Fluorescence Lifetime Phasor Analysis of the Decamer–Dimer Equilibrium of Human Peroxiredoxin 1
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.
| 2022 | |
| Agencia Nacional de Investigación e Innovación | |
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Peroxirredoxina Ciencias Naturales y Exactas Ciencias Químicas Ciencias Biológicas Bioquímica y Biología Molecular |
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| Inglés | |
| Agencia Nacional de Investigación e Innovación | |
| REDI | |
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https://hdl.handle.net/20.500.12381/3289
https://doi.org/10.3390/ijms23095260 |
|
| Acceso abierto | |
| Reconocimiento 4.0 Internacional. (CC BY) |
| _version_ | 1814959258586841088 |
|---|---|
| author | Villar, Sebastián F. |
| author2 | Dalla-Rizza, Joaquín Möller, Matías N. Ferrer-Sueta, Gerardo Malacrida, Leonel Jameson, David M. Denicola, , Ana |
| author2_role | author author author author author author |
| author_facet | Villar, Sebastián F. Dalla-Rizza, Joaquín Möller, Matías N. Ferrer-Sueta, Gerardo Malacrida, Leonel Jameson, David M. Denicola, , Ana |
| author_role | author |
| bitstream.checksum.fl_str_mv | a4ce09f01b5dd771727aa05c73851623 68df270841570e74eae737791c1493e9 |
| bitstream.checksumAlgorithm.fl_str_mv | MD5 MD5 |
| bitstream.url.fl_str_mv | https://redi.anii.org.uy/jspui/bitstream/20.500.12381/3289/2/license.txt https://redi.anii.org.uy/jspui/bitstream/20.500.12381/3289/1/2022%20-%20Villar%20-%20IJMS.pdf |
| collection | REDI |
| dc.creator.none.fl_str_mv | Villar, Sebastián F. Dalla-Rizza, Joaquín Möller, Matías N. Ferrer-Sueta, Gerardo Malacrida, Leonel Jameson, David M. Denicola, , Ana |
| dc.date.accessioned.none.fl_str_mv | 2023-09-27T16:48:16Z |
| dc.date.available.none.fl_str_mv | 2023-09-27T16:48:16Z |
| dc.date.issued.none.fl_str_mv | 2022-05-09 |
| 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.citation.es.fl_str_mv | Villar, S.F.; Dalla-Rizza, J.; Möller, M.N.; Ferrer-Sueta, G.; Malacrida, L.; Jameson, D.M.; Denicola, A. Fluorescence Lifetime Phasor Analysis of the Decamer–Dimer Equilibrium of Human Peroxiredoxin 1. Int. J. Mol. Sci. 2022, 23, 5260. https://doi.org/ 10.3390/ijms23095260 |
| dc.identifier.doi.none.fl_str_mv | https://doi.org/10.3390/ijms23095260 |
| dc.identifier.uri.none.fl_str_mv | https://hdl.handle.net/20.500.12381/3289 |
| dc.language.iso.none.fl_str_mv | eng |
| dc.publisher.es.fl_str_mv | MDPI |
| dc.rights.*.fl_str_mv | Acceso abierto |
| dc.rights.license.none.fl_str_mv | Reconocimiento 4.0 Internacional. (CC BY) |
| dc.rights.none.fl_str_mv | info:eu-repo/semantics/openAccess |
| dc.source.es.fl_str_mv | International Journal of Molecular Sciences |
| 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 Químicas Ciencias Biológicas Bioquímica y Biología Molecular |
| dc.subject.es.fl_str_mv | Peroxirredoxina |
| dc.title.none.fl_str_mv | Fluorescence Lifetime Phasor Analysis of the Decamer–Dimer Equilibrium of Human Peroxiredoxin 1 |
| 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 | openAccess |
| format | article |
| id | REDI_e71604a5ddcb0e1458163b74ce61ad29 |
| identifier_str_mv | Villar, S.F.; Dalla-Rizza, J.; Möller, M.N.; Ferrer-Sueta, G.; Malacrida, L.; Jameson, D.M.; Denicola, A. Fluorescence Lifetime Phasor Analysis of the Decamer–Dimer Equilibrium of Human Peroxiredoxin 1. Int. J. Mol. Sci. 2022, 23, 5260. https://doi.org/ 10.3390/ijms23095260 FCE_1_2019_1_155969 |
| 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:20.500.12381/3289 |
| publishDate | 2022 |
| 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 4.0 Internacional. (CC BY) Acceso abierto |
| spelling | Reconocimiento 4.0 Internacional. (CC BY)Acceso abiertoinfo:eu-repo/semantics/openAccess2023-09-27T16:48:16Z2023-09-27T16:48:16Z2022-05-09Villar, S.F.; Dalla-Rizza, J.; Möller, M.N.; Ferrer-Sueta, G.; Malacrida, L.; Jameson, D.M.; Denicola, A. Fluorescence Lifetime Phasor Analysis of the Decamer–Dimer Equilibrium of Human Peroxiredoxin 1. Int. J. Mol. Sci. 2022, 23, 5260. https://doi.org/ 10.3390/ijms23095260https://hdl.handle.net/20.500.12381/3289FCE_1_2019_1_155969https://doi.org/10.3390/ijms23095260Peroxiredoxins (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 InnovaciónengMDPIInternational Journal of Molecular Sciencesreponame:REDIinstname:Agencia Nacional de Investigación e Innovacióninstacron:Agencia Nacional de Investigación e InnovaciónPeroxirredoxinaCiencias Naturales y ExactasCiencias QuímicasCiencias BiológicasBioquímica y Biología MolecularFluorescence Lifetime Phasor Analysis of the Decamer–Dimer Equilibrium of Human Peroxiredoxin 1ArtículoPublicadoinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleUniversidad de la República. Facultad de Ciencias//Ciencias Naturales y Exactas/Ciencias Químicas/Ciencias Químicas//Ciencias Naturales y Exactas/Ciencias Biológicas/Bioquímica y Biología MolecularVillar, Sebastián F.Dalla-Rizza, JoaquínMöller, Matías N.Ferrer-Sueta, GerardoMalacrida, LeonelJameson, David M.Denicola, , AnaLICENSElicense.txtlicense.txttext/plain; charset=utf-84967https://redi.anii.org.uy/jspui/bitstream/20.500.12381/3289/2/license.txta4ce09f01b5dd771727aa05c73851623MD52ORIGINAL2022 - Villar - IJMS.pdf2022 - Villar - IJMS.pdfArtículo publicadoapplication/pdf2659457https://redi.anii.org.uy/jspui/bitstream/20.500.12381/3289/1/2022%20-%20Villar%20-%20IJMS.pdf68df270841570e74eae737791c1493e9MD5120.500.12381/32892023-09-27 13:48:18.135oai:redi.anii.org.uy:20.500.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Gobiernohttps://www.anii.org.uy/https://redi.anii.org.uy/oai/requestjmaldini@anii.org.uyUruguayopendoar:94212023-09-27T16:48:18REDI - Agencia Nacional de Investigación e Innovaciónfalse |
| spellingShingle | Fluorescence Lifetime Phasor Analysis of the Decamer–Dimer Equilibrium of Human Peroxiredoxin 1 Villar, Sebastián F. Peroxirredoxina Ciencias Naturales y Exactas Ciencias Químicas Ciencias Biológicas Bioquímica y Biología Molecular |
| status_str | publishedVersion |
| title | Fluorescence Lifetime Phasor Analysis of the Decamer–Dimer Equilibrium of Human Peroxiredoxin 1 |
| title_full | Fluorescence Lifetime Phasor Analysis of the Decamer–Dimer Equilibrium of Human Peroxiredoxin 1 |
| title_fullStr | Fluorescence Lifetime Phasor Analysis of the Decamer–Dimer Equilibrium of Human Peroxiredoxin 1 |
| title_full_unstemmed | Fluorescence Lifetime Phasor Analysis of the Decamer–Dimer Equilibrium of Human Peroxiredoxin 1 |
| title_short | Fluorescence Lifetime Phasor Analysis of the Decamer–Dimer Equilibrium of Human Peroxiredoxin 1 |
| title_sort | Fluorescence Lifetime Phasor Analysis of the Decamer–Dimer Equilibrium of Human Peroxiredoxin 1 |
| topic | Peroxirredoxina Ciencias Naturales y Exactas Ciencias Químicas Ciencias Biológicas Bioquímica y Biología Molecular |
| url | https://hdl.handle.net/20.500.12381/3289 https://doi.org/10.3390/ijms23095260 |
