{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,1]],"date-time":"2026-11-01T03:57:41Z","timestamp":1793505461808,"version":"4.5.0"},"reference-count":133,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,8,1]],"date-time":"2025-08-01T00:00:00Z","timestamp":1754006400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,8,1]],"date-time":"2025-08-01T00:00:00Z","timestamp":1754006400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,8,1]],"date-time":"2025-08-01T00:00:00Z","timestamp":1754006400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,8,1]],"date-time":"2025-08-01T00:00:00Z","timestamp":1754006400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,8,1]],"date-time":"2025-08-01T00:00:00Z","timestamp":1754006400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,8,1]],"date-time":"2025-08-01T00:00:00Z","timestamp":1754006400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,8,1]],"date-time":"2025-08-01T00:00:00Z","timestamp":1754006400000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100020923","name":"I. K. Gujral Punjab Technical University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100020923","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100020921","name":"ISF College of Pharmacy","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100020921","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Bioorganic Chemistry"],"published-print":{"date-parts":[[2025,8]]},"DOI":"10.1016\/j.bioorg.2025.108762","type":"journal-article","created":{"date-parts":[[2025,7,18]],"date-time":"2025-07-18T23:06:38Z","timestamp":1752879998000},"page":"108762","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":45,"special_numbering":"C","title":["Dual \u03b1-amylase and \u03b1-glucosidase inhibitors: recent progress from natural and synthetic resources"],"prefix":"10.1016","volume":"163","author":[{"given":"Ritesh","family":"Jha","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kamya","family":"Goyal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sidharth","family":"Mehan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gurpreet","family":"Singh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bioorg.2025.108762_bb0005","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/j.diabres.2018.02.023","article-title":"IDF diabetes atlas: global estimates of diabetes prevalence for 2017 and projections for 2045","volume":"138","author":"Cho","year":"2018","journal-title":"Diabetes Res. Clin. Pract."},{"issue":"11","key":"10.1016\/j.bioorg.2025.108762_bb0010","doi-asserted-by":"crossref","first-page":"1987","DOI":"10.2337\/dc16-0614","article-title":"Risk of cause-specific death in individuals with diabetes: a competing risks analysis","volume":"39","author":"Baena-D\u00edez","year":"2016","journal-title":"Diabetes Care"},{"issue":"7","key":"10.1016\/j.bioorg.2025.108762_bb0015","doi-asserted-by":"crossref","first-page":"1335","DOI":"10.2337\/dc09-9032","article-title":"Hyperglycemic crises in adult patients with diabetes","volume":"32","author":"Kitabchi","year":"2009","journal-title":"Diabetes Care"},{"issue":"7","key":"10.1016\/j.bioorg.2025.108762_bb0020","doi-asserted-by":"crossref","first-page":"1167","DOI":"10.2337\/diacare.21.7.1167","article-title":"Effects of diabetes and level of glycemia on all-cause and cardiovascular mortality: the San Antonio heart study","volume":"21","author":"Wei","year":"1998","journal-title":"Diabetes Care"},{"issue":"4","key":"10.1016\/j.bioorg.2025.108762_bb0025","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1172\/JCI10762","article-title":"Insulin resistance and cardiovascular disease","volume":"106","author":"Ginsberg","year":"2000","journal-title":"J. Clin. Invest."},{"issue":"6865","key":"10.1016\/j.bioorg.2025.108762_bb0030","doi-asserted-by":"crossref","first-page":"813","DOI":"10.1038\/414813a","article-title":"Biochemistry and molecular cell biology of diabetic complications","volume":"414","author":"Brownlee","year":"2001","journal-title":"Nature"},{"issue":"14","key":"10.1016\/j.bioorg.2025.108762_bb0035","doi-asserted-by":"crossref","first-page":"977","DOI":"10.1056\/NEJM199309303291401","article-title":"The effect of intensive treatment of diabetes on the development and progression of long-term complications in insulin-dependent diabetes mellitus","volume":"329","author":"Control D, Group CTR","year":"1993","journal-title":"N. Engl. J. Med."},{"issue":"9131","key":"10.1016\/j.bioorg.2025.108762_bb0040","doi-asserted-by":"crossref","first-page":"837","DOI":"10.1016\/S0140-6736(98)07019-6","article-title":"Intensive blood-glucose control with sulphonylureas or insulin compared with conventional treatment and risk of complications in patients with type 2 diabetes (UKPDS 33)","volume":"352","author":"Group UPDS","year":"1998","journal-title":"Lancet"},{"issue":"1","key":"10.1016\/j.bioorg.2025.108762_bb0045","doi-asserted-by":"crossref","first-page":"3","DOI":"10.4103\/2468-8827.184853","article-title":"WHO global report on diabetes: a summary","volume":"1","author":"Roglic","year":"2016","journal-title":"Int. J. Noncommunicable Dis."},{"key":"10.1016\/j.bioorg.2025.108762_bb0050","series-title":"Global Report on Diabetes","author":"Organization WH","year":"2016"},{"issue":"10467","key":"10.1016\/j.bioorg.2025.108762_bb0055","doi-asserted-by":"crossref","first-page":"2077","DOI":"10.1016\/S0140-6736(24)02317-1","article-title":"Worldwide trends in diabetes prevalence and treatment from 1990 to 2022: a pooled analysis of 1108 population-representative studies with 141 million participants","volume":"404","author":"Zhou","year":"2024","journal-title":"Lancet"},{"issue":"1","key":"10.1016\/j.bioorg.2025.108762_bb0060","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1016\/j.diabres.2009.10.007","article-title":"Global estimates of the prevalence of diabetes for 2010 and 2030","volume":"87","author":"Shaw","year":"2010","journal-title":"Diabetes Res. Clin. Pract."},{"issue":"3","key":"10.1016\/j.bioorg.2025.108762_bb0065","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1016\/j.diabres.2011.10.029","article-title":"IDF diabetes atlas: global estimates of the prevalence of diabetes for 2011 and 2030","volume":"94","author":"Whiting","year":"2011","journal-title":"Diabetes Res. Clin. Pract."},{"key":"10.1016\/j.bioorg.2025.108762_bb0070","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.diabres.2017.03.024","article-title":"IDF diabetes atlas: global estimates for the prevalence of diabetes for 2015 and 2040","volume":"128","author":"Ogurtsova","year":"2017","journal-title":"Diabetes Res. Clin. Pract."},{"issue":"3","key":"10.1016\/j.bioorg.2025.108762_bb0075","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1016\/j.diabres.2011.10.040","article-title":"The international diabetes Federation diabetes atlas methodology for estimating global and national prevalence of diabetes in adults","volume":"94","author":"Guariguata","year":"2011","journal-title":"Diabetes Res. Clin. Pract."},{"key":"10.1016\/j.bioorg.2025.108762_bb0080","doi-asserted-by":"crossref","DOI":"10.1016\/j.diabres.2021.109119","article-title":"IDF diabetes atlas: global, regional and country-level diabetes prevalence estimates for 2021 and projections for 2045","volume":"183","author":"Sun","year":"2022","journal-title":"Diabetes Res. Clin. Pract."},{"key":"10.1016\/j.bioorg.2025.108762_bb0085","doi-asserted-by":"crossref","unstructured":"Kumar A, Gangwar R, Ahmad Zargar A, Kumar R, Sharma A. Prevalence of diabetes in India: a review of IDF diabetes atlas 10th edition. Curr. Diabetes Rev. 2024;20(1):105\u201314.","DOI":"10.2174\/1573399819666230413094200"},{"key":"10.1016\/j.bioorg.2025.108762_bb0090","unstructured":"Federation ID. IDF diabetes atlas 8th edition. Int.l Diabetes Federation. 2017:905\u201311."},{"key":"10.1016\/j.bioorg.2025.108762_bb0095","doi-asserted-by":"crossref","DOI":"10.1016\/j.diabres.2021.109119","article-title":"IDF diabetes atlas: global, regional and country-level diabetes prevalence estimates for 2021 and projections for 2045","volume":"183","author":"Sun","year":"2022","journal-title":"Diabetes Res. Clin. Pract."},{"issue":"Supplement_1","key":"10.1016\/j.bioorg.2025.108762_bb0100","doi-asserted-by":"crossref","first-page":"S20","DOI":"10.2337\/dc24-S002","volume":"47","year":"2024","journal-title":"Diabetes Care"},{"issue":"16","key":"10.1016\/j.bioorg.2025.108762_bb0105","doi-asserted-by":"crossref","first-page":"12676","DOI":"10.3390\/ijms241612676","article-title":"Diabetes mellitus secondary to endocrine diseases: an update of diagnostic and treatment particularities","volume":"24","author":"Popoviciu","year":"2023","journal-title":"Int. J. Mol. Sci."},{"issue":"Supplement_1","key":"10.1016\/j.bioorg.2025.108762_bb0110","doi-asserted-by":"crossref","first-page":"S62","DOI":"10.2337\/dc10-S062","article-title":"Diagnosis and classification of diabetes mellitus","volume":"33","author":"Association AD","year":"2010","journal-title":"Diabetes Care"},{"issue":"9626","key":"10.1016\/j.bioorg.2025.108762_bb0115","doi-asserted-by":"crossref","first-page":"1777","DOI":"10.1016\/S0140-6736(08)60765-5","article-title":"Time trends in the incidence of type 1 diabetes in Finnish children: a cohort study","volume":"371","author":"Harjutsalo","year":"2008","journal-title":"Lancet"},{"issue":"4","key":"10.1016\/j.bioorg.2025.108762_bb0120","doi-asserted-by":"crossref","first-page":"773","DOI":"10.2337\/db09-9028","article-title":"From the triumvirate to the ominous octet: a new paradigm for the treatment of type 2 diabetes mellitus","volume":"58","author":"DeFronzo","year":"2009","journal-title":"Diabetes"},{"key":"10.1016\/j.bioorg.2025.108762_bb0125","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1111\/j.1463-1326.2008.00969.x","article-title":"Pancreatic \u03b2-cell mass in European subjects with type 2 diabetes","volume":"10","author":"Rahier","year":"2008","journal-title":"Diabetes Obes. Metab."},{"issue":"5","key":"10.1016\/j.bioorg.2025.108762_bb0130","doi-asserted-by":"crossref","first-page":"569","DOI":"10.2174\/092986707780059643","article-title":"Genetics of gestational diabetes mellitus","volume":"14","author":"Shaat","year":"2007","journal-title":"Curr. Med. Chem."},{"issue":"6","key":"10.1016\/j.bioorg.2025.108762_bb0135","doi-asserted-by":"crossref","first-page":"393","DOI":"10.2174\/157339910793499155","article-title":"Genetics in gestational diabetes mellitus: association with incidence, severity, pregnancy outcome and response to treatment","volume":"6","author":"Lambrinoudaki","year":"2010","journal-title":"Curr. Diabetes Rev."},{"issue":"3","key":"10.1016\/j.bioorg.2025.108762_bb0140","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1016\/S0889-8529(05)70263-2","article-title":"Lifestyle modifications for diabetes management","volume":"26","author":"Franz","year":"1997","journal-title":"Endocrinol. Metab. Clin. N. Am."},{"issue":"1","key":"10.1016\/j.bioorg.2025.108762_bb0145","doi-asserted-by":"crossref","first-page":"4","DOI":"10.2337\/diacare.16.1.4","article-title":"Effect of meal frequency on blood glucose, insulin, and free fatty acids in NIDDM subjects","volume":"16","author":"Bertelsen","year":"1993","journal-title":"Diabetes Care"},{"issue":"Supplement_1","key":"10.1016\/j.bioorg.2025.108762_bb0150","article-title":"Nutrition recommendations and principles for people with diabetes mellitus","volume":"20","author":"Association AD","year":"1997","journal-title":"Diabetes Care"},{"issue":"11","key":"10.1016\/j.bioorg.2025.108762_bb0155","doi-asserted-by":"crossref","first-page":"2065","DOI":"10.2337\/dc16-1728","article-title":"Physical activity\/exercise and diabetes: a position statement of the American Diabetes Association","volume":"39","author":"Colberg","year":"2016","journal-title":"Diabetes Care"},{"key":"10.1016\/j.bioorg.2025.108762_bb0160","doi-asserted-by":"crossref","first-page":"877","DOI":"10.2147\/IJGM.S51665","article-title":"Pathogenesis and management of postprandial hyperglycemia: role of incretin-based therapies","author":"Gerich","year":"2013","journal-title":"Int. J. General Med."},{"issue":"2","key":"10.1016\/j.bioorg.2025.108762_bb0165","doi-asserted-by":"crossref","first-page":"263","DOI":"10.2337\/dc06-1612","article-title":"The loss of postprandial glycemic control precedes stepwise deterioration of fasting with worsening diabetes","volume":"30","author":"Monnier","year":"2007","journal-title":"Diabetes Care"},{"issue":"Supplement_1","key":"10.1016\/j.bioorg.2025.108762_bb0170","doi-asserted-by":"crossref","first-page":"S11","DOI":"10.2337\/dc11-S011","article-title":"Standards of medical care in diabetes\u20142011","volume":"34","author":"Association AD","year":"2011","journal-title":"Diabetes Care"},{"issue":"11","key":"10.1016\/j.bioorg.2025.108762_bb0175","doi-asserted-by":"crossref","first-page":"1306","DOI":"10.1001\/archinte.163.11.1306","article-title":"Clinical significance, pathogenesis, and management of postprandial hyperglycemia","volume":"163","author":"Gerich","year":"2003","journal-title":"Arch. Intern. Med."},{"issue":"2","key":"10.1016\/j.bioorg.2025.108762_bb0180","doi-asserted-by":"crossref","first-page":"233","DOI":"10.2337\/diacare.22.2.233","article-title":"The relationship between glucose and incident cardiovascular events. A metaregression analysis of published data from 20 studies of 95,783 individuals followed for 12.4 years","volume":"22","author":"Coutinho","year":"1999","journal-title":"Diabetes Care"},{"issue":"9","key":"10.1016\/j.bioorg.2025.108762_bb0185","doi-asserted-by":"crossref","first-page":"1721","DOI":"10.2337\/dc08-2337","article-title":"Postprandial glucose improves the risk prediction of cardiovascular death beyond the metabolic syndrome in the nondiabetic population","volume":"32","author":"Lin","year":"2009","journal-title":"Diabetes Care"},{"issue":"1","key":"10.1016\/j.bioorg.2025.108762_bb0190","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1097\/SMJ.0b013e318188898e","article-title":"Importance of postprandial glucose levels as a target for glycemic control in type 2 diabetes","volume":"102","author":"Tibaldi","year":"2009","journal-title":"South. Med. J."},{"issue":"10","key":"10.1016\/j.bioorg.2025.108762_bb0195","doi-asserted-by":"crossref","first-page":"1211","DOI":"10.1161\/01.CIR.0000027569.76671.A8","article-title":"Evidence for an independent and cumulative effect of postprandial hypertriglyceridemia and hyperglycemia on endothelial dysfunction and oxidative stress generation: effects of short-and long-term simvastatin treatment","volume":"106","author":"Ceriello","year":"2002","journal-title":"Circulation"},{"issue":"16","key":"10.1016\/j.bioorg.2025.108762_bb0200","doi-asserted-by":"crossref","first-page":"2944","DOI":"10.3390\/plants12162944","article-title":"New insights into the latest advancement in \u03b1-amylase inhibitors of plant origin with anti-diabetic effects","volume":"12","author":"Kashtoh","year":"2023","journal-title":"Plants"},{"issue":"7","key":"10.1016\/j.bioorg.2025.108762_bb0205","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1002\/star.201000150","article-title":"Human \u03b1-amylase and starch digestion: an interesting marriage","volume":"63","author":"Butterworth","year":"2011","journal-title":"Starch-St\u00e4rke."},{"key":"10.1016\/j.bioorg.2025.108762_bb0210","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1016\/j.carbpol.2017.01.040","article-title":"Structural and enzyme kinetic studies of retrograded starch: inhibition of \u03b1-amylase and consequences for intestinal digestion of starch","volume":"164","author":"Patel","year":"2017","journal-title":"Carbohydr. Polym."},{"issue":"1","key":"10.1016\/j.bioorg.2025.108762_bb0215","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/0014-5793(73)80079-1","article-title":"The metal specificity of mammalian \u03b1-amylase as revealed by enzyme activity and structural probes","volume":"31","author":"Steer","year":"1973","journal-title":"FEBS Lett."},{"issue":"11","key":"10.1016\/j.bioorg.2025.108762_bb0220","doi-asserted-by":"crossref","first-page":"2901","DOI":"10.1016\/S0021-9258(18)69691-7","article-title":"Metal content of \u03b1-amylases of various origins","volume":"234","author":"Vallee","year":"1959","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.bioorg.2025.108762_bb0225","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/S0167-4838(98)00147-2","article-title":"The human pancreatic \u03b1-amylase isoforms: isolation, structural studies and kinetics of inhibition by acarbose","volume":"1388","author":"Ferey-Roux","year":"1998","journal-title":"Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology."},{"issue":"1","key":"10.1016\/j.bioorg.2025.108762_bb0230","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1093\/clinchem\/30.1.62","article-title":"Amylase from human serous ovarian tumors: purification and characterization","volume":"30","author":"Zakowski","year":"1984","journal-title":"Clin. Chem."},{"key":"10.1016\/j.bioorg.2025.108762_bb0235","series-title":"\u03b1-Amylase inhibitors: a review of raw material and isolated compounds from plant source","author":"PMD","year":"2012"},{"issue":"4","key":"10.1016\/j.bioorg.2025.108762_bb0240","doi-asserted-by":"crossref","first-page":"669","DOI":"10.3390\/molecules22040669","article-title":"Polyphenolic compounds and digestive enzymes: in vitro non-covalent interactions","volume":"22","author":"Martinez-Gonzalez","year":"2017","journal-title":"Molecules"},{"issue":"9","key":"10.1016\/j.bioorg.2025.108762_bb0245","doi-asserted-by":"crossref","first-page":"744","DOI":"10.1002\/anie.198107441","article-title":"Chemistry and biochemistry of microbial \u03b1-glucosidase inhibitors","volume":"20","author":"Truscheit","year":"1981","journal-title":"Angew. Chem. Int. Ed. Eng."},{"issue":"3","key":"10.1016\/j.bioorg.2025.108762_bb0250","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1107\/S0907444995014119","article-title":"Structure of human salivary \u03b1-amylase at 1.6 \u00c5 resolution: implications for its role in the oral cavity","volume":"52","author":"Ramasubbu","year":"1996","journal-title":"Biological Crystallography."},{"issue":"9","key":"10.1016\/j.bioorg.2025.108762_bb0255","doi-asserted-by":"crossref","first-page":"1730","DOI":"10.1002\/pro.5560040908","article-title":"The structure of human pancreatic \u03b1-amylase at 1.8 \u00c5 resolution and comparisons with related enzymes","volume":"4","author":"Brayer","year":"1995","journal-title":"Protein Sci."},{"issue":"2","key":"10.1016\/j.bioorg.2025.108762_bb0260","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1111\/j.1432-1033.1996.0561z.x","article-title":"Crystal structure of pig pancreatic \u03b1-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose","volume":"238","author":"Gilles","year":"1996","journal-title":"Eur. J. Biochem."},{"issue":"6","key":"10.1016\/j.bioorg.2025.108762_bb0265","doi-asserted-by":"crossref","first-page":"1435","DOI":"10.1110\/ps.0202602","article-title":"Structural basis of \u03b1-amylase activation by chloride","volume":"11","author":"Aghajari","year":"2002","journal-title":"Protein Sci."},{"issue":"20","key":"10.1016\/j.bioorg.2025.108762_bb0270","doi-asserted-by":"crossref","first-page":"6284","DOI":"10.1021\/bi00186a031","article-title":"The active Center of a Mammalian. Alpha.-amylase. Structure of the complex of a Pancreatic. Alpha.-amylase with a carbohydrate inhibitor refined to 2.2-. ANG. Resolution","volume":"33","author":"Qian","year":"1994","journal-title":"Biochemistry"},{"issue":"39","key":"10.1016\/j.bioorg.2025.108762_bb0275","doi-asserted-by":"crossref","first-page":"23836","DOI":"10.1074\/jbc.271.39.23836","article-title":"Structural and functional aspects of chloride binding to Alteromonas haloplanctis \u03b1-amylase","volume":"271","author":"Feller","year":"1996","journal-title":"J. Biol. Chem."},{"issue":"S3","key":"10.1016\/j.bioorg.2025.108762_bb0280","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1111\/j.1365-2362.1994.tb02249.x","article-title":"Pharmacology of \u03b1-glucosidase inhibition","volume":"24","author":"AG HBB","year":"1994","journal-title":"Eur. J. Clin. Investig."},{"issue":"6","key":"10.1016\/j.bioorg.2025.108762_bb0285","doi-asserted-by":"crossref","first-page":"1189","DOI":"10.2147\/VHRM.S3119","article-title":"Alpha-glucosidase inhibitors in the early treatment of type 2 diabetes","volume":"4","author":"Van de Laar","year":"2008","journal-title":"Vasc. Health Risk Manag."},{"issue":"5","key":"10.1016\/j.bioorg.2025.108762_bb0290","doi-asserted-by":"crossref","first-page":"853","DOI":"10.3945\/jn.111.156984","article-title":"High endogenous salivary amylase activity is associated with improved glycemic homeostasis following starch ingestion in adults","volume":"142","author":"Mandel","year":"2012","journal-title":"J. Nutr."},{"key":"10.1016\/j.bioorg.2025.108762_bb0295","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s11892-016-0794-7","article-title":"Salivary amylase: digestion and metabolic syndrome","volume":"16","author":"Peyrot Des Gachons","year":"2016","journal-title":"Curr. Diab. Rep."},{"issue":"6","key":"10.1016\/j.bioorg.2025.108762_bb0300","doi-asserted-by":"crossref","first-page":"704","DOI":"10.1097\/MPG.0b013e3182a27438","article-title":"Maltase-glucoamylase modulates gluconeogenesis and sucrase-isomaltase dominates starch digestion glucogenesis","volume":"57","author":"Diaz-Sotomayor","year":"2013","journal-title":"J. Pediatr. Gastroenterol. Nutr."},{"issue":"3","key":"10.1016\/j.bioorg.2025.108762_bb0305","doi-asserted-by":"crossref","first-page":"1432","DOI":"10.1073\/pnas.0237170100","article-title":"The maltase-glucoamylase gene: common ancestry to sucrase-isomaltase with complementary starch digestion activities","volume":"100","author":"Nichols","year":"2003","journal-title":"Proc. Natl. Acad. Sci."},{"issue":"3","key":"10.1016\/j.bioorg.2025.108762_bb0310","doi-asserted-by":"crossref","first-page":"782","DOI":"10.1016\/j.jmb.2007.10.069","article-title":"Human intestinal maltase\u2013glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity","volume":"375","author":"Sim","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bioorg.2025.108762_bb0315","doi-asserted-by":"crossref","first-page":"4799","DOI":"10.1007\/s00018-020-03564-1","article-title":"A comprehensive overview of substrate specificity of glycoside hydrolases and transporters in the small intestine: \u201ca gut feeling\u201d","volume":"77","author":"Elferink","year":"2020","journal-title":"Cell. Mol. Life Sci."},{"issue":"1","key":"10.1016\/j.bioorg.2025.108762_bb0320","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1002\/mnfr.201200511","article-title":"Possible effects of dietary polyphenols on sugar absorption and digestion","volume":"57","author":"Williamson","year":"2013","journal-title":"Mol. Nutr. Food Res."},{"issue":"Suppl. 1","key":"10.1016\/j.bioorg.2025.108762_bb0325","first-page":"873","article-title":"Efficacy of 24-week monotherapy with acarbose, metformin or placebo in NIDDM patients with dietary failure","volume":"39","author":"Hoffman","year":"1996","journal-title":"Diabetologia"},{"issue":"6","key":"10.1016\/j.bioorg.2025.108762_bb0330","doi-asserted-by":"crossref","first-page":"561","DOI":"10.2337\/diacare.17.6.561","article-title":"Efficacy of 24-week Monotnerapy with Acarbose, Glibenclamide, or placebo in NIDDM patients: the Essen study","volume":"17","author":"Hoffmann","year":"1994","journal-title":"Diabetes Care"},{"issue":"5","key":"10.1016\/j.bioorg.2025.108762_bb0335","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1016\/S0002-9343(99)80343-X","article-title":"Multicenter, placebo-controlled trial comparing acarbose (BAY g 5421) with placebo, tolbutamide, and tolbutamide-plus-acarbose in non-insulin-dependent diabetes mellitus","volume":"98","author":"Coniff","year":"1995","journal-title":"Am. J. Med."},{"key":"10.1016\/j.bioorg.2025.108762_bb0340","first-page":"3","article-title":"Efficacy and tolerability of stepwise increasing dosage of acarbose in patients with non-insulin-dependent diabetes (NIDDM) treated with sulphonylureas","volume":"4","author":"May","year":"1995","journal-title":"Diabetes und Stoffwechsel."},{"issue":"04","key":"10.1016\/j.bioorg.2025.108762_bb0345","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1055\/s-2007-1012287","article-title":"Effects of prolonged (6 months) \u03b1-glucosidase inhibition on blood glucose control and insulin requirements in patients with insulin-dependent diabetes mellitus","volume":"18","author":"Dimitriadis","year":"1986","journal-title":"Horm. Metab. Res."},{"issue":"3","key":"10.1016\/j.bioorg.2025.108762_bb0350","doi-asserted-by":"crossref","first-page":"248","DOI":"10.2337\/diacare.20.3.248","article-title":"Acarbose in the treatment of type I diabetes","volume":"20","author":"Hollander","year":"1997","journal-title":"Diabetes Care"},{"issue":"6","key":"10.1016\/j.bioorg.2025.108762_bb0355","first-page":"286","article-title":"The acute effects of glucosidase inhibition on post-meal glucose increments in insulin-dependent diabetics","volume":"77","author":"Wing","year":"1990","journal-title":"South African Med. J.l= Suid-afrikaanse Tydskrif vir Geneeskunde."},{"issue":"9323","key":"10.1016\/j.bioorg.2025.108762_bb0360","doi-asserted-by":"crossref","first-page":"2072","DOI":"10.1016\/S0140-6736(02)08905-5","article-title":"Acarbose for prevention of type 2 diabetes mellitus: the STOP-NIDDM randomised trial","volume":"359","author":"Chiasson","year":"2002","journal-title":"Lancet"},{"key":"10.1016\/j.bioorg.2025.108762_bb0380","article-title":"Synthesis of 1, 4-dideoxy-1, 4-imino-L-arabinitol","author":"Behling","year":"1994","journal-title":"Google Patents"},{"key":"10.1016\/j.bioorg.2025.108762_bb0385","article-title":"Alpha-amylase inhibitors: the montbretins and uses thereof","author":"Withers","year":"2013","journal-title":"Google Patents"},{"key":"10.1016\/j.bioorg.2025.108762_bb0365","doi-asserted-by":"crossref","DOI":"10.1016\/j.fbio.2024.105456","article-title":"Dietary natural products as inhibitors of \u03b1-amylase and \u03b1-glucosidase: an updated review of ligand-receptor correlations validated by docking studies","volume":"62","author":"Rangel-Galv\u00e1n","year":"2024","journal-title":"Food Biosci."},{"issue":"1","key":"10.1016\/j.bioorg.2025.108762_bb0370","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1007\/s13659-023-00424-w","article-title":"Flavonoids as dual-target inhibitors against \u03b1-glucosidase and \u03b1-amylase: a systematic review of in vitro studies","volume":"14","author":"Lam","year":"2024","journal-title":"Nat. Products Bioprospecting."},{"issue":"12","key":"10.1016\/j.bioorg.2025.108762_bb0375","doi-asserted-by":"crossref","first-page":"782","DOI":"10.2174\/0113894501313365240722100902","article-title":"Recent advances in the development of alpha-glucosidase and alpha-amylase inhibitors in type 2 diabetes management: insights from in silico to in vitro studies","volume":"25","author":"Khan","year":"2024","journal-title":"Curr. Drug Targets"},{"key":"10.1016\/j.bioorg.2025.108762_bb0390","doi-asserted-by":"crossref","first-page":"2115","DOI":"10.2174\/0109298673272908231115101520","article-title":"Recent Progress on natural \u03b1-glucosidase inhibitors derived from the plants and microorganisms, 32(11)","author":"Deng","year":"2025","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.bioorg.2025.108762_bb0395","first-page":"1","article-title":"Key molecular scaffolds in the development of clinically viable \u03b1-amylase inhibitors. Future","author":"Singh","year":"2025","journal-title":"Med. Chem."},{"issue":"4","key":"10.1016\/j.bioorg.2025.108762_bb0400","doi-asserted-by":"crossref","DOI":"10.2174\/0115701638336128250122223221","article-title":"In silico based diabetic wound healer from nature: an update","volume":"22","author":"Lather","year":"2025","journal-title":"Curr. Drug Discov. Technol."},{"key":"10.1016\/j.bioorg.2025.108762_bb0405","article-title":"Natural products with potential hypoglycemic activity in T2DM: 2019-2023","volume":"114130","author":"Fei","year":"2024","journal-title":"Phytochemistry"},{"key":"10.1016\/j.bioorg.2025.108762_bb0410","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12906-018-2381-8","article-title":"Phytochemical analysis and antidiabetic potential of Elaeagnus umbellata (Thunb.) in streptozotocin-induced diabetic rats: pharmacological and computational approach","volume":"18","author":"Nazir","year":"2018","journal-title":"BMC Complement. Altern. Med."},{"key":"10.1016\/j.bioorg.2025.108762_bb0415","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12906-021-03228-y","article-title":"Chemical composition, in vitro antioxidant, anticholinesterase, and antidiabetic potential of essential oil of Elaeagnus umbellata Thunb","volume":"21","author":"Nazir","year":"2021","journal-title":"BMC Complementary Med. Therapies."},{"key":"10.1016\/j.bioorg.2025.108762_bb0420","doi-asserted-by":"crossref","DOI":"10.1016\/j.jep.2019.112027","article-title":"Antidiabetic activity of root tubers of Asparagus gonoclados baker in streptozotocin induced diabetic rats","volume":"242","author":"Rajasekhar","year":"2019","journal-title":"J. Ethnopharmacol."},{"key":"10.1016\/j.bioorg.2025.108762_bb0425","doi-asserted-by":"crossref","first-page":"9739","DOI":"10.1007\/s11356-019-04339-3","article-title":"\u0391-Amylase and \u03b1-glucosidase inhibitor effects and pancreatic response to diabetes mellitus on Wistar rats of Ephedra alata areal part decoction with immunohistochemical analyses","volume":"26","author":"Ben Lamine","year":"2019","journal-title":"Environ. Sci. Pollut. Res."},{"issue":"9","key":"10.1016\/j.bioorg.2025.108762_bb0430","doi-asserted-by":"crossref","first-page":"1776","DOI":"10.3390\/molecules24091776","article-title":"Investigation on the enzymatic profile of mulberry alkaloids by enzymatic study and molecular docking","volume":"24","author":"Liu","year":"2019","journal-title":"Molecules"},{"key":"10.1016\/j.bioorg.2025.108762_bb0435","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12906-019-2622-5","article-title":"In vitro \u03b1-amylase inhibitory effect of TLC isolates of aloe megalacantha baker and Aloe monticola Reynolds","volume":"19","author":"Tekulu","year":"2019","journal-title":"BMC Complement. Altern. Med."},{"issue":"1","key":"10.1016\/j.bioorg.2025.108762_bb0440","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1007\/s11130-018-0711-0","article-title":"The antidiabetic potential of black mulberry extract-enriched pasta through inhibition of enzymes and glycemic index","volume":"74","author":"Yazdankhah","year":"2019","journal-title":"Plant Foods Hum. Nutr."},{"key":"10.1016\/j.bioorg.2025.108762_bb0445","doi-asserted-by":"crossref","DOI":"10.1016\/j.foodchem.2020.127240","article-title":"Phenolic profiling and evaluation of in vitro antioxidant, \u03b1-glucosidase and \u03b1-amylase inhibitory activities of Lepisanthes fruticosa (Roxb) Leenh fruit extracts","volume":"331","author":"Salahuddin","year":"2020","journal-title":"Food Chem."},{"issue":"4","key":"10.1016\/j.bioorg.2025.108762_bb0450","doi-asserted-by":"crossref","first-page":"1530","DOI":"10.1002\/jsfa.10771","article-title":"Polyphenol fingerprinting and hypoglycemic attributes of optimized Cycas circinalis leaf extracts","volume":"101","author":"Arshad","year":"2021","journal-title":"J. Sci. Food Agric."},{"issue":"23","key":"10.1016\/j.bioorg.2025.108762_bb0455","doi-asserted-by":"crossref","first-page":"5537","DOI":"10.3390\/molecules25235537","article-title":"Chromatographic separation of Breynia retusa (Dennst.) Alston bark, fruit and leaf constituents from bioactive extracts","volume":"25","author":"S","year":"2020","journal-title":"Molecules"},{"issue":"12","key":"10.1016\/j.bioorg.2025.108762_bb0460","doi-asserted-by":"crossref","first-page":"2854","DOI":"10.3390\/molecules25122854","article-title":"Flavonoids in decorticated sorghum grains exert antioxidant, antidiabetic and antiobesity activities","volume":"25","author":"Ofosu","year":"2020","journal-title":"Molecules"},{"issue":"2","key":"10.1016\/j.bioorg.2025.108762_bb0465","doi-asserted-by":"crossref","DOI":"10.1515\/jbcpp-2019-0220","article-title":"Toxicological, anticholinesterase, antilipidemic, antidiabetic and antioxidant potentials of Grewia optiva Drummond ex Burret extracts","volume":"31","author":"Zahoor","year":"2020","journal-title":"J. Basic Clin. Physiol. Pharmacol."},{"issue":"2","key":"10.1016\/j.bioorg.2025.108762_bb0470","doi-asserted-by":"crossref","first-page":"317","DOI":"10.3390\/molecules26020317","article-title":"Forty-one plant extracts screened for dual antidiabetic and antioxidant functions: evaluating the types of correlation between \u03b1-amylase inhibition and free radical scavenging","volume":"26","author":"Bashkin","year":"2021","journal-title":"Molecules"},{"key":"10.1016\/j.bioorg.2025.108762_bb0475","doi-asserted-by":"crossref","DOI":"10.1016\/j.biopha.2021.111379","article-title":"Myrianthus libericus: possible mechanisms of hypoglycaemic action and in silico prediction of pharmacokinetics and toxicity profile of its bioactive metabolite, friedelan-3-one","volume":"137","author":"Harley","year":"2021","journal-title":"Biomed. Pharmacother."},{"issue":"29","key":"10.1016\/j.bioorg.2025.108762_bb0480","doi-asserted-by":"crossref","first-page":"19045","DOI":"10.1021\/acsomega.1c02350","article-title":"Phytochemical profiling in conjunction with in vitro and in silico studies to identify human \u03b1-amylase inhibitors in Leucaena leucocephala (Lam.) De wit for the treatment of diabetes mellitus","volume":"6","author":"Renganathan","year":"2021","journal-title":"ACS omega."},{"key":"10.1016\/j.bioorg.2025.108762_bb0485","doi-asserted-by":"crossref","DOI":"10.1177\/11779322221115436","article-title":"Phytochemical characterization, functional nutrition, and anti-diabetic potentials of Leptadenia hastata (pers) decne leaves: in silico and in vitro studies","volume":"16","author":"Chukwuma","year":"2022","journal-title":"Bioinfo. Biol. Insights."},{"issue":"9","key":"10.1016\/j.bioorg.2025.108762_bb0490","doi-asserted-by":"crossref","first-page":"1712","DOI":"10.3390\/antiox11091712","article-title":"Phytochemical screening, antioxidant, and enzyme inhibitory properties of three Prangos species (P. heyniae, P. meliocarpoides var. meliocarpoides, and P. uechtritzii) depicted by comprehensive LC-MS and multivariate data analysis","volume":"11","author":"Dall\u2019Acqua","year":"2022","journal-title":"Antioxidants"},{"issue":"10","key":"10.1016\/j.bioorg.2025.108762_bb0500","doi-asserted-by":"crossref","first-page":"1852","DOI":"10.3390\/antiox11101852","article-title":"Phytochemical composition and biological activities of Arctium minus (hill) Bernh.: a potential candidate as antioxidant, enzyme inhibitor, and cytotoxic agent","volume":"11","author":"\u0130lg\u00fcn","year":"2022","journal-title":"Antioxidants"},{"issue":"19","key":"10.1016\/j.bioorg.2025.108762_bb0505","doi-asserted-by":"crossref","first-page":"6222","DOI":"10.3390\/molecules27196222","article-title":"Phyto-computational intervention of diabetes mellitus at multiple stages using isoeugenol from Ocimum tenuiflorum: a combination of pharmacokinetics and molecular modelling approaches","volume":"27","author":"Martiz","year":"2022","journal-title":"Molecules"},{"key":"10.1016\/j.bioorg.2025.108762_bb0510","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2022.866719","article-title":"Inhibition mechanism of alpha-amylase, a diabetes target, by a steroidal pregnane and pregnane glycosides derived from Gongronema latifolium Benth","volume":"9","author":"Ogunyemi","year":"2022","journal-title":"Front. Mol. Biosci."},{"issue":"15","key":"10.1016\/j.bioorg.2025.108762_bb0515","doi-asserted-by":"crossref","first-page":"4707","DOI":"10.3390\/molecules27154707","article-title":"Biological evaluation, phytochemical screening, and fabrication of Indigofera linifolia leaves extract-loaded nanoparticles","volume":"27","author":"Talha","year":"2022","journal-title":"Molecules"},{"key":"10.1016\/j.bioorg.2025.108762_bb0525","doi-asserted-by":"crossref","DOI":"10.1016\/j.biopha.2020.110561","article-title":"Swertiamarin and quercetin combination ameliorates hyperglycemia, hyperlipidemia and oxidative stress in streptozotocin-induced type 2 diabetes mellitus in wistar rats","volume":"130","author":"Jaishree","year":"2020","journal-title":"Biomed. Pharmacother."},{"key":"10.1016\/j.bioorg.2025.108762_bb0530","doi-asserted-by":"crossref","first-page":"831","DOI":"10.3389\/fphar.2020.00831","article-title":"Structural dependence of sulfated polysaccharide for diabetes management: Fucoidan from Undaria pinnatifida inhibiting \u03b1-glucosidase more strongly than \u03b1-amylase and amyloglucosidase","volume":"11","author":"Koh","year":"2020","journal-title":"Front. Pharmacol."},{"issue":"10","key":"10.1016\/j.bioorg.2025.108762_bb0535","doi-asserted-by":"crossref","first-page":"9048","DOI":"10.1039\/D0FO01195A","article-title":"A novel hypoglycemic agent: polysaccharides from laver (Porphyra spp.)","volume":"11","author":"Zeng","year":"2020","journal-title":"Food Funct."},{"key":"10.1016\/j.bioorg.2025.108762_bb0540","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/j.ijbiomac.2021.06.062","article-title":"Inhibitory effects of chondroitin sulfate on alpha-amylase activity: a potential hypoglycemic agent","volume":"184","author":"Pang","year":"2021","journal-title":"Int. J. Biol. Macromol."},{"issue":"3","key":"10.1016\/j.bioorg.2025.108762_bb0545","doi-asserted-by":"crossref","first-page":"384","DOI":"10.3390\/life12030384","article-title":"New alpha-amylase inhibitory metabolites from pericarps of Garcinia mangostana","volume":"12","author":"Alhakamy","year":"2022","journal-title":"Life"},{"issue":"10","key":"10.1016\/j.bioorg.2025.108762_bb0550","doi-asserted-by":"crossref","first-page":"3283","DOI":"10.3390\/molecules27103283","article-title":"Multitarget action of xanthones from Garcinia mangostana against \u03b1-amylase, \u03b1-glucosidase and pancreatic lipase","volume":"27","author":"Cardozo-Mu\u00f1oz","year":"2022","journal-title":"Molecules"},{"issue":"3","key":"10.1016\/j.bioorg.2025.108762_bb0555","doi-asserted-by":"crossref","first-page":"857","DOI":"10.3390\/molecules27030857","article-title":"Potential mechanisms involved in the protective effect of dicaffeoylquinic acids from Artemisia annua L. leaves against diabetes and its complications","volume":"27","author":"El-Askary","year":"2022","journal-title":"Molecules"},{"issue":"6","key":"10.1016\/j.bioorg.2025.108762_bb0560","doi-asserted-by":"crossref","first-page":"1888","DOI":"10.3390\/molecules27061888","article-title":"Inhibitory effect of polyphenols from the whole green jackfruit flour against \u03b1-glucosidase, \u03b1-amylase, aldose reductase and glycation at multiple stages and their interaction: inhibition kinetics and molecular simulations","volume":"27","author":"Maradesha","year":"2022","journal-title":"Molecules"},{"key":"10.1016\/j.bioorg.2025.108762_bb0565","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2020.103713","article-title":"Multifunctional isoxazolidine derivatives as \u03b1-amylase and \u03b1-glucosidase inhibitors","volume":"98","author":"Ghabi","year":"2020","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.bioorg.2025.108762_bb0570","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/j.ijbiomac.2020.03.090","article-title":"Exploring efficacy of indole-based dual inhibitors for \u03b1-glucosidase and \u03b1-amylase enzymes: in silico, biochemical and kinetic studies","volume":"154","author":"Kawde","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"issue":"11","key":"10.1016\/j.bioorg.2025.108762_bb0575","doi-asserted-by":"crossref","DOI":"10.1016\/j.bmc.2020.115467","article-title":"Syntheses, in vitro \u03b1-amylase and \u03b1-glucosidase dual inhibitory activities of 4-amino-1, 2, 4-triazole derivatives their molecular docking and kinetic studies","volume":"28","author":"Yeye","year":"2020","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.bioorg.2025.108762_bb0580","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2020.104489","article-title":"Synthesis of azachalcones, their \u03b1-amylase, \u03b1-glucosidase inhibitory activities, kinetics, and molecular docking studies","volume":"106","author":"Saleem","year":"2021","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.bioorg.2025.108762_bb0585","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2020.103979","article-title":"Synthesis and screening of (E)-3-(2-benzylidenehydrazinyl)-5, 6-diphenyl-1, 2, 4-triazine analogs as novel dual inhibitors of \u03b1-amylase and \u03b1-glucosidase","volume":"101","author":"Shamim","year":"2020","journal-title":"Bioorg. Chem."},{"issue":"18","key":"10.1016\/j.bioorg.2025.108762_bb0590","doi-asserted-by":"crossref","first-page":"8340","DOI":"10.1080\/07391102.2021.1911854","article-title":"Synthesis, \u03b1-glucosidase and \u03b1-amylase inhibitory activities, acute toxicity and molecular docking studies of thiazolidine-2, 4-diones derivatives","volume":"40","author":"Fettach","year":"2022","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.bioorg.2025.108762_bb0595","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2021.105291","article-title":"Novel cinnamic acid magnolol derivatives as potent \u03b1-glucosidase and \u03b1-amylase inhibitors: synthesis, in vitro and in silico studies","volume":"116","author":"Hu","year":"2021","journal-title":"Bioorg. Chem."},{"issue":"8","key":"10.1016\/j.bioorg.2025.108762_bb0600","doi-asserted-by":"crossref","first-page":"1035","DOI":"10.3390\/ph15081035","article-title":"\u0391-Glucosidase and \u03b1-amylase inhibitory potentials of quinoline\u20131, 3, 4-oxadiazole conjugates bearing 1, 2, 3-triazole with antioxidant activity, kinetic studies, and computational validation","volume":"15","author":"Cele","year":"2022","journal-title":"Pharmaceuticals"},{"key":"10.1016\/j.bioorg.2025.108762_bb0605","doi-asserted-by":"crossref","DOI":"10.3389\/fchem.2022.1023316","article-title":"Molecular iodine-promoted oxidative cyclization for the synthesis of 1, 3, 4-thiadiazole-fused-[1, 2, 4]-thiadiazole incorporating 1, 4-benzodioxine moiety as potent inhibitors of \u03b1-amylase and \u03b1-glucosidase: in vitro and in silico study","volume":"10","author":"Hussain","year":"2022","journal-title":"Front. Chem."},{"key":"10.1016\/j.bioorg.2025.108762_bb0610","doi-asserted-by":"crossref","DOI":"10.1016\/j.molstruc.2022.133812","article-title":"Synthesis, in vitro \u03b1-amylase, \u03b1-glucosidase activities and molecular docking study of new benzimidazole bearing thiazolidinone derivatives","volume":"1269","author":"Khan","year":"2022","journal-title":"J. Mol. Struct."},{"issue":"19","key":"10.1016\/j.bioorg.2025.108762_bb0615","doi-asserted-by":"crossref","first-page":"6564","DOI":"10.3390\/molecules27196564","article-title":"New biologically hybrid pharmacophore thiazolidinone-based indole derivatives: synthesis, in vitro alpha-amylase and alpha-glucosidase along with molecular docking investigations","volume":"27","author":"Khan","year":"2022","journal-title":"Molecules"},{"issue":"10","key":"10.1016\/j.bioorg.2025.108762_bb0620","doi-asserted-by":"crossref","first-page":"1164","DOI":"10.3390\/ph15101164","article-title":"Design, synthesis, in silico testing, and in vitro evaluation of thiazolidinone-based benzothiazole derivatives as inhibitors of \u03b1-amylase and \u03b1-glucosidase","volume":"15","author":"Khan","year":"2022","journal-title":"Pharmaceuticals"},{"issue":"9","key":"10.1016\/j.bioorg.2025.108762_bb0625","doi-asserted-by":"crossref","first-page":"2692","DOI":"10.3390\/molecules26092692","article-title":"Synthesis, structure, carbohydrate enzyme inhibition, antioxidant activity, in silico drug-receptor interactions and drug-like profiling of the 5-styryl-2-aminochalcone hybrids","volume":"26","author":"Mphahlele","year":"2021","journal-title":"Molecules"},{"issue":"1","key":"10.1016\/j.bioorg.2025.108762_bb0630","doi-asserted-by":"crossref","first-page":"106","DOI":"10.3390\/ph15010106","article-title":"Identification of cyclic sulfonamides with an N-arylacetamide group as \u03b1-glucosidase and \u03b1-amylase inhibitors: biological evaluation and molecular modeling","volume":"15","author":"Saddique","year":"2022","journal-title":"Pharmaceuticals"},{"key":"10.1016\/j.bioorg.2025.108762_bb0635","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2023.106709","article-title":"Arylureidoaurones: synthesis, in vitro \u03b1-glucosidase, and \u03b1-amylase inhibition activity","volume":"139","author":"Kazempour-Dizaji","year":"2023","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.bioorg.2025.108762_bb0640","doi-asserted-by":"crossref","DOI":"10.1016\/j.molstruc.2022.133650","article-title":"Design, synthesis, and in silico studies of benzimidazole bearing phenoxyacetamide derivatives as \u03b1-glucosidase and \u03b1-amylase inhibitors","volume":"1268","author":"Shayegan","year":"2022","journal-title":"J. Mol. Struct."},{"key":"10.1016\/j.bioorg.2025.108762_bb0645","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2024.116600","article-title":"Novel carbazole-oxadiazole derivatives as anti-\u03b1-glucosidase and anti-\u03b1-amylase agents: design, synthesis, molecular docking, and biological evaluation","volume":"275","author":"Luo","year":"2024","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.bioorg.2025.108762_bb0650","doi-asserted-by":"crossref","DOI":"10.1016\/j.molstruc.2023.134954","article-title":"Synthesis and molecular modeling studies of naphthazarin derivatives as novel selective inhibitors of \u03b1-glucosidase and \u03b1-amylase","volume":"1278","author":"Abadan","year":"2023","journal-title":"J. Mol. Struct."},{"key":"10.1016\/j.bioorg.2025.108762_bb0655","doi-asserted-by":"crossref","DOI":"10.1016\/j.molstruc.2023.135672","article-title":"Exploring thiazole-based Schiff base analogs as potent \u03b1-glucosidase and \u03b1-amylase inhibitor: their synthesis and in-silico study","volume":"1287","author":"Taha","year":"2023","journal-title":"J. Mol. Struct."},{"key":"10.1016\/j.bioorg.2025.108762_bb0660","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2024.107207","article-title":"Pyrano [2, 3-b] chromone derivatives as novel dual inhibitors of \u03b1-glucosidase and \u03b1-amylase: design, synthesis, biological evaluation, and in silico studies","volume":"145","author":"Farzaneh","year":"2024","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.bioorg.2025.108762_bb0665","doi-asserted-by":"crossref","DOI":"10.1016\/j.cdc.2023.101035","article-title":"Synthesis, in vitro \u03b1-glucosidase and \u03b1-amylase activities, and an in silico molecular docking study of triazinoindole-thiazolidinone hybrid derivatives","volume":"45","author":"Khan","year":"2023","journal-title":"Chemical Data Collections."},{"key":"10.1016\/j.bioorg.2025.108762_bb0670","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2024.116139","article-title":"3, 5-Disubstituted-thiazolidine-2, 4-dione hybrids as antidiabetic agents: design, synthesis, in-vitro and in vivo evaluation","volume":"266","author":"Singh","year":"2024","journal-title":"Eur. J. Med. Chem."},{"issue":"8","key":"10.1016\/j.bioorg.2025.108762_bb0675","doi-asserted-by":"crossref","first-page":"2826","DOI":"10.1039\/D4MD00199K","article-title":"Thiazolidine-2, 4-dione hybrids as dual alpha-amylase and alpha-glucosidase inhibitors: design, synthesis, in vitro and in vivo anti-diabetic evaluation","volume":"15","author":"Singh","year":"2024","journal-title":"RSC Med. Chem."}],"container-title":["Bioorganic Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S004520682500642X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S004520682500642X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,4,23]],"date-time":"2026-04-23T04:56:59Z","timestamp":1776920219000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S004520682500642X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,8]]},"references-count":133,"alternative-id":["S004520682500642X"],"URL":"https:\/\/doi.org\/10.1016\/j.bioorg.2025.108762","relation":{},"ISSN":["0045-2068"],"issn-type":[{"value":"0045-2068","type":"print"}],"subject":[],"published":{"date-parts":[[2025,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Dual \u03b1-amylase and \u03b1-glucosidase inhibitors: recent progress from natural and synthetic resources","name":"articletitle","label":"Article Title"},{"value":"Bioorganic Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bioorg.2025.108762","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"108762"}}