The peptidic posttranslational modifiers of the ubiquitin (Ub) family (ubiquitin-like, UbLs) are conjugated to thousands of proteins to modify their function and fate. Dysregulation of their conjugation/deconjugation pathways is associated with a variety of pathological disorders. However, the techniques currently available to monitor the levels of target modification by UbLs as well as the activity of UbL-conjugating enzymes are limited and generally not quantitative.
View Article and Find Full Text PDFUbiquitin and the ubiquitin-like SUMO are covalently conjugated to thousands of proteins to modulate their function and fate. Many of the enzymes involved in their conjugation are dysregulated in cancers and involved in cancer cell response to therapies. We describe here the identification of biomarkers of the activity of these enzymes and their use to predict acute myeloid leukemias (AML) response to standard chemotherapy (daunorubicin-DNR and cytarabine-Ara-C).
View Article and Find Full Text PDFUbiquitin defines a family of approximately 20 peptidic posttranslational modifiers collectively called the Ubiquitin-like (UbLs). They are conjugated to thousands of proteins, modifying their function and fate in many ways. Dysregulation of these modifications has been implicated in a variety of pathologies, in particular cancer.
View Article and Find Full Text PDFJ Gynecol Obstet Biol Reprod (Paris)
February 2005
In newborn and premature infants whose lung immaturity entails a limited capacity for O2 detoxification, the use of supplemental oxygen should be continuously and non-invasively monitored. Pulse oximetry and transcutaneous O2 monitoring are the systems most used in the NICU. Major limitations of pulse oximetry are motion artifact, sensitivity to excessive light, cutaneous hypoperfusion, hypothermia, venous congestion, arterio-venous shunting, strong skin pigmentation, anemia and high percentage of abnormal hemoglobin.
View Article and Find Full Text PDF