Alpha-amylase (Uzbek Wikipedia)

Analysis of information sources in references of the Wikipedia article "Alpha-amylase" in Uzbek language version.

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archive.org

doi.org

  • „Passage of salivary amylase through the stomach in humans“. Digestive Diseases and Sciences. 32-jild, № 10. October 1987. 1097–103-bet. doi:10.1007/bf01300195. PMID 3652896.
  • „Starch and glucose oligosaccharides protect salivary-type amylase activity at acid pH“. The American Journal of Physiology. 254-jild, № 5 Pt 1. May 1988. G775–80-bet. doi:10.1152/ajpgi.1988.254.5.G775. PMID 2452576.
  • „Diet and the evolution of human amylase gene copy number variation“. Nature Genetics. 39-jild, № 10. October 2007. 1256–60-bet. doi:10.1038/ng2123. PMC 2377015. PMID 17828263. Manba xatosi: Invalid <ref> tag; name "pmid17828263" defined multiple times with different content
  • „The relationship between salivary biomarkers and state-trait anxiety inventory score under mental arithmetic stress: a pilot study“. Anesthesia and Analgesia. 101-jild, № 6. December 2005. 1873–6-bet. doi:10.1213/01.ANE.0000184196.60838.8D. PMID 16301277.
  • „Salivary alpha-amylase in biobehavioral research: recent developments and applications“. Annals of the New York Academy of Sciences. 1098-jild. March 2007. 122–44-bet. doi:10.1196/annals.1384.008. PMID 17332070.
  • „Salivary alpha-amylase as a non-invasive biomarker for the sympathetic nervous system: current state of research“. Psychoneuroendocrinology. 34-jild, № 4. May 2009. 486–96-bet. doi:10.1016/j.psyneuen.2009.01.014. PMID 19249160.
  • „Approaches to Dispersing Medical Biofilms“. Microorganisms. 5-jild, № 2. April 2017. 15-bet. doi:10.3390/microorganisms5020015. PMC 5488086. PMID 28368320.
  • „Glycoside Hydrolases Degrade Polymicrobial Bacterial Biofilms in Wounds“. Antimicrobial Agents and Chemotherapy. 61-jild, № 2. February 2017. AAC.01998–16-bet. doi:10.1128/AAC.01998-16. PMC 5278739. PMID 27872074.
  • „Binding of Tris to Bacillus licheniformis alpha-amylase can affect its starch hydrolysis activity“. Protein and Peptide Letters. 15-jild, № 2. 2008. 212–4-bet. doi:10.2174/092986608783489616. PMID 18289113.
  • „Crystal structures of the psychrophilic alpha-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor“. Protein Science. 7-jild, № 3. March 1998. 564–72-bet. doi:10.1002/pro.5560070304. PMC 2143949. PMID 9541387.
  • Pimstone, Neville R. (1964). „A Study of the Starch-Iodine Complex: A Modified Colourimetric Micro Determination of Amylase in Biological Fluids“. Clinical Chemistry. American Association for Clinical Chemistry. 891–906-bet. doi:10.1093/clinchem/10.10.891. 14–may 2022–yilda asl nusxadan arxivlandi.{{cite magazine}}: CS1 maint: date format ()
  • „Complexes of Thermoactinomyces vulgaris R-47 alpha-amylase 1 and pullulan model oligossacharides provide new insight into the mechanism for recognizing substrates with alpha-(1,6) glycosidic linkages“. The FEBS Journal. 272-jild, № 23. December 2005. 6145–53-bet. doi:10.1111/j.1742-4658.2005.05013.x. PMID 16302977.
  • „Molecular structure of a barley alpha-amylase-inhibitor complex: implications for starch binding and catalysis“. Journal of Molecular Biology. 278-jild, № 1. April 1998. 205–17-bet. doi:10.1006/jmbi.1998.1683. PMID 9571044.
  • „Crystal and molecular structure of barley alpha-amylase“. Journal of Molecular Biology. 239-jild, № 1. May 1994. 104–21-bet. doi:10.1006/jmbi.1994.1354. PMID 8196040.
  • „Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 A resolution“. Journal of Molecular Biology. 246-jild, № 4. March 1995. 545–59-bet. doi:10.1006/jmbi.1994.0106. PMID 7877175.

lsbu.ac.uk

www1.lsbu.ac.uk

nih.gov

pubmed.ncbi.nlm.nih.gov

  • „Passage of salivary amylase through the stomach in humans“. Digestive Diseases and Sciences. 32-jild, № 10. October 1987. 1097–103-bet. doi:10.1007/bf01300195. PMID 3652896.
  • „Starch and glucose oligosaccharides protect salivary-type amylase activity at acid pH“. The American Journal of Physiology. 254-jild, № 5 Pt 1. May 1988. G775–80-bet. doi:10.1152/ajpgi.1988.254.5.G775. PMID 2452576.
  • „Diet and the evolution of human amylase gene copy number variation“. Nature Genetics. 39-jild, № 10. October 2007. 1256–60-bet. doi:10.1038/ng2123. PMC 2377015. PMID 17828263. Manba xatosi: Invalid <ref> tag; name "pmid17828263" defined multiple times with different content
  • „The relationship between salivary biomarkers and state-trait anxiety inventory score under mental arithmetic stress: a pilot study“. Anesthesia and Analgesia. 101-jild, № 6. December 2005. 1873–6-bet. doi:10.1213/01.ANE.0000184196.60838.8D. PMID 16301277.
  • „Salivary alpha-amylase in biobehavioral research: recent developments and applications“. Annals of the New York Academy of Sciences. 1098-jild. March 2007. 122–44-bet. doi:10.1196/annals.1384.008. PMID 17332070.
  • „Salivary alpha-amylase as a non-invasive biomarker for the sympathetic nervous system: current state of research“. Psychoneuroendocrinology. 34-jild, № 4. May 2009. 486–96-bet. doi:10.1016/j.psyneuen.2009.01.014. PMID 19249160.
  • „Approaches to Dispersing Medical Biofilms“. Microorganisms. 5-jild, № 2. April 2017. 15-bet. doi:10.3390/microorganisms5020015. PMC 5488086. PMID 28368320.
  • „Glycoside Hydrolases Degrade Polymicrobial Bacterial Biofilms in Wounds“. Antimicrobial Agents and Chemotherapy. 61-jild, № 2. February 2017. AAC.01998–16-bet. doi:10.1128/AAC.01998-16. PMC 5278739. PMID 27872074.
  • „Binding of Tris to Bacillus licheniformis alpha-amylase can affect its starch hydrolysis activity“. Protein and Peptide Letters. 15-jild, № 2. 2008. 212–4-bet. doi:10.2174/092986608783489616. PMID 18289113.
  • „Crystal structures of the psychrophilic alpha-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor“. Protein Science. 7-jild, № 3. March 1998. 564–72-bet. doi:10.1002/pro.5560070304. PMC 2143949. PMID 9541387.
  • „Complexes of Thermoactinomyces vulgaris R-47 alpha-amylase 1 and pullulan model oligossacharides provide new insight into the mechanism for recognizing substrates with alpha-(1,6) glycosidic linkages“. The FEBS Journal. 272-jild, № 23. December 2005. 6145–53-bet. doi:10.1111/j.1742-4658.2005.05013.x. PMID 16302977.
  • „Molecular structure of a barley alpha-amylase-inhibitor complex: implications for starch binding and catalysis“. Journal of Molecular Biology. 278-jild, № 1. April 1998. 205–17-bet. doi:10.1006/jmbi.1998.1683. PMID 9571044.
  • „Crystal and molecular structure of barley alpha-amylase“. Journal of Molecular Biology. 239-jild, № 1. May 1994. 104–21-bet. doi:10.1006/jmbi.1994.1354. PMID 8196040.
  • „Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 A resolution“. Journal of Molecular Biology. 246-jild, № 4. March 1995. 545–59-bet. doi:10.1006/jmbi.1994.0106. PMID 7877175.

ncbi.nlm.nih.gov

  • „Diet and the evolution of human amylase gene copy number variation“. Nature Genetics. 39-jild, № 10. October 2007. 1256–60-bet. doi:10.1038/ng2123. PMC 2377015. PMID 17828263. Manba xatosi: Invalid <ref> tag; name "pmid17828263" defined multiple times with different content
  • „Approaches to Dispersing Medical Biofilms“. Microorganisms. 5-jild, № 2. April 2017. 15-bet. doi:10.3390/microorganisms5020015. PMC 5488086. PMID 28368320.
  • „Glycoside Hydrolases Degrade Polymicrobial Bacterial Biofilms in Wounds“. Antimicrobial Agents and Chemotherapy. 61-jild, № 2. February 2017. AAC.01998–16-bet. doi:10.1128/AAC.01998-16. PMC 5278739. PMID 27872074.
  • „Crystal structures of the psychrophilic alpha-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor“. Protein Science. 7-jild, № 3. March 1998. 564–72-bet. doi:10.1002/pro.5560070304. PMC 2143949. PMID 9541387.

oup.com

academic.oup.com

perten.com

snl.no

sml.snl.no

  • „Amylase“. Store Medisinske Leksikon. Store Norske Leksikon. Qaraldi: 24-yanvar 2021-yil.

web.archive.org

worthington-biochem.com