Littérature scientifique sur le sujet « Histidine decarboxyase »
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Articles de revues sur le sujet "Histidine decarboxyase"
MORII, HIDEAKI, et KENTARO KASAMA. « Activity of Two Histidine Decarboxylases from Photobacterium phosphoreum at Different Temperatures, pHs, and NaCl Concentrations ». Journal of Food Protection 67, no 8 (1 août 2004) : 1736–42. http://dx.doi.org/10.4315/0362-028x-67.8.1736.
Texte intégralAkirthasary, Desty. « REVIEW ARTIKEL : ENZIM L-HISTIDIN DEKARBOKSILASE DAN MEKANISME PENGHAMBATAN ». Unesa Journal of Chemistry 10, no 2 (30 mai 2021) : 147–57. http://dx.doi.org/10.26740/ujc.v10n2.p147-157.
Texte intégralWENDAKOON, CHITRA N., et MORIHIKO SAKAGUCHI. « Inhibition of Amino Acid Decarboxylase Activity of Enterobacter aerogenes by Active Components in Spices ». Journal of Food Protection 58, no 3 (1 mars 1995) : 280–83. http://dx.doi.org/10.4315/0362-028x-58.3.280.
Texte intégralKomori, Hirofumi, Yoko Nitta, Hiroshi Ueno et Yoshiki Higuchi. « Structural basis for the histamine synthesis by human histidine decarboxylase ». Acta Crystallographica Section A Foundations and Advances 70, a1 (5 août 2014) : C458. http://dx.doi.org/10.1107/s2053273314095412.
Texte intégralde las RIVAS, BLANCA, ÁNGELA MARCOBAL, ALFONSO V. CARRASCOSA et ROSARIO MUÑOZ. « PCR Detection of Foodborne Bacteria Producing the Biogenic Amines Histamine, Tyramine, Putrescine, and Cadaverine ». Journal of Food Protection 69, no 10 (1 octobre 2006) : 2509–14. http://dx.doi.org/10.4315/0362-028x-69.10.2509.
Texte intégralSköldberg, Filip, Fredrik Rorsman, Jaakko Perheentupa, Mona Landin-Olsson, Eystein S. Husebye, Jan Gustafsson et Olle Kämpe. « Analysis of Antibody Reactivity against Cysteine Sulfinic Acid Decarboxylase, A Pyridoxal Phosphate-Dependent Enzyme, in Endocrine Autoimmune Disease ». Journal of Clinical Endocrinology & ; Metabolism 89, no 4 (1 avril 2004) : 1636–40. http://dx.doi.org/10.1210/jc.2003-031161.
Texte intégralBurdychová, Radka. « Identification and typization of bacteria of the genus Enterococcus supposed to be used for the production of functional foods ». Acta Universitatis Agriculturae et Silviculturae Mendelianae Brunensis 55, no 2 (2007) : 9–14. http://dx.doi.org/10.11118/actaun200755020009.
Texte intégralPak, Won-Min, Koth-Bong-Woo-Ri Kim, Min-Ji Kim, Ji-Hye Park, Nan-Young Bae, Sun-Hee Park et Dong-Hyun Ahn. « Effects of Thermal Treatments on Inactivation of Histidine Decarboxylase from Morganella morganii and Photobacterium phosphoreum ». Journal of the Korean Society of Food Science and Nutrition 45, no 3 (31 mars 2016) : 396–401. http://dx.doi.org/10.3746/jkfn.2016.45.3.396.
Texte intégralCOSTANTINI, ANTONELLA, MANUELA CERSOSIMO, VINCENZO DEL PRETE et EMILIA GARCIA-MORUNO. « Production of Biogenic Amines by Lactic Acid Bacteria : Screening by PCR, Thin-Layer Chromatography, and High-Performance Liquid Chromatography of Strains Isolated from Wine and Must ». Journal of Food Protection 69, no 2 (1 février 2006) : 391–96. http://dx.doi.org/10.4315/0362-028x-69.2.391.
Texte intégralFLEMING, John V., Francisca SÁNCHEZ-JIMÉNEZ, Aurelio A. MOYA-GARCÍA, Michael R. LANGLOIS et Timothy C. WANG. « Mapping of catalytically important residues in the rat l-histidine decarboxylase enzyme using bioinformatic and site-directed mutagenesis approaches ». Biochemical Journal 379, no 2 (15 avril 2004) : 253–61. http://dx.doi.org/10.1042/bj20031525.
Texte intégralThèses sur le sujet "Histidine decarboxyase"
Furuta, Kazuyuki. « Regulation of histamine synthesis through post-translational processing of histidine decarboxylase ». 京都大学 (Kyoto University), 2006. http://hdl.handle.net/2433/144287.
Texte intégralSantibanez, Rodrigo. « The effect of high hydrostatic pressure on histidine decarboxylase and histamine forming bacteria / ». Thesis, McGill University, 2007. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=101172.
Texte intégralCommercial histidine decarboxylase suspended in different media (buffer solution and fish slurry with and without added histidine) was submitted to different high pressure treatments (200--400 MPa) with distinct time durations (0--60 min) at room temperature (20°C--25°C). Enzymatic activity of pressure treated and control samples were then compared by measuring histamine formation. Results were similar in all media; a 200 MPa treatment increased the enzymatic activity a little more than 20% as time increased; a 300 MPa treatment increased activity over 20% at first, followed by a decrease in activity as time increased only to reach a level of residual activity similar or only slightly lower than control samples; and a 400 MPa treatment reduced enzyme activity as time increased to a level of 55% residual activity in a buffer solution where the greatest inactivation was observed.
Enzyme activation and inactivation were affected by a dual effect attributed to a pulse effect, which caused a shift in activity and was independent of the length of the treatment, and a pressure-hold effect, during which activation or inactivation followed first order kinetics. The enzyme appeared highly resistant to pressure in all media as observed from D-values (>2700 min) and pressure sensitivity of destruction rate (zp) values (>500 MPa).
Inactivation of non-pathogen histamine forming bacteria (HFB) Escherichia coli K12 and Bacillus megaterium was evaluated by inoculating cultures in a fish tissue homogenate. Surviving colonies were enumerated after the treatments observing inactivation described by the same dual effect described earlier. Pressures above 300 MPa achieved a significant destruction of E. coli K12 (> 4 log-cycles) while B. megaterium appeared highly resistant for only a 2 log-cycle reduction was observed after at the highest pressure treatment conditions (400 MPa, 20 min).
D-values for both microorganisms decreased as pressure increased being significantly smaller for E. coli K 12, which also appeared to be more sensitive to pressure changes as observed from the zp values (zp = 151.51 MPa and zp = 909.10 MPa for E. coli and B. megaterium respectively. Inactivation caused by the pulse effect appeared very effective for both microorganisms as pressure increased, particularly at 400 MPa (PE > 1.25).
Sköldberg, Filip. « Studies of Autoantibodies in Systemic and Organ-Specific Autoimmune Disease ». Doctoral thesis, Uppsala universitet, Institutionen för medicinska vetenskaper, 2003. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-3421.
Texte intégralHöcker, Michael. « Differentielle Regulation von Schlüsselgenen der gastralen Säuresekretion durch Gastrin, oxidativen Stress und Helicobacter pylori ». Doctoral thesis, Humboldt-Universität zu Berlin, Medizinische Fakultät - Universitätsklinikum Charité, 2002. http://dx.doi.org/10.18452/13811.
Texte intégralTranscriptional activation of the genes encoding histidine decarboxylase and chromogranin A represents a key mechanism of gastrin-dependent acid regulation and also appears to be involved in the pathogenesis of gastroduodenal ulcer disease. Our results for the first time identify the molecular mechanisms underlying gastrin-dependent activation of both genes, and define the transcription factors, regulatory DNA elements and signal transduction pathways involved in this process. Furthermore, transgenic studies confirmed the principle of gastrin-dependent transcriptional activation of the chromogranin A gene in vivo, and demonstrated neuroendocrine-specific expression of a 4.8kB-CgA promotor fragment. In addition, the pathobiological stimuli oxidative stress and H. pylori were molecularly characterized regarding their activating effects on the key gene of gastric histamine sythesis. These results provide potential mechanisms for the interaction of both stimuli with regulatory circuits of gastric acid secretion, and can probably contribute via definition of new molecular targets to the development of inovative therapeutic strategies.
Rossignoli, Giada. « Aromatic amino acids decarboxylase and histidine decarboxylase : deep functional investigations give insights into pathophysiological mechanisms with possible therapeutic implications ». Doctoral thesis, 2019. http://hdl.handle.net/11562/995224.
Texte intégralFernandes, Henrique Silva. « Computational studies addressed to Histidine decarboxylase ». Master's thesis, 2016. https://repositorio-aberto.up.pt/handle/10216/89937.
Texte intégralFernandes, Henrique Silva. « Computational studies addressed to Histidine decarboxylase ». Dissertação, 2016. https://repositorio-aberto.up.pt/handle/10216/89937.
Texte intégralAbell, Lynn M. « Isotope effects on pyruvoyl and pyridoxal 5'-phosphate dependent histidine decarboxylases a comparison of cofactor energetics / ». 1987. http://catalog.hathitrust.org/api/volumes/oclc/16948155.html.
Texte intégralTypescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 204-211).
Livres sur le sujet "Histidine decarboxyase"
Barancin, Courtney Ellen. Vibrio anguillarum histidine decarboxylase : Role in histamine biosynthesis and iron acquisition. 1996.
Trouver le texte intégralChapitres de livres sur le sujet "Histidine decarboxyase"
Schomburg, Dietmar, et Margit Salzmann. « Histidine decarboxylase ». Dans Enzyme Handbook 1, 83–87. Berlin, Heidelberg : Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-86605-0_20.
Texte intégralSchayer, Richard W. « Determination of Histidine Decarboxylase Activity ». Dans Methods of Biochemical Analysis, 273–91. Hoboken, NJ, USA : John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470110348.ch5.
Texte intégralWatanabe, T., Y. Taguchi, K. Maeyama et H. Wada. « Formation of Histamine : Histidine Decarboxylase ». Dans Histamine and Histamine Antagonists, 145–63. Berlin, Heidelberg : Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-75840-9_13.
Texte intégralTanaka, Satoshi, et Atsushi Ichikawa. « Regulation of Mammalian Histamine Synthesis : Histidine Decarboxylase ». Dans Biomedical Aspects of Histamine, 15–30. Dordrecht : Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-90-481-9349-3_2.
Texte intégralHackert, M. L., K. Clinger, S. R. Ernst, E. H. Parks et E. E. Snell. « Structures of Pyruvoyl-Dependent Histidine Decarboxylase and Mutant-3 Prohistidine Decarboxylase from Lactobacillus 30A ». Dans Crystallography in Molecular Biology, 403–11. Boston, MA : Springer US, 1987. http://dx.doi.org/10.1007/978-1-4684-5272-3_37.
Texte intégralOhtsu, Hiroshi. « Histamine Synthesis and Lessons Learned from Histidine Decarboxylase Deficient Mice ». Dans Advances in Experimental Medicine and Biology, 21–31. Boston, MA : Springer US, 2010. http://dx.doi.org/10.1007/978-1-4419-8056-4_3.
Texte intégralWada, H., M. Ando-Yamamoto, H. Hayashi, Y. Taguchi, H. Fukui et T. Watanabe. « Demonstration of Immunochemical Cross-Reactivity of Dopa Decarboxylase and Histidine Decarboxylase Using Antibodies Against the Two Enzymes ». Dans Biochemistry of Vitamin B6, 55–58. Basel : Birkhäuser Basel, 1987. http://dx.doi.org/10.1007/978-3-0348-9308-4_11.
Texte intégralPanula, P., O. Häppölä, T. Watanabe, H. Wada et H. Päivärinta. « Immunohistochemistry of Histamine and Histidine Decarboxylase in SIF Cells and Intestinal Nerves ». Dans Histochemistry and Cell Biology of Autonomic Neurons and Paraganglia, 51–55. Berlin, Heidelberg : Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-72749-8_9.
Texte intégralShan, Ling, Ai-Min Bao et Dick F. Swaab. « Changes in Histidine Decarboxylase, Histamine N-Methyltransferase and Histamine Receptors in Neuropsychiatric Disorders ». Dans Handbook of Experimental Pharmacology, 259–76. Cham : Springer International Publishing, 2017. http://dx.doi.org/10.1007/164_2016_125.
Texte intégralPittenger, Christopher. « Histidine Decarboxylase Knockout Mice as a Model of the Pathophysiology of Tourette Syndrome and Related Conditions ». Dans Handbook of Experimental Pharmacology, 189–215. Cham : Springer International Publishing, 2017. http://dx.doi.org/10.1007/164_2016_127.
Texte intégralActes de conférences sur le sujet "Histidine decarboxyase"
Schulman, ES, SC Pugliese, S. Ansaloni, P. Mannam, H. Nishi, M. Bouchard et SA Saunders. « RNA Interference-Induced Gene Silencing of Histidine Decarboxylase Produces Human Mast Cells Deficient in Histamine. » Dans American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a3708.
Texte intégralChen, Xiaowei, Yoshihiro Takemoto, Karan K. Nagar, Timothy H. Chu, Zhengyu Jiang, Wenju Chang, Richard A. Friedman, Yagnesh H. Tailor, Daniel L. Worthley et Timothy C. Wang. « Abstract LB-272 : Histidine decarboxylase (Hdc)-expressing myeloid cells support Foxp3+ Treg cells and promote colorectal cancer progression ». Dans Proceedings : AACR 107th Annual Meeting 2016 ; April 16-20, 2016 ; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-lb-272.
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