The multifaceted nature of peroxiredoxins in chemical biology

Villar, Sebastián F. - Ferrer-Sueta, Gerardo - Denicola, Ana

Resumen:

Peroxiredoxins (Prx), thiol-dependent peroxidases, were first identified as H2O2 detoxifiers, and more recently as H2O2 sensors, intermediates in redox-signaling pathways, metabolism modulators, and chaperones. The multifaceted nature of Prx is not only dependent on their peroxidase activity but also strongly associated with specific protein–protein interactions that are being identified, and where the Prx oligomerization dynamics plays a role. Their oxidation by a peroxide substrate forms a sulfenic acid that opens a route to channel the redox signal to diverse protein targets. Recent research underscores the importance of different Prx isoforms in the cellular processes behind disease development with potential therapeutic applications.


Detalles Bibliográficos
2023
Agencia Nacional de Investigación e Innovación
Peroxirredoxina
Ciencias Naturales y Exactas
Ciencias Biológicas
Inglés
Agencia Nacional de Investigación e Innovación
REDI
https://hdl.handle.net/20.500.12381/3292
Acceso embargado
Reconocimiento-CompartirIgual 4.0 Internacional. (CC BY-SA)
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author Villar, Sebastián F.
author2 Ferrer-Sueta, Gerardo
Denicola, Ana
author2_role author
author
author_facet Villar, Sebastián F.
Ferrer-Sueta, Gerardo
Denicola, Ana
author_role author
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https://redi.anii.org.uy/jspui/bitstream/20.500.12381/3292/5/COCHB%202023%20The%20multifaceted%20nature%20of%20prx.pdf
collection REDI
dc.creator.none.fl_str_mv Villar, Sebastián F.
Ferrer-Sueta, Gerardo
Denicola, Ana
dc.date.accessioned.none.fl_str_mv 2023-09-28T19:17:04Z
dc.date.issued.none.fl_str_mv 2023-10
dc.description.abstract.none.fl_txt_mv Peroxiredoxins (Prx), thiol-dependent peroxidases, were first identified as H2O2 detoxifiers, and more recently as H2O2 sensors, intermediates in redox-signaling pathways, metabolism modulators, and chaperones. The multifaceted nature of Prx is not only dependent on their peroxidase activity but also strongly associated with specific protein–protein interactions that are being identified, and where the Prx oligomerization dynamics plays a role. Their oxidation by a peroxide substrate forms a sulfenic acid that opens a route to channel the redox signal to diverse protein targets. Recent research underscores the importance of different Prx isoforms in the cellular processes behind disease development with potential therapeutic applications.
dc.description.sponsorship.none.fl_txt_mv Agencia Nacional de Investigación e Innovación
dc.identifier.anii.es.fl_str_mv FCE_1_2019_1_155969
dc.identifier.doi.none.fl_str_mv 10.1016/j.cbpa.2023.102355
dc.identifier.uri.none.fl_str_mv https://hdl.handle.net/20.500.12381/3292
dc.language.iso.none.fl_str_mv eng
dc.publisher.es.fl_str_mv Elsevier
dc.rights.*.fl_str_mv Acceso embargado
dc.rights.embargoend.*.fl_str_mv 2025-06-28
dc.rights.embargoterm.*.fl_str_mv 2025-06-28
dc.rights.license.none.fl_str_mv Reconocimiento-CompartirIgual 4.0 Internacional. (CC BY-SA)
dc.rights.none.fl_str_mv info:eu-repo/semantics/embargoedAccess
dc.source.es.fl_str_mv Current Opinion in Chemical Biology
dc.source.none.fl_str_mv reponame:REDI
instname:Agencia Nacional de Investigación e Innovación
instacron:Agencia Nacional de Investigación e Innovación
dc.subject.anii.none.fl_str_mv Ciencias Naturales y Exactas
Ciencias Biológicas
dc.subject.es.fl_str_mv Peroxirredoxina
dc.title.none.fl_str_mv The multifaceted nature of peroxiredoxins in chemical biology
dc.type.es.fl_str_mv Artículo
dc.type.none.fl_str_mv info:eu-repo/semantics/article
dc.type.version.es.fl_str_mv Publicado
dc.type.version.none.fl_str_mv info:eu-repo/semantics/publishedVersion
description Peroxiredoxins (Prx), thiol-dependent peroxidases, were first identified as H2O2 detoxifiers, and more recently as H2O2 sensors, intermediates in redox-signaling pathways, metabolism modulators, and chaperones. The multifaceted nature of Prx is not only dependent on their peroxidase activity but also strongly associated with specific protein–protein interactions that are being identified, and where the Prx oligomerization dynamics plays a role. Their oxidation by a peroxide substrate forms a sulfenic acid that opens a route to channel the redox signal to diverse protein targets. Recent research underscores the importance of different Prx isoforms in the cellular processes behind disease development with potential therapeutic applications.
eu_rights_str_mv embargoedAccess
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id REDI_9b92a7e68384d741462eb5985aae42a2
identifier_str_mv FCE_1_2019_1_155969
10.1016/j.cbpa.2023.102355
instacron_str Agencia Nacional de Investigación e Innovación
institution Agencia Nacional de Investigación e Innovación
instname_str Agencia Nacional de Investigación e Innovación
language eng
network_acronym_str REDI
network_name_str REDI
oai_identifier_str oai:redi.anii.org.uy:20.500.12381/3292
publishDate 2023
reponame_str REDI
repository.mail.fl_str_mv jmaldini@anii.org.uy
repository.name.fl_str_mv REDI - Agencia Nacional de Investigación e Innovación
repository_id_str 9421
rights_invalid_str_mv Reconocimiento-CompartirIgual 4.0 Internacional. (CC BY-SA)
Acceso embargado
2025-06-28
spelling Reconocimiento-CompartirIgual 4.0 Internacional. (CC BY-SA)Acceso embargado2025-06-28La revista ofrece opciones de acceso abierto, pero el costo está más allá de nuestras posibilidades o del financiamiento recibido2025-06-28info:eu-repo/semantics/embargoedAccess2023-09-28T19:17:04Z2023-10https://hdl.handle.net/20.500.12381/3292FCE_1_2019_1_15596910.1016/j.cbpa.2023.102355Peroxiredoxins (Prx), thiol-dependent peroxidases, were first identified as H2O2 detoxifiers, and more recently as H2O2 sensors, intermediates in redox-signaling pathways, metabolism modulators, and chaperones. The multifaceted nature of Prx is not only dependent on their peroxidase activity but also strongly associated with specific protein–protein interactions that are being identified, and where the Prx oligomerization dynamics plays a role. Their oxidation by a peroxide substrate forms a sulfenic acid that opens a route to channel the redox signal to diverse protein targets. Recent research underscores the importance of different Prx isoforms in the cellular processes behind disease development with potential therapeutic applications.Agencia Nacional de Investigación e InnovaciónengElsevierCurrent Opinion in Chemical Biologyreponame:REDIinstname:Agencia Nacional de Investigación e Innovacióninstacron:Agencia Nacional de Investigación e InnovaciónPeroxirredoxinaCiencias Naturales y ExactasCiencias BiológicasThe multifaceted nature of peroxiredoxins in chemical biologyArtículoPublicadoinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleUniversidad de la República. Facultad de Ciencias//Ciencias Naturales y Exactas/Ciencias Biológicas/Ciencias BiológicasVillar, Sebastián F.Ferrer-Sueta, GerardoDenicola, AnaLICENSElicense.txtlicense.txttext/plain; charset=utf-84967https://redi.anii.org.uy/jspui/bitstream/20.500.12381/3292/6/license.txta4ce09f01b5dd771727aa05c73851623MD56Correo de ANII - Fwd_ Share your article [COCHBI_102355] published in Current Opinion in Chemical Biology.pdfCorreo de ANII - Fwd_ Share your article [COCHBI_102355] published in Current Opinion in Chemical Biology.pdfapplication/pdf257440https://redi.anii.org.uy/jspui/bitstream/20.500.12381/3292/7/Correo%20de%20ANII%20-%20Fwd_%20Share%20your%20article%20%5bCOCHBI_102355%5d%20published%20in%20Current%20Opinion%20in%20Chemical%20Biology.pdfd54149da0756970d164af02cb04e11e4MD57ORIGINALCOCHB 2023 The multifaceted nature of prx.pdfCOCHB 2023 The multifaceted nature of prx.pdfDocumento aceptadoapplication/pdf838859https://redi.anii.org.uy/jspui/bitstream/20.500.12381/3292/5/COCHB%202023%20The%20multifaceted%20nature%20of%20prx.pdf7cedaeded1db84960a512fccfea50703MD5520.500.12381/32922023-09-28 16:17:05.905oai:redi.anii.org.uy:20.500.12381/3292Gobiernohttps://www.anii.org.uy/https://redi.anii.org.uy/oai/requestjmaldini@anii.org.uyUruguayopendoar:94212023-09-28T19:17:05REDI - Agencia Nacional de Investigación e Innovaciónfalse
spellingShingle The multifaceted nature of peroxiredoxins in chemical biology
Villar, Sebastián F.
Peroxirredoxina
Ciencias Naturales y Exactas
Ciencias Biológicas
status_str publishedVersion
title The multifaceted nature of peroxiredoxins in chemical biology
title_full The multifaceted nature of peroxiredoxins in chemical biology
title_fullStr The multifaceted nature of peroxiredoxins in chemical biology
title_full_unstemmed The multifaceted nature of peroxiredoxins in chemical biology
title_short The multifaceted nature of peroxiredoxins in chemical biology
title_sort The multifaceted nature of peroxiredoxins in chemical biology
topic Peroxirredoxina
Ciencias Naturales y Exactas
Ciencias Biológicas
url https://hdl.handle.net/20.500.12381/3292