Xavier Parés

TL;DR: It is demonstrated that AKR1B10 also acts as a retinaldehyde reductase in vivo, which may be relevant in controlling the first step of retinoic acid synthesis and the design of specific inhibitors for cancer and diabetes treatments.

TL;DR: It is demonstrated that none of the enzymes, including the SDR members, are active withCRBPI-bound retinoids, which questions the previously suggested role of CRBPI as a retinol supplier in the retinoic acid synthesis pathway.

TL;DR: It is suggested that the rate-limiting step in the reaction mechanism with retinaldehyde differs between AKR1B1 and AKR2B10, and supports that overexpression of AKR 1B10 in cancer (an updated review on this topic is included) may contribute to dedifferentiation and tumor development.

TL;DR: Several aldo-keto reductase (AKR) enzymes from subfamilies 1B and 1C have been shown to have low Km and kcat values.

TL;DR: The development of selective inhibitors for AKR enzymes 1B1 and 1B10, of clinical relevance in diabetes and cancer, granted the investigation of some structure-activity relationships, and the inhibitory properties of some synthetic retinoids were explored.