Resultats globals: 2 registres trobats en 0.02 segons.
Articles, 2 registres trobats
Articles 2 registres trobats  
1.
Oxidovanadium(IV) sulfate catalyses light-driven C-N bond formation / Gaspa, Silvia (Università di Sassari. Dipartimento di Scienze Chimiche) ; Sciortino, Giuseppe (Institut d'Investigacions Químiques de Catalunya) ; Porcheddu, Andrea (Università degli Studi di Cagliari) ; Dell'Osa, Chiara (Università di Sassari. Dipartimento di Scienze Chimiche) ; Satta, Giuseppe (Università di Sassari. Dipartimento di Scienze Chimiche) ; Azzena, Ugo (Università di Sassari. Dipartimento di Scienze Chimiche) ; Pisano, Luisa (Università di Sassari. Dipartimento di Scienze Chimiche) ; Carraro, Massimo (Università di Sassari. Dipartimento di Scienze Chimiche) ; Sanna, Daniele (Istituto CNR di Chimica Biomolecolare) ; Garribba, Eugenio (Università di Sassari. Dipartimento di Medicina, Chirurgia e Farmacia) ; Maseras Cuní, Feliu (Institut d'Investigacions Químiques de Catalunya) ; De Luca, Lidia (Università di Sassari. Dipartimento di Scienze Chimiche)
Oxidovanadium(IV) sulfate, VIVOSO4, is shown to catalyze efficiently the amidation of the C-H bond of aldehydes by N-chloramine derivatives for the selective synthesis of amides. The catalytic process is driven by visible light irradiation at room temperature, and the reaction is carried out in ethyl acetate, a green and bio-based solvent. [...]
2023 - 10.1016/j.mcat.2023.113054
Molecular Catalysis, Vol. 541 (April 2023) , art. 113054  
2.
19 p, 2.5 MB Substrate Specificity, Inhibitor Selectivity and Structure-Function Relationships of Aldo-Keto Reductase 1B15 : a Novel Human Retinaldehyde Reductase / Giménez Dejoz, Joan (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Kolář, Michal H. (Academy of Sciences of the Czech Republic. Institute of Organic Chemistry and Biochemistry) ; Ruiz, Francesc X. (Centre de Biologie Intégrative (Illkirch-Graffenstaden, França)) ; Crespo, Isidro (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Cousido-Siah, Alexandra (Centre de Biologie Intégrative (Illkirch-Graffenstaden, França)) ; Podjarny, Alberto (Centre de Biologie Intégrative (Illkirch-Graffenstaden, França)) ; Barski, Oleg A. (University of Louisville. School of Medicine) ; Fanfrlík, Jindřich (Academy of Sciences of the Czech Republic. Institute of Organic Chemistry and Biochemistry) ; Parés i Casasampera, Xavier (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Farrés, Jaume (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Porté Orduna, Sergio (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Human aldo-keto reductase 1B15 (AKR1B15) is a newly discovered enzyme which shares 92% amino acid sequence identity with AKR1B10. While AKR1B10 is a well characterized enzyme with high retinaldehyde reductase activity, involved in the development of several cancer types, the enzymatic activity and physiological role of AKR1B15 are still poorly known. [...]
2015 - 10.1371/journal.pone.0134506
PloS one, Vol. 10 Núm. 7 (July 2015) , p. e0134506  

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