R. Quezada‐Calvillo

发表

Expression and function of P2X(7) receptor and CD39/Entpd1 in patients with type 2 diabetes and their association with biochemical parameters.

J. Vargas-Morales, N. Cortez-Espinosa, D. Portales-Pérez, 2011, Cellular immunology.

Dietary phenolic compounds selectively inhibit the individual subunits of maltase-glucoamylase and sucrase-isomaltase with the potential of modulating glucose release.

B. Hamaker, B. Nichols, M. Ferruzzi, 2015, Journal of agricultural and food chemistry.

Enzyme-Synthesized Highly Branched Maltodextrins Have Slow Glucose Generation at the Mucosal α-Glucosidase Level and Are Slowly Digestible In Vivo

S. Yoo, B. Hamaker, B. Nichols, 2013, PloS one.

Modulation of Starch Digestion for Slow Glucose Release through “Toggling” of Activities of Mucosal α-Glucosidases*

B. Hamaker, B. M. Pinto, B. Nichols, 2012, The Journal of Biological Chemistry.

Enterocyte loss of polarity and gut wound healing rely upon the F-actin–severing function of villin

M. Chamaillard, Florent Ubelmann, T. Grandjean, 2013, Proceedings of the National Academy of Sciences.

Taste cell-expressed α-glucosidase enzymes contribute to gustatory responses to disaccharides

B. M. Pinto, S. Mohan, R. Margolskee, 2016, Proceedings of the National Academy of Sciences.

IgA protease in Entamoeba histolytica trophozoites.

R. López-Revilla, R. Quezada‐Calvillo, R. López-Revilla, 1987, Advances in experimental medicine and biology.

Conditioning with slowly digestible starch diets in mice reduces jejunal α-glucosidase activity and glucogenesis from a digestible starch feeding.

F. Vohra, B. Hamaker, B. Nichols, 2020, Nutrition.

Mapping the intestinal alpha-glucogenic enzyme specificities of starch digesting maltase-glucoamylase and sucrase-isomaltase.

B. M. Pinto, S. Mohan, H. Naim, 2011, Bioorganic & medicinal chemistry.

DDR2 plays a role in fibroblast migration independent of adhesion ligand and collagen activated DDR2 tyrosine kinase.

R. Quezada‐Calvillo, M. Herrera-Herrera, 2012, Biochemical and biophysical research communications.

Luminal Substrate “Brake” on Mucosal Maltase-glucoamylase Activity Regulates Total Rate of Starch Digestion to Glucose

G. Brayer, B. Hamaker, S. Baker, 2007, Journal of pediatric gastroenterology and nutrition.

Luminal starch substrate "brake" on maltase-glucoamylase activity is located within the glucoamylase subunit.

G. Brayer, B. Hamaker, B. Nichols, 2008, The Journal of nutrition.

Moderating carbohydrate digestion rate promotes metabolic flexibility in mice

N. Butte, B. Hamaker, B. Nichols, 2023, bioRxiv.

Starch Digestion and Patients With Congenital Sucrase-Isomaltase Deficiency

B. Hamaker, Byung-Hoo Lee, R. Quezada‐Calvillo, 2012, Journal of pediatric gastroenterology and nutrition.

Contribution of mucosal maltase-glucoamylase activities to mouse small intestinal starch alpha-glucogenesis.

S. Wattler, M. Nehls, G. Brayer, 2007, The Journal of nutrition.

Partial characterization of murine intestinal maltase-glucoamylase.

B. Underdown, R. Quezada‐Calvillo, Francisco Rodriguez-Zuñiga, 2002, Biochemical and biophysical research communications.

Contribution of the Individual Small Intestinal α-Glucosidases to Digestion of Unusual α-Linked Glycemic Disaccharides.

B. Hamaker, B. Nichols, D. Rose, 2016, Journal of agricultural and food chemistry.

The Nature of Raw Starch Digestion

B. Hamaker, B. Nichols, D. Rose, 2012, Journal of pediatric gastroenterology and nutrition.

Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.

B. Nichols, D. Rose, E. Sterchi, 2008, Journal of molecular biology.

Phenolic compounds increase the transcription of mouse intestinal maltase-glucoamylase and sucrase-isomaltase.

B. Hamaker, B. Nichols, M. Simsek, 2017, Food & function.

Mucosal maltase-glucoamylase plays a crucial role in starch digestion and prandial glucose homeostasis of mice.

N. Butte, J. Marini, B. Hamaker, 2009, The Journal of nutrition.

Milk glucosidase activity enables suckled pup starch digestion

B. Hamaker, S. Baker, B. Nichols, 2016, Molecular and Cellular Pediatrics.

Branch pattern of starch internal structure influences the glucogenesis by mucosal Nt-maltase-glucoamylase.

B. Hamaker, B. Nichols, Chi-Tien Lin, 2014, Carbohydrate polymers.

Mucosal C-terminal maltase-glucoamylase hydrolyzes large size starch digestion products that may contribute to rapid postprandial glucose generation.

B. Hamaker, B. Nichols, D. Rose, 2014, Molecular nutrition & food research.

Inhibition of Maltase-Glucoamylase Activity to Hydrolyze &agr;-1,4 Linkages by the Presence of Undigested Sucrose

B. Hamaker, B. Nichols, D. Rose, 2012, Journal of pediatric gastroenterology and nutrition.

Unexpected High Digestion Rate of Cooked Starch by the Ct-Maltase-Glucoamylase Small Intestine Mucosal α-Glucosidase Subunit

B. Hamaker, H. Naim, Amy Hui-Mei Lin, 2012, PloS one.

Metabolic Impacts of Maltase Deficiencies

S. Baker, B. Nichols, R. Quezada‐Calvillo, 2018, Journal of pediatric gastroenterology and nutrition.

Maltase-Glucoamylase Modulates Gluconeogenesis and Sucrase-Isomaltase Dominates Starch Digestion Glucogenesis

B. Hamaker, B. Nichols, S. Chacko, 2013, Journal of pediatric gastroenterology and nutrition.

Disaccharide digestion: clinical and molecular aspects.

B. Nichols, R. Quezada‐Calvillo, Claudia C. Robayo-Torres, 2006, Clinical gastroenterology and hepatology : the official clinical practice journal of the American Gastroenterological Association.

Different sucrose-isomaltase response of Caco-2 cells to glucose and maltose suggests dietary maltose sensing

B. Hamaker, Kee-Hong Kim, B. Nichols, 2013, Journal of clinical biochemistry and nutrition.

Improved Starch Digestion of Sucrase-deficient Shrews Treated With Oral Glucoamylase Enzyme Supplements

D. Burrin, S. Oda, B. Hamaker, 2017, Journal of pediatric gastroenterology and nutrition.

13C-Breath Tests for Sucrose Digestion in Congenital Sucrase Isomaltase–deficient and Sacrosidase-supplemented Patients

S. Baker, B. Nichols, A. Opekun, 2009, Journal of pediatric gastroenterology and nutrition.

Evidence of native starch degradation with human small intestinal maltase‐glucoamylase (recombinant)

B. Hamaker, B. Nichols, E. Sterchi, 2007, FEBS letters.

M. Waldor, V. Burrus, Joeli Marrero, 2006, Applied and Environmental Microbiology.

Starch Source Influences Dietary Glucose Generation at the Mucosal α-Glucosidase Level*

B. Hamaker, H. Naim, B. Nichols, 2012, The Journal of Biological Chemistry.

A potential control point of glucose delivery from starchy foods: intestinal mucosal α‐glucosidase digestion

B. Hamaker, R. Quezada‐Calvillo, A. Lin, 2011 .

Dysregulated miR-155 expression in peripheral blood mononuclear cells from patients with type 2 diabetes.

N. Cortez-Espinosa, D. Portales-Pérez, M. Salgado-Bustamante, 2013, Experimental and clinical endocrinology & diabetes : official journal, German Society of Endocrinology [and] German Diabetes Association.

Taste cell-expressed α-glucosidase enzymes contribute to gustatory responses to disaccharides

S. Mohan, R. Margolskee, Y. Ninomiya, 2016, Proceedings of the National Academy of Sciences.