[ { "key": "I3FSWDSF", "version": 328, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/I3FSWDSF", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/I3FSWDSF", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Courraud et al.", "parsedDate": "2013-12", "numChildren": 0 }, "data": { "key": "I3FSWDSF", "version": 328, "itemType": "journalArticle", "title": "In vitro lipid peroxidation of intestinal bile salt-based nanoemulsions: Potential role of antioxidants", "creators": [ { "creatorType": "author", "firstName": "J", "lastName": "Courraud" }, { "creatorType": "author", "firstName": "C", "lastName": "Charnay" }, { "creatorType": "author", "firstName": "J P", "lastName": "Cristol" }, { "creatorType": "author", "firstName": "J", "lastName": "Berger" }, { "creatorType": "author", "firstName": "S", "lastName": "Avallone" } ], "abstractNote": "Abstract Over the last decades, oxidative stress has been described as a deleterious phenomenon contributing to numerous noncommunicable diseases such as cardiovascular disease, diabetes, and cancers. As many authors ascribed the healthy effect of fruit and vegetable consumption mainly to their antioxidant contents, it has been hypothesized that their protection could occur from the gut. Therefore, the aim of this study was to develop an original and physiological model of nanoemulsions to study lipid peroxidation within the intestine and to assess the properties of potential antioxidants in this setting. Several nanoemulsions were compared in terms of physical characteristics and reactivity to 2,2'-azobis-(2-amidinopropane) hydrochloride (AAPH)-induced oxidation. Formulations included different types of lipids, a detergent (a conjugated bile salt or sodium dodecyl sulfate) and, finally, lipophilic antioxidants. Hemin and myoglobin were also tested as relevant potential oxidants. Fatty acid (FA) peroxidation was monitored by gas chromatography while malondialdehyde and antioxidant contents were measured by HPLC. Investigated nanoemulsions were composed of spherical or cylindrical mixed micelles, the latter being the least resistant to oxidation. In the experimental conditions, AAPH was the only efficient oxidant. Alpha-tocopherol and lutein significantly slowed FA degradation from 4 to 1 μM, respectively. On the contrary, beta-carotene did not show any protective capacity at 4 μM. In conclusion, the tested nanoemulsions were appropriate to assess antioxidant capacity during the intestinal phase of digestion.", "publicationTitle": "Free radical research", "publisher": "", "place": "", "date": "Dec 2013", "volume": "47", "issue": "12", "section": "", "partNumber": "", "partTitle": "", "pages": "1076-1087", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Free Radic. Res.", "DOI": "10.3109/10715762.2013.853877", "citationKey": "", "url": "", "accessDate": "", "PMID": "", "PMCID": "", "ISSN": "1029-2470", "archive": "", "archiveLocation": "", "shortTitle": "In vitro lipid peroxidation of intestinal bile salt-based nanoemulsions", "language": "eng", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 24128050", "tags": [], "collections": [], "relations": {}, "dateAdded": "2013-12-15T22:43:18Z", "dateModified": "2013-12-15T22:43:18Z" } }, { "key": "TF8MXTRB", "version": 328, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/TF8MXTRB", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/TF8MXTRB", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Avallone et al.", "parsedDate": "2008-11", "numChildren": 0 }, "data": { "key": "TF8MXTRB", "version": 328, "itemType": "journalArticle", "title": "Nutritional value of six multi-ingredient sauces from Burkina Faso", "creators": [ { "creatorType": "author", "firstName": "Sylvie", "lastName": "Avallone" }, { "creatorType": "author", "firstName": "T.-W. Estelle", "lastName": "Tiemtore" }, { "creatorType": "author", "firstName": "Claire", "lastName": "Mouquet-Rivier" }, { "creatorType": "author", "firstName": "Serge", "lastName": "Trèche" } ], "abstractNote": "Multi-ingredient sauces (n=36), which are traditionally consumed with dishes containing starch (millet-based-tô, rice), were collected in rural Burkina Faso and analysed for their dry matter (DM), macronutrient (lipids, proteins) and micronutrient (iron, zinc, carotenoids and retinol) contents. DM content varied from 7.8% to 21.8% depending on the sauce. Groundnut sauces had the highest DM content. Protein contents were similar (22.2–32.3 g/100 g DM). The highest lipid contents were found in groundnut sauces (∼45 g/100 g DM). Sauces made from green-leafy vegetables formed a homogeneous group with a high content of retinol activity equivalents (RAE) (p<0.0001) and, to a lesser extent, of iron (p<0.05) compared to the dried okra or groundnut sauces. An isomer of β-carotene was detected in sauces made from green-leafy vegetables. The content of this isomer was strongly correlated with β-carotene content and not with cooking time.", "publicationTitle": "Journal of Food Composition and Analysis", "publisher": "", "place": "", "date": "novembre 2008", "volume": "21", "issue": "7", "section": "", "partNumber": "", "partTitle": "", "pages": "553-558", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "10.1016/j.jfca.2008.04.012", "citationKey": "", "url": "http://www.sciencedirect.com/science/article/pii/S0889157508000720", "accessDate": "2011-09-16T12:38:26Z", "PMID": "", "PMCID": "", "ISSN": "0889-1575", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "ScienceDirect", "callNumber": "", "rights": "", "extra": "", "tags": [ { "tag": "Africa", "type": 1 }, { "tag": "Cooking", "type": 1 }, { "tag": "Iron", "type": 1 }, { "tag": "Provitamins A", "type": 1 }, { "tag": "Sauces", "type": 1 }, { "tag": "Zinc", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2012-10-22T14:06:33Z", "dateModified": "2013-12-14T15:14:55Z" } }, { "key": "UHCF2768", "version": 326, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/UHCF2768", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/UHCF2768", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Lu and Li", "parsedDate": "2008", "numChildren": 0 }, "data": { "key": "UHCF2768", "version": 326, "itemType": "journalArticle", "title": "Carotenoid Metabolism: Biosynthesis, Regulation, and Beyond", "creators": [ { "creatorType": "author", "firstName": "Shan", "lastName": "Lu" }, { "creatorType": "author", "firstName": "Li", "lastName": "Li" } ], "abstractNote": "", "publicationTitle": "Journal of Integrative Plant Biology", "publisher": "", "place": "", "date": "07/2008", "volume": "50", "issue": "7", "section": "", "partNumber": "", "partTitle": "", "pages": "778-785", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "10.1111/j.1744-7909.2008.00708.x", "citationKey": "", "url": "http://doi.wiley.com/10.1111/j.1744-7909.2008.00708.x", "accessDate": "2013-12-14T11:23:31Z", "PMID": "", "PMCID": "", "ISSN": "16729072, 17447909", "archive": "", "archiveLocation": "", "shortTitle": "Carotenoid Metabolism", "language": "", "libraryCatalog": "CrossRef", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2013-12-14T11:23:31Z", "dateModified": "2013-12-14T11:23:31Z" } }, { "key": "FBJ5NTF3", "version": 324, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/FBJ5NTF3", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/FBJ5NTF3", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Fruscione et al.", "parsedDate": "2008-01-04", "numChildren": 0 }, "data": { "key": "FBJ5NTF3", "version": 324, "itemType": "journalArticle", "title": "Differential Role of NADP+ and NADPH in the Activity and Structure of GDP-D-mannose 4,6-Dehydratase from Two Chlorella Viruses", "creators": [ { "creatorType": "author", "firstName": "Floriana", "lastName": "Fruscione" }, { "creatorType": "author", "firstName": "Laura", "lastName": "Sturla" }, { "creatorType": "author", "firstName": "Garry", "lastName": "Duncan" }, { "creatorType": "author", "firstName": "James L. Van", "lastName": "Etten" }, { "creatorType": "author", "firstName": "Paola", "lastName": "Valbuzzi" }, { "creatorType": "author", "firstName": "Antonio De", "lastName": "Flora" }, { "creatorType": "author", "firstName": "Eleonora Di", "lastName": "Zanni" }, { "creatorType": "author", "firstName": "Michela", "lastName": "Tonetti" } ], "abstractNote": "GDP-d-mannose 4,6-dehydratase (GMD) is a key enzyme involved in the synthesis of 6-deoxyhexoses in prokaryotes and eukaryotes. Paramecium bursaria chlorella virus-1 (PBCV-1) encodes a functional GMD, which is unique among characterized GMDs because it also has a strong stereospecific NADPH-dependent reductase activity leading to GDP-d-rhamnose formation (Tonetti, M., Zanardi, D., Gurnon, J., Fruscione, F., Armirotti, A., Damonte, G., Sturla, L., De Flora, A., and Van Etten, J.L. (2003) J. Biol. Chem. 278, 21559–21565). In the present study we characterized a recombinant GMD encoded by another chlorella virus, Acanthocystis turfacea chlorella virus 1 (ATCV-1), demonstrating that it has the expected dehydratase activity. However, it also displayed significant differences when compared with PBCV-1 GMD. In particular, ATCV-1 GMD lacks the reductase activity present in the PBCV-1 enzyme. Using recombinant PBCV-1 and ATCV-1 GMDs, we determined that the enzymatically active proteins contain tightly bound NADPH and that NADPH is essential for maintaining the oligomerization status as well as for the stabilization and function of both enzymes. Phylogenetic analysis indicates that PBCV-1 GMD is the most evolutionary diverged of the GMDs. We conclude that this high degree of divergence was the result of the selection pressures that led to the acquisition of new reductase activity to synthesize GDP-d-rhamnose while maintaining the dehydratase activity in order to continue to synthesize GDP-l-fucose.", "publicationTitle": "Journal of Biological Chemistry", "publisher": "", "place": "", "date": "01/04/2008", "volume": "283", "issue": "1", "section": "", "partNumber": "", "partTitle": "", "pages": "184-193", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "J. Biol. Chem.", "DOI": "10.1074/jbc.M706614200", "citationKey": "", "url": "http://www.jbc.org/content/283/1/184", "accessDate": "2013-10-26T20:20:42Z", "PMID": "", "PMCID": "", "ISSN": "0021-9258, 1083-351X", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "en", "libraryCatalog": "www.jbc.org", "callNumber": "", "rights": "", "extra": "PMID: 17974560", "tags": [], "collections": [], "relations": {}, "dateAdded": "2013-10-26T20:20:42Z", "dateModified": "2013-10-26T20:20:42Z" } }, { "key": "KCMQPMRD", "version": 324, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/KCMQPMRD", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/KCMQPMRD", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Paglia and Valentine", "parsedDate": "1967-07", "numChildren": 0 }, "data": { "key": "KCMQPMRD", "version": 324, "itemType": "journalArticle", "title": "Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase", "creators": [ { "creatorType": "author", "firstName": "D E", "lastName": "Paglia" }, { "creatorType": "author", "firstName": "W N", "lastName": "Valentine" } ], "abstractNote": "", "publicationTitle": "The Journal of laboratory and clinical medicine", "publisher": "", "place": "", "date": "Jul 1967", "volume": "70", "issue": "1", "section": "", "partNumber": "", "partTitle": "", "pages": "158-169", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "J. Lab. Clin. Med.", "DOI": "", "citationKey": "", "url": "", "accessDate": "", "PMID": "", "PMCID": "", "ISSN": "0022-2143", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "eng", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 6066618", "tags": [ { "tag": "Chemical Precipitation", "type": 1 }, { "tag": "Chromatography, Gel", "type": 1 }, { "tag": "Erythrocytes", "type": 1 }, { "tag": "Glutathione", "type": 1 }, { "tag": "Hemoglobins", "type": 1 }, { "tag": "Humans", "type": 1 }, { "tag": "Oxidoreductases", "type": 1 }, { "tag": "Peroxidases", "type": 1 }, { "tag": "Spectrophotometry", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2013-10-26T20:20:27Z", "dateModified": "2013-10-26T20:20:27Z" } }, { "key": "GVEIQPE9", "version": 324, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/GVEIQPE9", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/GVEIQPE9", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Ying", "parsedDate": "2008", "numChildren": 0 }, "data": { "key": "GVEIQPE9", "version": 324, "itemType": "journalArticle", "title": "NAD + /NADH and NADP + /NADPH in Cellular Functions and Cell Death: Regulation and Biological Consequences", "creators": [ { "creatorType": "author", "firstName": "Weihai", "lastName": "Ying" } ], "abstractNote": "", "publicationTitle": "Antioxidants & Redox Signaling", "publisher": "", "place": "", "date": "02/2008", "volume": "10", "issue": "2", "section": "", "partNumber": "", "partTitle": "", "pages": "179-206", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "10.1089/ars.2007.1672", "citationKey": "", "url": "http://online.liebertpub.com/doi/abs/10.1089/ars.2007.1672", "accessDate": "2013-10-26T20:15:56Z", "PMID": "", "PMCID": "", "ISSN": "1523-0864, 1557-7716", "archive": "", "archiveLocation": "", "shortTitle": "NAD + /NADH and NADP + /NADPH in Cellular Functions and Cell Death", "language": "", "libraryCatalog": "CrossRef", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2013-10-26T20:15:56Z", "dateModified": "2013-10-26T20:15:56Z" } }, { "key": "97K8J6KS", "version": 324, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/97K8J6KS", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/97K8J6KS", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Bergmeyer", "parsedDate": "1975-11", "numChildren": 0 }, "data": { "key": "97K8J6KS", "version": 324, "itemType": "journalArticle", "title": "[New values for the molar extinction coefficients of NADH and NADPH for the use in routine laboratories (author's transl)]", "creators": [ { "creatorType": "author", "firstName": "H U", "lastName": "Bergmeyer" } ], "abstractNote": "Extensive re-investigations with regard to the molar extinction coefficients of NADH and NADPH proved that in future, calculations in routine work can be performed with the following much more accurate epsilon-values: 6.15 x 10(3) 1 x mol-1 x cm-1 at Hg 334 nm (NADH and NADPH), 6.3 X 10(3) 1 X mol-1 x cm-1 at 340 nm (NADH and NADPH), 3.4 X 10(3) 1 X mol-1 X Cm-1 (NADH) and 3.5 x 10(3) 1 x mol-1 x cm-1 (NADPH) at Hg 365 nm, respectively. The safest measurement is performed at Hg 334 nm, because here epsilon is identical for both coenzymes and deviations of the epsilon-value caused by temperature, pH and ionic strength are less than 0.5%.", "publicationTitle": "Zeitschrift für klinische Chemie und klinische Biochemie", "publisher": "", "place": "", "date": "Nov 1975", "volume": "13", "issue": "11", "section": "", "partNumber": "", "partTitle": "", "pages": "507-508", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Z Klin Chem Klin Biochem", "DOI": "", "citationKey": "", "url": "", "accessDate": "", "PMID": "", "PMCID": "", "ISSN": "0044-2933", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "ger", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 3038", "tags": [ { "tag": "Colorimetry", "type": 1 }, { "tag": "Hydrogen-Ion Concentration", "type": 1 }, { "tag": "NAD", "type": 1 }, { "tag": "NADP", "type": 1 }, { "tag": "Quality Control", "type": 1 }, { "tag": "Temperature", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2013-10-26T20:14:46Z", "dateModified": "2013-10-26T20:14:46Z" } }, { "key": "J6HA7FH8", "version": 324, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/J6HA7FH8", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/J6HA7FH8", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Gupta and Baquer", "parsedDate": "1998-12", "numChildren": 0 }, "data": { "key": "J6HA7FH8", "version": 324, "itemType": "journalArticle", "title": "Hexokinase, glucose-6-phosphate dehydrogenase and antioxidant enzymes in diabetic reticulocytes: effects of insulin and vanadate", "creators": [ { "creatorType": "author", "firstName": "B L", "lastName": "Gupta" }, { "creatorType": "author", "firstName": "N Z", "lastName": "Baquer" } ], "abstractNote": "Experimentally induced diabetic rats were treated separately with insulin and vanadate. The activities of hexokinase (HK) and glucose-6-phosphate dehydrogenase (G-6PDH) were increased in reticulocyte hemolysate isolated from the diabetic rats and were restored to normal levels by insulin. The restoration was not detected in vanadate treated diabetic animals. The enzymes of glutathione metabolism namely glutathione peroxidase (GPx), glutathione reductase (GR) and glutathione-s-transferase (GST) exhibited increases in their activities with diabetes and were restored to almost control values by insulin treatment. Vanadate given to diabetic animals further increased GPx, and GST. The level of superoxide dismutase(SOD) decreased in the reticulocytes of diabetic rats and catalase (CAT) was unchanged. Both CAT and SOD had normal values when the diabetic rats were treated with insulin and vanadate. It is proposed that vanadate may cause an increase in the activity of GR which may stimulate glucose transporters and glucose metabolism.", "publicationTitle": "Biochemistry and molecular biology international", "publisher": "", "place": "", "date": "Dec 1998", "volume": "46", "issue": "6", "section": "", "partNumber": "", "partTitle": "", "pages": "1145-1152", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Biochem. Mol. Biol. Int.", "DOI": "", "citationKey": "", "url": "", "accessDate": "", "PMID": "", "PMCID": "", "ISSN": "1039-9712", "archive": "", "archiveLocation": "", "shortTitle": "Hexokinase, glucose-6-phosphate dehydrogenase and antioxidant enzymes in diabetic reticulocytes", "language": "eng", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 9891847", "tags": [ { "tag": "Catalase", "type": 1 }, { "tag": "Diabetes Mellitus, Experimental", "type": 1 }, { "tag": "Glucosephosphate Dehydrogenase", "type": 1 }, { "tag": "Glutathione Transferase", "type": 1 }, { "tag": "Glutathione peroxidase", "type": 1 }, { "tag": "Insulin", "type": 1 }, { "tag": "Male", "type": 1 }, { "tag": "Peroxidases", "type": 1 }, { "tag": "Rats", "type": 1 }, { "tag": "Rats, Wistar", "type": 1 }, { "tag": "Reference Values", "type": 1 }, { "tag": "Reticulocytes", "type": 1 }, { "tag": "Superoxide dismutase", "type": 1 }, { "tag": "Vanadates", "type": 1 }, { "tag": "animals", "type": 1 }, { "tag": "glutathione reductase", "type": 1 }, { "tag": "hexokinase", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2013-10-26T20:12:09Z", "dateModified": "2013-10-26T20:12:09Z" } }, { "key": "8GSA25TE", "version": 324, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/8GSA25TE", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/8GSA25TE", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Mannervik", "parsedDate": "1985", "numChildren": 0 }, "data": { "key": "8GSA25TE", "version": 324, "itemType": "journalArticle", "title": "Glutathione peroxidase", "creators": [ { "creatorType": "author", "firstName": "Bengt", "lastName": "Mannervik" }, { "creatorType": "editor", "name": "Alton Meister" } ], "abstractNote": "Publisher Summary\nGlutathione peroxidases catalyze the reduction of hydroperoxides (ROOH) by glutathione (GSH). “R” may be an aliphatic or aromatic organic group or, simply, hydrogen. The products are H2O, an alcohol (ROH), and glutathione disulfide (GSSG). Regeneration of GSH from GSSG in the cell is effected by the enzyme glutathione reductase. Assays of glutathione peroxidase activity are based on the measurement of ROOH or GSH consumption. Alternatively, GSSG production is monitored by coupling to the reaction catalyzed by glutathione reductase. Oxidation of NADPH is recorded spectrophotometrically or fluorometrically. This chapter provides an overview of the assay methods of glutathione peroxidase enzyme. There are two major types of glutathione peroxidase. One type is distinguished by containing selenium in the form of covalently bound selenocysteine in its active site. This selenium-dependent enzyme is active with both organic hydroperoxides and H202. The second type of glutathione peroxidase consists of proteins that do not depend on selenium for catalysis and have negligible activity with H202. This class is constituted by glutathione transferases.", "publicationTitle": "Methods in Enzymology", "publisher": "", "place": "", "date": "1985", "volume": "113", "issue": "", "section": "", "partNumber": "", "partTitle": "", "pages": "490-495", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "", "citationKey": "", "url": "http://www.sciencedirect.com/science/article/pii/S0076687985130636", "accessDate": "2013-10-26T20:08:19Z", "PMID": "", "PMCID": "", "ISSN": "", "archive": "", "archiveLocation": "", "shortTitle": "Glutamate, Glutamine, Glutathione, and Related Compounds", "language": "", "libraryCatalog": "ScienceDirect", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2013-10-26T20:08:19Z", "dateModified": "2013-10-26T20:09:19Z" } }, { "key": "DAJUIA7I", "version": 324, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/DAJUIA7I", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/DAJUIA7I", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Racker", "parsedDate": "1955-12-01", "numChildren": 0 }, "data": { "key": "DAJUIA7I", "version": 324, "itemType": "journalArticle", "title": "Glutathione Reductase from Bakers' Yeast and Beef Liver", "creators": [ { "creatorType": "author", "firstName": "E.", "lastName": "Racker" } ], "abstractNote": "", "publicationTitle": "Journal of Biological Chemistry", "publisher": "", "place": "", "date": "12/01/1955", "volume": "217", "issue": "2", "section": "", "partNumber": "", "partTitle": "", "pages": "855-866", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "J. Biol. Chem.", "DOI": "", "citationKey": "", "url": "http://www.jbc.org/content/217/2/855", "accessDate": "2013-10-26T20:01:19Z", "PMID": "", "PMCID": "", "ISSN": "0021-9258, 1083-351X", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "en", "libraryCatalog": "www.jbc.org", "callNumber": "", "rights": "", "extra": "PMID: 13271446", "tags": [], "collections": [], "relations": {}, "dateAdded": "2013-10-26T20:01:19Z", "dateModified": "2013-10-26T20:01:19Z" } }, { "key": "3GCI3D7F", "version": 324, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/3GCI3D7F", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/3GCI3D7F", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Carlberg and Mannervik", "parsedDate": "1975-07-25", "numChildren": 0 }, "data": { "key": "3GCI3D7F", "version": 324, "itemType": "journalArticle", "title": "Purification and characterization of the flavoenzyme glutathione reductase from rat liver.", "creators": [ { "creatorType": "author", "firstName": "I.", "lastName": "Carlberg" }, { "creatorType": "author", "firstName": "B.", "lastName": "Mannervik" } ], "abstractNote": "Glutathione reductase from rat liver has been purified greater than 5000-fold in a yield of 20%. The molecular weights of the enzyme and its subunits were estimated to be 125,000 and 60,000, respectively, indicating that the native enzyme is a dimer. The enzyme molecular contains 2 FAD molecules, which are reducible by NADPH, GSH or dithioerythritol. The reduced flavin is instantaneously reoxidized by addition of GSSG. The steady state kinetic data are consistent with a branching reaction mechanism previously proposed for glutathione reductase from yeast (MANNERVIK, B. (1973) Biochem. Biophy. Res. Commun. 53, 1151-1158). This mechanism is also favored by the nonlinear inhibition pattern produced by NADP-+. However, at low GSSG concentrations the rate equation can be approximated by that of a simple ping pong mechanism. NADPH and the mixed disulfide of coenzyme A and GSH were about 10% as active as NADPH and GSSG, respectively, whereas some sulfenyl derivatives related to GSSG were less active as substrates. The pH activity profiles of these substrates differed from that of the NADPH-GSSG substrate pair.", "publicationTitle": "Journal of Biological Chemistry", "publisher": "", "place": "", "date": "07/25/1975", "volume": "250", "issue": "14", "section": "", "partNumber": "", "partTitle": "", "pages": "5475-5480", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "J. Biol. Chem.", "DOI": "", "citationKey": "", "url": "http://www.jbc.org/content/250/14/5475", "accessDate": "2013-10-26T19:57:59Z", "PMID": "", "PMCID": "", "ISSN": "0021-9258, 1083-351X", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "en", "libraryCatalog": "www.jbc.org", "callNumber": "", "rights": "", "extra": "PMID: 237922", "tags": [], "collections": [], "relations": {}, "dateAdded": "2013-10-26T19:57:59Z", "dateModified": "2013-10-26T19:57:59Z" } }, { "key": "2DVFHNDA", "version": 324, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/2DVFHNDA", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/2DVFHNDA", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Katayama et al.", "parsedDate": "2007", "numChildren": 0 }, "data": { "key": "2DVFHNDA", "version": 324, "itemType": "journalArticle", "title": "Oligophosphopeptides Derived from Egg Yolk Phosvitin Up-regulate γ-Glutamylcysteine Synthetase and Antioxidant Enzymes against Oxidative Stress in Caco-2 Cells", "creators": [ { "creatorType": "author", "firstName": "Shigeru", "lastName": "Katayama" }, { "creatorType": "author", "firstName": "Shin-ichi", "lastName": "Ishikawa" }, { "creatorType": "author", "firstName": "Ming Z.", "lastName": "Fan" }, { "creatorType": "author", "firstName": "Yoshinori", "lastName": "Mine" } ], "abstractNote": "", "publicationTitle": "Journal of Agricultural and Food Chemistry", "publisher": "", "place": "", "date": "04/2007", "volume": "55", "issue": "8", "section": "", "partNumber": "", "partTitle": "", "pages": "2829-2835", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "10.1021/jf0628936", "citationKey": "", "url": "http://pubs.acs.org/doi/abs/10.1021/jf0628936", "accessDate": "2013-10-26T19:53:45Z", "PMID": "", "PMCID": "", "ISSN": "0021-8561, 1520-5118", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "CrossRef", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2013-10-26T19:53:45Z", "dateModified": "2013-10-26T19:53:45Z" } }, { "key": "8TJ8HR22", "version": 324, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/8TJ8HR22", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/8TJ8HR22", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Mavis and Stellwagen", "parsedDate": "1968-02-25", "numChildren": 0 }, "data": { "key": "8TJ8HR22", "version": 324, "itemType": "journalArticle", "title": "Purification and Subunit Structure of Glutathione Reductase from Bakers' Yeast", "creators": [ { "creatorType": "author", "firstName": "Richard D.", "lastName": "Mavis" }, { "creatorType": "author", "firstName": "Earle", "lastName": "Stellwagen" } ], "abstractNote": "A scheme has been devised for the purification of glutathione reductase from bakers' yeast. The purified protein is homogeneous with respect to chromatographic, electrophoretic, and sedimentation criteria. A molecular weight of 1.24 ± 0.05 x 105 was calculated for the protein from sedimentation equilibrium and osmotic pressure measurements. In the presence of 5 m guanidine hydrochloride, the molecular weight is reduced to 5.15 ± 0.3 x 104 calculated from sedimentation equilibrium experiments, assuming no preferential interaction with the solvent, or to 5.60 x 104 calculated from osmotic pressure measurements. These values indicate that the native protein contains two polypeptide chains. The dissociated polypeptide chains appear identical with respect to net charge and molecular size. The native enzyme was found to contain 2 moles of FAD per mole of protein. Both FAD moieties can be separated from the dissociated protein by dialysis or electrophoresis, indicating that FAD is attached to the native protein by noncovalent bonds.", "publicationTitle": "Journal of Biological Chemistry", "publisher": "", "place": "", "date": "02/25/1968", "volume": "243", "issue": "4", "section": "", "partNumber": "", "partTitle": "", "pages": "809-814", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "J. Biol. Chem.", "DOI": "", "citationKey": "", "url": "http://www.jbc.org/content/243/4/809", "accessDate": "2013-10-26T19:44:06Z", "PMID": "", "PMCID": "", "ISSN": "0021-9258, 1083-351X", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "en", "libraryCatalog": "www.jbc.org", "callNumber": "", "rights": "", "extra": "PMID: 5638597", "tags": [], "collections": [], "relations": {}, "dateAdded": "2013-10-26T19:44:06Z", "dateModified": "2013-10-26T19:44:06Z" } }, { "key": "P9TQ7VWS", "version": 324, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/P9TQ7VWS", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/P9TQ7VWS", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Commission Européenne", "parsedDate": "2010", "numChildren": 0 }, "data": { "key": "P9TQ7VWS", "version": 324, "itemType": "report", "title": "Liste et description des méthodes d'analyses visées à l'article 120 octies, premier alinéa, du règlement (CE) n°1234/2007 du Conseil", "creators": [ { "creatorType": "author", "firstName": "", "lastName": "Commission Européenne" } ], "abstractNote": "", "reportNumber": "", "reportType": "", "institution": "", "place": "", "date": "2010", "seriesTitle": "Journal officiel de l’Union européenne", "seriesNumber": "", "pages": "C 43/1-C 43/60", "DOI": "", "ISBN": "", "citationKey": "", "url": "http://eur-lex.europa.eu/LexUriServ/LexUriServ.do?uri=OJ:C:2010:043:0001:0060:FR:PDF", "accessDate": "2013-10-26T19:28:05Z", "ISSN": "", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2013-10-26T19:27:14Z", "dateModified": "2013-10-26T19:33:37Z" } }, { "key": "JQ4NI7J2", "version": 324, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/JQ4NI7J2", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/JQ4NI7J2", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Hewitt and Dickes", "parsedDate": "1961-02", "numChildren": 0 }, "data": { "key": "JQ4NI7J2", "version": 324, "itemType": "journalArticle", "title": "Spectrophotometric measurements on ascorbic acid and their use for the estimation of ascorbic acid and dehydroascorbic acid in plant tissues.", "creators": [ { "creatorType": "author", "firstName": "E. J.", "lastName": "Hewitt" }, { "creatorType": "author", "firstName": "G. J.", "lastName": "Dickes" } ], "abstractNote": "", "publicationTitle": "The Biochemical journal", "publisher": "", "place": "", "date": "1961 Feb", "volume": "78", "issue": "", "section": "", "partNumber": "", "partTitle": "", "pages": "384-391", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "", "citationKey": "", "url": "", "accessDate": "", "PMID": "", "PMCID": "", "ISSN": "0264-6021", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "ISI Web of Knowledge", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2012-10-22T14:06:33Z", "dateModified": "2013-10-26T19:11:55Z" } }, { "key": "XZX7H9A4", "version": 324, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/XZX7H9A4", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/XZX7H9A4", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Hu et al.", "parsedDate": "2008-01-08", "numChildren": 0 }, "data": { "key": "XZX7H9A4", "version": 324, "itemType": "journalArticle", "title": "The N-end rule pathway is a sensor of heme", "creators": [ { "creatorType": "author", "firstName": "Rong-Gui", "lastName": "Hu" }, { "creatorType": "author", "firstName": "Haiqing", "lastName": "Wang" }, { "creatorType": "author", "firstName": "Zanxian", "lastName": "Xia" }, { "creatorType": "author", "firstName": "Alexander", "lastName": "Varshavsky" } ], "abstractNote": "The conjugation of arginine, by arginyl-transferase, to N-terminal aspartate, glutamate or oxidized cysteine is a part of the N-end rule pathway of protein degradation. We report that arginyl-transferase of either the mouse or the yeast Saccharomyces cerevisiae is inhibited by hemin (Fe3+-heme). Furthermore, we show that hemin inhibits arginyl-transferase through a redox mechanism that involves the formation of disulfide between the enzyme's Cys-71 and Cys-72 residues. Remarkably, hemin also induces the proteasome-dependent degradation of arginyl-transferase in vivo, thus acting as both a “stoichiometric” and “catalytic” down-regulator of the N-end rule pathway. In addition, hemin was found to interact with the yeast and mouse E3 ubiquitin ligases of the N-end rule pathway. One of substrate-binding sites of the yeast N-end rule's ubiquitin ligase UBR1 targets CUP9, a transcriptional repressor. This site of UBR1 is autoinhibited but can be allosterically activated by peptides that bear destabilizing N-terminal residues and interact with two other substrate-binding sites of UBR1. We show that hemin does not directly occlude the substrate-binding sites of UBR1 but blocks the activation of its CUP9-binding site by dipeptides. The N-end rule pathway, a known sensor of short peptides, nitric oxide, and oxygen, is now a sensor of heme as well. One function of the N-end rule pathway may be to coordinate the activities of small effectors, both reacting to and controlling the redox dynamics of heme, oxygen, nitric oxide, thiols, and other compounds, in part through conditional degradation of specific transcription factors and G protein regulators.", "publicationTitle": "Proceedings of the National Academy of Sciences", "publisher": "", "place": "", "date": "01/08/2008", "volume": "105", "issue": "1", "section": "", "partNumber": "", "partTitle": "", "pages": "76-81", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "PNAS", "DOI": "10.1073/pnas.0710568105", "citationKey": "", "url": "http://www.pnas.org/content/105/1/76/suppl/DC1", "accessDate": "2013-10-26T19:02:14Z", "PMID": "", "PMCID": "", "ISSN": "0027-8424, 1091-6490", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "en", "libraryCatalog": "www.pnas.org", "callNumber": "", "rights": "", "extra": "PMID: 18162538", "tags": [ { "tag": "ATE1", "type": 1 }, { "tag": "UBR1", "type": 1 }, { "tag": "arginylation", "type": 1 }, { "tag": "ubiquitin", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2013-10-26T19:02:14Z", "dateModified": "2013-10-26T19:07:50Z" } }, { "key": "6XIGK73V", "version": 324, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/6XIGK73V", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/6XIGK73V", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Carlberg and Mannervik", "parsedDate": "1985", "numChildren": 0 }, "data": { "key": "6XIGK73V", "version": 324, "itemType": "journalArticle", "title": "Glutathione reductase", "creators": [ { "creatorType": "author", "firstName": "Inger", "lastName": "Carlberg" }, { "creatorType": "author", "firstName": "Bengt", "lastName": "Mannervik" }, { "creatorType": "editor", "name": "Alton Meister" } ], "abstractNote": "Publisher Summary\nGlutathione reductase is a flavoprotein catalyzing the NADPH-dependent reduction of glutathione disulfide (GSSG) to glutathione (GSH). The reaction is essential for the maintenance of glutathione levels. Glutathione has a major role as a reductant in oxidation–reduction processes, and serves in detoxication and several other cellular functions of great importance. A purification method of this enzyme from calf liver and rat liver is described in this chapter. Similar methods are used for the purification of the enzyme from yeast, porcine, and human erythrocytes. All the steps are carried out at about 5°. The purification method from calf liver consists of various steps including preparation of cytosol fraction, chromatography on DEAE-sephadex, precipitation with ammonium sulfate, and chromatography on hydroxyapatite. The purification of glutathione reductase from rat liver is usually combined with the preparation of glutathione transferases, thioltransferase, and glyoxalase I.", "publicationTitle": "Methods in Enzymology", "publisher": "", "place": "", "date": "1985", "volume": "113", "issue": "", "section": "", "partNumber": "", "partTitle": "", "pages": "484-490", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "", "citationKey": "", "url": "http://www.sciencedirect.com/science/article/pii/S0076687985130624", "accessDate": "2013-10-26T18:35:20Z", "PMID": "", "PMCID": "", "ISSN": "", "archive": "", "archiveLocation": "", "shortTitle": "Glutamate, Glutamine, Glutathione, and Related Compounds", "language": "", "libraryCatalog": "ScienceDirect", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2013-10-26T18:35:20Z", "dateModified": "2013-10-26T18:36:14Z" } }, { "key": "IRI6ZAPC", "version": 324, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/IRI6ZAPC", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/IRI6ZAPC", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Katayama and Mine", "parsedDate": "2007", "numChildren": 0 }, "data": { "key": "IRI6ZAPC", "version": 324, "itemType": "journalArticle", "title": "Antioxidative Activity of Amino Acids on Tissue Oxidative Stress in Human Intestinal Epithelial Cell Model", "creators": [ { "creatorType": "author", "firstName": "Shigeru", "lastName": "Katayama" }, { "creatorType": "author", "firstName": "Yoshinori", "lastName": "Mine" } ], "abstractNote": "", "publicationTitle": "Journal of Agricultural and Food Chemistry", "publisher": "", "place": "", "date": "10/2007", "volume": "55", "issue": "21", "section": "", "partNumber": "", "partTitle": "", "pages": "8458-8464", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "10.1021/jf070866p", "citationKey": "", "url": "http://pubs.acs.org/doi/abs/10.1021/jf070866p", "accessDate": "2013-10-26T18:29:22Z", "PMID": "", "PMCID": "", "ISSN": "0021-8561, 1520-5118", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "CrossRef", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2013-10-26T18:29:22Z", "dateModified": "2013-10-26T18:29:22Z" } }, { "key": "DD8GC6QM", "version": 324, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/DD8GC6QM", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/DD8GC6QM", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Precourt et al.", "parsedDate": "2012-09-01", "numChildren": 0 }, "data": { "key": "DD8GC6QM", "version": 324, "itemType": "journalArticle", "title": "Antioxidative properties of paraoxonase 2 in intestinal epithelial cells", "creators": [ { "creatorType": "author", "firstName": "Louis-Philippe", "lastName": "Precourt" }, { "creatorType": "author", "firstName": "Valerie", "lastName": "Marcil" }, { "creatorType": "author", "firstName": "Thierry", "lastName": "Ntimbane" }, { "creatorType": "author", "firstName": "Rame", "lastName": "Taha" }, { "creatorType": "author", "firstName": "Jean-Claude", "lastName": "Lavoie" }, { "creatorType": "author", "firstName": "Edgard", "lastName": "Delvin" }, { "creatorType": "author", "firstName": "Ernest G.", "lastName": "Seidman" }, { "creatorType": "author", "firstName": "Jean-Francois", "lastName": "Beaulieu" }, { "creatorType": "author", "firstName": "Emile", "lastName": "Levy" } ], "abstractNote": "Paraoxonase (PON) family members seem central to a wide variety of human illnesses, but appreciation of their antioxidative function in the gastrointestinal tract is in its infancy. The major objective of the present work is to highlight the role of the ubiquitously expressed PON2 in the small intestine. With use of pLKO lentiviral vector containing short hairpin RNA (shRNA) lentivirus, PON2 expression was knocked down in intestinal Caco-2/15 cells, where antioxidative status, lipid peroxidation, and degree of inflammation were evaluated. As a consequence of PON2 inactivation in the epithelial cells, we observed 1) imbalanced primary and secondary antioxidative responses, characterized by increased superoxide dismutases and decreased catalase, 2) high concentrations of H2O2 and malondialdehyde, along with low glutathione-to-glutathione disulfide ratio, 3) upregulation of TNF-α, IL-6, and monocyte chemoattractant protein-1 gene expression after induction of oxidative stress, and 4) raised level of the activation of transcription factor NF-κB, which was likely implicated in exacerbation of the inflammatory activation. These results suggest that PON2 is involved in the antioxidative and anti-inflammatory response in intestinal epithelial cells.", "publicationTitle": "American Journal of Physiology - Gastrointestinal and Liver Physiology", "publisher": "", "place": "", "date": "2012-9-1", "volume": "303", "issue": "5", "section": "", "partNumber": "", "partTitle": "", "pages": "G623-G634", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Am J Physiol Gastrointest Liver Physiol", "DOI": "10.1152/ajpgi.00039.2012", "citationKey": "", "url": "http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3468556/", "accessDate": "2013-10-26T18:24:25Z", "PMID": "", "PMCID": "", "ISSN": "0193-1857", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "PubMed Central", "callNumber": "", "rights": "", "extra": "PMID: 22744335\nPMCID: PMC3468556", "tags": [], "collections": [], "relations": {}, "dateAdded": "2013-10-26T18:24:25Z", "dateModified": "2013-10-26T18:26:41Z" } }, { "key": "84PHNPFT", "version": 324, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/84PHNPFT", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/84PHNPFT", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Forman et al.", "parsedDate": "2013", "numChildren": 0 }, "data": { "key": "84PHNPFT", "version": 324, "itemType": "journalArticle", "title": "How do nutritional antioxidants really work: Nucleophilic tone and para-hormesis versus free radical scavenging in vivo", "creators": [ { "creatorType": "author", "firstName": "Henry J.", "lastName": "Forman" }, { "creatorType": "author", "firstName": "Kelvin J.A.", "lastName": "Davies" }, { "creatorType": "author", "firstName": "Fulvio", "lastName": "Ursini" } ], "abstractNote": "Abstract \nWe present arguments for an evolution in our understanding of how antioxidants in fruits and vegetables exert their health-protective effects. There is much epidemiological evidence for disease prevention by dietary antioxidants and chemical evidence that such compounds react in one-electron reactions with free radicals in vitro. Nonetheless, kinetic constraints indicate that in vivo scavenging of radicals is ineffective in antioxidant defense. Instead, enzymatic removal of nonradical electrophiles, such as hydroperoxides, in two-electron redox reactions is the major antioxidant mechanism. Furthermore, we propose that a major mechanism of action for nutritional antioxidants is the paradoxical oxidative activation of the Nrf2 (NF-E2-related factor 2) signaling pathway, which maintains protective oxidoreductases and their nucleophilic substrates. This maintenance of “nucleophilic tone,” by a mechanism that can be called “para-hormesis,” provides a means for regulating physiological nontoxic concentrations of the nonradical oxidant electrophiles that boost antioxidant enzymes, and damage removal and repair systems (for proteins, lipids, and DNA), at the optimal levels consistent with good health.", "publicationTitle": "Free Radical Biology and Medicine", "publisher": "", "place": "", "date": "2013", "volume": "", "issue": "", "section": "", "partNumber": "", "partTitle": "", "pages": ", In Press", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "10.1016/j.freeradbiomed.2013.05.045", "citationKey": "", "url": "http://www.sciencedirect.com/science/article/pii/S0891584913002736", "accessDate": "2013-08-27T20:31:01Z", "PMID": "", "PMCID": "", "ISSN": "0891-5849", "archive": "", "archiveLocation": "", "shortTitle": "How do nutritional antioxidants really work", "language": "", "libraryCatalog": "ScienceDirect", "callNumber": "", "rights": "", "extra": "", "tags": [ { "tag": "Antioxidants", "type": 1 }, { "tag": "Glutathione", "type": 1 }, { "tag": "Keap1/Nrf2", "type": 1 }, { "tag": "Nucleophilic tone", "type": 1 }, { "tag": "Peroxidases", "type": 1 }, { "tag": "Redox signaling", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2013-08-27T20:31:01Z", "dateModified": "2013-10-23T21:50:42Z" } }, { "key": "5G95CAFE", "version": 324, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/5G95CAFE", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/5G95CAFE", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Forman et al.", "parsedDate": "2013-06-06", "numChildren": 0 }, "data": { "key": "5G95CAFE", "version": 324, "itemType": "journalArticle", "title": "How do nutritional antioxidants really work: Nucleophilic tone and para-hormesis versus free radical scavenging in vivo", "creators": [ { "creatorType": "author", "firstName": "Henry J", "lastName": "Forman" }, { "creatorType": "author", "firstName": "Kelvin J A", "lastName": "Davies" }, { "creatorType": "author", "firstName": "Fulvio", "lastName": "Ursini" } ], "abstractNote": "We present arguments for an evolution in our understanding of how antioxidants in fruits and vegetables exert their health-protective effects. There is much epidemiological evidence for disease prevention by dietary antioxidants and chemical evidence that such compounds react in one-electron reactions with free radicals in vitro. Nonetheless, kinetic constraints indicate that in vivo scavenging of radicals is ineffective in antioxidant defense. Instead, enzymatic removal of nonradical electrophiles, such as hydroperoxides, in two-electron redox reactions is the major antioxidant mechanism. Furthermore, we propose that a major mechanism of action for nutritional antioxidants is the paradoxical oxidative activation of the Nrf2 (NF-E2-related factor 2) signaling pathway, which maintains protective oxidoreductases and their nucleophilic substrates. This maintenance of \"nucleophilic tone,\" by a mechanism that can be called \"para-hormesis,\" provides a means for regulating physiological nontoxic concentrations of the nonradical oxidant electrophiles that boost antioxidant enzymes, and damage removal and repair systems (for proteins, lipids, and DNA), at the optimal levels consistent with good health.", "publicationTitle": "Free radical biology & medicine", "publisher": "", "place": "", "date": "Jun 6, 2013", "volume": "", "issue": "", "section": "", "partNumber": "", "partTitle": "", "pages": "", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Free Radic. Biol. Med.", "DOI": "10.1016/j.freeradbiomed.2013.05.045", "citationKey": "", "url": "", "accessDate": "", "PMID": "", "PMCID": "", "ISSN": "1873-4596", "archive": "", "archiveLocation": "", "shortTitle": "How do nutritional antioxidants really work", "language": "ENG", "libraryCatalog": "NCBI PubMed", "callNumber": "", "rights": "", "extra": "PMID: 23747930", "tags": [], "collections": [], "relations": {}, "dateAdded": "2013-10-23T21:50:11Z", "dateModified": "2013-10-23T21:50:11Z" } }, { "key": "F9WMN8PZ", "version": 324, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/F9WMN8PZ", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/F9WMN8PZ", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "numChildren": 0 }, "data": { "key": "F9WMN8PZ", "version": 324, "itemType": "webpage", "title": "Grooveshark - Listen to Free Music Online - Internet Radio - Free MP3 Streaming", "creators": [], "abstractNote": "Grooveshark is free music, online radio, and so much more. Enjoy unlimited free music streaming with a worldwide community of artists and music lovers.", "websiteTitle": "Grooveshark", "websiteType": "", "date": "", "publisher": "", "place": "", "DOI": "", "citationKey": "", "url": "http://grooveshark.com/", "accessDate": "2013-10-23T19:36:44Z", "shortTitle": "", "language": "", "rights": "", "extra": "", "tags": [ { "tag": "free mp3", "type": 1 }, { "tag": "free music", "type": 1 }, { "tag": "free songs", "type": 1 }, { "tag": "internet radio", "type": 1 }, { "tag": "music", "type": 1 }, { "tag": "music songs", "type": 1 }, { "tag": "music videos", "type": 1 }, { "tag": "musica", "type": 1 }, { "tag": "online radio", "type": 1 }, { "tag": "radio", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2013-10-23T19:36:44Z", "dateModified": "2013-10-23T19:36:44Z" } }, { "key": "N3TFNRP3", "version": 322, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/N3TFNRP3", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/N3TFNRP3", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Backhed et al.", "parsedDate": "2005-03-25", "numChildren": 0 }, "data": { "key": "N3TFNRP3", "version": 322, "itemType": "journalArticle", "title": "Host-bacterial mutualism in the human intestine", "creators": [ { "creatorType": "author", "firstName": "F.", "lastName": "Backhed" }, { "creatorType": "author", "firstName": "R. E.", "lastName": "Ley" }, { "creatorType": "author", "firstName": "J. L.", "lastName": "Sonnenburg" }, { "creatorType": "author", "firstName": "D. A.", "lastName": "Peterson" }, { "creatorType": "author", "firstName": "J. I.", "lastName": "Gordon" } ], "abstractNote": "The distal human intestine represents an anaerobic bioreactor programmed with an enormous population of bacteria, dominated by relatively few divisions that are highly diverse at the strain/subspecies level. This microbiota and its collective genomes (microbiome) provide us with genetic and metabolic attributes we have not been required to evolve on our own, including the ability to harvest otherwise inaccessible nutrients. New studies are revealing how the gut microbiota has co-evolved with us and how it manipulates and complements our biology in ways that are mutually beneficial. We are also starting to understand how certain keystone members of the microbiota operate to maintain the stability and functional adaptability of this microbial organ.", "publicationTitle": "Science", "publisher": "", "place": "", "date": "MAR 25 2005", "volume": "307", "issue": "5717", "section": "", "partNumber": "", "partTitle": "", "pages": "1915-1920", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "Science", "DOI": "10.1126/science.1104816", "citationKey": "", "url": "", "accessDate": "", "PMID": "", "PMCID": "", "ISSN": "0036-8075", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "English", "libraryCatalog": "ISI Web of Knowledge", "callNumber": "", "rights": "", "extra": "WOS:000227957300045", "tags": [ { "tag": "anaerobic-bacteria", "type": 1 }, { "tag": "bacteroides-thetaiotaomicron", "type": 1 }, { "tag": "cell-surface", "type": 1 }, { "tag": "communities", "type": 1 }, { "tag": "diversity", "type": 1 }, { "tag": "environments", "type": 1 }, { "tag": "extensive dna inversions", "type": 1 }, { "tag": "gene-expression", "type": 1 }, { "tag": "gut", "type": 1 }, { "tag": "human feces", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2013-10-21T23:48:03Z", "dateModified": "2013-10-21T23:48:03Z" } }, { "key": "GVBVBPG9", "version": 322, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/GVBVBPG9", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/GVBVBPG9", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Ruel and Alderman", "parsedDate": "2013", "numChildren": 0 }, "data": { "key": "GVBVBPG9", "version": 322, "itemType": "journalArticle", "title": "Nutrition-sensitive interventions and programmes: how can they help to accelerate progress in improving maternal and child nutrition?", "creators": [ { "creatorType": "author", "firstName": "Marie T", "lastName": "Ruel" }, { "creatorType": "author", "firstName": "Harold", "lastName": "Alderman" } ], "abstractNote": "Summary\nAcceleration of progress in nutrition will require effective, large-scale nutrition-sensitive programmes that address key underlying determinants of nutrition and enhance the coverage and effectiveness of nutrition-specific interventions. We reviewed evidence of nutritional effects of programmes in four sectors—agriculture, social safety nets, early child development, and schooling. The need for investments to boost agricultural production, keep prices low, and increase incomes is undisputable; targeted agricultural programmes can complement these investments by supporting livelihoods, enhancing access to diverse diets in poor populations, and fostering women's empowerment. However, evidence of the nutritional effect of agricultural programmes is inconclusive—except for vitamin A from biofortification of orange sweet potatoes—largely because of poor quality evaluations. Social safety nets currently provide cash or food transfers to a billion poor people and victims of shocks (eg, natural disasters). Individual studies show some effects on younger children exposed for longer durations, but weaknesses in nutrition goals and actions, and poor service quality probably explain the scarcity of overall nutritional benefits. Combined early child development and nutrition interventions show promising additive or synergistic effects on child development—and in some cases nutrition—and could lead to substantial gains in cost, efficiency, and effectiveness, but these programmes have yet to be tested at scale. Parental schooling is strongly associated with child nutrition, and the effectiveness of emerging school nutrition education programmes needs to be tested. Many of the programmes reviewed were not originally designed to improve nutrition yet have great potential to do so. Ways to enhance programme nutrition-sensitivity include: improve targeting; use conditions to stimulate participation; strengthen nutrition goals and actions; and optimise women's nutrition, time, physical and mental health, and empowerment. Nutrition-sensitive programmes can help scale up nutrition-specific interventions and create a stimulating environment in which young children can grow and develop to their full potential.", "publicationTitle": "The Lancet", "publisher": "", "place": "", "date": "2013", "volume": "382", "issue": "9891", "section": "", "partNumber": "", "partTitle": "", "pages": "536-551", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "The Lancet", "DOI": "10.1016/S0140-6736(13)60843-0", "citationKey": "", "url": "http://www.sciencedirect.com/science/article/pii/S0140673613608430", "accessDate": "2013-10-21T19:32:18Z", "PMID": "", "PMCID": "", "ISSN": "0140-6736", "archive": "", "archiveLocation": "", "shortTitle": "Nutrition-sensitive interventions and programmes", "language": "", "libraryCatalog": "ScienceDirect", "callNumber": "", "rights": "", "extra": "", "tags": [], "collections": [], "relations": {}, "dateAdded": "2013-10-21T19:32:18Z", "dateModified": "2013-10-21T20:14:04Z" } }, { "key": "X938T68T", "version": 322, "library": { "type": "group", "id": 100183, "name": "Nutrition PhD Julie Courraud 2013", "links": { "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013", "type": "text/html" } } }, "links": { "self": { "href": "https://api.zotero.org/groups/100183/items/X938T68T", "type": "application/json" }, "alternate": { "href": "https://www.zotero.org/groups/nutrition_phd_julie_courraud_2013/items/X938T68T", "type": "text/html" } }, "meta": { "createdByUser": { "id": 603999, "username": "Althalis", "name": "Julie Courraud", "links": { "alternate": { "href": "https://www.zotero.org/althalis", "type": "text/html" } } }, "creatorSummary": "Hotz et al.", "parsedDate": "2012", "numChildren": 0 }, "data": { "key": "X938T68T", "version": 322, "itemType": "journalArticle", "title": "A large-scale intervention to introduce orange sweet potato in rural Mozambique increases vitamin A intakes among children and women", "creators": [ { "creatorType": "author", "firstName": "Christine", "lastName": "Hotz" }, { "creatorType": "author", "firstName": "Cornelia", "lastName": "Loechl" }, { "creatorType": "author", "firstName": "Alan", "lastName": "de Brauw" }, { "creatorType": "author", "firstName": "Patrick", "lastName": "Eozenou" }, { "creatorType": "author", "firstName": "Daniel", "lastName": "Gilligan" }, { "creatorType": "author", "firstName": "Mourad", "lastName": "Moursi" }, { "creatorType": "author", "firstName": "Bernardino", "lastName": "Munhaua" }, { "creatorType": "author", "firstName": "Paul", "lastName": "van Jaarsveld" }, { "creatorType": "author", "firstName": "Alicia", "lastName": "Carriquiry" }, { "creatorType": "author", "firstName": "J. V.", "lastName": "Meenakshi" } ], "abstractNote": "β-Carotene-rich orange sweet potato (OSP) has been shown to improve vitamin A status of infants and young children in controlled efficacy trials and in a small-scale effectiveness study with intensive exposure to project inputs. However, the potential of this important food crop to reduce the risk of vitamin A deficiency in deficient populations will depend on the ability to distribute OSP vines and promote its household production and consumption on a large scale. In rural Mozambique, we conducted a randomised, controlled effectiveness study of a large-scale intervention to promote household-level OSP production and consumption using integrated agricultural, demand creation/behaviour change and marketing components. The following two intervention models were compared: a low-intensity (1 year) and a high-intensity (nearly 3 years) training model. The primary nutrition outcomes were OSP and vitamin A intakes by children 6–35 months and 3–5·5 years of age, and women. The intervention resulted in significant net increases in OSP intakes (model 1: 46, 48 and 97 g/d) and vitamin A intakes (model 1: 263, 254 and 492 μg retinol activity equivalents/d) among the younger children, older children and women, respectively. OSP accounted for 47–60 % of all sweet potato consumed and, among reference children, provided 80 % of total vitamin A intakes. A similar magnitude of impact was observed for both models, suggesting that group-level trainings in nutrition and agriculture could be limited to the first project year without compromising impact. Introduction of OSP to rural, sweet potato-producing communities in Mozambique is an effective way to improve vitamin A intakes.", "publicationTitle": "British Journal of Nutrition", "publisher": "", "place": "", "date": "2012", "volume": "108", "issue": "01", "section": "", "partNumber": "", "partTitle": "", "pages": "163-176", "series": "", "seriesTitle": "", "seriesText": "", "journalAbbreviation": "", "DOI": "10.1017/S0007114511005174", "citationKey": "", "url": "", "accessDate": "", "PMID": "", "PMCID": "", "ISSN": "", "archive": "", "archiveLocation": "", "shortTitle": "", "language": "", "libraryCatalog": "Cambridge Journals Online", "callNumber": "", "rights": "", "extra": "", "tags": [ { "tag": "Mozambique", "type": 1 }, { "tag": "Orange sweet potato", "type": 1 }, { "tag": "Randomised effectiveness studies", "type": 1 }, { "tag": "Vitamin A", "type": 1 } ], "collections": [], "relations": {}, "dateAdded": "2013-10-21T19:59:57Z", "dateModified": "2013-10-21T19:59:57Z" } } ]