Статті в журналах з теми "Alpha glycosidase"
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M., Amin Mir* Yangchan Dolma Tsering Yangchan Jigmat Stanzin Bilal Ahmad Mir. "ANTIDIABETIC PROPERTIES OF VARIOUS EXTRACTS OF HIPPOPHAE RHAMNOIDE." Indo American Journal of Pharmaceutical Sciences 04, no. 11 (2017): 4507–715. https://doi.org/10.5281/zenodo.1068273.
Повний текст джерелаSha, Bi Ying, Qing Shan Liu, Lin Cheng, and Xiao Ying Yin. "Preparation and Application of Core-Shell PMMA/Chitosan Nanoparticle." Advanced Materials Research 535-537 (June 2012): 271–74. http://dx.doi.org/10.4028/www.scientific.net/amr.535-537.271.
Повний текст джерелаal Daher, S., G. Fleet, S. K. Namgoong, and B. Winchester. "Change in specificity of glycosidase inhibition by N-alkylation of amino sugars." Biochemical Journal 258, no. 2 (1989): 613–15. http://dx.doi.org/10.1042/bj2580613.
Повний текст джерелаRura, Sarniati Rante, Yulia Yusrini Djabir, Abdul Rahim, Sri Ningsih, and Nisrina Firdausi. "Evaluation of the Anti-Diabetic Activity of Paliasa Leaf Ethanol Fraction (Kleinhovia hospita L) Through Inhibition of the Enzymes $\alpha$-Glucosidase and $\alpha$-Amylase." Jurnal Ilmiah Kesehatan (JIKA) 5, no. 2 (2023): 342–51. http://dx.doi.org/10.36590/jika.v5i2.509.
Повний текст джерелаWidyawati, Paini Sri, Yesiana D. W. Werdani, and Christine Setiokusumo. "IN VITRO ANTIOXIDANT CAPACITIES AND ANTIDIABETIC PROPERTIES OF PLUCHEA LEAVES AND GREEN TEA MIXTURES AT VARIOUS PROPORTIONS." International Journal of Pharmacy and Pharmaceutical Sciences 9, no. 8 (2017): 203. http://dx.doi.org/10.22159/ijpps.2017v9i8.19545.
Повний текст джерелаField, R. A., A. H. Haines, E. J. T. Chrystal, and M. C. Luszniak. "Histidines, histamines and imidazoles as glycosidase inhibitors." Biochemical Journal 274, no. 3 (1991): 885–89. http://dx.doi.org/10.1042/bj2740885.
Повний текст джерелаYan, Lin, Haiwei Xu, Fengwu Liu, Jin Zhao, and Hongmin Liu. "Synthesis and Biological Evaluation of Andrographolide C-Glycoside Derivatives as α-Glycosidase Inhibitors." Chinese Journal of Chemistry 30, no. 4 (2012): 914–18. http://dx.doi.org/10.1002/cjoc.201100179.
Повний текст джерелаOrtíz-Martinez, David Mizael, Catalina Rivas-Morales, Myriam Angelica de la Garza-Ramos, Maria Julia Verde-Star, Maria Adriana Nuñez-Gonzalez, and Catalina Leos-Rivas. "Miconiasp. Increases mRNA Levels of PPAR Gamma and Inhibits Alpha Amylase and Alpha Glucosidase." Evidence-Based Complementary and Alternative Medicine 2016 (2016): 1–6. http://dx.doi.org/10.1155/2016/5123519.
Повний текст джерелаAmin Mir, M., Shalini Upadhay, and Bilal Ahmad Mir. "Inhibition of Alpha Amylase and Alpha Glycosidase Enzymes by Various Earth Worm Extracts." Biomedical and Pharmacology Journal 11, no. 3 (2018): 1261–68. http://dx.doi.org/10.13005/bpj/1487.
Повний текст джерелаKimura, Atsuo, Toshiyuki Nishio, Wataru Hakamada, et al. "Affinity Labelling of Glycosidase by .OMEGA.-Epoxyalkyl .ALPHA.-Glucoside." Journal of Applied Glycoscience 47, no. 2 (2000): 235–41. http://dx.doi.org/10.5458/jag.47.235.
Повний текст джерелаShi, Hao, Yue Liu, Jiannan Guo та ін. "Thermostable manganese (II) dependent α-glycosidase from Pseudothermotoga thermarum". BioResources 14, № 3 (2019): 7266–74. http://dx.doi.org/10.15376/biores.14.3.7266-7274.
Повний текст джерелаNash, Robert J., Barbara Bartholomew, Yana B. Penkova, and Ekaterina Kozuharova. "Iminosugars of the Invasive Arboreal Amorpha fruticosa and Glycosidase Inhibition Potential." Plants 14, no. 14 (2025): 2205. https://doi.org/10.3390/plants14142205.
Повний текст джерелаSperti, Simonetta, Mariacristina Zamboni, Maurizio Brigotti, Fioretta Rambelli, and Lucio Montanaro. "Alpha-sarcin impairs the N-glycosidase activity of ricin on ribosomes." Biochemical and Biophysical Research Communications 160, no. 2 (1989): 857–61. http://dx.doi.org/10.1016/0006-291x(89)92513-8.
Повний текст джерелаBenešová, E., M. Marková, and B. Králová. " α-Glucosidase and β-glucosidase from psychrotrophic strain arthrobacter sp. C2-2." Czech Journal of Food Sciences 23, No. 3 (2011): 116–20. http://dx.doi.org/10.17221/3380-cjfs.
Повний текст джерелаSun, Y., and W. J. Ball. "Determination of Na(+)-K(+)-ATPase alpha- and beta-isoforms and kinetic properties in mammalian liver." American Journal of Physiology-Cell Physiology 262, no. 6 (1992): C1491—C1499. http://dx.doi.org/10.1152/ajpcell.1992.262.6.c1491.
Повний текст джерелаKęska, Paulina, Joanna Stadnik, Aleksandra Łupawka та Agata Michalska. "Novel α-Glucosidase Inhibitory Peptides Identified In Silico from Dry-Cured Pork Loins with Probiotics through Peptidomic and Molecular Docking Analysis". Nutrients 15, № 16 (2023): 3539. http://dx.doi.org/10.3390/nu15163539.
Повний текст джерелаNishio, Toshiyuki. "Effect of Sugar Hydroxyl Groups on Activities and Specificities of .ALPHA.-Glycosidase and Lipase." Journal of Applied Glycoscience 49, no. 1 (2002): 45–55. http://dx.doi.org/10.5458/jag.49.45.
Повний текст джерелаNishio, Toshiyuki, Wataru Hakamata, Masahiro Ogawa, et al. "Investigations of a Useful .ALPHA.-Glycosidase for the Enzymatic Synthesis of Rare Sugar Oligosaccharides." Journal of Applied Glycoscience 52, no. 2 (2005): 153–60. http://dx.doi.org/10.5458/jag.52.153.
Повний текст джерелаSaniya, A., R. Divya, M. Sharmila, and C. Prakash. "ANTI-DIABETIC AND ANTIMICROBIAL ACTIVITIES OF GRONA TRIFLORA MEDICINAL PLANT." Archives for Technical Sciences 32, no. 1 (2025): 176–87. https://doi.org/10.70102/afts.2025.1732.176.
Повний текст джерелаBolmer, Sally D., and Jerome Kleinerman. "Altered Glycosidase Activity in the Liver of Rats with Galactosamine-Induced Alpha(1)-Antiprotease Deficiency." Enzyme 34, no. 3 (1985): 144–51. http://dx.doi.org/10.1159/000469377.
Повний текст джерелаGopal, B. Anitha, Sridevi A. Singh, and G. Muralikrishna. "Porcine pancreatic alpha amylase and its isoforms—Effect of deglycosylation by peptide-N-glycosidase F." International Journal of Biological Macromolecules 43, no. 2 (2008): 100–105. http://dx.doi.org/10.1016/j.ijbiomac.2008.03.008.
Повний текст джерелаKaraulova, E. P., H. D. Yoon, J. G. Kim, S. H. Park, T. N. Slutskaya, and E. V. Yakush. "Study on biological activity of tissues from bivalve mollusks." Izvestiya TINRO 195 (December 27, 2018): 253–64. http://dx.doi.org/10.26428/1606-9919-2018-195-253-264.
Повний текст джерелаFrengki, Frengki, Deddi Prima, Fatma Sri Wahyuni, et al. "UJI IN VITRO DAN IN SILICO SENYAWA 5,7,2’,5’-TETRAHYDROXY FLAVAN-3-OL TERHADAP ENZIM ALPHA GLUCOSIDASE." Jurnal Fitofarmaka Indonesia 5, no. 2 (2018): 279–83. http://dx.doi.org/10.33096/jffi.v5i2.416.
Повний текст джерелаDonald, A. S. R., and J. Feeney. "Oligosaccharides obtained from a blood-group-Sd(a+) Tamm-Horsfall glycoprotein. An n.m.r. study." Biochemical Journal 236, no. 3 (1986): 821–28. http://dx.doi.org/10.1042/bj2360821.
Повний текст джерелаKeinänen, K. P. "Effect of deglycosylation on the structure and hormone-binding activity of the lutropin receptor." Biochemical Journal 256, no. 3 (1988): 719–24. http://dx.doi.org/10.1042/bj2560719.
Повний текст джерелаKaur, Virender, Kumud Upadhyaya, and Milind Pande. "BIOASSAY-GUIDED EVALUATION OF FICUS SEMICORDATA FOR ANTIDIABETIC ACTIVITY." International Journal of Pharmacy and Pharmaceutical Sciences 9, no. 3 (2017): 71. http://dx.doi.org/10.22159/ijpps.2017v9i3.16441.
Повний текст джерелаHosie, L., та M. L. Sinnott. "Effects of deuterium substitution α and β to the reaction centre, 18O substitution in the leaving group, and aglycone acidity on hydrolyses of aryl glucosides and glucosyl pyridinium ions by yeast α-glucosidase. A probable failure of the antiperiplanar-lone-pair hypothesis in glycosidase catalysis". Biochemical Journal 226, № 2 (1985): 437–46. http://dx.doi.org/10.1042/bj2260437.
Повний текст джерелаTerman, B. I., J. F. Reece, R. D. Brown та P. A. Insel. "The oligosaccharide component of α 1-adrenergic receptors from BC3H1 and DDT1 muscle cells. Studies with glycosidases and photoaffinity labelling of intact cells". Biochemical Journal 253, № 2 (1988): 363–70. http://dx.doi.org/10.1042/bj2530363.
Повний текст джерелаDohi, T., A. Nishikawa, I. Ishizuka, et al. "Substrate specificity and distribution of UDP-GalNAc:sialylparagloboside N-acetylgalactosaminyltransferase in the human stomach." Biochemical Journal 288, no. 1 (1992): 161–65. http://dx.doi.org/10.1042/bj2880161.
Повний текст джерелаDecastel, M., M. A. Doyennette-Moyne, E. Gouet, M. Aubery, and P. Codogno. "Biosynthesis, surface expression and function of the fibronectin receptor after rat liver cell transformation to tumorigenicity." Biochemical Journal 291, no. 1 (1993): 247–55. http://dx.doi.org/10.1042/bj2910247.
Повний текст джерелаMcGuire, E. J., R. Kerlin, J. J. Cebra, and S. Roth. "A human milk galactosyltransferase is specific for secreted, but not plasma, IgA." Journal of Immunology 143, no. 9 (1989): 2933–38. http://dx.doi.org/10.4049/jimmunol.143.9.2933.
Повний текст джерелаMach, L., W. Scherf, M. Ammann, et al. "Purification and partial characterization of a novel lectin from elder (Sambucus nigra L.) fruit." Biochemical Journal 278, no. 3 (1991): 667–71. http://dx.doi.org/10.1042/bj2780667.
Повний текст джерелаSato, N., C. Caux, T. Kitamura, et al. "Expression and factor-dependent modulation of the interleukin-3 receptor subunits on human hematopoietic cells." Blood 82, no. 3 (1993): 752–61. http://dx.doi.org/10.1182/blood.v82.3.752.752.
Повний текст джерелаSato, N., C. Caux, T. Kitamura, et al. "Expression and factor-dependent modulation of the interleukin-3 receptor subunits on human hematopoietic cells." Blood 82, no. 3 (1993): 752–61. http://dx.doi.org/10.1182/blood.v82.3.752.bloodjournal823752.
Повний текст джерелаDahms, N. M., and G. W. Hart. "Lymphocyte function-associated antigen 1 (LFA-1) contains sulfated N-linked oligosaccharides." Journal of Immunology 134, no. 6 (1985): 3978–86. http://dx.doi.org/10.4049/jimmunol.134.6.3978.
Повний текст джерелаKiyohara, T., J. W. Dennis, R. J. Boegman, and J. C. Roder. "An exoglycosidase-sensitive triggering site on NK cells which is coupled to transmethylation of membrane phospholipids." Journal of Immunology 135, no. 1 (1985): 659–64. http://dx.doi.org/10.4049/jimmunol.135.1.659.
Повний текст джерелаDogara, Abdulrahaman Mahmoud, Sawsan Sadiq Al-Rawi, Ateeq Ahmed Al-Zahrani, et al. "Biological Activities, Chemical Composition and Molecular Docking of Urelytrum giganteum Pilg." Acta Chimica Slovenica 72, no. 1 (2025): 107–18. https://doi.org/10.17344/acsi.2024.9077.
Повний текст джерелаPetäjä-Repo, U. E., W. E. Merz, and H. J. Rajaniemi. "Significance of the carbohydrate moiety of the rat ovarian luteinizing-hormone/chorionic-gonadotropin receptor for ligand-binding specificity and signal transduction." Biochemical Journal 292, no. 3 (1993): 839–44. http://dx.doi.org/10.1042/bj2920839.
Повний текст джерелаHolt, G. D., S. J. Swiedler, J. H. Freed, and G. W. Hart. "Murine Ia-associated invariant chain's processing to complex oligosaccharide forms and its dissociation from the I-Ak complex." Journal of Immunology 135, no. 1 (1985): 399–407. http://dx.doi.org/10.4049/jimmunol.135.1.399.
Повний текст джерелаIto, N., K. Nishi, M. Nakajima, Y. Okamura, and T. Hirota. "Histochemical analysis of the chemical structure of blood group-related carbohydrate chains in serous cells of human submandibular glands using lectin staining and glycosidase digestion." Journal of Histochemistry & Cytochemistry 37, no. 7 (1989): 1115–24. http://dx.doi.org/10.1177/37.7.2499620.
Повний текст джерелаNajjar, S. M., L. T. Hampp, R. Rabkin, and G. M. Gray. "Sucrase-alpha-dextrinase in diabetic BioBreed rats: reversible alteration of subunit structure." American Journal of Physiology-Gastrointestinal and Liver Physiology 260, no. 2 (1991): G275—G283. http://dx.doi.org/10.1152/ajpgi.1991.260.2.g275.
Повний текст джерелаLityńska, Anna, Ewa Pocheć, Dorota Hoja-Lukowicz, et al. "The structure of the oligosaccharides of alpha3beta1 integrin from human ureter epithelium (HCV29) cell line." Acta Biochimica Polonica 49, no. 2 (2002): 491–500. http://dx.doi.org/10.18388/abp.2002_3808.
Повний текст джерелаAxamawaty, M. T. H., G. W. J. Fleet, K. A. Hannah, S. K. Namgoong та M. L. Sinnott. "Inhibition of the α-l-arabinofuranosidase III of Monilinia fructigena by 1,4-dideoxy-1,4-imino-l-threitol and 1,4-dideoxy-1,4-imino-l-arabinitol". Biochemical Journal 266, № 1 (1990): 245–49. http://dx.doi.org/10.1042/bj2660245.
Повний текст джерелаP. Samba Siva Rao, P. Samba Siva Rao, Dr G. Nagaraju Dr. G. Nagaraju, A. Sanjay A. Sanjay, et al. "Review on Formulation and Evaluation of Voglibose Mouth Dissolving Tablets." International Journal of Pharmaceutical Research and Applications 10, no. 2 (2025): 309–17. https://doi.org/10.35629/4494-1002309317.
Повний текст джерелаMaecker, H. T., and R. Levy. "Spontaneous T cell antigen receptor variants of a human T leukemia cell line." Journal of Immunology 141, no. 9 (1988): 2994–3002. http://dx.doi.org/10.4049/jimmunol.141.9.2994.
Повний текст джерелаPriyanka. "Anti-Diabetic Activity of Selected Medicinal Plant Extracts Used By Tribals in the Adilabad District of Telangana State By in Vitro." Biolife 11, no. 2 (2023): 72–78. https://doi.org/10.5281/zenodo.7855153.
Повний текст джерелаThibaudeau, K., L. Borche, JP Soulillou, and D. Blanchard. "Characterization of porcine platelet glycoproteins recognized by human natural "anti-gal" antibodies." Blood 87, no. 11 (1996): 4636–42. http://dx.doi.org/10.1182/blood.v87.11.4636.bloodjournal87114636.
Повний текст джерелаHidaka, H., and N. H. Fidge. "Affinity purification of the hepatic high-density lipoprotein receptor identifies two acidic glycoproteins and enables further characterization of their binding properties." Biochemical Journal 284, no. 1 (1992): 161–67. http://dx.doi.org/10.1042/bj2840161.
Повний текст джерелаDe Oliveira, Letícia Gomes, Júlia Carneiro Almeida, Carlos Alberto Mourão Júnior, and Ana Eliza Andreazzi. "Efeitos dos inibidores de alfa-amilase e alfa-glicosidase no tratamento da obesidade: uma revisão integrativa / Effects of alpha-amylase and alpha-glycosidase inhibitors on obesity treatment: an integrative review." Brazilian Journal of Health Review 4, no. 6 (2021): 26125–41. http://dx.doi.org/10.34119/bjhrv4n6-200.
Повний текст джерелаBerry, Leslie R., and Anthony K. C. Chan. "Age-Related Differences in the Glycosylation of Anticoagulant Protein C." Blood 112, no. 11 (2008): 2031. http://dx.doi.org/10.1182/blood.v112.11.2031.2031.
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