Статті в журналах з теми "Glyceraldehyde-3-phosphate (GAP)"
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Yugueros, Javier, Alejandro Temprano, Beatriz Berzal, Marı́a Sánchez, Carmen Hernanz, José Marı́a Luengo, and Germán Naharro. "Glyceraldehyde-3-Phosphate Dehydrogenase-Encoding Gene as a Useful Taxonomic Tool for Staphylococcusspp." Journal of Clinical Microbiology 38, no. 12 (2000): 4351–55. http://dx.doi.org/10.1128/jcm.38.12.4351-4355.2000.
Повний текст джерелаYang, Shao-Qing, Jian Deng, Qian-Qian Wu, Heng Li, and Wen-Yun Gao. "A Specific Process to Purify 2-Methyl-D-Erythritol-4-Phosphate Enzymatically Converted from D-Glyceraldehyde-3-Phosphate and Pyruvate." Natural Product Communications 10, no. 2 (February 2015): 1934578X1501000. http://dx.doi.org/10.1177/1934578x1501000233.
Повний текст джерелаKomati Reddy, Gajendar, Steffen N. Lindner, and Volker F. Wendisch. "Metabolic Engineering of an ATP-Neutral Embden-Meyerhof-Parnas Pathway in Corynebacterium glutamicum: Growth Restoration by an Adaptive Point Mutation in NADH Dehydrogenase." Applied and Environmental Microbiology 81, no. 6 (January 9, 2015): 1996–2005. http://dx.doi.org/10.1128/aem.03116-14.
Повний текст джерелаScott, Israel M., Gabriel M. Rubinstein, Farris L. Poole, Gina L. Lipscomb, Gerrit J. Schut, Amanda M. Williams-Rhaesa, David M. Stevenson, Daniel Amador-Noguez, Robert M. Kelly, and Michael W. W. Adams. "The thermophilic biomass-degrading bacterium Caldicellulosiruptor bescii utilizes two enzymes to oxidize glyceraldehyde 3-phosphate during glycolysis." Journal of Biological Chemistry 294, no. 25 (May 16, 2019): 9995–10005. http://dx.doi.org/10.1074/jbc.ra118.007120.
Повний текст джерелаVellanki, Ravi N., Ravichandra Potumarthi, Kiran K. Doddapaneni, Naveen Anubrolu, and Lakshmi N. Mangamoori. "Constitutive Optimized Production of Streptokinase inSaccharomyces cerevisiaeUtilizing Glyceraldehyde 3-Phosphate Dehydrogenase Promoter ofPichia pastoris." BioMed Research International 2013 (2013): 1–10. http://dx.doi.org/10.1155/2013/268249.
Повний текст джерелаdel Castillo, Teresa, Estrella Duque, and Juan L. Ramos. "A Set of Activators and Repressors Control Peripheral Glucose Pathways in Pseudomonas putida To Yield a Common Central Intermediate." Journal of Bacteriology 190, no. 7 (February 1, 2008): 2331–39. http://dx.doi.org/10.1128/jb.01726-07.
Повний текст джерелаRisse, Karin, Karen Schlez, Tobias Eisenberg, Christina Geiger, Anna Balbutskaya, Osama Sammra, Christoph Lämmler, and Amir Abdulmawjood. "Phenotypical and Genotypical Properties of an Arcanobacterium pluranimalium Strain Isolated from a Juvenile Giraffe (Giraffa camelopardalis reticulata)." Journal of Veterinary Medicine 2014 (April 30, 2014): 1–5. http://dx.doi.org/10.1155/2014/408724.
Повний текст джерелаKormanec, J., A. Lempel'ova, R. Novakova, B. ReZuchova, and D. Homerova. "Expression of the Streptomyces aureofaciens glyceraldehyde-3-phosphate dehydrogenase gene (gap) is developmentally regulated and induced by glucose." Microbiology 143, no. 11 (November 1, 1997): 3555–61. http://dx.doi.org/10.1099/00221287-143-11-3555.
Повний текст джерелаGilboa, Rotem, Alan Joseph Bauer, and Gil Shoham. "Crystallization and preliminary crystallographic analysis of glyceraldehyde 3-phosphate dehydrogenase from Sacchromyces cerevisiae (baker's yeast)." Acta Crystallographica Section D Biological Crystallography 54, no. 6 (November 1, 1998): 1467–70. http://dx.doi.org/10.1107/s0907444997019720.
Повний текст джерелаMcFarlane, Ciaran R., Nita R. Shah, Burak V. Kabasakal, Blanca Echeverria, Charles A. R. Cotton, Doryen Bubeck, and James W. Murray. "Structural basis of light-induced redox regulation in the Calvin–Benson cycle in cyanobacteria." Proceedings of the National Academy of Sciences 116, no. 42 (September 30, 2019): 20984–90. http://dx.doi.org/10.1073/pnas.1906722116.
Повний текст джерелаCancilla, M. R., A. J. Hillier, and B. E. Davidson. "Lactococcus lactis glyceraldehyde-3-phosphate dehydrogenase gene, gap: further evidence for strongly biased codon usage in glycolytic pathway genes." Microbiology 141, no. 4 (April 1, 1995): 1027–36. http://dx.doi.org/10.1099/13500872-141-4-1027.
Повний текст джерелаHernández-Ochoa, Beatriz, Saúl Gómez-Manzo, Erick Alcaraz-Carmona, Hugo Serrano-Posada, Sara Centeno-Leija, Roberto Arreguin-Espinosa, Miguel Cuevas-Cruz, et al. "Gene Cloning, Recombinant Expression, Characterization, and Molecular Modeling of the Glycolytic Enzyme Triosephosphate Isomerase from Fusarium oxysporum." Microorganisms 8, no. 1 (December 24, 2019): 40. http://dx.doi.org/10.3390/microorganisms8010040.
Повний текст джерелаImber, Marcel, Nguyen Thi Thu Huyen, Agnieszka J. Pietrzyk-Brzezinska, Vu Van Loi, Melanie Hillion, Jörg Bernhardt, Lena Thärichen, et al. "ProteinS-Bacillithiolation Functions in Thiol Protection and Redox Regulation of the Glyceraldehyde-3-Phosphate Dehydrogenase Gap inStaphylococcus aureusUnder Hypochlorite Stress." Antioxidants & Redox Signaling 28, no. 6 (February 20, 2018): 410–30. http://dx.doi.org/10.1089/ars.2016.6897.
Повний текст джерелаHomerová, D., O. Sprušanský, E. Kutejová, and J. Kormanec. "Some features of DNA-binding proteins involved in the regulation of theStreptomyces aureofaciens gap gene, encoding glyceraldehyde-3-phosphate dehydrogenase." Folia Microbiologica 47, no. 4 (August 2002): 311–17. http://dx.doi.org/10.1007/bf02818688.
Повний текст джерелаAlssahen, Mazen, Geoffrey Foster, Abdulwahed Ahmed Hassan, Jörg Rau, Christoph Lämmler, Ellen Prenger-Berninghoff, Tobias Eisenberg, Mathew Robinson, and Amir Abdulmawjood. "First isolation of Arcanobacterium pinnipediorum from a grey seal pup (Halichoerus grypus) in the UK." Folia Microbiologica 67, no. 2 (November 26, 2021): 291–97. http://dx.doi.org/10.1007/s12223-021-00932-7.
Повний текст джерелаGawriljuk, Victor Oliveira, Rick Oerlemans, Robin M. Gierse, Riya Jotwani, Anna K. H. Hirsch, and Matthew R. Groves. "Structure of Mycobacterium tuberculosis 1-Deoxy-D-Xylulose 5-Phosphate Synthase in Complex with Butylacetylphosphonate." Crystals 13, no. 5 (April 27, 2023): 737. http://dx.doi.org/10.3390/cryst13050737.
Повний текст джерелаConley, T. R., S. C. Park, H. B. Kwon, H. P. Peng, and M. C. Shih. "Characterization of cis-acting elements in light regulation of the nuclear gene encoding the A subunit of chloroplast isozymes of glyceraldehyde-3-phosphate dehydrogenase from Arabidopsis thaliana." Molecular and Cellular Biology 14, no. 4 (April 1994): 2525–33. http://dx.doi.org/10.1128/mcb.14.4.2525-2533.1994.
Повний текст джерелаConley, T. R., S. C. Park, H. B. Kwon, H. P. Peng, and M. C. Shih. "Characterization of cis-acting elements in light regulation of the nuclear gene encoding the A subunit of chloroplast isozymes of glyceraldehyde-3-phosphate dehydrogenase from Arabidopsis thaliana." Molecular and Cellular Biology 14, no. 4 (April 1994): 2525–33. http://dx.doi.org/10.1128/mcb.14.4.2525.
Повний текст джерелаAsanuma, Narito, and Tsuneo Hino. "Effects of pH and Energy Supply on Activity and Amount of Pyruvate Formate-Lyase in Streptococcus bovis." Applied and Environmental Microbiology 66, no. 9 (September 1, 2000): 3773–77. http://dx.doi.org/10.1128/aem.66.9.3773-3777.2000.
Повний текст джерелаMeijer, W. G., E. R. van den Bergh, and L. M. Smith. "Induction of the gap-pgk operon encoding glyceraldehyde-3-phosphate dehydrogenase and 3-phosphoglycerate kinase of Xanthobacter flavus requires the LysR-type transcriptional activator CbbR." Journal of bacteriology 178, no. 3 (1996): 881–87. http://dx.doi.org/10.1128/jb.178.3.881-887.1996.
Повний текст джерелаZhou, Jieyu, Luying Yang, Alicia DeColli, Caren Freel Meyers, Natalia S. Nemeria, and Frank Jordan. "Conformational dynamics of 1-deoxy-d-xylulose 5-phosphate synthase on ligand binding revealed by H/D exchange MS." Proceedings of the National Academy of Sciences 114, no. 35 (August 14, 2017): 9355–60. http://dx.doi.org/10.1073/pnas.1619981114.
Повний текст джерелаXiong, Liangrong, Hui Du, Keyan Zhang, Duo Lv, Huanle He, Junsong Pan, Run Cai, and Gang Wang. "A Mutation in CsYL2.1 Encoding a Plastid Isoform of Triose Phosphate Isomerase Leads to Yellow Leaf 2.1 (yl2.1) in Cucumber (Cucumis Sativus L.)." International Journal of Molecular Sciences 22, no. 1 (December 30, 2020): 322. http://dx.doi.org/10.3390/ijms22010322.
Повний текст джерелаWilding, E. Imogen, James R. Brown, Alexander P. Bryant, Alison F. Chalker, David J. Holmes, Karen A. Ingraham, Serban Iordanescu, Chi Y. So, Martin Rosenberg, and Michael N. Gwynn. "Identification, Evolution, and Essentiality of the Mevalonate Pathway for Isopentenyl Diphosphate Biosynthesis in Gram-Positive Cocci." Journal of Bacteriology 182, no. 15 (August 1, 2000): 4319–27. http://dx.doi.org/10.1128/jb.182.15.4319-4327.2000.
Повний текст джерелаKang, Tae Sun, Darren R. Korber, and Takuji Tanaka. "Regulation of Dual Glycolytic Pathways for Fructose Metabolism in Heterofermentative Lactobacillus panis PM1." Applied and Environmental Microbiology 79, no. 24 (October 4, 2013): 7818–26. http://dx.doi.org/10.1128/aem.02377-13.
Повний текст джерелаRichard, John P. "Enzymatic catalysis of proton transfer and decarboxylation reactions." Pure and Applied Chemistry 83, no. 8 (July 8, 2011): 1555–65. http://dx.doi.org/10.1351/pac-con-11-02-05.
Повний текст джерелаLorite, María J., Ariana Casas-Román, Lourdes Girard, Sergio Encarnación, Natalia Díaz-Garrido, Josefa Badía, Laura Baldomá, Daniel Pérez-Mendoza, and Juan Sanjuán. "Impact of c-di-GMP on the Extracellular Proteome of Rhizobium etli." Biology 12, no. 1 (December 26, 2022): 44. http://dx.doi.org/10.3390/biology12010044.
Повний текст джерелаGITZENDANNER, M. A., and P. S. SOLTIS. "GENETIC VARIATION IN RARE AND WIDESPREAD LOMATIUM SPECIES (APIACEAE): A COMPARISON OF AFLP AND SSCP DATA." Edinburgh Journal of Botany 58, no. 2 (June 2001): 347–56. http://dx.doi.org/10.1017/s0960428601000671.
Повний текст джерелаAhmed, Marwa F. E., Mazen Alssahen, Christoph Lämmler, Bernd Köhler, Martin Metzner, Madeleine Plötz, and Amir Abdulmawjood. "Identification of Trueperella bernardiae isolated from peking ducks (Anas platyrhynchos domesticus) by phenotypical and genotypical investigations and by a newly developed loop-mediated isothermal amplification (LAMP) assay." Folia Microbiologica 67, no. 2 (November 15, 2021): 277–84. http://dx.doi.org/10.1007/s12223-021-00927-4.
Повний текст джерелаElkhalfi, Bouchra, José Miguel Araya-Garay, Jorge Rodríguez-Castro, Manuel Rey-Méndez, Abdelaziz Soukri, and Aurelio Serrano Delgado. "Cloning and heterologous overexpression of three gap genes encoding different glyceraldehyde-3-phosphate dehydrogenases from the plant pathogenic bacterium Pseudomonas syringae pv. tomato strain DC3000." Protein Expression and Purification 89, no. 2 (June 2013): 146–55. http://dx.doi.org/10.1016/j.pep.2013.02.005.
Повний текст джерелаRupasinghe, H. P. V., K. C. Almquist, G. Paliyath та D. P. Murr. "083 Is HMGR the Key Regulator of α-Farnesene Biosynthesis of Apple?" HortScience 35, № 3 (червень 2000): 403A—403. http://dx.doi.org/10.21273/hortsci.35.3.403a.
Повний текст джерелаArias-Álvarez, M., R. M. García-García, J. López-Tello, P. G. Rebollar, A. Gutiérrez-Adán, and P. L. Lorenzo. "In vivo and in vitro maturation of rabbit oocytes differently affects the gene expression profile, mitochondrial distribution, apoptosis and early embryo development." Reproduction, Fertility and Development 29, no. 9 (2017): 1667. http://dx.doi.org/10.1071/rd15553.
Повний текст джерелаValverde, F., M. Losada, and A. Serrano. "Functional complementation of an Escherichia coli gap mutant supports an amphibolic role for NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase of Synechocystis sp. strain PCC 6803." Journal of bacteriology 179, no. 14 (1997): 4513–22. http://dx.doi.org/10.1128/jb.179.14.4513-4522.1997.
Повний текст джерелаTurner, R. T., S. N. Kapelner, and T. C. Spelsberg. "Tissue-specific expression of bone proteins in femora of growing rats." American Journal of Physiology-Endocrinology and Metabolism 263, no. 4 (October 1, 1992): E724—E729. http://dx.doi.org/10.1152/ajpendo.1992.263.4.e724.
Повний текст джерелаBRANLANT, Guy, and Christiane BRANLANT. "Nucleotide sequence of the Escherichia coli gap gene. Different evolutionary behavior of the NAD+-binding domain and of the catalytic domain of D-glyceraldehyde-3-phosphate dehydrogenase." European Journal of Biochemistry 150, no. 1 (July 1985): 61–66. http://dx.doi.org/10.1111/j.1432-1033.1985.tb08988.x.
Повний текст джерелаTurner, R. T., and T. C. Spelsberg. "Correlation between mRNA levels for bone cell proteins and bone formation in long bones of maturing rats." American Journal of Physiology-Endocrinology and Metabolism 261, no. 3 (September 1, 1991): E348—E353. http://dx.doi.org/10.1152/ajpendo.1991.261.3.e348.
Повний текст джерелаAde, Julia, Katharina Hoelzle, Julia Stadler, Mathias Ritzmann, and Ludwig E. Hoelzle. "Occurrence of Mycoplasma parvum in German Pigs of Different Age Groups Using a Novel Quantitative Real-Time PCR Assay." Pathogens 11, no. 11 (November 18, 2022): 1374. http://dx.doi.org/10.3390/pathogens11111374.
Повний текст джерелаSchreiber, Wiebke, and Peter Dürre. "The glyceraldehyde-3-phosphate dehydrogenase of Clostridium acetobutylicum: isolation and purification of the enzyme, and sequencing and localization of the gap gene within a cluster of other glycolytic genes." Microbiology 145, no. 8 (August 1, 1999): 1839–47. http://dx.doi.org/10.1099/13500872-145-8-1839.
Повний текст джерелаZou, Xiaojin, Zhanxiang Sun, Ning Yang, Lizhen Zhang, Wentao Sun, Shiwei Niu, Lining Tan, Huiyu Liu, Dario Fornara, and Long Li. "Interspecific root interactions enhance photosynthesis and biomass of intercropped millet and peanut plants." Crop and Pasture Science 70, no. 3 (2019): 234. http://dx.doi.org/10.1071/cp18269.
Повний текст джерелаSchläpfer, Beatrice S., and Herbert Zuber. "Cloning and sequencing of the genes encoding glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase and triosephosphate isomerase (gap operon) from mesophilic Bacillus megaterium: comparison with corresponding sequences from thermophilic Bacillus stearothermophilus." Gene 122, no. 1 (December 1992): 53–62. http://dx.doi.org/10.1016/0378-1119(92)90031-j.
Повний текст джерелаGoswami, Ashis Kumar, Hemanta Kumar Sharma, Neelutpal Gogoi, and Bhaskar Jyoti Gogoi. "Network-Pharmacology and DFT Based Approach Towards Identification of Leads from Homalomena aromatica for Multi-Target In-Silico Screening on Entamoeba histolytica Proteins." Current Drug Therapy 15, no. 3 (October 14, 2020): 226–37. http://dx.doi.org/10.2174/1574885514666190801102336.
Повний текст джерелаPark, Myong-Ok, Taeko Mizutani, and Patrik R. Jones. "Glyceraldehyde-3-Phosphate Ferredoxin Oxidoreductase from Methanococcus maripaludis." Journal of Bacteriology 189, no. 20 (August 17, 2007): 7281–89. http://dx.doi.org/10.1128/jb.00828-07.
Повний текст джерелаSprušanský, O., B. Řežuchová, D. Homerová, and J. Kormanec. "Expression of the gap gene encoding glyceraldehyde-3-phosphate dehydrogenase of Streptomyces aureofaciens requires GapR, a member of the AraC/XylS family of transcriptional activators The GenBank/EMBL/DDBJ accession number for the sequence described in this paper is U21191." Microbiology 147, no. 5 (May 1, 2001): 1291–301. http://dx.doi.org/10.1099/00221287-147-5-1291.
Повний текст джерелаRubessa, M., S. Di Francesco, M. V. Suárez Novoa, L. Boccia, V. Longobardi, M. De Blasi, and B. Gasparrini. "125 EFFECT OF GLYCERALDEHYDE-3-PHOSPHATE DURING BOVINE IN VITRO EMBRYO CULTURE." Reproduction, Fertility and Development 23, no. 1 (2011): 167. http://dx.doi.org/10.1071/rdv23n1ab125.
Повний текст джерелаSong, Jiaqi, Huanran Sun, Shuai Zhang, and Changliang Shan. "The Multiple Roles of Glucose-6-Phosphate Dehydrogenase in Tumorigenesis and Cancer Chemoresistance." Life 12, no. 2 (February 12, 2022): 271. http://dx.doi.org/10.3390/life12020271.
Повний текст джерелаZhang, Li, Meiruo Liu, Luyao Bao, Kristina I. Boström, Yucheng Yao, Jixi Li, Shaohua Gu, and Chaoneng Ji. "Novel Structures of Type 1 Glyceraldehyde-3-phosphate Dehydrogenase from Escherichia coli Provide New Insights into the Mechanism of Generation of 1,3-Bisphosphoglyceric Acid." Biomolecules 11, no. 11 (October 22, 2021): 1565. http://dx.doi.org/10.3390/biom11111565.
Повний текст джерелаZhang, Xuan, Yan-Bin Teng, Jian-Ping Liu, Yong-Xing He, Kang Zhou, Yuxing Chen, and Cong-Zhao Zhou. "Structural insights into the catalytic mechanism of the yeast pyridoxal 5-phosphate synthase Snz1." Biochemical Journal 432, no. 3 (November 25, 2010): 445–54. http://dx.doi.org/10.1042/bj20101241.
Повний текст джерелаRomani, Rita, Vincenzo Nicola Talesa, and Cinzia Antognelli. "The Glyoxalase System Is a Novel Cargo of Amniotic Fluid Stem-Cell-Derived Extracellular Vesicles." Antioxidants 11, no. 8 (August 5, 2022): 1524. http://dx.doi.org/10.3390/antiox11081524.
Повний текст джерелаErshov, Yuri V., R. Raymond Gantt, Francis X. Cunningham,, and Elisabeth Gantt. "Isoprenoid Biosynthesis in Synechocystis sp. Strain PCC6803 Is Stimulated by Compounds of the Pentose Phosphate Cycle but Not by Pyruvate or Deoxyxylulose-5-Phosphate." Journal of Bacteriology 184, no. 18 (September 15, 2002): 5045–51. http://dx.doi.org/10.1128/jb.184.18.5045-5051.2002.
Повний текст джерелаDeb, G. K., S. R. Dey, J. I. Bang, S. J. Cho, T. H. Kwon, and I. K. Kong. "254 9-cis RETINOIC ACID INHIBITS CUMULUS CELL APOPTOSIS DURING IN VITRO MATURATION OF BOVINE OOCYTES THROUGH INHIBITION OF AP-1 PATHWAY." Reproduction, Fertility and Development 23, no. 1 (2011): 225. http://dx.doi.org/10.1071/rdv23n1ab254.
Повний текст джерелаGuitart Font, Emma, and Georg A. Sprenger. "Opening a Novel Biosynthetic Pathway to Dihydroxyacetone and Glycerol in Escherichia coli Mutants through Expression of a Gene Variant (fsaAA129S) for Fructose 6-Phosphate Aldolase." International Journal of Molecular Sciences 21, no. 24 (December 17, 2020): 9625. http://dx.doi.org/10.3390/ijms21249625.
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