Artículos de revistas sobre el tema "Functional Modeling - Heme Enzymes"
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Timmins, Amy y Sam P. de Visser. "A Comparative Review on the Catalytic Mechanism of Nonheme Iron Hydroxylases and Halogenases". Catalysts 8, n.º 8 (31 de julio de 2018): 314. http://dx.doi.org/10.3390/catal8080314.
Texto completoRobins, Tiina, Jonas Carlsson, Maria Sunnerhagen, Anna Wedell y Bengt Persson. "Molecular Model of Human CYP21 Based on Mammalian CYP2C5: Structural Features Correlate with Clinical Severity of Mutations Causing Congenital Adrenal Hyperplasia". Molecular Endocrinology 20, n.º 11 (1 de noviembre de 2006): 2946–64. http://dx.doi.org/10.1210/me.2006-0172.
Texto completoKrone, Nils, Yulia Grischuk, Marina Müller, Ruth Elisabeth Volk, Joachim Grötzinger, Paul-Martin Holterhus, Wolfgang G. Sippell y Felix G. Riepe. "Analyzing the Functional and Structural Consequences of Two Point Mutations (P94L and A368D) in the CYP11B1 Gene Causing Congenital Adrenal Hyperplasia Resulting from 11-Hydroxylase Deficiency". Journal of Clinical Endocrinology & Metabolism 91, n.º 7 (1 de julio de 2006): 2682–88. http://dx.doi.org/10.1210/jc.2006-0209.
Texto completoFontecave, M., S. Ménage y C. Duboc-Toia. "Functional models of non-heme diiron enzymes". Coordination Chemistry Reviews 178-180 (diciembre de 1998): 1555–72. http://dx.doi.org/10.1016/s0010-8545(98)00119-2.
Texto completoShteinman, A. A. "Structural-functional modeling of non-heme oxygenases". Russian Chemical Bulletin 60, n.º 7 (julio de 2011): 1290–300. http://dx.doi.org/10.1007/s11172-011-0197-5.
Texto completoYadav, Rahul y Emily E. Scott. "Endogenous insertion of non-native metalloporphyrins into human membrane cytochrome P450 enzymes". Journal of Biological Chemistry 293, n.º 43 (14 de septiembre de 2018): 16623–34. http://dx.doi.org/10.1074/jbc.ra118.005417.
Texto completoNemukhin, A. V., B. L. Grigorenko, I. A. Topol y S. K. Burt. "Modeling dioxygen binding to the non-heme iron-containing enzymes". International Journal of Quantum Chemistry 106, n.º 10 (2006): 2184–90. http://dx.doi.org/10.1002/qua.20910.
Texto completoBoynton, Tye O., Svetlana Gerdes, Sarah H. Craven, Ellen L. Neidle, John D. Phillips y Harry A. Dailey. "Discovery of a Gene Involved in a Third Bacterial Protoporphyrinogen Oxidase Activity through Comparative Genomic Analysis and Functional Complementation". Applied and Environmental Microbiology 77, n.º 14 (3 de junio de 2011): 4795–801. http://dx.doi.org/10.1128/aem.00171-11.
Texto completoKojima, T., T. Amano, Y. Ishii y Y. Matsuda. "Ruthenium-pyridylamine complexes as functional models of non-heme iron enzymes". Journal of Inorganic Biochemistry 67, n.º 1-4 (julio de 1997): 238. http://dx.doi.org/10.1016/s0162-0134(97)80111-0.
Texto completoMatsunaga, Isamu y Yoshitsugu Shiro. "Peroxide-utilizing biocatalysts: structural and functional diversity of heme-containing enzymes". Current Opinion in Chemical Biology 8, n.º 2 (abril de 2004): 127–32. http://dx.doi.org/10.1016/j.cbpa.2004.01.001.
Texto completoAtteia, Ariane, Robert van Lis y Samuel I. Beale. "Enzymes of the Heme Biosynthetic Pathway in the Nonphotosynthetic Alga Polytomella sp." Eukaryotic Cell 4, n.º 12 (diciembre de 2005): 2087–97. http://dx.doi.org/10.1128/ec.4.12.2087-2097.2005.
Texto completoPark, Hyunchang y Dongwhan Lee. "Ligand Taxonomy for Bioinorganic Modeling of Dioxygen‐Activating Non‐Heme Iron Enzymes". Chemistry – A European Journal 26, n.º 27 (17 de marzo de 2020): 5916–26. http://dx.doi.org/10.1002/chem.201904975.
Texto completoShiro, Yoshitsugu. "Functional Studies on Hemoproteins and Heme-enzymes Based on Their Molecular Structures". Bulletin of Japan Society of Coordination Chemistry 75 (31 de mayo de 2020): 51–56. http://dx.doi.org/10.4019/bjscc.75.51.
Texto completoBelsare, Ketaki D., Anna Joëlle Ruff, Ronny Martinez y Ulrich Schwaneberg. "Insights on intermolecular FMN-heme domain interaction and the role of linker length in cytochrome P450cin fusion proteins". Biological Chemistry 401, n.º 11 (25 de octubre de 2020): 1249–55. http://dx.doi.org/10.1515/hsz-2020-0134.
Texto completoMirts, Evan N., Igor D. Petrik, Parisa Hosseinzadeh, Mark J. Nilges y Yi Lu. "A designed heme-[4Fe-4S] metalloenzyme catalyzes sulfite reduction like the native enzyme". Science 361, n.º 6407 (13 de septiembre de 2018): 1098–101. http://dx.doi.org/10.1126/science.aat8474.
Texto completoHa, Edward H., Raymond Y. N. Ho, James F. Kisiel y Joan Selverstone Valentine. "Modeling the Reactivity of .alpha.-Ketoglutarate-Dependent Non-Heme Iron(II)-Containing Enzymes". Inorganic Chemistry 34, n.º 9 (abril de 1995): 2265–66. http://dx.doi.org/10.1021/ic00113a002.
Texto completoMohammadi, Mahnaz, Fatematossadat Pourseyed Aghaei, Banafsheh Noori y Esmaeil Pakizeh. "Density Functional Theory modeling of the magnetic susceptibility of heme derivatives". Chemical Physics 527 (noviembre de 2019): 110498. http://dx.doi.org/10.1016/j.chemphys.2019.110498.
Texto completoBadawy, Abdulla A.-B. "Kynurenine Pathway of Tryptophan Metabolism: Regulatory and Functional Aspects". International Journal of Tryptophan Research 10 (1 de enero de 2017): 117864691769193. http://dx.doi.org/10.1177/1178646917691938.
Texto completoLaBella, Frank S. "Cytochrome P450 enzymes: ubiquitous "receptors" for drugs". Canadian Journal of Physiology and Pharmacology 69, n.º 8 (1 de agosto de 1991): 1129–32. http://dx.doi.org/10.1139/y91-165.
Texto completoCarrasco, Maria C. y Shabnam Hematian. "(Hydr)oxo-bridged heme complexes: From structure to reactivity". Journal of Porphyrins and Phthalocyanines 23, n.º 11n12 (diciembre de 2019): 1286–307. http://dx.doi.org/10.1142/s1088424619300258.
Texto completoArnhold, Jürgen y Ernst Malle. "Halogenation Activity of Mammalian Heme Peroxidases". Antioxidants 11, n.º 5 (30 de abril de 2022): 890. http://dx.doi.org/10.3390/antiox11050890.
Texto completoKellmann, Ralf, Toby Mills y Brett A. Neilan. "Functional Modeling and Phylogenetic Distribution of Putative Cylindrospermopsin Biosynthesis Enzymes". Journal of Molecular Evolution 62, n.º 3 (25 de febrero de 2006): 267–80. http://dx.doi.org/10.1007/s00239-005-0030-6.
Texto completoChance, M., L. Powers, C. Kumar y B. Chance. "X-ray absorption studies of myoglobin peroxide reveal functional differences between globins and heme enzymes". Biochemistry 25, n.º 6 (marzo de 1986): 1259–65. http://dx.doi.org/10.1021/bi00354a010.
Texto completoSavino, Maria, Claudio Carmine Guida, Maria Nardella, Emanuele Murgo, Bartolomeo Augello, Giuseppe Merla, Salvatore De Cosmo et al. "Circadian Genes Expression Patterns in Disorders Due to Enzyme Deficiencies in the Heme Biosynthetic Pathway". Biomedicines 10, n.º 12 (9 de diciembre de 2022): 3198. http://dx.doi.org/10.3390/biomedicines10123198.
Texto completoKitanishi, Kenichi, Kazuo Kobayashi, Takeshi Uchida, Koichiro Ishimori, Jotaro Igarashi y Toru Shimizu. "Identification and Functional and Spectral Characterization of a Globin-coupled Histidine Kinase from Anaeromyxobacter sp. Fw109-5". Journal of Biological Chemistry 286, n.º 41 (18 de agosto de 2011): 35522–34. http://dx.doi.org/10.1074/jbc.m111.274811.
Texto completoKonduri, Purna Chaitanya, Tianyuan Wang, Narges Salamat y Li Zhang. "Heme, A Metabolic Sensor, Directly Regulates the Activity of the KDM4 Histone Demethylase Family and Their Interactions with Partner Proteins". Cells 9, n.º 3 (22 de marzo de 2020): 773. http://dx.doi.org/10.3390/cells9030773.
Texto completoHagadorn, John R., Lawrence Que y William B. Tolman. "A Bulky Benzoate Ligand for Modeling the Carboxylate-Rich Active Sites of Non-Heme Diiron Enzymes". Journal of the American Chemical Society 120, n.º 51 (diciembre de 1998): 13531–32. http://dx.doi.org/10.1021/ja983333t.
Texto completoBabandi, Abba, Chioma A. Anosike, Lawrence U. S. Ezeanyika, Kemal Yelekçi y Abdullahi Ibrahim Uba. "Molecular modeling studies of some phytoligands from Ficus sycomorus fraction as potential inhibitors of cytochrome CYP6P3 enzyme of Anopheles coluzzii". Jordan Journal of Pharmaceutical Sciences 15, n.º 2 (1 de junio de 2022): 258–75. http://dx.doi.org/10.35516/jjps.v15i2.324.
Texto completoPark, Kiyoung y Edward I. Solomon. "Modeling nuclear resonance vibrational spectroscopic data of binuclear nonheme iron enzymes using density functional theory". Canadian Journal of Chemistry 92, n.º 10 (octubre de 2014): 975–78. http://dx.doi.org/10.1139/cjc-2014-0067.
Texto completoSiletsky, Sergey A. y Vitaliy B. Borisov. "Proton Pumping and Non-Pumping Terminal Respiratory Oxidases: Active Sites Intermediates of These Molecular Machines and Their Derivatives". International Journal of Molecular Sciences 22, n.º 19 (7 de octubre de 2021): 10852. http://dx.doi.org/10.3390/ijms221910852.
Texto completoNaruta, Yoshinori, Masa-aki Sasayama y Kanako Ichihara. "Functional modeling of managanese-containing O2 evolution enzymes with managanese porphyrin dimers". Journal of Molecular Catalysis A: Chemical 117, n.º 1-3 (marzo de 1997): 115–21. http://dx.doi.org/10.1016/s1381-1169(96)00416-5.
Texto completoMajumdar, Amit y Sabyasachi Sarkar. "Bioinorganic chemistry of molybdenum and tungsten enzymes: A structural–functional modeling approach". Coordination Chemistry Reviews 255, n.º 9-10 (mayo de 2011): 1039–54. http://dx.doi.org/10.1016/j.ccr.2010.11.027.
Texto completoWan, Dun, Li Fu Liao y Ying Wu Lin. "Impacts of Uranyl Ion on the Structure and Function of Cytochrome b5 His39Ser Mutant". Advanced Materials Research 455-456 (enero de 2012): 1204–9. http://dx.doi.org/10.4028/www.scientific.net/amr.455-456.1204.
Texto completoShumyantseva, Victoria V., Polina I. Koroleva, Tatiana V. Bulko y Lyubov E. Agafonova. "Alternative Electron Sources for Cytochrome P450s Catalytic Cycle: Biosensing and Biosynthetic Application". Processes 11, n.º 6 (13 de junio de 2023): 1801. http://dx.doi.org/10.3390/pr11061801.
Texto completoTewari, Rajesh Kumar. "Nitric Oxide-Mediated Modulation of Functional Iron Status in Iron-Deficient Maize Plants". INTERNATIONAL JOURNAL OF PLANT AND ENVIRONMENT 5, n.º 02 (30 de abril de 2019): 78–83. http://dx.doi.org/10.18811/ijpen.v5i02.2.
Texto completoRondelli, Catherine, Aiden Danoff, Hector Bergonia, Samantha Gillis, Julia Free, John D. Phillips y Yvette Y. Yien. "Regulation of Erythroid Heme Synthesis By the Mitochondrial Clpx Unfoldase". Blood 134, Supplement_1 (13 de noviembre de 2019): 427. http://dx.doi.org/10.1182/blood-2019-132039.
Texto completoBela, Krisztina, Riyazuddin Riyazuddin y Jolán Csiszár. "Plant Glutathione Peroxidases: Non-Heme Peroxidases with Large Functional Flexibility as a Core Component of ROS-Processing Mechanisms and Signalling". Antioxidants 11, n.º 8 (21 de agosto de 2022): 1624. http://dx.doi.org/10.3390/antiox11081624.
Texto completoAcerbi, Enzo, Marcela Hortova-Kohoutkova, Tsokyi Choera, Nancy Keller, Jan Fric, Fabio Stella, Luigina Romani y Teresa Zelante. "Modeling Approaches Reveal New Regulatory Networks in Aspergillus fumigatus Metabolism". Journal of Fungi 6, n.º 3 (14 de julio de 2020): 108. http://dx.doi.org/10.3390/jof6030108.
Texto completoSatarug, Soisungwan, David A. Vesey y Glenda C. Gobe. "Mitigation of Cadmium Toxicity through Modulation of the Frontline Cellular Stress Response". Stresses 2, n.º 3 (15 de septiembre de 2022): 355–72. http://dx.doi.org/10.3390/stresses2030025.
Texto completoRovaletti, Anna, Luca De Gioia, Piercarlo Fantucci, Claudio Greco, Jacopo Vertemara, Giuseppe Zampella, Federica Arrigoni y Luca Bertini. "Recent Theoretical Insights into the Oxidative Degradation of Biopolymers and Plastics by Metalloenzymes". International Journal of Molecular Sciences 24, n.º 7 (28 de marzo de 2023): 6368. http://dx.doi.org/10.3390/ijms24076368.
Texto completoBarreiro, Esther, Alain S. Comtois, Shawn Mohammed, Larry C. Lands y Sabah N. A. Hussain. "Role of heme oxygenases in sepsis-induced diaphragmatic contractile dysfunction and oxidative stress". American Journal of Physiology-Lung Cellular and Molecular Physiology 283, n.º 2 (1 de agosto de 2002): L476—L484. http://dx.doi.org/10.1152/ajplung.00495.2001.
Texto completoKim, In Jung, Yannik Brack, Thomas Bayer y Uwe T. Bornscheuer. "Two novel cyanobacterial α-dioxygenases for the biosynthesis of fatty aldehydes". Applied Microbiology and Biotechnology 106, n.º 1 (9 de diciembre de 2021): 197–210. http://dx.doi.org/10.1007/s00253-021-11724-x.
Texto completoEmpel, Claire, Sripati Jana y Rene M. Koenigs. "C-H Functionalization via Iron-Catalyzed Carbene-Transfer Reactions". Molecules 25, n.º 4 (17 de febrero de 2020): 880. http://dx.doi.org/10.3390/molecules25040880.
Texto completoClark, RA y N. Borregaard. "Neutrophils autoinactivate secretory products by myeloperoxidase- catalyzed oxidation". Blood 65, n.º 2 (1 de febrero de 1985): 375–81. http://dx.doi.org/10.1182/blood.v65.2.375.375.
Texto completoClark, RA y N. Borregaard. "Neutrophils autoinactivate secretory products by myeloperoxidase- catalyzed oxidation". Blood 65, n.º 2 (1 de febrero de 1985): 375–81. http://dx.doi.org/10.1182/blood.v65.2.375.bloodjournal652375.
Texto completoYudenfreund Kravitz, Joslyn y Vincent L. Pecoraro. "Synthetic and computational modeling of the vanadium-dependent haloperoxidases". Pure and Applied Chemistry 77, n.º 9 (1 de enero de 2005): 1595–605. http://dx.doi.org/10.1351/pac200577091595.
Texto completoBruijnincx, Pieter C. A., Gerard van Koten y Robertus J. M. Klein Gebbink. "Mononuclear non-heme iron enzymes with the 2-His-1-carboxylate facial triad: recent developments in enzymology and modeling studies". Chemical Society Reviews 37, n.º 12 (2008): 2716. http://dx.doi.org/10.1039/b707179p.
Texto completoLee, Dongwhan y Stephen J. Lippard. "Structural and Functional Models of the Dioxygen-Activating Centers of Non-Heme Diiron Enzymes Ribonucleotide Reductase and Soluble Methane Monooxygenase". Journal of the American Chemical Society 120, n.º 46 (noviembre de 1998): 12153–54. http://dx.doi.org/10.1021/ja9831094.
Texto completoRodrigues, Carolina F., Patrícia T. Borges, Magali F. Scocozza, Diogo Silva, André Taborda, Vânia Brissos, Carlos Frazão y Lígia O. Martins. "Loops around the Heme Pocket Have a Critical Role in the Function and Stability of BsDyP from Bacillus subtilis". International Journal of Molecular Sciences 22, n.º 19 (8 de octubre de 2021): 10862. http://dx.doi.org/10.3390/ijms221910862.
Texto completoDhar, Manoj Kumar, Sonal Mishra, Archana Bhat, Sudha Chib y Sanjana Kaul. "Plant carotenoid cleavage oxygenases: structure–function relationships and role in development and metabolism". Briefings in Functional Genomics 19, n.º 1 (26 de diciembre de 2019): 1–9. http://dx.doi.org/10.1093/bfgp/elz037.
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