| Mechanistic Pathway on Human alpha-Glucosidase Maltase-Glucoamylase Unveiled by QM/MM Calculations | Mechanistic Pathway on Human α-Glucosidase Maltase-Glucoamylase Unveiled by QM/MM Calculations.
Brás NF, Santos-Martins D, Fernandes PA, Ramos MJ. | 06/2/2018 |
| MGAM, or nearby regulatory elements, may be involved in the etiology of oral clefts. | A genome-wide study of inherited deletions identified two regions associated with nonsyndromic isolated oral clefts.
Younkin SG, Scharpf RB, Schwender H, Parker MM, Scott AF, Marazita ML, Beaty TH, Ruczinski I., Free PMC Article | 01/16/2016 |
| Starch internal structure modulates its susceptibility to MGAM. The internal branch amounts negatively affect the glucose release rate. | Branch pattern of starch internal structure influences the glucogenesis by mucosal Nt-maltase-glucoamylase.
Lin AH, Ao Z, Quezada-Calvillo R, Nichols BL, Lin CT, Hamaker BR. | 10/10/2015 |
| The over-expression of MGAM was confirmed with a 6.6 fold increase in expression at the mRNA level whereas the fold change in ADAM9 demonstrated a 1.6 fold increase. | Genome wide analysis of chromosomal alterations in oral squamous cell carcinomas revealed over expression of MGAM and ADAM9.
Vincent-Chong VK, Anwar A, Karen-Ng LP, Cheong SC, Yang YH, Pradeep PJ, Rahman ZA, Ismail SM, Zaini ZM, Prepageran N, Kallarakkal TG, Ramanathan A, Mohayadi NA, Rosli NS, Mustafa WM, Abraham MT, Tay KK, Zain RB., Free PMC Article | 12/7/2013 |
| Findings suggest that C-terminal subunits of recombinant maltase-glucoamylase (MGAM) assists alpha-amylase in digesting starch molecules and potentially may compensate for developmental or pathological amylase deficiencies. | Unexpected high digestion rate of cooked starch by the Ct-maltase-glucoamylase small intestine mucosal α-glucosidase subunit.
Lin AH, Nichols BL, Quezada-Calvillo R, Avery SE, Sim L, Rose DR, Naim HY, Hamaker BR., Free PMC Article | 09/22/2012 |
| These results suggest that the N-terminal and C-terminal catalytic domains of maltase-glucoamylase differ in their substrate specificities and inhibitor tolerance despite their structural relationship | Study of the inhibition of two human maltase-glucoamylases catalytic domains by different α-glucosidase inhibitors.
Ren L, Cao X, Geng P, Bai F, Bai G. | 03/24/2012 |
| we report crystal structures of C-terminal maltase-glucoamylase alone at a resolution of 3.1 angstroms, and in complex with its inhibitor acarbose | Structural insight into substrate specificity of human intestinal maltase-glucoamylase.
Ren L, Qin X, Cao X, Wang L, Bai F, Bai G, Shen Y., Free PMC Article | 02/25/2012 |
| Observational study of gene-disease association, gene-environment interaction, and pharmacogenomic / toxicogenomic. (HuGE Navigator) | Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study.
Bailey SD, Xie C, Do R, Montpetit A, Diaz R, Mohan V, Keavney B, Yusuf S, Gerstein HC, Engert JC, Anand S, DREAM investigators., Free PMC Article | 09/15/2010 |
| Observational study of gene-disease association. (HuGE Navigator) | Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip.
Talmud PJ, Drenos F, Shah S, Shah T, Palmen J, Verzilli C, Gaunt TR, Pallas J, Lovering R, Li K, Casas JP, Sofat R, Kumari M, Rodriguez S, Johnson T, Newhouse SJ, Dominiczak A, Samani NJ, Caulfield M, Sever P, Stanton A, Shields DC, Padmanabhan S, Melander O, Hastie C, Delles C, Ebrahim S, Marmot MG, Smith GD, Lawlor DA, Munroe PB, Day IN, Kivimaki M, Whittaker J, Humphries SE, Hingorani AD, ASCOT investigators, NORDIL investigators, BRIGHT Consortium., Free PMC Article | 09/15/2010 |
| analysis of substrate selectivity of human maltase-glucoamylase and sucrase-isomaltase N-terminal domains | Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains.
Sim L, Willemsma C, Mohan S, Naim HY, Pinto BM, Rose DR., Free PMC Article | 06/28/2010 |
| This study reported the first diagnosed Finnish patient with a phenotype compatible with the late-onset form of Pompe disease. Molecular genetic analysis of the GAA gene revealed a novel missense mutation (Y575X),combined with (P545L) mutation. | A novel mutation of the GAA gene in a Finnish late-onset Pompe disease patient: clinical phenotype and follow-up with enzyme replacement therapy.
Korpela MP, Paetau A, Löfberg MI, Timonen MH, Lamminen AE, Kiuru-Enari SM. | 01/21/2010 |
| Acarbose has been found to improve insulin levels and thus glucose/insulin ratios more effectively in overweight patients compared with nonoverweight patients with PCOS. | Clinical, endocrine, and metabolic effects of acarbose, a alpha-glucosidase inhibitor, in overweight and nonoverweight patients with polycystic ovarian syndrome.
Tuğrul S, Kutlu T, Pekin O, Bağlam E, Kiyak H, Oral O. | 01/21/2010 |
| Intestinal maltase-glycoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity. | Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.
Sim L, Quezada-Calvillo R, Sterchi EE, Nichols BL, Rose DR. | 01/21/2010 |
| Raw starch granule degradation with recombinanat human MGAM indicates that pancreatic alpha-amylase hydrolysis is not a requirement for native starch digestion in the human small intestine. | Evidence of native starch degradation with human small intestinal maltase-glucoamylase (recombinant).
Ao Z, Quezada-Calvillo R, Sim L, Nichols BL, Rose DR, Sterchi EE, Hamaker BR. | 01/21/2010 |
| genetic analysis of MGAM, exon boundaries, and chromosome mapping | The maltase-glucoamylase gene: common ancestry to sucrase-isomaltase with complementary starch digestion activities.
Nichols BL, Avery S, Sen P, Swallow DM, Hahn D, Sterchi E., Free PMC Article | 01/21/2010 |