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><channel><title>Natural Sciences Bibliography &#187; Kinase</title> <atom:link href="http://scien.net/category/enzyme/kinase/feed" rel="self" type="application/rss+xml" /><link>http://scien.net</link> <description>200,000 References and 140,000 Tags</description> <lastBuildDate>Mon, 20 May 2013 03:38:33 +0000</lastBuildDate> <language>en-US</language> <sy:updatePeriod>hourly</sy:updatePeriod> <sy:updateFrequency>1</sy:updateFrequency> <generator>http://wordpress.org/?v=3.5.1</generator> <item><title>Nucleoside diphosphate kinase from pea chloroplasts: purification, cDNA cloning and import into chloroplasts</title><link>http://scien.net/enzyme/kinase/nucleoside-diphosphate-kinase-from-pea-chloroplasts-purification-cdna-cloning-and-import-into-chloroplasts</link> <comments>http://scien.net/enzyme/kinase/nucleoside-diphosphate-kinase-from-pea-chloroplasts-purification-cdna-cloning-and-import-into-chloroplasts#comments</comments> <pubDate>Mon, 20 May 2013 03:11:32 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[ndpk]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/nucleoside-diphosphate-kinase-from-pea-chloroplasts-purification-cdna-cloning-and-import-into-chloroplasts</guid> <description><![CDATA[Lubeck, J.; Soll, J., 1995: Nucleoside diphosphate kinase from pea chloroplasts: purification, cDNA cloning and import into chloroplasts. Planta 196(4): 668-673 Nucleoside diphosphate kinase (Ndpk; Ec 2.7.4.6) was enriched 1900-fold from purified pea (Pisum sativum L. cv. Golf.) chloroplasts. The active enzyme preparation contained two polypeptides of apparent molecular weight 18.5 kDa and 17.4 kDa. [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/nucleoside-diphosphate-kinase-from-pea-chloroplasts-purification-cdna-cloning-and-import-into-chloroplasts/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Nuclear casein-kinase II type activity in pea root tip cells during germination</title><link>http://scien.net/enzyme/kinase/nuclear-casein-kinase-ii-type-activity-in-pea-root-tip-cells-during-germination</link> <comments>http://scien.net/enzyme/kinase/nuclear-casein-kinase-ii-type-activity-in-pea-root-tip-cells-during-germination#comments</comments> <pubDate>Mon, 20 May 2013 03:11:10 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[ckii]]></category> <category><![CDATA[decapeptide]]></category> <category><![CDATA[rrreeeteee]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/nuclear-casein-kinase-ii-type-activity-in-pea-root-tip-cells-during-germination</guid> <description><![CDATA[Brusa, Paola; Nannariello, Lorenzo; Sparvoli, Elio, 1994: Nuclear casein-kinase II type activity in pea root tip cells during germination. Plant Science (limerick). 102(1): 31-40 A protein kinase activity having the same characteristics as that of casein kinase Ii was detected in pea nuclei isolated from meristematic root tips at different times of germination. Like casein [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/nuclear-casein-kinase-ii-type-activity-in-pea-root-tip-cells-during-germination/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Molecular genetics of the maize (Zea mays L.) aspartate kinase-homoserine dehydrogenase gene family</title><link>http://scien.net/enzyme/kinase/molecular-genetics-of-the-maize-zea-mays-l-aspartate-kinase-homoserine-dehydrogenase-gene-family</link> <comments>http://scien.net/enzyme/kinase/molecular-genetics-of-the-maize-zea-mays-l-aspartate-kinase-homoserine-dehydrogenase-gene-family#comments</comments> <pubDate>Mon, 20 May 2013 02:43:28 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[hsdh]]></category> <category><![CDATA[monofunctional]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/molecular-genetics-of-the-maize-zea-mays-l-aspartate-kinase-homoserine-dehydrogenase-gene-family</guid> <description><![CDATA[Muehlbauer, G. J.; Somers, D. A.; Matthews, B. F.; Gengenbach, B. G., 1994: Molecular genetics of the maize (Zea mays L.) aspartate kinase-homoserine dehydrogenase gene family. Plant Physiology 106(4): 1303-1312 Aspartate kinase (Ak) and homoserine dehydrogenase (Hsdh) are enzymes in the aspartate-derived amino acid biosynthetic pathway. Recent biochemical evidence indicates that an Ak-Hsdh bifunctional enzyme [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/molecular-genetics-of-the-maize-zea-mays-l-aspartate-kinase-homoserine-dehydrogenase-gene-family/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Modulation of the molecular organization and activity of casein kinase 2 by naturally occurring polyamines</title><link>http://scien.net/enzyme/kinase/modulation-of-the-molecular-organization-and-activity-of-casein-kinase-2-by-naturally-occurring-polyamines</link> <comments>http://scien.net/enzyme/kinase/modulation-of-the-molecular-organization-and-activity-of-casein-kinase-2-by-naturally-occurring-polyamines#comments</comments> <pubDate>Mon, 20 May 2013 02:38:23 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[protomers]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/modulation-of-the-molecular-organization-and-activity-of-casein-kinase-2-by-naturally-occurring-polyamines</guid> <description><![CDATA[Leroy, Didier; Valero, Emmanuelle; Filhol, Odile; Heriche, Jean Karim; Goldberg, Yves; Chambaz, Edmond M.; Cochet, Claude, 1994: Modulation of the molecular organization and activity of casein kinase 2 by naturally occurring polyamines. Cellular &#038; Molecular Biology Research. 40(5-6): 441-453 Polyamines have been reported to stimulate casein kinase 2 (Ck2) in vitro. We have shown that [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/modulation-of-the-molecular-organization-and-activity-of-casein-kinase-2-by-naturally-occurring-polyamines/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Metabolic fate of adenosine and purine metabolism enzymes in young plants of peach tree</title><link>http://scien.net/enzyme/kinase/metabolic-fate-of-adenosine-and-purine-metabolism-enzymes-in-young-plants-of-peach-tree</link> <comments>http://scien.net/enzyme/kinase/metabolic-fate-of-adenosine-and-purine-metabolism-enzymes-in-young-plants-of-peach-tree#comments</comments> <pubDate>Mon, 20 May 2013 02:23:54 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[aminohydrolase]]></category> <category><![CDATA[batsch]]></category> <category><![CDATA[nucleosidase]]></category> <category><![CDATA[radiolabelling]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/metabolic-fate-of-adenosine-and-purine-metabolism-enzymes-in-young-plants-of-peach-tree</guid> <description><![CDATA[Le Floc&#8217;h, Francois; Faye, Florence, 1995: Metabolic fate of adenosine and purine metabolism enzymes in young plants of peach tree. Journal Of Plant Physiology. 145(4): 398-404 Extracts of young plants of peach tree, Prunus persica L. Batsch, exhibited the ability to recycle adenosine into adenine nucleotides either by phosphorylation into Amp by a very active [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/metabolic-fate-of-adenosine-and-purine-metabolism-enzymes-in-young-plants-of-peach-tree/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Mechanism for sodium bicarbonate inhibition of trichothecene biosynthesis in Fusarium tricinctum</title><link>http://scien.net/enzyme/kinase/mechanism-for-sodium-bicarbonate-inhibition-of-trichothecene-biosynthesis-in-fusarium-tricinctum</link> <comments>http://scien.net/enzyme/kinase/mechanism-for-sodium-bicarbonate-inhibition-of-trichothecene-biosynthesis-in-fusarium-tricinctum#comments</comments> <pubDate>Mon, 20 May 2013 02:20:58 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[biosynthesized]]></category> <category><![CDATA[furanone]]></category> <category><![CDATA[hydroy]]></category> <category><![CDATA[mevalonic]]></category> <category><![CDATA[pentenoic]]></category> <category><![CDATA[trichothecene]]></category> <category><![CDATA[tricinctum]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/mechanism-for-sodium-bicarbonate-inhibition-of-trichothecene-biosynthesis-in-fusarium-tricinctum</guid> <description><![CDATA[Roinestad, Ks; Montville, Tj; Rosen, Jd, 1994: Mechanism for sodium bicarbonate inhibition of trichothecene biosynthesis in Fusarium tricinctum. Journal of agricultural and food chemistry 42(9): 2025-2028 Treatment of Fusarium tricinctum Nrrl 13426 cultures with dilute sodium bicarbonate resulted in dramatic reductions in the production of trichothecene mycotoxins, geraniol, and carotenoids. All of these compounds are [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/mechanism-for-sodium-bicarbonate-inhibition-of-trichothecene-biosynthesis-in-fusarium-tricinctum/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Lysine accumulation in transgenic tobacco expressing dihydrodipicolinate synthase of Escherichia coli</title><link>http://scien.net/enzyme/kinase/lysine-accumulation-in-transgenic-tobacco-expressing-dihydrodipicolinate-synthase-of-escherichia-coli</link> <comments>http://scien.net/enzyme/kinase/lysine-accumulation-in-transgenic-tobacco-expressing-dihydrodipicolinate-synthase-of-escherichia-coli#comments</comments> <pubDate>Mon, 20 May 2013 02:09:06 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[dhdps]]></category> <category><![CDATA[dihydrodipicolinate]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/lysine-accumulation-in-transgenic-tobacco-expressing-dihydrodipicolinate-synthase-of-escherichia-coli</guid> <description><![CDATA[Kwon, Taeho; Sasahara, Takeo; Abe, Toshinori, 1995: Lysine accumulation in transgenic tobacco expressing dihydrodipicolinate synthase of Escherichia coli. Journal Of Plant Physiology. 146(5-6): 615-621 The dihydrodipicolinate synthase (Dhdps; Ec 4.2.1.52) gene from E. coli was introduced into tobacco to examine the ability and role of chimeric Dhdps in the biosynthesis of lysine in higher plants. [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/lysine-accumulation-in-transgenic-tobacco-expressing-dihydrodipicolinate-synthase-of-escherichia-coli/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Lack of stereospecificity of suid pseudorabies virus thymidine kinase</title><link>http://scien.net/enzyme/kinase/lack-of-stereospecificity-of-suid-pseudorabies-virus-thymidine-kinase</link> <comments>http://scien.net/enzyme/kinase/lack-of-stereospecificity-of-suid-pseudorabies-virus-thymidine-kinase#comments</comments> <pubDate>Sun, 19 May 2013 06:02:56 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[mchgt]]></category> <category><![CDATA[stereospecificity]]></category> <category><![CDATA[suid]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/lack-of-stereospecificity-of-suid-pseudorabies-virus-thymidine-kinase</guid> <description><![CDATA[Maga, Giovanni; Verri, Annalisa; Bonizzi, Luigi; Ponti, Wilma; Poli, Giorgio; Garbesi, Anna; Niccolai, Daniela; Spadari, Silvio; Focher, Federico, 1993: Lack of stereospecificity of suid pseudorabies virus thymidine kinase. Biochemical Journal. 294(2): 381-385 We have partially purified suid pseudorabies virus (Prv) thymidine kinase from infected thymidine kinase- mouse cells, and cytosolic swine thymidine kinase from lymphatic [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/lack-of-stereospecificity-of-suid-pseudorabies-virus-thymidine-kinase/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Isolation and characterization of a cDNA encoding Arabidopsis thaliana mevalonate kinase by genetic complementation in yeast</title><link>http://scien.net/enzyme/kinase/isolation-and-characterization-of-a-cdna-encoding-arabidopsis-thaliana-mevalonate-kinase-by-genetic-complementation-in-yeast</link> <comments>http://scien.net/enzyme/kinase/isolation-and-characterization-of-a-cdna-encoding-arabidopsis-thaliana-mevalonate-kinase-by-genetic-complementation-in-yeast#comments</comments> <pubDate>Sun, 19 May 2013 05:48:37 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/isolation-and-characterization-of-a-cdna-encoding-arabidopsis-thaliana-mevalonate-kinase-by-genetic-complementation-in-yeast</guid> <description><![CDATA[Riou, Catherine; Tourte, Yves; Lacroute, Francois; Karst, Francis, 1994: Isolation and characterization of a cDNA encoding Arabidopsis thaliana mevalonate kinase by genetic complementation in yeast. Gene (amsterdam). 148(2): 293-297 A 1.64-kb cDNA encoding an Arabidopsis thaliana mevalonate kinase (Mk) was cloned by complementation of the erg12-1 mutation affecting Mk in the yeast Saccharomyces cerevisiae, and [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/isolation-and-characterization-of-a-cdna-encoding-arabidopsis-thaliana-mevalonate-kinase-by-genetic-complementation-in-yeast/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Interactive effects of soil moisture and food on glycolytic metabolism in Eisenia fetida (Oligochaeta)</title><link>http://scien.net/enzyme/kinase/interactive-effects-of-soil-moisture-and-food-on-glycolytic-metabolism-in-eisenia-fetida-oligochaeta</link> <comments>http://scien.net/enzyme/kinase/interactive-effects-of-soil-moisture-and-food-on-glycolytic-metabolism-in-eisenia-fetida-oligochaeta#comments</comments> <pubDate>Sun, 19 May 2013 05:36:13 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[diehl]]></category> <category><![CDATA[fetida]]></category> <category><![CDATA[moisturelow]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/interactive-effects-of-soil-moisture-and-food-on-glycolytic-metabolism-in-eisenia-fetida-oligochaeta</guid> <description><![CDATA[Williams, D. L.; Diehl, W. J., 1992: Interactive effects of soil moisture and food on glycolytic metabolism in Eisenia fetida (Oligochaeta). Comparative Biochemistry and Physiology B, Comparative Biochemistry 102(4): 911-917 Activities of hexokinase, phosphorylase, phosphofructokinase, pyruvate kinase, and fructose bis-phosphatase and tissue levels of glucose and glycogen were measured in Eisenia fetida raised in four [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/interactive-effects-of-soil-moisture-and-food-on-glycolytic-metabolism-in-eisenia-fetida-oligochaeta/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>High-level expression of functional cGMP-dependent protein kinase using the baculovirus system</title><link>http://scien.net/enzyme/kinase/high-level-expression-of-functional-cgmp-dependent-protein-kinase-using-the-baculovirus-system</link> <comments>http://scien.net/enzyme/kinase/high-level-expression-of-functional-cgmp-dependent-protein-kinase-using-the-baculovirus-system#comments</comments> <pubDate>Sun, 19 May 2013 04:00:18 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/high-level-expression-of-functional-cgmp-dependent-protein-kinase-using-the-baculovirus-system</guid> <description><![CDATA[Feil, Robert; Mueller, Stefan; Hofmann, Franz, 1993: High-level expression of functional cGMP-dependent protein kinase using the baculovirus system. Febs (federation Of European Biochemical Societies) Letters. 336(1): 163-167 The understanding of the structure and function of cGMP-dependent protein kinase (cGMP kinase) has been hindered by the difficulty to obtain large quantities of functional enzyme. A recombinant [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/high-level-expression-of-functional-cgmp-dependent-protein-kinase-using-the-baculovirus-system/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Glucose transport and glycolytic enzyme activities in erythrocytes of two-year-old thoroughbreds undergoing training exercise</title><link>http://scien.net/enzyme/kinase/glucose-transport-and-glycolytic-enzyme-activities-in-erythrocytes-of-two-year-old-thoroughbreds-undergoing-training-exercise</link> <comments>http://scien.net/enzyme/kinase/glucose-transport-and-glycolytic-enzyme-activities-in-erythrocytes-of-two-year-old-thoroughbreds-undergoing-training-exercise#comments</comments> <pubDate>Sat, 18 May 2013 07:23:26 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/glucose-transport-and-glycolytic-enzyme-activities-in-erythrocytes-of-two-year-old-thoroughbreds-undergoing-training-exercise</guid> <description><![CDATA[Arai, T.; Washizu, T.; Hamada, S.; Sako, T.; Takagi, S.; Yashiki, K.; Motoyoshi, S., 1994: Glucose transport and glycolytic enzyme activities in erythrocytes of two-year-old thoroughbreds undergoing training exercise. Veterinary Research Communications. 18(6): 417-422 D-Glucose transport and cytosolic enzyme activities were measured in erythrocytes from 2-year-old thoroughbreds under continuous training exercise (race horses) and compared [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/glucose-transport-and-glycolytic-enzyme-activities-in-erythrocytes-of-two-year-old-thoroughbreds-undergoing-training-exercise/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Gibberellin stimulates synthesis of a protein kinase in dwarf pea epicotyls</title><link>http://scien.net/enzyme/kinase/gibberellin-stimulates-synthesis-of-a-protein-kinase-in-dwarf-pea-epicotyls</link> <comments>http://scien.net/enzyme/kinase/gibberellin-stimulates-synthesis-of-a-protein-kinase-in-dwarf-pea-epicotyls#comments</comments> <pubDate>Sat, 18 May 2013 07:22:19 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[dwarfs]]></category> <category><![CDATA[epicotyls]]></category> <category><![CDATA[phosphothreonine]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/gibberellin-stimulates-synthesis-of-a-protein-kinase-in-dwarf-pea-epicotyls</guid> <description><![CDATA[Aggarwal, Kamal K.; Sachar, R. C., 1995: Gibberellin stimulates synthesis of a protein kinase in dwarf pea epicotyls. Phytochemistry (oxford). 40(2): 383-387 Application of gibberellin A-3 (Ga-3, 1 mu-M) stimulated protein kinase activity two-fold in light-grown dwarf pea epicotyls. This response was almost completely blocked by the simultaneous application of abscisic acid (Aba, 10 mu-M). [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/gibberellin-stimulates-synthesis-of-a-protein-kinase-in-dwarf-pea-epicotyls/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Gibberellin promotes histone H1 kinase activity and the expression of cdc2 and cyclin genes during the induction of rapid growth in deepwater rice internodes</title><link>http://scien.net/enzyme/kinase/gibberellin-promotes-histone-h1-kinase-activity-and-the-expression-of-cdc2-and-cyclin-genes-during-the-induction-of-rapid-growth-in-deepwater-rice-internodes</link> <comments>http://scien.net/enzyme/kinase/gibberellin-promotes-histone-h1-kinase-activity-and-the-expression-of-cdc2-and-cyclin-genes-during-the-induction-of-rapid-growth-in-deepwater-rice-internodes#comments</comments> <pubDate>Sat, 18 May 2013 07:22:19 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/gibberellin-promotes-histone-h1-kinase-activity-and-the-expression-of-cdc2-and-cyclin-genes-during-the-induction-of-rapid-growth-in-deepwater-rice-internodes</guid> <description><![CDATA[Sauter, Margret; Mekhedov, Sergei L.; Kende, Hans, 1995: Gibberellin promotes histone H1 kinase activity and the expression of cdc2 and cyclin genes during the induction of rapid growth in deepwater rice internodes. Plant Journal. 7(4): 623-632 Partial submergence or treatment with either ethylene or gibberellin (Ga) promotes rapid internodal growth in deepwater rice (Oryza saliva [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/gibberellin-promotes-histone-h1-kinase-activity-and-the-expression-of-cdc2-and-cyclin-genes-during-the-induction-of-rapid-growth-in-deepwater-rice-internodes/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Genetic and amino-acid analysis of two maize threonine-overproducing, lysine-insensitive aspartate kinase mutants</title><link>http://scien.net/enzyme/kinase/genetic-and-amino-acid-analysis-of-two-maize-threonine-overproducing-lysine-insensitive-aspartate-kinase-mutants</link> <comments>http://scien.net/enzyme/kinase/genetic-and-amino-acid-analysis-of-two-maize-threonine-overproducing-lysine-insensitive-aspartate-kinase-mutants#comments</comments> <pubDate>Sat, 18 May 2013 07:10:23 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[expressivity]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/genetic-and-amino-acid-analysis-of-two-maize-threonine-overproducing-lysine-insensitive-aspartate-kinase-mutants</guid> <description><![CDATA[Muehlbauer, Gj; Gengenbach, Bg; Somers, Da; Donovan, Cm, 1994: Genetic and amino-acid analysis of two maize threonine-overproducing, lysine-insensitive aspartate kinase mutants. Theoretical and applied genetics 89(6): 767-774 The aspartate-derived amino-acid pathway leads to the production of the essential amino-acids lysine, methionine, threonine and isoleucine. Aspartate kinase (Ak) is the first enzyme in this pathway and [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/genetic-and-amino-acid-analysis-of-two-maize-threonine-overproducing-lysine-insensitive-aspartate-kinase-mutants/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Evidence from transgenic mice that myc regulates hepatic glycolysis</title><link>http://scien.net/enzyme/kinase/evidence-from-transgenic-mice-that-myc-regulates-hepatic-glycolysis</link> <comments>http://scien.net/enzyme/kinase/evidence-from-transgenic-mice-that-myc-regulates-hepatic-glycolysis#comments</comments> <pubDate>Sat, 18 May 2013 06:23:26 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[cacgtg]]></category> <category><![CDATA[enolpyruvate]]></category> <category><![CDATA[pepck]]></category> <category><![CDATA[phosphofructo]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/evidence-from-transgenic-mice-that-myc-regulates-hepatic-glycolysis</guid> <description><![CDATA[Valera, Alfons; Pujol, Anna; Gregori, Xavier; Riu, Efren; Visa, Joana; Bosch, Fatima, 1995: Evidence from transgenic mice that myc regulates hepatic glycolysis. Faseb Journal. 9(11): 1067-1078 The product of the c-myc proto-oncogene (c-Myc) is involved in the control of cell proliferation, differentiation, and apoptosis. It acts as a transcription factor that recognizes the Cacgtg motif. [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/evidence-from-transgenic-mice-that-myc-regulates-hepatic-glycolysis/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Evaluation of a viral thymidine kinase gene for suicide selection in transfected mosquito cells</title><link>http://scien.net/enzyme/kinase/evaluation-of-a-viral-thymidine-kinase-gene-for-suicide-selection-in-transfected-mosquito-cells</link> <comments>http://scien.net/enzyme/kinase/evaluation-of-a-viral-thymidine-kinase-gene-for-suicide-selection-in-transfected-mosquito-cells#comments</comments> <pubDate>Sat, 18 May 2013 06:14:31 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[bromovinyl]]></category> <category><![CDATA[bvdu]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/evaluation-of-a-viral-thymidine-kinase-gene-for-suicide-selection-in-transfected-mosquito-cells</guid> <description><![CDATA[Mazzacano, C. A.; Fallon, A. M., 1995: Evaluation of a viral thymidine kinase gene for suicide selection in transfected mosquito cells. Insect Molecular Biology. 4(2): 125-134 An Aedes albopictus cell line previously shown to be deficient in thymidine kinase activity was transfected with a thymidine kinase gene (tk) from Herpes simplex virus. Survival of the [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/evaluation-of-a-viral-thymidine-kinase-gene-for-suicide-selection-in-transfected-mosquito-cells/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Enzyme activity profiles in an overwintering population of freeze-tolerant larvae of the gall fly, Eurosta solidaginis</title><link>http://scien.net/enzyme/kinase/enzyme-activity-profiles-in-an-overwintering-population-of-freeze-tolerant-larvae-of-the-gall-fly-eurosta-solidaginis</link> <comments>http://scien.net/enzyme/kinase/enzyme-activity-profiles-in-an-overwintering-population-of-freeze-tolerant-larvae-of-the-gall-fly-eurosta-solidaginis#comments</comments> <pubDate>Sat, 18 May 2013 06:04:03 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[eurosta]]></category> <category><![CDATA[solidaginis]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/enzyme-activity-profiles-in-an-overwintering-population-of-freeze-tolerant-larvae-of-the-gall-fly-eurosta-solidaginis</guid> <description><![CDATA[Joanisse, Dr; Storey, Kb, 1994: Enzyme activity profiles in an overwintering population of freeze-tolerant larvae of the gall fly, Eurosta solidaginis. Journal of comparative physiology B Biochemical systemic and environmental physiology64(3): 247-255 The activity of some enzymes of intermediary metabolism, including enzymes of glycolysis, the hexose monophosphate shunt, and polyol cryoprotectant synthesis, were measured in [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/enzyme-activity-profiles-in-an-overwintering-population-of-freeze-tolerant-larvae-of-the-gall-fly-eurosta-solidaginis/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Effects of trans- and cis-zeatin and optical isomers of synthetic cytokinins on protein kinase activity in vitro</title><link>http://scien.net/enzyme/kinase/effects-of-trans-and-cis-zeatin-and-optical-isomers-of-synthetic-cytokinins-on-protein-kinase-activity-in-vitro</link> <comments>http://scien.net/enzyme/kinase/effects-of-trans-and-cis-zeatin-and-optical-isomers-of-synthetic-cytokinins-on-protein-kinase-activity-in-vitro#comments</comments> <pubDate>Fri, 17 May 2013 03:35:56 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/effects-of-trans-and-cis-zeatin-and-optical-isomers-of-synthetic-cytokinins-on-protein-kinase-activity-in-vitro</guid> <description><![CDATA[Kulaeva, On; Corse, J; Selivankina, Sy, 1995: Effects of trans- and cis-zeatin and optical isomers of synthetic cytokinins on protein kinase activity in vitro. Journal of plant growth regulationer 14(1): 41-47 The effects of cis- and trans-zeatin on the activity of the protein kinase associated with barley leaf chromatin were studied. Substances tested were added [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/effects-of-trans-and-cis-zeatin-and-optical-isomers-of-synthetic-cytokinins-on-protein-kinase-activity-in-vitro/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Effects of acute exercise on hepatic lipogenic enzymes in fasted and refed rats</title><link>http://scien.net/enzyme/kinase/effects-of-acute-exercise-on-hepatic-lipogenic-enzymes-in-fasted-and-refed-rats</link> <comments>http://scien.net/enzyme/kinase/effects-of-acute-exercise-on-hepatic-lipogenic-enzymes-in-fasted-and-refed-rats#comments</comments> <pubDate>Fri, 17 May 2013 03:10:51 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[cornstarch]]></category> <category><![CDATA[mmin]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/effects-of-acute-exercise-on-hepatic-lipogenic-enzymes-in-fasted-and-refed-rats</guid> <description><![CDATA[Griffiths, Margaret A.; Baker, David H.; Yu, Xing Xian; Novakofski, Jan; Oscai, Lawrence; Ji, Li Li, 1995: Effects of acute exercise on hepatic lipogenic enzymes in fasted and refed rats. Journal Of Applied Physiology. 79(3): 879-885 The effects of an acute bout of prolonged exhaustive exercise on the activities of hepatic lipogenic enzymes have been [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/effects-of-acute-exercise-on-hepatic-lipogenic-enzymes-in-fasted-and-refed-rats/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Effect of dihydrooxadiazines on the octopamine-sensitive adenylate cyclase complex of two-spotted spider mite, Tetranychus urticae Koch</title><link>http://scien.net/enzyme/kinase/effect-of-dihydrooxadiazines-on-the-octopamine-sensitive-adenylate-cyclase-complex-of-two-spotted-spider-mite-tetranychus-urticae-koch</link> <comments>http://scien.net/enzyme/kinase/effect-of-dihydrooxadiazines-on-the-octopamine-sensitive-adenylate-cyclase-complex-of-two-spotted-spider-mite-tetranychus-urticae-koch#comments</comments> <pubDate>Fri, 17 May 2013 02:42:29 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[bromophenyl]]></category> <category><![CDATA[cyproheptadine]]></category> <category><![CDATA[dibromophenyl]]></category> <category><![CDATA[dihydrooxadiazine]]></category> <category><![CDATA[dihydrooxadiazines]]></category> <category><![CDATA[dimethylphenyl]]></category> <category><![CDATA[fluoroethyl]]></category> <category><![CDATA[gramine]]></category> <category><![CDATA[mianserin]]></category> <category><![CDATA[octopamine]]></category> <category><![CDATA[octopaminergic]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/effect-of-dihydrooxadiazines-on-the-octopamine-sensitive-adenylate-cyclase-complex-of-two-spotted-spider-mite-tetranychus-urticae-koch</guid> <description><![CDATA[Ismail, Saad M. M.; Dekeyser, Mark A.; Downer, Roger G. H., 1993: Effect of dihydrooxadiazines on the octopamine-sensitive adenylate cyclase complex of two-spotted spider mite, Tetranychus urticae Koch. Pesticide Biochemistry &#038; Physiology. 47(1): 1-7 The interaction of dihydrooxadiazine insecticides with the octopamine-sensitive adenylate cyclase complex was investigated in homogenates of the two-spotted spider mite, Tetranychus [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/effect-of-dihydrooxadiazines-on-the-octopamine-sensitive-adenylate-cyclase-complex-of-two-spotted-spider-mite-tetranychus-urticae-koch/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Directed mutagenesis of deoxyguanosine site at arginine 79 up-regulates turnover on deoxyadenosine kinase subunit of heterodimeric enzyme from Lactobacillus acidophilus R26</title><link>http://scien.net/enzyme/kinase/directed-mutagenesis-of-deoxyguanosine-site-at-arginine-79-up-regulates-turnover-on-deoxyadenosine-kinase-subunit-of-heterodimeric-enzyme-from-lactobacillus-acidophilus-r26</link> <comments>http://scien.net/enzyme/kinase/directed-mutagenesis-of-deoxyguanosine-site-at-arginine-79-up-regulates-turnover-on-deoxyadenosine-kinase-subunit-of-heterodimeric-enzyme-from-lactobacillus-acidophilus-r26#comments</comments> <pubDate>Fri, 17 May 2013 02:13:00 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[dgtp]]></category> <category><![CDATA[dguo]]></category> <category><![CDATA[kinasedeoxyadenosine]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/directed-mutagenesis-of-deoxyguanosine-site-at-arginine-79-up-regulates-turnover-on-deoxyadenosine-kinase-subunit-of-heterodimeric-enzyme-from-lactobacillus-acidophilus-r26</guid> <description><![CDATA[Hong, Young Soo; Ma, Grace T.; Ives, David H., 1995: Directed mutagenesis of deoxyguanosine site at arginine 79 up-regulates turnover on deoxyadenosine kinase subunit of heterodimeric enzyme from Lactobacillus acidophilus R26. Journal Of Biological Chemistry. 270(12): 6602-6606 Examination of conserved motifs on the cloned subunits of the deoxyguanosine kinase/deoxyadenosine kinase (dGK/dAK) of Lactobacillus acidophilus R-26 [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/directed-mutagenesis-of-deoxyguanosine-site-at-arginine-79-up-regulates-turnover-on-deoxyadenosine-kinase-subunit-of-heterodimeric-enzyme-from-lactobacillus-acidophilus-r26/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Differential transcript levels of genes associated with glycolysis and alcohol fermentation in rice plants (Oryza sativa L.) under submergence stress</title><link>http://scien.net/enzyme/kinase/differential-transcript-levels-of-genes-associated-with-glycolysis-and-alcohol-fermentation-in-rice-plants-oryza-sativa-l-under-submergence-stress</link> <comments>http://scien.net/enzyme/kinase/differential-transcript-levels-of-genes-associated-with-glycolysis-and-alcohol-fermentation-in-rice-plants-oryza-sativa-l-under-submergence-stress#comments</comments> <pubDate>Fri, 17 May 2013 02:10:05 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/differential-transcript-levels-of-genes-associated-with-glycolysis-and-alcohol-fermentation-in-rice-plants-oryza-sativa-l-under-submergence-stress</guid> <description><![CDATA[Umeda, M.; Uchimiya, H., 1994: Differential transcript levels of genes associated with glycolysis and alcohol fermentation in rice plants (Oryza sativa L.) under submergence stress. Plant Physiology 106(3): 1015-1022 Expression of genes encoding enzymes involved in specialized metabolic pathways is assumed to be regulated coordinately to maintain homeostasis in plant cells. We analyzed transcript levels [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/differential-transcript-levels-of-genes-associated-with-glycolysis-and-alcohol-fermentation-in-rice-plants-oryza-sativa-l-under-submergence-stress/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Different transmission rates of herpesvirus thymidine kinase reporter transgenes from founder male parents and male parents of subsequent generations</title><link>http://scien.net/enzyme/kinase/different-transmission-rates-of-herpesvirus-thymidine-kinase-reporter-transgenes-from-founder-male-parents-and-male-parents-of-subsequent-generations</link> <comments>http://scien.net/enzyme/kinase/different-transmission-rates-of-herpesvirus-thymidine-kinase-reporter-transgenes-from-founder-male-parents-and-male-parents-of-subsequent-generations#comments</comments> <pubDate>Fri, 17 May 2013 02:07:32 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/different-transmission-rates-of-herpesvirus-thymidine-kinase-reporter-transgenes-from-founder-male-parents-and-male-parents-of-subsequent-generations</guid> <description><![CDATA[Ellison, Aaron R.; Wallace, Helen; Al Shawi, Raya; Bishop, John O., 1995: Different transmission rates of herpesvirus thymidine kinase reporter transgenes from founder male parents and male parents of subsequent generations. Molecular Reproduction &#038; Development. 41(4): 425-434 Previously we demonstrated that lines of transgenic mice carrying the herpes simplex type 1 virus thymidine kinase (Hsv1-tk) [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/different-transmission-rates-of-herpesvirus-thymidine-kinase-reporter-transgenes-from-founder-male-parents-and-male-parents-of-subsequent-generations/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Defective DNA-dependent protein kinase activity is linked to V(D)J recombination and DNA repair defects associated with the murine scid mutation</title><link>http://scien.net/enzyme/kinase/defective-dna-dependent-protein-kinase-activity-is-linked-to-vdj-recombination-and-dna-repair-defects-associated-with-the-murine-scid-mutation</link> <comments>http://scien.net/enzyme/kinase/defective-dna-dependent-protein-kinase-activity-is-linked-to-vdj-recombination-and-dna-repair-defects-associated-with-the-murine-scid-mutation#comments</comments> <pubDate>Wed, 15 May 2013 03:05:57 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[pkcs]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/defective-dna-dependent-protein-kinase-activity-is-linked-to-vdj-recombination-and-dna-repair-defects-associated-with-the-murine-scid-mutation</guid> <description><![CDATA[Blunt, T.; Finnie, N. J.; Taccioli, G. E.; Smith, G. C. M.; Demengeot, J.; Gottlieb, T. M.; Mizuta, R.; Varghese, A. J.; Alt, F. W.; Jeggo, P. A.; Jackson, S. P., 1995: Defective DNA-dependent protein kinase activity is linked to V(D)J recombination and DNA repair defects associated with the murine scid mutation. Cell Cambridge 80(5): [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/defective-dna-dependent-protein-kinase-activity-is-linked-to-vdj-recombination-and-dna-repair-defects-associated-with-the-murine-scid-mutation/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>D-glucose transport and glycolytic enzyme activities in erythrocytes of dogs, pigs, cats, horses, cattle and sheep</title><link>http://scien.net/enzyme/kinase/d-glucose-transport-and-glycolytic-enzyme-activities-in-erythrocytes-of-dogs-pigs-cats-horses-cattle-and-sheep</link> <comments>http://scien.net/enzyme/kinase/d-glucose-transport-and-glycolytic-enzyme-activities-in-erythrocytes-of-dogs-pigs-cats-horses-cattle-and-sheep#comments</comments> <pubDate>Wed, 15 May 2013 03:01:57 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/d-glucose-transport-and-glycolytic-enzyme-activities-in-erythrocytes-of-dogs-pigs-cats-horses-cattle-and-sheep</guid> <description><![CDATA[Arai, T.; Washizu, T.; Sagara, M.; Sako, T.; Nigi, H.; Matsumoto, H.; Sasaki, M.; Tomoda, I., 1995: D-glucose transport and glycolytic enzyme activities in erythrocytes of dogs, pigs, cats, horses, cattle and sheep. Research In Veterinary Science. 58(2): 196 The activities of D-glucose transport (D-Gt) and the glycolytic enzymes hexokinase (Hk) and pyruvate kinase (Pk), [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/d-glucose-transport-and-glycolytic-enzyme-activities-in-erythrocytes-of-dogs-pigs-cats-horses-cattle-and-sheep/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Cloning, sequencing, and expression in Escherichia coli of cDNA encoding porcine brain UMP-CMP kinase</title><link>http://scien.net/enzyme/kinase/cloning-sequencing-and-expression-in-escherichia-coli-of-cdna-encoding-porcine-brain-ump-cmp-kinase</link> <comments>http://scien.net/enzyme/kinase/cloning-sequencing-and-expression-in-escherichia-coli-of-cdna-encoding-porcine-brain-ump-cmp-kinase#comments</comments> <pubDate>Wed, 15 May 2013 02:15:14 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[thiogalactoside]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/cloning-sequencing-and-expression-in-escherichia-coli-of-cdna-encoding-porcine-brain-ump-cmp-kinase</guid> <description><![CDATA[Okajima, Toshihide; Goto, Sachio; Tanizawa, Katsuyuki; Tagaya, Mitsuo; Fukui, Toshio; Shimofuruya, Hiroshi; Suzuki, Jiro, 1995: Cloning, sequencing, and expression in Escherichia coli of cDNA encoding porcine brain UMP-CMP kinase. Journal Of Biochemistry (tokyo). 117(5): 980-986 A cDNA encoding porcine brain Ump-Cmp kinase has been isolated using two oligonucleotide probes synthesized on the basis of the [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/cloning-sequencing-and-expression-in-escherichia-coli-of-cdna-encoding-porcine-brain-ump-cmp-kinase/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Cloning, sequencing and expression of the pyrophosphate-dependent phosphofructo-1-kinase from Naegleria fowleri</title><link>http://scien.net/enzyme/kinase/cloning-sequencing-and-expression-of-the-pyrophosphate-dependent-phosphofructo-1-kinase-from-naegleria-fowleri</link> <comments>http://scien.net/enzyme/kinase/cloning-sequencing-and-expression-of-the-pyrophosphate-dependent-phosphofructo-1-kinase-from-naegleria-fowleri#comments</comments> <pubDate>Wed, 15 May 2013 02:15:14 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[chaotropic]]></category> <category><![CDATA[fowleri]]></category> <category><![CDATA[freudenreichii]]></category> <category><![CDATA[jonckheere]]></category> <category><![CDATA[kscn]]></category> <category><![CDATA[mertens]]></category> <category><![CDATA[naegleria]]></category> <category><![CDATA[phosphofructo]]></category> <category><![CDATA[phosphofructokinases]]></category> <category><![CDATA[schaftingen]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/cloning-sequencing-and-expression-of-the-pyrophosphate-dependent-phosphofructo-1-kinase-from-naegleria-fowleri</guid> <description><![CDATA[Wessberg, Kathleen L.; Skolnick, Sara; Xu, Jun; Marciano Cabral, Francine; Kemp, Robert G., 1995: Cloning, sequencing and expression of the pyrophosphate-dependent phosphofructo-1-kinase from Naegleria fowleri. Biochemical Journal. 307(1): 143-149 The cDNA for the Pp-i-dependent phosphofructo-1-kinase has been cloned and sequenced from a cDNA library prepared from the free-living amoeba Naegleria-fowleri. The coding sequence of the [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/cloning-sequencing-and-expression-of-the-pyrophosphate-dependent-phosphofructo-1-kinase-from-naegleria-fowleri/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Cloning of the gene for phosphoglycerate kinase from Schistosoma mansoni and characterization of its gene product</title><link>http://scien.net/enzyme/kinase/cloning-of-the-gene-for-phosphoglycerate-kinase-from-schistosoma-mansoni-and-characterization-of-its-gene-product</link> <comments>http://scien.net/enzyme/kinase/cloning-of-the-gene-for-phosphoglycerate-kinase-from-schistosoma-mansoni-and-characterization-of-its-gene-product#comments</comments> <pubDate>Wed, 15 May 2013 02:14:37 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[immunoscreen]]></category> <category><![CDATA[microsequencing]]></category> <category><![CDATA[pgks]]></category> <category><![CDATA[schistosomula]]></category> <category><![CDATA[smpgk]]></category> <category><![CDATA[tegumental]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/cloning-of-the-gene-for-phosphoglycerate-kinase-from-schistosoma-mansoni-and-characterization-of-its-gene-product</guid> <description><![CDATA[Lee, Keung W.; Shalaby, Kamal A.; Thakur, Arvind; Medhat, Amina M.; Karim, Amr M.; Loverde, Philip T., 1995: Cloning of the gene for phosphoglycerate kinase from Schistosoma mansoni and characterization of its gene product. Molecular &#038; Biochemical Parasitology. 71(2): 221-231 As molecules on the surface or associated with the outer covering (tegument) of Schistosoma mansoni [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/cloning-of-the-gene-for-phosphoglycerate-kinase-from-schistosoma-mansoni-and-characterization-of-its-gene-product/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Cloning and functional expression analysis of the alpha subunit of mouse ATP synthase</title><link>http://scien.net/enzyme/kinase/cloning-and-functional-expression-analysis-of-the-alpha-subunit-of-mouse-atp-synthase</link> <comments>http://scien.net/enzyme/kinase/cloning-and-functional-expression-analysis-of-the-alpha-subunit-of-mouse-atp-synthase#comments</comments> <pubDate>Wed, 15 May 2013 02:12:23 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/cloning-and-functional-expression-analysis-of-the-alpha-subunit-of-mouse-atp-synthase</guid> <description><![CDATA[Yotov, Wagner V.; St Arnaud, Rene, 1993: Cloning and functional expression analysis of the alpha subunit of mouse ATP synthase. Biochemical &#038; Biophysical Research Communications. 1: 142-148 The alpha subunit of the mitochondrial Atp synthase is part of the F-1 enzymatic complex known to bind Adp, phosphate and Atp and is at the heart of [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/cloning-and-functional-expression-analysis-of-the-alpha-subunit-of-mouse-atp-synthase/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Cloning and characterization of a cDNA encoding rat PKR, the double-stranded RNA-dependent eukaryotic initiation factor-2 kinase</title><link>http://scien.net/enzyme/kinase/cloning-and-characterization-of-a-cdna-encoding-rat-pkr-the-double-stranded-rna-dependent-eukaryotic-initiation-factor-2-kinase</link> <comments>http://scien.net/enzyme/kinase/cloning-and-characterization-of-a-cdna-encoding-rat-pkr-the-double-stranded-rna-dependent-eukaryotic-initiation-factor-2-kinase#comments</comments> <pubDate>Wed, 15 May 2013 02:10:47 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/cloning-and-characterization-of-a-cdna-encoding-rat-pkr-the-double-stranded-rna-dependent-eukaryotic-initiation-factor-2-kinase</guid> <description><![CDATA[Mellor, Harry; Flowers, Kevin M.; Kimball, Scot R.; Jefferson, Leonard S., 1994: Cloning and characterization of a cDNA encoding rat PKR, the double-stranded RNA-dependent eukaryotic initiation factor-2 kinase. Biochimica Et Biophysica Acta. 1219(3): 693-696 We have isolated and sequenced a full-length cDNA encoding the double-stranded Rna-dependent protein kinase Pkr from rat. The derived amino acid [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/cloning-and-characterization-of-a-cdna-encoding-rat-pkr-the-double-stranded-rna-dependent-eukaryotic-initiation-factor-2-kinase/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Cloning and biochemical characterization of a plant protein kinase that phosphorylates serine, threonine, and tyrosine</title><link>http://scien.net/enzyme/kinase/cloning-and-biochemical-characterization-of-a-plant-protein-kinase-that-phosphorylates-serine-threonine-and-tyrosine</link> <comments>http://scien.net/enzyme/kinase/cloning-and-biochemical-characterization-of-a-plant-protein-kinase-that-phosphorylates-serine-threonine-and-tyrosine#comments</comments> <pubDate>Wed, 15 May 2013 02:10:37 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[antiphosphotyrosine]]></category> <category><![CDATA[autophosphorylated]]></category> <category><![CDATA[glutyr]]></category> <category><![CDATA[phosphoamino]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/cloning-and-biochemical-characterization-of-a-plant-protein-kinase-that-phosphorylates-serine-threonine-and-tyrosine</guid> <description><![CDATA[Ali, N; Halfter, U; Chua, Nh, 1994: Cloning and biochemical characterization of a plant protein kinase that phosphorylates serine, threonine, and tyrosine. Journal of biological chemistry, 269(50): 31626-31629 Phosphorylation of proteins on serine, threonine, or tyrosine residues represents an important biochemical mechanism to regulate the activity of enzymes and is used in many cellular processes. [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/cloning-and-biochemical-characterization-of-a-plant-protein-kinase-that-phosphorylates-serine-threonine-and-tyrosine/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Casein kinase-2-type protein kinases in plants: possible targets of polyamine action during growth regulation?</title><link>http://scien.net/enzyme/kinase/casein-kinase-2-type-protein-kinases-in-plants-possible-targets-of-polyamine-action-during-growth-regulation</link> <comments>http://scien.net/enzyme/kinase/casein-kinase-2-type-protein-kinases-in-plants-possible-targets-of-polyamine-action-during-growth-regulation#comments</comments> <pubDate>Tue, 14 May 2013 02:37:46 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/casein-kinase-2-type-protein-kinases-in-plants-possible-targets-of-polyamine-action-during-growth-regulation</guid> <description><![CDATA[Roux, S. J., 1993: Casein kinase-2-type protein kinases in plants: possible targets of polyamine action during growth regulation?. Plant Growth Regulation 12(3): 189-193 The biochemical mechanisms by which polyamines influence plant growth and development are not known. One of mechanisms frequently proposed is that polyamines can bind to key cellular enzymes and modulate their activity. [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/casein-kinase-2-type-protein-kinases-in-plants-possible-targets-of-polyamine-action-during-growth-regulation/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Carbohydrate metabolism during seed germination and seedling growth in green gram under saline stress</title><link>http://scien.net/enzyme/kinase/carbohydrate-metabolism-during-seed-germination-and-seedling-growth-in-green-gram-under-saline-stress</link> <comments>http://scien.net/enzyme/kinase/carbohydrate-metabolism-during-seed-germination-and-seedling-growth-in-green-gram-under-saline-stress#comments</comments> <pubDate>Tue, 14 May 2013 02:35:25 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[embden]]></category> <category><![CDATA[meyerhof]]></category> <category><![CDATA[nonsaline]]></category> <category><![CDATA[parnas]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/carbohydrate-metabolism-during-seed-germination-and-seedling-growth-in-green-gram-under-saline-stress</guid> <description><![CDATA[Misra, Neelam; Dwivedi, Upendra N., 1995: Carbohydrate metabolism during seed germination and seedling growth in green gram under saline stress. Plant Physiology &#038; Biochemistry (montrouge). 33(1): 33-38 The developmental profiles of some enzymes of the Embden-Meyerhof-Parnas (Emp) and pentose phosphate (Pp), pathways (namely, pyruvate kinase (Pk), lactate dehydrogenase (Ldh), alcohol dehydrogenase (Adh), glucose 6-phosphate dehydrogenase [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/carbohydrate-metabolism-during-seed-germination-and-seedling-growth-in-green-gram-under-saline-stress/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Biosynthesis of casein kinase II in lymphoid cell lines</title><link>http://scien.net/enzyme/kinase/biosynthesis-of-casein-kinase-ii-in-lymphoid-cell-lines</link> <comments>http://scien.net/enzyme/kinase/biosynthesis-of-casein-kinase-ii-in-lymphoid-cell-lines#comments</comments> <pubDate>Tue, 14 May 2013 02:12:05 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/biosynthesis-of-casein-kinase-ii-in-lymphoid-cell-lines</guid> <description><![CDATA[Luescher, Bernhard; Litchfield, David W., 1994: Biosynthesis of casein kinase II in lymphoid cell lines. European Journal Of Biochemistry. 220(2): 521-526 We have analyzed the biosynthesis of casein kinase I In exponentially growing tissue culture cells, the beta subunit was synthesized in excess of the catalytic subunit (a). A substantial fraction of newly synthesized beta [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/biosynthesis-of-casein-kinase-ii-in-lymphoid-cell-lines/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Biochemical properties of rice adenylate kinase and subcellular location in plant cells</title><link>http://scien.net/enzyme/kinase/biochemical-properties-of-rice-adenylate-kinase-and-subcellular-location-in-plant-cells</link> <comments>http://scien.net/enzyme/kinase/biochemical-properties-of-rice-adenylate-kinase-and-subcellular-location-in-plant-cells#comments</comments> <pubDate>Tue, 14 May 2013 02:07:17 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[immunomicroscopic]]></category> <category><![CDATA[monophosphates]]></category> <category><![CDATA[pentaphospho]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/biochemical-properties-of-rice-adenylate-kinase-and-subcellular-location-in-plant-cells</guid> <description><![CDATA[Kawai, M; Uchimiya, H., 1995: Biochemical properties of rice adenylate kinase and subcellular location in plant cells. Plant molecular biology 27(5): 943-951 Previously, we characterized nucleotide sequences of two cDNAs encoding adenylate kinase from rice plants (Oryza sativa L.). Each cDNA (Adk-a or Adk-b) was cloned into the expression vector pET 11d-Gst to produce Gst-Ak [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/biochemical-properties-of-rice-adenylate-kinase-and-subcellular-location-in-plant-cells/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Autophosphorylation-independent activation of Acanthamoeba myosin I heavy chain kinase by plasma membranes</title><link>http://scien.net/enzyme/kinase/autophosphorylation-independent-activation-of-acanthamoeba-myosin-i-heavy-chain-kinase-by-plasma-membranes</link> <comments>http://scien.net/enzyme/kinase/autophosphorylation-independent-activation-of-acanthamoeba-myosin-i-heavy-chain-kinase-by-plasma-membranes#comments</comments> <pubDate>Tue, 14 May 2013 01:59:55 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[autophosphorylate]]></category> <category><![CDATA[myosins]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/autophosphorylation-independent-activation-of-acanthamoeba-myosin-i-heavy-chain-kinase-by-plasma-membranes</guid> <description><![CDATA[Kulesza Lipka, Dorota; Baines, Hanna Vv Brzeskaan C.; Korn, Edward D., 1993: Autophosphorylation-independent activation of Acanthamoeba myosin I heavy chain kinase by plasma membranes. Journal Of Biological Chemistry. 268(24): 17995-18001 The three isoforms of Acanthamoeba myosin I (non-filamentous myosin with only a single heavy chain) express actin-activated Mg-2+-ATPase activity only when phosphorylated at a single [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/autophosphorylation-independent-activation-of-acanthamoeba-myosin-i-heavy-chain-kinase-by-plasma-membranes/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Assays for three enzymes involved in mevalonic acid metabolism</title><link>http://scien.net/enzyme/kinase/assays-for-three-enzymes-involved-in-mevalonic-acid-metabolism</link> <comments>http://scien.net/enzyme/kinase/assays-for-three-enzymes-involved-in-mevalonic-acid-metabolism#comments</comments> <pubDate>Tue, 14 May 2013 01:54:15 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[isopentenol]]></category> <category><![CDATA[isopentenyl]]></category> <category><![CDATA[mevalonic]]></category> <category><![CDATA[microcolumns]]></category> <category><![CDATA[mvap]]></category> <category><![CDATA[mvapp]]></category> <category><![CDATA[phycomyces]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/assays-for-three-enzymes-involved-in-mevalonic-acid-metabolism</guid> <description><![CDATA[Sandmann, Gerhard; Albrecht, Manuela, 1994: Assays for three enzymes involved in mevalonic acid metabolism. Physiologia Plantarum. 92(2): 297-301 Enzyme assays have been developed for mevalonate (Mva) kinase, mevalonate phosphate (Mvap) kinase and mevalonate pyrophosphate (Mvapp) anhydrodecarboxylase. The procedures involve radioactively labelled substrates and separation of the reaction products by anion exchange chromatography. The separation on [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/assays-for-three-enzymes-involved-in-mevalonic-acid-metabolism/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Application of metabolic control analysis to the pathways of carbohydrate breakdown in Hymenolepis diminuta</title><link>http://scien.net/enzyme/kinase/application-of-metabolic-control-analysis-to-the-pathways-of-carbohydrate-breakdown-in-hymenolepis-diminuta</link> <comments>http://scien.net/enzyme/kinase/application-of-metabolic-control-analysis-to-the-pathways-of-carbohydrate-breakdown-in-hymenolepis-diminuta#comments</comments> <pubDate>Tue, 14 May 2013 01:50:15 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[branchpoint]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/application-of-metabolic-control-analysis-to-the-pathways-of-carbohydrate-breakdown-in-hymenolepis-diminuta</guid> <description><![CDATA[Barrett, John; Precious, Wendy Y., 1995: Application of metabolic control analysis to the pathways of carbohydrate breakdown in Hymenolepis diminuta. International Journal For Parasitology. 25(4): 431-436 The application of metabolic control theory to carbohydrate breakdown in the tapeworm Hymenolepis diminuta shows that it is not necessary for both phosphoenolpyruvate carboxykinase and pyruvate kinase to be [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/application-of-metabolic-control-analysis-to-the-pathways-of-carbohydrate-breakdown-in-hymenolepis-diminuta/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> <item><title>Alteration of pyruvate metabolism in African trypanosomes during differentiation from bloodstream into insect forms</title><link>http://scien.net/enzyme/kinase/alteration-of-pyruvate-metabolism-in-african-trypanosomes-during-differentiation-from-bloodstream-into-insect-forms</link> <comments>http://scien.net/enzyme/kinase/alteration-of-pyruvate-metabolism-in-african-trypanosomes-during-differentiation-from-bloodstream-into-insect-forms#comments</comments> <pubDate>Tue, 14 May 2013 01:22:33 +0000</pubDate> <dc:creator>admin</dc:creator> <category><![CDATA[Kinase]]></category> <category><![CDATA[barnard]]></category> <category><![CDATA[parasitol]]></category> <category><![CDATA[pedersen]]></category> <category><![CDATA[reynafarje]]></category><guid
isPermaLink="false">http://scien.net/enzyme/kinase/alteration-of-pyruvate-metabolism-in-african-trypanosomes-during-differentiation-from-bloodstream-into-insect-forms</guid> <description><![CDATA[Barnard, John P.; Pedersen, Peter L., 1994: Alteration of pyruvate metabolism in African trypanosomes during differentiation from bloodstream into insect forms. Archives Of Biochemistry &#038; Biophysics. 313(1): 77-82 In the presence of glucose and ample oxygen, insect form African trypanosomes release pyruvate more than 100-fold more slowly than do bloodstream forms. This rate decrease could [...]]]></description> <wfw:commentRss>http://scien.net/enzyme/kinase/alteration-of-pyruvate-metabolism-in-african-trypanosomes-during-differentiation-from-bloodstream-into-insect-forms/feed</wfw:commentRss> <slash:comments>0</slash:comments> </item> </channel> </rss>