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    AMY2A amylase alpha 2A [ Homo sapiens (human) ]

    Gene ID: 279, updated on 4-Jan-2025

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Recurrent evolution and selection shape structural diversity at the amylase locus.

    Recurrent evolution and selection shape structural diversity at the amylase locus.
    Bolognini D, Halgren A, Lou RN, Raveane A, Rocha JL, Guarracino A, Soranzo N, Chin CS, Garrison E, Sudmant PH., Free PMC Article

    10/25/2024
    In silico assessment of potential leads identified from Bauhinia rufescens Lam. as alpha-glucosidase and alpha-amylase inhibitors.

    In silico assessment of potential leads identified from Bauhinia rufescens Lam. as α-glucosidase and α-amylase inhibitors.
    Osman W, Ismail EMOA, Shantier SW, Mohammed MS, Mothana RA, Muddathir A, Khalid HS.

    10/16/2021
    Association of AMY1A/AMY2A copy numbers and AMY1/AMY2 serum enzymatic activity with obesity in Mexican children.

    Association of AMY1A/AMY2A copy numbers and AMY1/AMY2 serum enzymatic activity with obesity in Mexican children.
    Vázquez-Moreno M, Mejía-Benítez A, Sharma T, Peralta-Romero J, Locia-Morales D, Klünder-Klünder M, National Obesity Network Mexico, Cruz M, Meyre D.

    02/27/2021
    It was concluded that the genetic variant determining starch metabolism influences the response to weight-loss dietary intervention. Overweight and obese individuals carrying the AMY1-AMY2 rs11185098 genotype associated with higher amylase activity may have greater loss of adiposity during low-calorie diet interventions.

    Starch Digestion-Related Amylase Genetic Variant Affects 2-Year Changes in Adiposity in Response to Weight-Loss Diets: The POUNDS Lost Trial.
    Heianza Y, Sun D, Wang T, Huang T, Bray GA, Sacks FM, Qi L., Free PMC Article

    10/21/2017
    Data show that serum amylase was found to be correlated with waist circumference, ghrelin and PYY3-36.

    Relationships Between Fasting Serum Amylase and Ghrelin or Peptide YY3-36 Levels in Healthy Men.
    Tak YJ, Yi YH, Lee SY, Kim YJ, Lee JG, Cho YH.

    12/17/2016
    Data show that amylase-alpha2A autoantibodies may help to diagnosis of autoimmune pancreatitis (AIP) and to differentiate AIP subtypes.

    Role of Amylase-α2A Autoantibodies in the Diagnosis of Autoimmune Pancreatitis.
    Sánchez Castañón M, Zuliani V, Amodio A, Campagnola P, Granato A, Gabbrielli A, Benini L, López Hoyos M, Frulloni L.

    06/28/2016
    Mammalian pancreatic alpha-amylases share a common carbohydrate binding activity and specifically bind to the intestinal brush border.

    Functional regulation of sugar assimilation by N-glycan-specific interaction of pancreatic α-amylase with glycoproteins of duodenal brush border membrane.
    Asanuma-Date K, Hirano Y, Le N, Sano K, Kawasaki N, Hashii N, Hiruta Y, Nakayama K, Umemura M, Ishikawa K, Sakagami H, Ogawa H., Free PMC Article

    09/15/2012
    Studies indicate that chloride activates alpha-amylases and ACE, and gaining insight into the potential mechanisms by which chloride functions in PSII.

    Chloride regulation of enzyme turnover: application to the role of chloride in photosystem II.
    Pokhrel R, McConnell IL, Brudvig GW.

    01/12/2015
    We demonstrated that AMY2A is frequently silenced in gastric carcinoma deletion 1p21.1.

    AMY2A: a possible tumor-suppressor gene of 1p21.1 loss in gastric carcinoma.
    Kang JU, Koo SH, Kwon KC, Park JW.

    08/23/2010
    Autoantibody against amylase alpha-2A is a novel diagnostic marker for both autoimmune pancreatitis and fulminant type 1 diabetes.

    Amylase alpha-2A autoantibodies: novel marker of autoimmune pancreatitis and fulminant type 1 diabetes.
    Endo T, Takizawa S, Tanaka S, Takahashi M, Fujii H, Kamisawa T, Kobayashi T., Free PMC Article

    01/21/2010
    Observational study of genotype prevalence. (HuGE Navigator)See all PubMed (3) articles03/13/2008
    A new approach for the discovery and subsequent structural elucidation of oligosaccharide-based inhibitors of alpha-amylases based upon autoglucosylation of known alpha-glucosidase inhibitors is presented.

    In situ extension as an approach for identifying novel alpha-amylase inhibitors.
    Numao S, Damager I, Li C, Wrodnigg TM, Begum A, Overall CM, Brayer GD, Withers SG.

    01/21/2010
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