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Buford L Nichols

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Articles 43
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Recent Articles
11.
Cisse F, Erickson D, Hayes A, Opekun A, Nichols B, Hamaker B
Nutrients . 2018 Jan; 10(2). PMID: 29373493
From anecdotal evidence that traditional African sorghum and millet foods are filling and provide sustained energy, we hypothesized that gastric emptying rates of sorghum and millet foods are slow, particularly...
12.
Simsek M, Quezada-Calvillo R, Nichols B, Hamaker B
Food Funct . 2017 Apr; 8(5):1915-1924. PMID: 28443839
Diverse natural phenolic compounds show inhibition activity of intestinal α-glucosidases, which may constitute the molecular basis for their ability to control systemic glycemia. Additionally, phenolics can modify mRNA expression for...
13.
Nichols B, Avery S, Quezada-Calvillo R, Kilani S, Lin A, Burrin D, et al.
J Pediatr Gastroenterol Nutr . 2017 Mar; 65(2):e35-e42. PMID: 28267073
Background And Objective: Although named because of its sucrose hydrolytic activity, this mucosal enzyme plays a leading role in starch digestion because of its maltase and glucoamylase activities. Sucrase-deficient mutant...
14.
Lee B, Rose D, Lin A, Quezada-Calvillo R, Nichols B, Hamaker B
J Agric Food Chem . 2016 Aug; 64(33):6487-94. PMID: 27480812
The mammalian mucosal α-glucosidase complexes, maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI), have two catalytic subunits (N- and C-termini). Concurrent with the desire to modulate glycemic response, there has been a focus...
15.
Sukumaran S, Yee K, Iwata S, Kotha R, Quezada-Calvillo R, Nichols B, et al.
Proc Natl Acad Sci U S A . 2016 May; 113(21):6035-40. PMID: 27162343
The primary sweet sensor in mammalian taste cells for sugars and noncaloric sweeteners is the heteromeric combination of type 1 taste receptors 2 and 3 (T1R2+T1R3, encoded by Tas1r2 and...
16.
Simsek M, Quezada-Calvillo R, Ferruzzi M, Nichols B, Hamaker B
J Agric Food Chem . 2015 Mar; 63(15):3873-9. PMID: 25816913
In this study, it was hypothesized that dietary phenolic compounds selectively inhibit the individual C- and N-terminal (Ct, Nt) subunits of the two small intestinal α-glucosidases, maltase-glucoamylase (MGAM) and sucrase-isomaltase...
17.
Lin A, Ao Z, Quezada-Calvillo R, Nichols B, Lin C, Hamaker B
Carbohydr Polym . 2014 Jul; 111:33-40. PMID: 25037326
To produce sufficient amounts of glucose from food starch, both α-amylase and mucosal α-glucosidases are required. We found previously that the digestion rate of starch is influenced by its susceptibility...
18.
Lee B, Lin A, Nichols B, Jones K, Rose D, Quezada-Calvillo R, et al.
Mol Nutr Food Res . 2014 Jan; 58(5):1111-21. PMID: 24442968
Scope: The four mucosal α-glucosidases, which differ in their digestive roles, generate glucose from glycemic carbohydrates and accordingly can be viewed as a control point for rate of glucose delivery...
19.
Cheng M, Chegeni M, Kim K, Zhang G, Benmoussa M, Quezada-Calvillo R, et al.
J Clin Biochem Nutr . 2014 Jan; 54(1):55-60. PMID: 24426192
Using the small intestine enterocyte Caco-2 cell model, sucrase-isomaltase (SI, the mucosal α-glucosidase complex) expression and modification were examined relative to exposure to different mono- and disaccharide glycemic carbohydrates. Caco-2/TC7...
20.
Diaz-Sotomayor M, Quezada-Calvillo R, Avery S, Chacko S, Yan L, Lin A, et al.
J Pediatr Gastroenterol Nutr . 2013 Jul; 57(6):704-12. PMID: 23838818
Objectives: Six enzyme activities are needed to digest starch to absorbable free glucose; 2 luminal α-amylases (AMY) and 4 mucosal maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) subunit activities are involved in...