Статті в журналах з теми "CoA ligases"
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Ознайомтеся з топ-50 статей у журналах для дослідження на тему "CoA ligases".
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Villemur, Richard. "Coenzyme A ligases involved in anaerobic biodegradation of aromatic compounds." Canadian Journal of Microbiology 41, no. 10 (October 1, 1995): 855–61. http://dx.doi.org/10.1139/m95-118.
Повний текст джерелаNolte, Johannes Christoph, Marc Schürmann, Catherine-Louise Schepers, Elvira Vogel, Jan Hendrik Wübbeler, and Alexander Steinbüchel. "Novel Characteristics of Succinate Coenzyme A (Succinate-CoA) Ligases: Conversion of Malate to Malyl-CoA and CoA-Thioester Formation of Succinate AnaloguesIn Vitro." Applied and Environmental Microbiology 80, no. 1 (October 18, 2013): 166–76. http://dx.doi.org/10.1128/aem.03075-13.
Повний текст джерелаLazo, O., M. Contreras, and I. Singh. "Topographical localization of peroxisomal acyl-CoA ligases: differential localization of palmitoyl-CoA and lignoceroyl-CoA ligases." Biochemistry 29, no. 16 (April 24, 1990): 3981–86. http://dx.doi.org/10.1021/bi00468a027.
Повний текст джерелаSingh, Inderjit, Oscar Lazo, and Miguel Contreras. "72 Topographical localization of Peroxisomal Acyl-CoA Ligases: Differential localization of Palmitoyl-CoA and Lignoceroyl-CoA Ligases." Pediatric Research 28, no. 3 (September 1990): 289. http://dx.doi.org/10.1203/00006450-199009000-00096.
Повний текст джерелаEl-Said Mohamed, Magdy. "Biochemical and Molecular Characterization of Phenylacetate-Coenzyme A Ligase, an Enzyme Catalyzing the First Step in Aerobic Metabolism of Phenylacetic Acid inAzoarcus evansii." Journal of Bacteriology 182, no. 2 (January 15, 2000): 286–94. http://dx.doi.org/10.1128/jb.182.2.286-294.2000.
Повний текст джерелаLamas-Maceiras, Mónica, Inmaculada Vaca, Esther Rodríguez, Javier Casqueiro, and Juan F. Martín. "Amplification and disruption of the phenylacetyl-CoA ligase gene of Penicillium chrysogenum encoding an aryl-capping enzyme that supplies phenylacetic acid to the isopenicillin N-acyltransferase." Biochemical Journal 395, no. 1 (March 15, 2006): 147–55. http://dx.doi.org/10.1042/bj20051599.
Повний текст джерелаChen, Janice S., Brendan Colón, Brendon Dusel, Marika Ziesack, Jeffrey C. Way та Joseph P. Torella. "Production of fatty acids inRalstonia eutrophaH16 by engineeringβ-oxidation and carbon storage". PeerJ 3 (7 грудня 2015): e1468. http://dx.doi.org/10.7717/peerj.1468.
Повний текст джерелаKnights, K., and C. Drogemuller. "Xenobiotic-CoA Ligases: Kinetic and Molecular Characterization." Current Drug Metabolism 1, no. 1 (July 1, 2000): 49–66. http://dx.doi.org/10.2174/1389200003339261.
Повний текст джерелаBarragán, María J. López, Manuel Carmona, María T. Zamarro, Bärbel Thiele, Matthias Boll, Georg Fuchs, José L. García, and Eduardo Díaz. "The bzd Gene Cluster, Coding for Anaerobic Benzoate Catabolism, in Azoarcus sp. Strain CIB." Journal of Bacteriology 186, no. 17 (September 1, 2004): 5762–74. http://dx.doi.org/10.1128/jb.186.17.5762-5774.2004.
Повний текст джерелаPhilpott, Helena K., Pamela J. Thomas, David Tew, Doug E. Fuerst, and Sarah L. Lovelock. "A versatile biosynthetic approach to amide bond formation." Green Chemistry 20, no. 15 (2018): 3426–31. http://dx.doi.org/10.1039/c8gc01697f.
Повний текст джерелаSunstrum, Frederick G., Hannah L. Liu, Sharon Jancsik, Lufiani L. Madilao, Joerg Bohlmann, and Sandra Irmisch. "4-Coumaroyl-CoA ligases in the biosynthesis of the anti-diabetic metabolite montbretin A." PLOS ONE 16, no. 10 (October 7, 2021): e0257478. http://dx.doi.org/10.1371/journal.pone.0257478.
Повний текст джерелаArora, Pooja, Archana Vats, Priti Saxena, Debasisa Mohanty, and Rajesh S. Gokhale. "Promiscuous Fatty Acyl CoA Ligases Produce Acyl-CoA and Acyl-SNAC Precursors for Polyketide Biosynthesis." Journal of the American Chemical Society 127, no. 26 (July 2005): 9388–89. http://dx.doi.org/10.1021/ja052991s.
Повний текст джерелаKlempien, Antje, Yasuhisa Kaminaga, Anthony Qualley, Dinesh A. Nagegowda, Joshua R. Widhalm, Irina Orlova, Ajit Kumar Shasany, et al. "Contribution of CoA Ligases to Benzenoid Biosynthesis in Petunia Flowers." Plant Cell 24, no. 5 (May 2012): 2015–30. http://dx.doi.org/10.1105/tpc.112.097519.
Повний текст джерелаSingh, Inderjit, Alok Bhushan, Nand Kishore Relan, and Takashi Hashimoto. "Acyl-CoA ligases from rat brain microsomes: An immunochemical study." Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism 963, no. 3 (December 1988): 509–14. http://dx.doi.org/10.1016/0005-2760(88)90319-0.
Повний текст джерелаColeman, James P., L. Lynn Hudson, Susan L. McKnight, John M. Farrow, M. Worth Calfee, Claire A. Lindsey, and Everett C. Pesci. "Pseudomonas aeruginosa PqsA Is an Anthranilate-Coenzyme A Ligase." Journal of Bacteriology 190, no. 4 (December 14, 2007): 1247–55. http://dx.doi.org/10.1128/jb.01140-07.
Повний текст джерелаKnights, Kathleen M., and Benjamin J. Roberts. "Xenobiotic acyl-CoA formation: evidence of kinetically distinct hepatic microsomal long-chain fatty acid and nafenopin-CoA ligases." Chemico-Biological Interactions 90, no. 3 (March 1994): 215–23. http://dx.doi.org/10.1016/0009-2797(94)90011-6.
Повний текст джерелаLuís, Paula B. M., Jos Ruiter, Lodewijk IJlst, Isabel Tavares de Almeida, Marinus Duran, Ronald J. A. Wanders, and Margarida F. B. Silva. "Valproyl-CoA inhibits the activity of ATP- and GTP-dependent succinate:CoA ligases." Journal of Inherited Metabolic Disease 37, no. 3 (October 24, 2013): 353–57. http://dx.doi.org/10.1007/s10545-013-9657-4.
Повний текст джерелаPeters, Franziska, Michael Rother, and Matthias Boll. "Selenocysteine-Containing Proteins in Anaerobic Benzoate Metabolism of Desulfococcus multivorans." Journal of Bacteriology 186, no. 7 (April 1, 2004): 2156–63. http://dx.doi.org/10.1128/jb.186.7.2156-2163.2004.
Повний текст джерелаBerger, Martine, Nelson L. Brock, Heiko Liesegang, Marco Dogs, Ines Preuth, Meinhard Simon, Jeroen S. Dickschat, and Thorsten Brinkhoff. "Genetic Analysis of the Upper Phenylacetate Catabolic Pathway in the Production of Tropodithietic Acid by Phaeobacter gallaeciensis." Applied and Environmental Microbiology 78, no. 10 (March 9, 2012): 3539–51. http://dx.doi.org/10.1128/aem.07657-11.
Повний текст джерелаLavhale, Santosh G., Rakesh S. Joshi, Yashwant Kumar, and Ashok P. Giri. "Functional insights into two Ocimum kilimandscharicum 4-coumarate-CoA ligases involved in phenylpropanoid biosynthesis." International Journal of Biological Macromolecules 181 (June 2021): 202–10. http://dx.doi.org/10.1016/j.ijbiomac.2021.03.129.
Повний текст джерелаKnights, Kathleen. "Long-Chain-Fatty-Acid CoA Ligases: The Key to Fatty Acid Activation, Formation of Xenobiotic Acyl-CoA Thioesters and Lipophilic Xenobiotic Conjugates." Current Medicinal Chemistry-Immunology, Endocrine & Metabolic Agents 3, no. 3 (September 1, 2003): 235–44. http://dx.doi.org/10.2174/1568013033483384.
Повний текст джерелаGo, Maybelle Kho, Jeng Yeong Chow, Vivian Wing Ngar Cheung, Yan Ping Lim, and Wen Shan Yew. "Establishing a Toolkit for Precursor-Directed Polyketide Biosynthesis: Exploring Substrate Promiscuities of Acid-CoA Ligases." Biochemistry 51, no. 22 (May 22, 2012): 4568–79. http://dx.doi.org/10.1021/bi300425j.
Повний текст джерелаLazo, O., M. Contreras, Y. Yoshida, AK Singh, W. Stanley, M. Weise, and I. Singh. "Cellular oxidation of lignoceric acid is regulated by the subcellular localization of lignoceroyl-CoA ligases." Journal of Lipid Research 31, no. 4 (April 1990): 583–95. http://dx.doi.org/10.1016/s0022-2275(20)42826-3.
Повний текст джерелаVessey, Donald A., Jie Hu, and Michael Kelley. "Interaction of salicylate and ibuprofen with the carboxylic acid: CoA ligases from bovine liver mitochondria." Journal of Biochemical Toxicology 11, no. 2 (1996): 73–78. http://dx.doi.org/10.1002/(sici)1522-7146(1996)11:2<73::aid-jbt4>3.0.co;2-r.
Повний текст джерелаBabbitt, Patricia C., George L. Kenyon, Brian M. Martin, Hugues Charest, Michel Slyvestre, Jeffrey D. Scholten, Kai Hsuan Chang, Po Huang Liang, and Debra Dunaway-Mariano. "Ancestry of the 4-chlorobenzoate dehalogenase: analysis of amino acid sequence identities among families of acyl:adenyl ligases, enoyl-CoA hydratases/isomerases, and acyl-CoA thioesterases." Biochemistry 31, no. 24 (June 1992): 5594–604. http://dx.doi.org/10.1021/bi00139a024.
Повний текст джерелаBaran, Marzena, Kimberly D. Grimes, Paul A. Sibbald, Peng Fu, Helena I. M. Boshoff, Daniel J. Wilson, and Courtney C. Aldrich. "Development of small-molecule inhibitors of fatty acyl-AMP and fatty acyl-CoA ligases in Mycobacterium tuberculosis." European Journal of Medicinal Chemistry 201 (September 2020): 112408. http://dx.doi.org/10.1016/j.ejmech.2020.112408.
Повний текст джерелаXu, Jaiwei, Haifang Zhao, and Tao Wang. "Suppression of retinal degeneration by two novel ERAD ubiquitin E3 ligases SORDD1/2 in Drosophila." PLOS Genetics 16, no. 11 (November 2, 2020): e1009172. http://dx.doi.org/10.1371/journal.pgen.1009172.
Повний текст джерелаMcInerney, Michael J., Lars Rohlin, Housna Mouttaki, UnMi Kim, Rebecca S. Krupp, Luis Rios-Hernandez, Jessica Sieber, et al. "The genome of Syntrophus aciditrophicus: Life at the thermodynamic limit of microbial growth." Proceedings of the National Academy of Sciences 104, no. 18 (April 18, 2007): 7600–7605. http://dx.doi.org/10.1073/pnas.0610456104.
Повний текст джерелаDong, Yanpeng, Huiqian Du, Chunxu Gao, Ting Ma, and Lu Feng. "Characterization of two long-chain fatty acid CoA ligases in the Gram-positive bacterium Geobacillus thermodenitrificans NG80-2." Microbiological Research 167, no. 10 (December 2012): 602–7. http://dx.doi.org/10.1016/j.micres.2012.05.001.
Повний текст джерелаVessey, Donald A., Michael Kelley, Eva Lau, and Shirley Z. Zhang. "Monovalent cation effects on the activity of the xenobiotic/medium-chain fatty acid: CoA ligases are substrate specific." Journal of Biochemical and Molecular Toxicology 14, no. 3 (2000): 162–68. http://dx.doi.org/10.1002/(sici)1099-0461(2000)14:3<162::aid-jbt6>3.0.co;2-8.
Повний текст джерелаKrawiec, Brian J., Gerald J. Nystrom, Robert A. Frost, Leonard S. Jefferson, and Charles H. Lang. "AMP-activated protein kinase agonists increase mRNA content of the muscle-specific ubiquitin ligases MAFbx and MuRF1 in C2C12 cells." American Journal of Physiology-Endocrinology and Metabolism 292, no. 6 (June 2007): E1555—E1567. http://dx.doi.org/10.1152/ajpendo.00622.2006.
Повний текст джерелаVessey, Donald A., and Michael Kelley. "Characterization of the monovalent and divalent cation requirements for the xenobiotic carboxylic acid: CoA ligases of bovine liver mitochondria." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1382, no. 2 (February 1998): 243–48. http://dx.doi.org/10.1016/s0167-4838(97)00163-5.
Повний текст джерелаLaw, Adrienne, and Martin J. Boulanger. "Defining a Structural and Kinetic Rationale for Paralogous Copies of Phenylacetate-CoA Ligases from the Cystic Fibrosis PathogenBurkholderia cenocepaciaJ2315." Journal of Biological Chemistry 286, no. 17 (March 8, 2011): 15577–85. http://dx.doi.org/10.1074/jbc.m111.219683.
Повний текст джерелаvan der Sluis, Rencia. "Analyses of the genetic diversity and protein expression variation of the acyl: CoA medium-chain ligases, ACSM2A and ACSM2B." Molecular Genetics and Genomics 293, no. 5 (June 14, 2018): 1279–92. http://dx.doi.org/10.1007/s00438-018-1460-3.
Повний текст джерелаJo, Y., P. C. W. Lee, P. V. Sguigna, and R. A. DeBose-Boyd. "Sterol-induced degradation of HMG CoA reductase depends on interplay of two Insigs and two ubiquitin ligases, gp78 and Trc8." Proceedings of the National Academy of Sciences 108, no. 51 (December 5, 2011): 20503–8. http://dx.doi.org/10.1073/pnas.1112831108.
Повний текст джерелаWilhovsky, Sharon, Richard Gardner, and Randolph Hampton. "HRDGene Dependence of Endoplasmic Reticulum-associated Degradation." Molecular Biology of the Cell 11, no. 5 (May 2000): 1697–708. http://dx.doi.org/10.1091/mbc.11.5.1697.
Повний текст джерелаGao, Shuai, Xin-Yan Liu, Rong Ni, Jie Fu, Hui Tan, Ai-Xia Cheng, and Hong-Xiang Lou. "Molecular cloning and functional analysis of 4-coumarate: CoA ligases from Marchantia paleacea and their roles in lignin and flavanone biosynthesis." PLOS ONE 19, no. 1 (January 8, 2024): e0296079. http://dx.doi.org/10.1371/journal.pone.0296079.
Повний текст джерелаRoberts, B. J., and K. M. Knights. "Differential induction of rat hepatic microsomal and peroxisomal long-chain and nafenopin-CoA ligases by clofibric acid and di-(2-ethylhexyl)phthalate." Xenobiotica 25, no. 5 (January 1995): 469–76. http://dx.doi.org/10.3109/00498259509061866.
Повний текст джерелаJo, Youngah, Isamu Z. Hartman, and Russell A. DeBose-Boyd. "Ancient ubiquitous protein-1 mediates sterol-induced ubiquitination of 3-hydroxy-3-methylglutaryl CoA reductase in lipid droplet–associated endoplasmic reticulum membranes." Molecular Biology of the Cell 24, no. 3 (February 2013): 169–83. http://dx.doi.org/10.1091/mbc.e12-07-0564.
Повний текст джерелаElsabrouty, Rania, Youngah Jo, Tammy T. Dinh, and Russell A. DeBose-Boyd. "Sterol-induced dislocation of 3-hydroxy-3-methylglutaryl coenzyme A reductase from membranes of permeabilized cells." Molecular Biology of the Cell 24, no. 21 (November 2013): 3300–3308. http://dx.doi.org/10.1091/mbc.e13-03-0157.
Повний текст джерелаViviani, V. R., R. A. Prado, D. R. Neves, D. Kato, and J. A. Barbosa. "A Route from Darkness to Light: Emergence and Evolution of Luciferase Activity in AMP-CoA-Ligases Inferred from a Mealworm Luciferase-like Enzyme." Biochemistry 52, no. 23 (May 30, 2013): 3963–73. http://dx.doi.org/10.1021/bi400141u.
Повний текст джерелаVessey, Donald A., Michael Kelley, and Robert S. Warren. "Characterization of the CoA ligases of human liver mitochondria catalyzing the activation of short- and medium-chain fatty acids and xenobiotic carboxylic acids." Biochimica et Biophysica Acta (BBA) - General Subjects 1428, no. 2-3 (August 1999): 455–62. http://dx.doi.org/10.1016/s0304-4165(99)00088-4.
Повний текст джерелаBains, Jasleen, and Martin J. Boulanger. "Biochemical and Structural Characterization of the Paralogous Benzoate CoA Ligases from Burkholderia xenovorans LB400: Defining the Entry Point into the Novel Benzoate Oxidation (box) Pathway." Journal of Molecular Biology 373, no. 4 (November 2007): 965–77. http://dx.doi.org/10.1016/j.jmb.2007.08.008.
Повний текст джерелаRobinson, Serina L., Barbara R. Terlouw, Megan D. Smith, Sacha J. Pidot, Timothy P. Stinear, Marnix H. Medema та Lawrence P. Wackett. "Global analysis of adenylate-forming enzymes reveals β-lactone biosynthesis pathway in pathogenic Nocardia". Journal of Biological Chemistry 295, № 44 (21 серпня 2020): 14826–39. http://dx.doi.org/10.1074/jbc.ra120.013528.
Повний текст джерелаErzurumlu, Yalcin, Deniz Catakli, and Hatice Kubra Dogan. "Circadian Oscillation Pattern of Endoplasmic Reticulum Quality Control (ERQC) Components in Human Embryonic Kidney HEK293 Cells." Journal of Circadian Rhythms 21 (April 3, 2023): 1. http://dx.doi.org/10.5334/jcr.219.
Повний текст джерелаDu, Yuanxu, Shuo Gao, Hui Ma, Siqi Lu, Zhenhua Zhang, and Mengmeng Zhao. "Catalytic Behavior of Cobalt Complexes Bearing Pyridine–Oxime Ligands in Isoprene Polymerization." Polymers 15, no. 24 (December 10, 2023): 4660. http://dx.doi.org/10.3390/polym15244660.
Повний текст джерелаZhuang, Zhihao, Karl-Heinz Gartemann, Rudolf Eichenlaub, and Debra Dunaway-Mariano. "Characterization of the 4-Hydroxybenzoyl-Coenzyme A Thioesterase from Arthrobacter sp. Strain SU." Applied and Environmental Microbiology 69, no. 5 (May 2003): 2707–11. http://dx.doi.org/10.1128/aem.69.5.2707-2711.2003.
Повний текст джерелаHawkins, Aaron B., Michael W. W. Adams, and Robert M. Kelly. "Conversion of 4-Hydroxybutyrate to Acetyl Coenzyme A and Its Anapleurosis in the Metallosphaera sedula 3-Hydroxypropionate/4-Hydroxybutyrate Carbon Fixation Pathway." Applied and Environmental Microbiology 80, no. 8 (February 14, 2014): 2536–45. http://dx.doi.org/10.1128/aem.04146-13.
Повний текст джерелаWong, Gail A., James D. Bergstrom, and John Edmond. "Acetoacetyl-CoA ligase activity in the isolated rat hepatocyte: Effects of 25-hydroxycholesterol and high density lipoprotein." Bioscience Reports 7, no. 3 (March 1, 1987): 217–24. http://dx.doi.org/10.1007/bf01124792.
Повний текст джерелаSchühle, Karola, Johannes Gescher, Ulrich Feil, Michael Paul, Martina Jahn, Hermann Schägger, and Georg Fuchs. "Benzoate-Coenzyme A Ligase from Thauera aromatica: an Enzyme Acting in Anaerobic and Aerobic Pathways." Journal of Bacteriology 185, no. 16 (August 15, 2003): 4920–29. http://dx.doi.org/10.1128/jb.185.16.4920-4929.2003.
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