoria Lucia; Tavernelli, Luis Emilio; Pezza, Alejandro; Cribb, Pamela; Ritagliati, Carla; et al.; Aim for the readers! Bromodomains as new targets against Chagas` disease; Bentham Science Publishers; Current Medicinal Chemistry; 25; 36; 10-2018; 1-17
0929-8673
CONICET Digital
CONICET
url http://hdl.handle.net/11336/92615
identifier_str_mv Alonso, Victoria Lucia; Tavernelli, Luis Emilio; Pezza, Alejandro; Cribb, Pamela; Ritagliati, Carla; et al.; Aim for the readers! Bromodomains as new targets against Chagas` disease; Bentham Science Publishers; Current Medicinal Chemistry; 25; 36; 10-2018; 1-17
0929-8673
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.eurekaselect.com/166814/article
info:eu-repo/semantics/altIdentifier/doi/10.2174/0929867325666181031132007
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/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Bentham Science Publishers
publisher.none.fl_str_mv Bentham Science Publishers
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str 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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