{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,14]],"date-time":"2026-05-14T20:33:49Z","timestamp":1778790829333,"version":"3.51.4"},"reference-count":38,"publisher":"Elsevier BV","issue":"6","license":[{"start":{"date-parts":[[2013,12,1]],"date-time":"2013-12-01T00:00:00Z","timestamp":1385856000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Obesity Research &amp; Clinical Practice"],"published-print":{"date-parts":[[2013,12]]},"DOI":"10.1016\/j.orcp.2012.07.007","type":"journal-article","created":{"date-parts":[[2012,8,28]],"date-time":"2012-08-28T19:31:09Z","timestamp":1346182269000},"page":"e487-e493","source":"Crossref","is-referenced-by-count":15,"title":["Xanthine derivatives as activators of alpha-amylase: Hypothesis on a link with the hyperglycemia induced by caffeine"],"prefix":"10.1016","volume":"7","author":[{"given":"Elaheh","family":"Kashani-Amin","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Parichehreh","family":"Yaghmaei","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bagher","family":"Larijani","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Azadeh","family":"Ebrahim-Habibi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.orcp.2012.07.007_bib0005","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1042\/bst0260198","article-title":"Structure, function and protein engineering of starch-degrading enzymes","volume":"26","author":"Gottschalk","year":"1998","journal-title":"Biochem Soc Trans"},{"key":"10.1016\/j.orcp.2012.07.007_bib0010","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1042\/bj2800051","article-title":"Comparison of the domain-level organization of starch hydrolases related enzymes","volume":"280","author":"Jespersen","year":"1991","journal-title":"J Biochem"},{"key":"10.1016\/j.orcp.2012.07.007_bib0015","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0167-4838(00)00302-2","article-title":"Relationship of sequence and structure to specificity in the [alpha]-amylase family of enzymes","volume":"1546","author":"MacGregor","year":"2001","journal-title":"Biochim Biophys Acta Protein Struct Mol Enzymol"},{"key":"10.1016\/j.orcp.2012.07.007_bib0020","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/0092-8674(80)90125-7","article-title":"Tissue-specific expression of mouse-alpha-amylase genes: nucleotide sequence of isoenzyme mRNAs from pancreas and salivary gland","volume":"21","author":"Hagenbuchle","year":"1980","journal-title":"Cell"},{"key":"10.1016\/j.orcp.2012.07.007_bib0025","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/j.jsb.2010.11.020","article-title":"Structures of human pancreatic alpha-amylase in complex with acarviostatins: implications for drug design against type II diabetes","volume":"174","author":"Shen","year":"2011","journal-title":"J Struct Biol"},{"key":"10.1016\/j.orcp.2012.07.007_bib0030","doi-asserted-by":"crossref","first-page":"3555","DOI":"10.1021\/jm800115x","article-title":"Flavonoids for controlling starch digestion: structural requirements for inhibiting human alpha-amylase","volume":"51","author":"Lo Piparo","year":"2008","journal-title":"J Med Chem"},{"key":"10.1016\/j.orcp.2012.07.007_bib0035","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1002\/cbic.200800547","article-title":"The high resolution NMR, structure of parvulustat (Z-2685) from Streptomyces parvulus FH-1641: comparison with tendamistat from Streptomyces tendae 4158","volume":"10","author":"Rehm","year":"2009","journal-title":"ChemBioChem"},{"issue":"10","key":"10.1016\/j.orcp.2012.07.007_bib0040","doi-asserted-by":"crossref","first-page":"5305","DOI":"10.1021\/jf200180n","article-title":"Inhibition of key digestive enzymes by cocoa extracts and procyanidins","volume":"59","author":"Gu","year":"2011","journal-title":"J Agric Food Chem"},{"key":"10.1016\/j.orcp.2012.07.007_bib0045","doi-asserted-by":"crossref","first-page":"1617","DOI":"10.1007\/s11033-010-0271-3","article-title":"Trans-chalcone: a novel small molecule inhibitor of mammalian alpha-amylase","volume":"38","author":"Najafian","year":"2011","journal-title":"Mol Biol Rep"},{"key":"10.1016\/j.orcp.2012.07.007_bib0050","doi-asserted-by":"crossref","first-page":"1435","DOI":"10.1110\/ps.0202602","article-title":"Structural basis of alpha-amylase activation by chloride","volume":"11","author":"Aghajari","year":"2002","journal-title":"Protein Sci"},{"key":"10.1016\/j.orcp.2012.07.007_bib0055","doi-asserted-by":"crossref","first-page":"743","DOI":"10.1110\/ps.041079305","article-title":"Structural and mechanistic studies of chloride induced activation of human pancreatic alpha-amylase","volume":"14","author":"Maurus","year":"2005","journal-title":"Protein Sci"},{"key":"10.1016\/j.orcp.2012.07.007_bib0060","doi-asserted-by":"crossref","first-page":"3332","DOI":"10.1021\/bi701652t","article-title":"Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity","volume":"47","author":"Maurus","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.orcp.2012.07.007_bib0065","doi-asserted-by":"crossref","first-page":"556","DOI":"10.1016\/j.enzmictec.2005.04.002","article-title":"Activation and stabilization of 10 starch-degrading enzymes by Triton X-100, polyethylene glycols, and polyvinyl alcohols","volume":"37","author":"Yoon","year":"2005","journal-title":"Enzyme Microb Technol"},{"key":"10.1016\/j.orcp.2012.07.007_bib0070","doi-asserted-by":"crossref","first-page":"1152","DOI":"10.1089\/jmf.2010.0194","article-title":"Effect of combination on the antioxidant and inhibitory properties of tropical pepper varieties against alpha-amylase and alpha-glucosidase activities in vitro","volume":"14","author":"Oboh","year":"2011","journal-title":"J Med Food"},{"key":"10.1016\/j.orcp.2012.07.007_bib0075","doi-asserted-by":"crossref","first-page":"3387","DOI":"10.3390\/ijms11093387","article-title":"Inhibitory activities of cyanidin and its glycosides and synergistic effect with acarbose against intestinal alpha-glucosidase and pancreatic alpha-amylase","volume":"11","author":"Akkarachiyasit","year":"2010","journal-title":"Int J Mol Sci"},{"key":"10.1016\/j.orcp.2012.07.007_bib0080","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1186\/1475-2891-10-24","article-title":"A proprietary alpha-amylase inhibitor from white bean (Phaseolus vulgaris): a review of clinical studies on weight loss and glycemic control","volume":"10","author":"Barrett","year":"2011","journal-title":"J Nutr"},{"key":"10.1016\/j.orcp.2012.07.007_bib0085","unstructured":"Najafian M. Investigation of the effect of several natural compounds on activity of alpha-amylase and level of blood sugar in diabetic rats. PhD thesis. Tehran: Science and Research Branch, Azad University; 2010."},{"key":"10.1016\/j.orcp.2012.07.007_bib0090","doi-asserted-by":"crossref","first-page":"1485","DOI":"10.1093\/clinchem\/28.7.1485","article-title":"Hydrolysis by human alpha-amylase of p-nitrophenyloligosaccharides containing four to seven glucose units","volume":"28","author":"David","year":"1982","journal-title":"Clin Chem"},{"key":"10.1016\/j.orcp.2012.07.007_bib0095","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/0076-6879(55)01021-5","article-title":"Amylases, alpha and beta","author":"Bernfeld","year":"1955","journal-title":"Methods Enzymol"},{"key":"10.1016\/j.orcp.2012.07.007_bib0100","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1002\/jcc.21334","article-title":"AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading","volume":"31","author":"Trott","year":"2010","journal-title":"J Comput Chem"},{"key":"10.1016\/j.orcp.2012.07.007_bib0105","doi-asserted-by":"crossref","first-page":"642","DOI":"10.5483\/BMBRep.2004.37.6.642","article-title":"Chemical modification of lysine residues in Bacillus licheniformis alpha-amylase: conversion of an endo-to an exo-type enzyme","volume":"37","author":"Ebrahim-Habibi","year":"2004","journal-title":"J Biochem Mol Biol"},{"key":"10.1016\/j.orcp.2012.07.007_bib0110","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/0003-9861(91)90451-N","article-title":"The pH dependence of the action pattern in porcine pancreatic [alpha]-amylase-catalyzed reaction for maltooligosaccharide substrates","volume":"289","author":"Ishikawa","year":"1991","journal-title":"Arch Biochem Biophys"},{"key":"10.1016\/j.orcp.2012.07.007_bib0115","first-page":"163","article-title":"Mechanism of porcine pancreatic alpha-amylase: inhibition of amylose and maltopentaose hydrolysis by various inhibitors","volume":"57","author":"Desseaux","year":"2002","journal-title":"Biologia (Bratisl)"},{"key":"10.1016\/j.orcp.2012.07.007_bib0120","series-title":"Working with enzymes, current protocols essential laboratory techniques","author":"Skrincosky","year":"2008"},{"key":"10.1016\/j.orcp.2012.07.007_bib0125","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1007\/978-3-642-13443-2_3","article-title":"Pharmacokinetics and metabolism of natural methylxanthines in animal and man","volume":"200","author":"Arnaud","year":"2011","journal-title":"Handb Exp Pharmacol"},{"issue":"13","key":"10.1016\/j.orcp.2012.07.007_bib0130","doi-asserted-by":"crossref","first-page":"1160","DOI":"10.1016\/j.addr.2011.06.015","article-title":"Molecular origins of surfactant-mediated stabilization of protein drugs","volume":"63","author":"Lee","year":"2011","journal-title":"Adv Drug Deliv Rev"},{"key":"10.1016\/j.orcp.2012.07.007_bib0135","doi-asserted-by":"crossref","first-page":"1232","DOI":"10.1016\/j.jmb.2008.09.089","article-title":"Probing the role of aromatic residues at the secondary saccharide-binding sites of human salivary alpha-amylase in substrate hydrolysis and bacterial binding","volume":"384","author":"Ragunath","year":"2008","journal-title":"J Mol Biol"},{"key":"10.1016\/j.orcp.2012.07.007_bib0140","doi-asserted-by":"crossref","first-page":"3101","DOI":"10.1021\/bi902183w","article-title":"X-ray crystallographic analyses of pig pancreatic alpha-amylase with limit dextrin, oligosaccharide, and alpha-cyclodextrin","volume":"49","author":"Larson","year":"2010","journal-title":"Biochemistry"},{"key":"10.1016\/j.orcp.2012.07.007_bib0145","doi-asserted-by":"crossref","first-page":"9099","DOI":"10.1021\/bi0000317","article-title":"Structural analysis of a chimeric bacterial alpha-amylase. High-resolution analysis of native and ligand complexes","volume":"39","author":"Brzozowski","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.orcp.2012.07.007_bib0150","doi-asserted-by":"crossref","first-page":"239","DOI":"10.4158\/EP.13.3.239","article-title":"Exaggeration of postprandial hyperglycemia in patients with type 2 diabetes by administration of caffeine in coffee","volume":"13","author":"Lane","year":"2007","journal-title":"Endocr Pract"},{"key":"10.1016\/j.orcp.2012.07.007_bib0155","doi-asserted-by":"crossref","first-page":"2385","DOI":"10.2337\/dc06-1084","article-title":"Does coffee consumption reduce the risk of type 2 diabetes in individuals with impaired glucose?","volume":"29","author":"Smith","year":"2006","journal-title":"Diabetes Care"},{"key":"10.1016\/j.orcp.2012.07.007_bib0160","doi-asserted-by":"crossref","first-page":"1290","DOI":"10.1139\/H08-123","article-title":"Coffee, glucose homeostasis, and insulin resistance: physiological mechanisms and mediators","volume":"33","author":"Tunnicliffe","year":"2008","journal-title":"Appl Physiol Nutr Metab"},{"key":"10.1016\/j.orcp.2012.07.007_bib0165","doi-asserted-by":"crossref","first-page":"848","DOI":"10.1016\/j.mehy.2004.03.037","article-title":"A chlorogenic acid-induced increase in GLP-1 production may mediate the impact of heavy coffee consumption on diabetes risk","volume":"64","author":"McCarty","year":"2005","journal-title":"Med Hypotheses"},{"key":"10.1016\/j.orcp.2012.07.007_bib0170","doi-asserted-by":"crossref","first-page":"1276","DOI":"10.1093\/jn\/136.5.1276","article-title":"The glucose intolerance induced by caffeinated coffee ingestion is less pronounced than that due to alkaloid caffeine in men","volume":"136","author":"Battram","year":"2006","journal-title":"J Nutr"},{"key":"10.1016\/j.orcp.2012.07.007_bib0175","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1007\/978-3-642-13443-2_21","article-title":"Methylxanthines and human health: epidemiological and experimental evidence","volume":"200","author":"Beaudoin","year":"2011","journal-title":"Handb Exp Pharmacol"},{"key":"10.1016\/j.orcp.2012.07.007_bib0180","doi-asserted-by":"crossref","first-page":"9218","DOI":"10.1021\/jf9017383","article-title":"Kinetic analysis and mechanism on the inhibition of chlorogenic acid and its components against porcine pancreas alpha-amylase isozymes I and II","volume":"57","author":"Narita","year":"2009","journal-title":"J Agric Food Chem"},{"key":"10.1016\/j.orcp.2012.07.007_bib0185","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1002\/hup.1126","article-title":"Caffeine and stress alter salivary alpha-amylase activity in young men","volume":"25","author":"Klein","year":"2010","journal-title":"Hum Psychopharmacol"},{"key":"10.1016\/j.orcp.2012.07.007_bib0190","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1016\/j.psyneuen.2008.12.004","article-title":"Determinants of salivary alpha-amylase in humans and methodological considerations","volume":"34","author":"Rohleder","year":"2009","journal-title":"Psychoneuroendocrinology"}],"container-title":["Obesity Research &amp; Clinical Practice"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1871403X12002311?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1871403X12002311?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,4,28]],"date-time":"2024-04-28T19:39:30Z","timestamp":1714333170000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1871403X12002311"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,12]]},"references-count":38,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2013,12]]}},"alternative-id":["S1871403X12002311"],"URL":"https:\/\/doi.org\/10.1016\/j.orcp.2012.07.007","relation":{},"ISSN":["1871-403X"],"issn-type":[{"value":"1871-403X","type":"print"}],"subject":[],"published":{"date-parts":[[2013,12]]}}}