Výsledky vyhledávání - "Carlotta Gozzer"

A path model analysis on predictors of dropout (at 6 and 12 months) during the weight loss interventions in endocrinology outpatient division

Autor: Mariangela Rondanelli, Mara Nichetti, Maurizio Naso, Chiara Edera, Gabriella Peroni, Beatrice Vigo, Pietro Allegrini, Simone Perna, Carlotta Gozzer, Milena Anna Faliva, Antonella Riva, Daniele Spadaccini

Publikováno v: Endocrine. 61:447-461

This study aimed to identify the dropout rate at 6 and 12 months from the first outpatient visit, and to analyze dropout risk factors among the following areas: biochemical examinations, anthropometric measures, psychological tests, personal data, an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e61b87d36efec4ff294803ca2e173ba
https://doi.org/10.1007/s12020-018-1563-y

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12-month effects of incretins versus SGLT2-Inhibitors on cognitive performance and metabolic profile. A randomized clinical trial in the elderly with Type-2 diabetes mellitus

Autor: Ruben Bacchio, Sebastiano Bruno Solerte, Manuela Mainardi, Simone Perna, Daniele Spadaccini, Mariangela Rondanelli, Paolo Astrone, Carlotta Gozzer, Anna Biava

Publikováno v: Clinical Pharmacology : Advances and Applications

Simone Perna,1 Manuela Mainardi,2 Paolo Astrone,2 Carlotta Gozzer,3 Anna Biava,1 Ruben Bacchio,3 Daniele Spadaccini,3 Sebastiano Bruno Solerte,2 Mariangela Rondanelli4 1Department of Biology, College of Science, University of Bahrain, Sakhir Campus,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1e3ada88cd21b7246ef29570b6b341f
https://pubmed.ncbi.nlm.nih.gov/30349407

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Purification and properties of NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase from spinach leaves

Autor: M.L. Speranza, Carlotta Gozzer

Publikováno v: Biochimica et Biophysica Acta (BBA) - Enzymology. 522:32-42

An NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase (D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating), EC. 1.2.1.12) has been purified from spinach leaves as a homogeneous protein of 150,000 daltons. Kinetic constants of 2.5

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e964e58e2c10ae74161a0e9475613bee
https://doi.org/10.1016/0005-2744(78)90319-4

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Radioimmunoassay and chemical properties of glucose-6-phosphate dehydrogenase and of a specific NADP(H)-binding protein (FX) from human erythrocytes

Autor: Monica Galliano, Giorgio Corte, Marco Frascio, Carlotta Gozzer, Gianfranco D. Gaetani, Alessandro Morelli, Lorenzo Minchiotti, Antonio De Flora, Cristina Mareni, Bruno Curti

Publikováno v: Biochimica et Biophysica Acta (BBA) - General Subjects. 500:109-123

Two sensitive radioimmunoassays, based on a double-antibody technique, were developed which allow detection of nanogram amounts of glucose-6-phosphate dehydrogenase (EC 1.1.1.49) and of a so far unknown NADP(H)-binding protein present in human erythr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28729165f560b81fb59186ae6c381143
https://doi.org/10.1016/0304-4165(77)90051-4

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Modification of arginyl residues in ferredoxin-NADP+ reductase from spinach leaves

Autor: Giuliana Zanetti, Gianattilio Sacchi, Carlotta Gozzer, Bruno Curti

Publikováno v: Biochimica et biophysica acta. 568(1)

Reaction of spinach leaves ferredoxin-NADP+ reductase (NADPH:ferredoxin oxidoreductase, EC 1.6.7.1) with alpha-dicarbonyl compounds results in a biphasic loss of activity. The rapid phase yields modified enzyme with about 30% of the original activity

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e61a09ce78edcd1d93a7f0f47896645
https://pubmed.ncbi.nlm.nih.gov/444539

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Molecular heterogeneity of ferredoxin-NADP+ reductase from spinach leaves

Autor: Monica Galliano, Giuliana Zanetti, Carlotta Gozzer, Bruno Curti, G.A. Sacchi, Lorenzo Minchiotti

Publikováno v: Biochimica et biophysica acta. 485(2)

Ferredoxin-NADP+ reductase (NADPH: ferredoxin oxidoreductase, EC 1.6.7.1) from spinach leaves has been purified according to a new procedure. The enzyme shows the presence of five molecular forms as identified by isoelectric focusing, namely a, b, c,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7038d8906722e64e0ab48d198e365ce9
https://pubmed.ncbi.nlm.nih.gov/922016

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