| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10556461 | Journal of Proteomics | 2012 | 14 Pages |
Abstract
⺠Redox fluorescence switch (RFS), a novel thiol redox proteomics technique. ⺠RFS detects reversible cysteine oxidation and protein amount simultaneously. ⺠Useful for detecting oxidative modifications after physiological stimuli. ⺠Acute hypoxia produces protein cysteine oxidation in specific targets. ⺠Identified cysteine oxidations may be implied in signaling and hypoxia adaptation.
Keywords
Room temperature.PHDGRP78HIFHspHUVECTwo-dimensional electrophoresis (2-DE)heat shock cognate 71 kDa proteinHsc70HIF prolyl hydroxylaseN-ethylmaleimideRFSFDRCysteine oxidationpost-translational modificationsCAMHuman umbilical vein endothelial cellsCell signalingHypoxia-inducible factorlactate dehydrogenaseLDHfalse discovery rateNEM78 kDa glucose-regulated proteinHeat shock protein
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Alicia Izquierdo-Álvarez, Elena Ramos, Joan Villanueva, Pablo Hernansanz-AgustÃn, Rubén Fernández-RodrÃguez, Daniel Tello, Montserrat Carrascal, Antonio MartÃnez-Ruiz,