ADP-ribosylation: From molecular mechanisms to human disease

Autores
Hoch, Nicolas Carlos; Polo Ilacqua, Luis Mariano
Año de publicación
2020
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Post-translational modification of proteins by ADP-ribosylation, catalysed by poly (ADP-ribose) polymerases (PARPs) using NAD+ as a substrate, plays central roles in DNA damage signalling and repair, modulates a range of cellular signalling cascades and initiates programmed cell death by parthanatos. Here, we present mechanistic aspects of ADP-ribose modification, PARP activation and the cellular functions of ADP-ribose signalling, and discuss how this knowledge is uncovering therapeutic avenues for the treatment of increasingly prevalent human diseases such as cancer, ischaemic damage and neurodegeneration.
Fil: Hoch, Nicolas Carlos. Universidade de Sao Paulo; Brasil
Fil: Polo Ilacqua, Luis Mariano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina. University of Sussex; Reino Unido
Materia
ADP RIBOSE
DNA DAMAGE RESPONSE
DNA REPAIR
PARP
PARTHANATOS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/115088
Acceder
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network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling ADP-ribosylation: From molecular mechanisms to human diseaseHoch, Nicolas CarlosPolo Ilacqua, Luis MarianoADP RIBOSEDNA DAMAGE RESPONSEDNA REPAIRPARPPARTHANATOShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Post-translational modification of proteins by ADP-ribosylation, catalysed by poly (ADP-ribose) polymerases (PARPs) using NAD+ as a substrate, plays central roles in DNA damage signalling and repair, modulates a range of cellular signalling cascades and initiates programmed cell death by parthanatos. Here, we present mechanistic aspects of ADP-ribose modification, PARP activation and the cellular functions of ADP-ribose signalling, and discuss how this knowledge is uncovering therapeutic avenues for the treatment of increasingly prevalent human diseases such as cancer, ischaemic damage and neurodegeneration.Fil: Hoch, Nicolas Carlos. Universidade de Sao Paulo; BrasilFil: Polo Ilacqua, Luis Mariano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina. University of Sussex; Reino UnidoSociedade Brasileira de Genética2020-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/115088Hoch, Nicolas Carlos; Polo Ilacqua, Luis Mariano; ADP-ribosylation: From molecular mechanisms to human disease; Sociedade Brasileira de Genética; Genetics and Molecular Biology; 43; 1; 1-2020; 1-141415-47571678-4685CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572020000200304&lng=en&nrm=isoinfo:eu-repo/semantics/altIdentifier/doi/10.1590/1678-4685-gmb-2019-0075info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7198025/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:18:53Zoai:ri.conicet.gov.ar:11336/115088instacron: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 10:18:53.701CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv ADP-ribosylation: From molecular mechanisms to human disease
title ADP-ribosylation: From molecular mechanisms to human disease
spellingShingle ADP-ribosylation: From molecular mechanisms to human disease
Hoch, Nicolas Carlos
ADP RIBOSE
DNA DAMAGE RESPONSE
DNA REPAIR
PARP
PARTHANATOS
title_short ADP-ribosylation: From molecular mechanisms to human disease
title_full ADP-ribosylation: From molecular mechanisms to human disease
title_fullStr ADP-ribosylation: From molecular mechanisms to human disease
title_full_unstemmed ADP-ribosylation: From molecular mechanisms to human disease
title_sort ADP-ribosylation: From molecular mechanisms to human disease
dc.creator.none.fl_str_mv Hoch, Nicolas Carlos
Polo Ilacqua, Luis Mariano
author Hoch, Nicolas Carlos
author_facet Hoch, Nicolas Carlos
Polo Ilacqua, Luis Mariano
author_role author
author2 Polo Ilacqua, Luis Mariano
author2_role author
dc.subject.none.fl_str_mv ADP RIBOSE
DNA DAMAGE RESPONSE
DNA REPAIR
PARP
PARTHANATOS
topic ADP RIBOSE
DNA DAMAGE RESPONSE
DNA REPAIR
PARP
PARTHANATOS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Post-translational modification of proteins by ADP-ribosylation, catalysed by poly (ADP-ribose) polymerases (PARPs) using NAD+ as a substrate, plays central roles in DNA damage signalling and repair, modulates a range of cellular signalling cascades and initiates programmed cell death by parthanatos. Here, we present mechanistic aspects of ADP-ribose modification, PARP activation and the cellular functions of ADP-ribose signalling, and discuss how this knowledge is uncovering therapeutic avenues for the treatment of increasingly prevalent human diseases such as cancer, ischaemic damage and neurodegeneration.
Fil: Hoch, Nicolas Carlos. Universidade de Sao Paulo; Brasil
Fil: Polo Ilacqua, Luis Mariano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina. University of Sussex; Reino Unido
description Post-translational modification of proteins by ADP-ribosylation, catalysed by poly (ADP-ribose) polymerases (PARPs) using NAD+ as a substrate, plays central roles in DNA damage signalling and repair, modulates a range of cellular signalling cascades and initiates programmed cell death by parthanatos. Here, we present mechanistic aspects of ADP-ribose modification, PARP activation and the cellular functions of ADP-ribose signalling, and discuss how this knowledge is uncovering therapeutic avenues for the treatment of increasingly prevalent human diseases such as cancer, ischaemic damage and neurodegeneration.
publishDate 2020
dc.date.none.fl_str_mv 2020-01
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/11336/115088
Hoch, Nicolas Carlos; Polo Ilacqua, Luis Mariano; ADP-ribosylation: From molecular mechanisms to human disease; Sociedade Brasileira de Genética; Genetics and Molecular Biology; 43; 1; 1-2020; 1-14
1415-4757
1678-4685
CONICET Digital
CONICET
url http://hdl.handle.net/11336/115088
identifier_str_mv Hoch, Nicolas Carlos; Polo Ilacqua, Luis Mariano; ADP-ribosylation: From molecular mechanisms to human disease; Sociedade Brasileira de Genética; Genetics and Molecular Biology; 43; 1; 1-2020; 1-14
1415-4757
1678-4685
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.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572020000200304&lng=en&nrm=iso
info:eu-repo/semantics/altIdentifier/doi/10.1590/1678-4685-gmb-2019-0075
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7198025/
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Sociedade Brasileira de Genética
publisher.none.fl_str_mv Sociedade Brasileira de Genética
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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score 13.070432

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