Sulforafano (Italian Wikipedia)

Analysis of information sources in references of the Wikipedia article "Sulforafano" in Italian language version.

refsWebsite

Global rank Italian rank

24nih.gov

4^th place

9^th place

24doi.org

2^nd place

7^th place

1sciencemag.org

857^th place

540^th place

1aspetjournals.org

6,663^rd place

5,217^th place

aspetjournals.org

jpet.aspetjournals.org

(EN) Rong Hu, Vidya Hebbar e Bok-Ryang Kim, In Vivo Pharmacokinetics and Regulation of Gene Expression Profiles by Isothiocyanate Sulforaphane in the Rat, in Journal of Pharmacology and Experimental Therapeutics, vol. 310, n. 1, 1º luglio 2004, pp. 263-271, DOI:10.1124/jpet.103.064261. URL consultato il 16 giugno 2017.

doi.org

dx.doi.org

Nathan V. Matusheski, Ranjan Swarup e John A. Juvik, Epithiospecifier protein from broccoli (Brassica oleracea L. ssp. italica) inhibits formation of the anticancer agent sulforaphane, in Journal of Agricultural and Food Chemistry, vol. 54, n. 6, 22 marzo 2006, pp. 2069-2076, DOI:10.1021/jf0525277. URL consultato il 16 giugno 2017.
Nathan V. Matusheski, John A. Juvik e Elizabeth H. Jeffery, Heating decreases epithiospecifier protein activity and increases sulforaphane formation in broccoli, in Phytochemistry, vol. 65, n. 9, May 2004, pp. 1273-1281, DOI:10.1016/j.phytochem.2004.04.013. URL consultato il 16 giugno 2017.
Shikha Saha, Wendy Hollands e Birgit Teucher, Isothiocyanate concentrations and interconversion of sulforaphane to erucin in human subjects after consumption of commercial frozen broccoli compared to fresh broccoli, in Molecular Nutrition & Food Research, vol. 56, n. 12, December 2012, pp. 1906-1916, DOI:10.1002/mnfr.201200225. URL consultato il 16 giugno 2017.
Ahmad F. Abdull Razis, Natalya Hanlon e Ewa Soltys, The naturally occurring aliphatic isothiocyanates sulforaphane and erucin are weak agonists but potent non-competitive antagonists of the aryl hydrocarbon receptor, in Archives of Toxicology, vol. 86, n. 10, October 2012, pp. 1505-1514, DOI:10.1007/s00204-012-0875-6. URL consultato il 16 giugno 2017.
D. Kalpana Deepa Priya, R. Gayathri e D. Sakthisekaran, Role of sulforaphane in the anti-initiating mechanism of lung carcinogenesis in vivo by modulating the metabolic activation and detoxification of benzo(a)pyrene, in Biomedicine & Pharmacotherapy = Biomedecine & Pharmacotherapie, vol. 65, n. 1, February 2011, pp. 9-16, DOI:10.1016/j.biopha.2010.08.009. URL consultato il 16 giugno 2017.
Nanqin Gan, Yu-Chieh Wu e Mathilde Brunet, Sulforaphane activates heat shock response and enhances proteasome activity through up-regulation of Hsp27, in The Journal of Biological Chemistry, vol. 285, n. 46, 12 novembre 2010, pp. 35528-35536, DOI:10.1074/jbc.M110.152686. URL consultato il 16 giugno 2017.
Mi-Kyoung Kwak, Nobunao Wakabayashi e Jennifer L. Greenlaw, Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway, in Molecular and Cellular Biology, vol. 23, n. 23, December 2003, pp. 8786-8794, DOI:10.1128/MCB.23.23.8786-8794.2003. URL consultato il 16 giugno 2017.
Young-Sam Keum, Regulation of the Keap1/Nrf2 system by chemopreventive sulforaphane: implications of posttranslational modifications, in Annals of the New York Academy of Sciences, vol. 1229, July 2011, pp. 184-189, DOI:10.1111/j.1749-6632.2011.06092.x. URL consultato il 16 giugno 2017.
Mandeep Pinky Gaidhu, Sergiu Fediuc e Rolando Bacis Ceddia, 5-Aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside-induced AMP-activated protein kinase phosphorylation inhibits basal and insulin-stimulated glucose uptake, lipid synthesis, and fatty acid oxidation in isolated rat adipocytes, in The Journal of Biological Chemistry, vol. 281, n. 36, 8 settembre 2006, pp. 25956-25964, DOI:10.1074/jbc.M602992200. URL consultato il 16 giugno 2017.
Ju-Hee Lee, Myung-Hee Moon e Jae-Kyo Jeong, Sulforaphane induced adipolysis via hormone sensitive lipase activation, regulated by AMPK signaling pathway, in Biochemical and Biophysical Research Communications, vol. 426, n. 4, 5 ottobre 2012, pp. 492-497, DOI:10.1016/j.bbrc.2012.08.107. URL consultato il 16 giugno 2017.
Emilie E. Vomhof-DeKrey e Matthew J. Picklo, NAD(P)H:quinone oxidoreductase 1 activity reduces hypertrophy in 3T3-L1 adipocytes, in Free Radical Biology & Medicine, vol. 53, n. 4, 15 agosto 2012, pp. 690-700, DOI:10.1016/j.freeradbiomed.2012.05.047. URL consultato il 16 giugno 2017.
(EN) Annika S. Axelsson, Emily Tubbs e Brig Mecham, Sulforaphane reduces hepatic glucose production and improves glucose control in patients with type 2 diabetes, in Science Translational Medicine, vol. 9, n. 394, 14 giugno 2017, pp. eaah4477, DOI:10.1126/scitranslmed.aah4477. URL consultato il 16 giugno 2017.
Carolina Guerini de Souza, José Augusto Sattler e Adriano Martimbianco de Assis, Metabolic effects of sulforaphane oral treatment in streptozotocin-diabetic rats, in Journal of Medicinal Food, vol. 15, n. 9, September 2012, pp. 795-801, DOI:10.1089/jmf.2012.0016. URL consultato il 16 giugno 2017.
E. Heiss, C. Herhaus e K. Klimo, Nuclear factor kappa B is a molecular target for sulforaphane-mediated anti-inflammatory mechanisms, in The Journal of Biological Chemistry, vol. 276, n. 34, 24 agosto 2001, pp. 32008-32015, DOI:10.1074/jbc.M104794200. URL consultato il 16 giugno 2017.
Elke Heiss e Clarissa Gerhäuser, Time-dependent modulation of thioredoxin reductase activity might contribute to sulforaphane-mediated inhibition of NF-kappaB binding to DNA, in Antioxidants & Redox Signaling, vol. 7, n. 11-12, November 2005, pp. 1601-1611, DOI:10.1089/ars.2005.7.1601. URL consultato il 16 giugno 2017.
Athanassios Fragoulis, Jendrik Laufs e Susanna Müller, Sulforaphane has opposing effects on TNF-alpha stimulated and unstimulated synoviocytes, in Arthritis Research & Therapy, vol. 14, n. 5, 27 ottobre 2012, pp. R220, DOI:10.1186/ar4059. URL consultato il 16 giugno 2017.
Melinda C. Myzak, P. Andrew Karplus e Fung-Lung Chung, A novel mechanism of chemoprotection by sulforaphane: inhibition of histone deacetylase, in Cancer Research, vol. 64, n. 16, 15 agosto 2004, pp. 5767-5774, DOI:10.1158/0008-5472.CAN-04-1326. URL consultato il 16 giugno 2017.
Yanxi Pei, Bo Wu e Qiuhui Cao, Hydrogen sulfide mediates the anti-survival effect of sulforaphane on human prostate cancer cells, in Toxicology and Applied Pharmacology, vol. 257, n. 3, 15 dicembre 2011, pp. 420-428, DOI:10.1016/j.taap.2011.09.026. URL consultato il 16 giugno 2017.
Su-Hyeong Kim e Shivendra V. Singh, D,L-Sulforaphane causes transcriptional repression of androgen receptor in human prostate cancer cells, in Molecular Cancer Therapeutics, vol. 8, n. 7, July 2009, pp. 1946-1954, DOI:10.1158/1535-7163.MCT-09-0104. URL consultato il 16 giugno 2017.
Eun-Ryeong Hahm, Kumar Chandra-Kuntal e Dhimant Desai, Notch activation is dispensable for D, L-sulforaphane-mediated inhibition of human prostate cancer cell migration, in PloS One, vol. 7, n. 9, 2012, pp. e44957, DOI:10.1371/journal.pone.0044957. URL consultato il 16 giugno 2017.
Wenpeng Cui, Yang Bai e Xiao Miao, Prevention of diabetic nephropathy by sulforaphane: possible role of Nrf2 upregulation and activation, in Oxidative Medicine and Cellular Longevity, vol. 2012, 2012, p. 821936, DOI:10.1155/2012/821936. URL consultato il 16 giugno 2017.
Young Woon Chang, Jae Young Jang e Yong Ho Kim, The Effects of Broccoli Sprout Extract Containing Sulforaphane on Lipid Peroxidation and Helicobacter pylori Infection in the Gastric Mucosa, in Gut and Liver, vol. 9, n. 4, July 2015, pp. 486-493, DOI:10.5009/gnl14040. URL consultato il 16 giugno 2017.
C. C. Conaway, S. M. Getahun e L. L. Liebes, Disposition of glucosinolates and sulforaphane in humans after ingestion of steamed and fresh broccoli, in Nutrition and Cancer, vol. 38, n. 2, 2000, pp. 168-178, DOI:10.1207/S15327914NC382_5. URL consultato il 16 giugno 2017.
(EN) Rong Hu, Vidya Hebbar e Bok-Ryang Kim, In Vivo Pharmacokinetics and Regulation of Gene Expression Profiles by Isothiocyanate Sulforaphane in the Rat, in Journal of Pharmacology and Experimental Therapeutics, vol. 310, n. 1, 1º luglio 2004, pp. 263-271, DOI:10.1124/jpet.103.064261. URL consultato il 16 giugno 2017.

nih.gov

ncbi.nlm.nih.gov

Nathan V. Matusheski, Ranjan Swarup e John A. Juvik, Epithiospecifier protein from broccoli (Brassica oleracea L. ssp. italica) inhibits formation of the anticancer agent sulforaphane, in Journal of Agricultural and Food Chemistry, vol. 54, n. 6, 22 marzo 2006, pp. 2069-2076, DOI:10.1021/jf0525277. URL consultato il 16 giugno 2017.
Nathan V. Matusheski, John A. Juvik e Elizabeth H. Jeffery, Heating decreases epithiospecifier protein activity and increases sulforaphane formation in broccoli, in Phytochemistry, vol. 65, n. 9, May 2004, pp. 1273-1281, DOI:10.1016/j.phytochem.2004.04.013. URL consultato il 16 giugno 2017.
Shikha Saha, Wendy Hollands e Birgit Teucher, Isothiocyanate concentrations and interconversion of sulforaphane to erucin in human subjects after consumption of commercial frozen broccoli compared to fresh broccoli, in Molecular Nutrition & Food Research, vol. 56, n. 12, December 2012, pp. 1906-1916, DOI:10.1002/mnfr.201200225. URL consultato il 16 giugno 2017.
Ahmad F. Abdull Razis, Natalya Hanlon e Ewa Soltys, The naturally occurring aliphatic isothiocyanates sulforaphane and erucin are weak agonists but potent non-competitive antagonists of the aryl hydrocarbon receptor, in Archives of Toxicology, vol. 86, n. 10, October 2012, pp. 1505-1514, DOI:10.1007/s00204-012-0875-6. URL consultato il 16 giugno 2017.
D. Kalpana Deepa Priya, R. Gayathri e D. Sakthisekaran, Role of sulforaphane in the anti-initiating mechanism of lung carcinogenesis in vivo by modulating the metabolic activation and detoxification of benzo(a)pyrene, in Biomedicine & Pharmacotherapy = Biomedecine & Pharmacotherapie, vol. 65, n. 1, February 2011, pp. 9-16, DOI:10.1016/j.biopha.2010.08.009. URL consultato il 16 giugno 2017.
Nanqin Gan, Yu-Chieh Wu e Mathilde Brunet, Sulforaphane activates heat shock response and enhances proteasome activity through up-regulation of Hsp27, in The Journal of Biological Chemistry, vol. 285, n. 46, 12 novembre 2010, pp. 35528-35536, DOI:10.1074/jbc.M110.152686. URL consultato il 16 giugno 2017.
Mi-Kyoung Kwak, Nobunao Wakabayashi e Jennifer L. Greenlaw, Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway, in Molecular and Cellular Biology, vol. 23, n. 23, December 2003, pp. 8786-8794, DOI:10.1128/MCB.23.23.8786-8794.2003. URL consultato il 16 giugno 2017.
E. R. Stadtman, Protein oxidation and aging, in Science (New York, N.Y.), vol. 257, n. 5074, 28 agosto 1992, pp. 1220-1224. URL consultato il 16 giugno 2017.
Young-Sam Keum, Regulation of the Keap1/Nrf2 system by chemopreventive sulforaphane: implications of posttranslational modifications, in Annals of the New York Academy of Sciences, vol. 1229, July 2011, pp. 184-189, DOI:10.1111/j.1749-6632.2011.06092.x. URL consultato il 16 giugno 2017.
Mandeep Pinky Gaidhu, Sergiu Fediuc e Rolando Bacis Ceddia, 5-Aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside-induced AMP-activated protein kinase phosphorylation inhibits basal and insulin-stimulated glucose uptake, lipid synthesis, and fatty acid oxidation in isolated rat adipocytes, in The Journal of Biological Chemistry, vol. 281, n. 36, 8 settembre 2006, pp. 25956-25964, DOI:10.1074/jbc.M602992200. URL consultato il 16 giugno 2017.
Ju-Hee Lee, Myung-Hee Moon e Jae-Kyo Jeong, Sulforaphane induced adipolysis via hormone sensitive lipase activation, regulated by AMPK signaling pathway, in Biochemical and Biophysical Research Communications, vol. 426, n. 4, 5 ottobre 2012, pp. 492-497, DOI:10.1016/j.bbrc.2012.08.107. URL consultato il 16 giugno 2017.
Emilie E. Vomhof-DeKrey e Matthew J. Picklo, NAD(P)H:quinone oxidoreductase 1 activity reduces hypertrophy in 3T3-L1 adipocytes, in Free Radical Biology & Medicine, vol. 53, n. 4, 15 agosto 2012, pp. 690-700, DOI:10.1016/j.freeradbiomed.2012.05.047. URL consultato il 16 giugno 2017.
Carolina Guerini de Souza, José Augusto Sattler e Adriano Martimbianco de Assis, Metabolic effects of sulforaphane oral treatment in streptozotocin-diabetic rats, in Journal of Medicinal Food, vol. 15, n. 9, September 2012, pp. 795-801, DOI:10.1089/jmf.2012.0016. URL consultato il 16 giugno 2017.
E. Heiss, C. Herhaus e K. Klimo, Nuclear factor kappa B is a molecular target for sulforaphane-mediated anti-inflammatory mechanisms, in The Journal of Biological Chemistry, vol. 276, n. 34, 24 agosto 2001, pp. 32008-32015, DOI:10.1074/jbc.M104794200. URL consultato il 16 giugno 2017.
Elke Heiss e Clarissa Gerhäuser, Time-dependent modulation of thioredoxin reductase activity might contribute to sulforaphane-mediated inhibition of NF-kappaB binding to DNA, in Antioxidants & Redox Signaling, vol. 7, n. 11-12, November 2005, pp. 1601-1611, DOI:10.1089/ars.2005.7.1601. URL consultato il 16 giugno 2017.
Athanassios Fragoulis, Jendrik Laufs e Susanna Müller, Sulforaphane has opposing effects on TNF-alpha stimulated and unstimulated synoviocytes, in Arthritis Research & Therapy, vol. 14, n. 5, 27 ottobre 2012, pp. R220, DOI:10.1186/ar4059. URL consultato il 16 giugno 2017.
Melinda C. Myzak, P. Andrew Karplus e Fung-Lung Chung, A novel mechanism of chemoprotection by sulforaphane: inhibition of histone deacetylase, in Cancer Research, vol. 64, n. 16, 15 agosto 2004, pp. 5767-5774, DOI:10.1158/0008-5472.CAN-04-1326. URL consultato il 16 giugno 2017.
Yanxi Pei, Bo Wu e Qiuhui Cao, Hydrogen sulfide mediates the anti-survival effect of sulforaphane on human prostate cancer cells, in Toxicology and Applied Pharmacology, vol. 257, n. 3, 15 dicembre 2011, pp. 420-428, DOI:10.1016/j.taap.2011.09.026. URL consultato il 16 giugno 2017.
Su-Hyeong Kim e Shivendra V. Singh, D,L-Sulforaphane causes transcriptional repression of androgen receptor in human prostate cancer cells, in Molecular Cancer Therapeutics, vol. 8, n. 7, July 2009, pp. 1946-1954, DOI:10.1158/1535-7163.MCT-09-0104. URL consultato il 16 giugno 2017.
Eun-Ryeong Hahm, Kumar Chandra-Kuntal e Dhimant Desai, Notch activation is dispensable for D, L-sulforaphane-mediated inhibition of human prostate cancer cell migration, in PloS One, vol. 7, n. 9, 2012, pp. e44957, DOI:10.1371/journal.pone.0044957. URL consultato il 16 giugno 2017.
Wenpeng Cui, Yang Bai e Xiao Miao, Prevention of diabetic nephropathy by sulforaphane: possible role of Nrf2 upregulation and activation, in Oxidative Medicine and Cellular Longevity, vol. 2012, 2012, p. 821936, DOI:10.1155/2012/821936. URL consultato il 16 giugno 2017.
Young Woon Chang, Jae Young Jang e Yong Ho Kim, The Effects of Broccoli Sprout Extract Containing Sulforaphane on Lipid Peroxidation and Helicobacter pylori Infection in the Gastric Mucosa, in Gut and Liver, vol. 9, n. 4, July 2015, pp. 486-493, DOI:10.5009/gnl14040. URL consultato il 16 giugno 2017.
C. C. Conaway, S. M. Getahun e L. L. Liebes, Disposition of glucosinolates and sulforaphane in humans after ingestion of steamed and fresh broccoli, in Nutrition and Cancer, vol. 38, n. 2, 2000, pp. 168-178, DOI:10.1207/S15327914NC382_5. URL consultato il 16 giugno 2017.
Yuesheng Zhang e Eileen C. Callaway, High cellular accumulation of sulphoraphane, a dietary anticarcinogen, is followed by rapid transporter-mediated export as a glutathione conjugate, in The Biochemical Journal, vol. 364, Pt 1, 15 maggio 2002, pp. 301-307. URL consultato il 16 giugno 2017.

sciencemag.org

stm.sciencemag.org

(EN) Annika S. Axelsson, Emily Tubbs e Brig Mecham, Sulforaphane reduces hepatic glucose production and improves glucose control in patients with type 2 diabetes, in Science Translational Medicine, vol. 9, n. 394, 14 giugno 2017, pp. eaah4477, DOI:10.1126/scitranslmed.aah4477. URL consultato il 16 giugno 2017.