Fluorescence Lifetime Phasor Analysis of the Decamer–Dimer Equilibrium of Human Peroxiredoxin 1

Villar, Sebastián F. - Dalla-Rizza, Joaquín - Möller, Matías N. - Ferrer-Sueta, Gerardo - Malacrida, Leonel - Jameson, David M. - 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
2022
Agencia Nacional de Investigación e Innovación
Peroxirredoxina
Ciencias Naturales y Exactas
Ciencias Químicas
Ciencias Biológicas
Bioquímica y Biología Molecular
Inglés
Agencia Nacional de Investigación e Innovación
REDI
https://hdl.handle.net/20.500.12381/3289
https://doi.org/10.3390/ijms23095260
Acceso abierto
Reconocimiento 4.0 Internacional. (CC BY)