Статті в журналах з теми "Cu cofactor"
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Ознайомтеся з топ-50 статей у журналах для дослідження на тему "Cu cofactor".
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Murakawa, Takeshi, Kazuo Kurihara, Mitsuo Shoji, Chie Shibazaki, Tomoko Sunami, Taro Tamada, Naomine Yano, et al. "Neutron crystallography of copper amine oxidase reveals keto/enolate interconversion of the quinone cofactor and unusual proton sharing." Proceedings of the National Academy of Sciences 117, no. 20 (May 5, 2020): 10818–24. http://dx.doi.org/10.1073/pnas.1922538117.
Повний текст джерелаKwok, Man Long, Xue Lei Hu, Qi Meng, and King Ming Chan. "Whole-transcriptome sequencing (RNA-seq) analyses of the zebrafish liver cell line, ZFL, after acute exposure to Cu2+ ions." Metallomics 12, no. 5 (2020): 732–51. http://dx.doi.org/10.1039/d0mt00005a.
Повний текст джерелаGoto, Norika, Hirokazu Hara, Mao Kondo, Naomi Yasuda, Tetsuro Kamiya, Kensuke Okuda, and Tetsuo Adachi. "Hydrogen sulfide increases copper-dependent neurotoxicity via intracellular copper accumulation." Metallomics 12, no. 6 (2020): 868–75. http://dx.doi.org/10.1039/d0mt00015a.
Повний текст джерелаMorpurgo, L., E. Agostinelli, O. Befani, and B. Mondovì. "Reactions of bovine serum amine oxidase with NN-diethyldithiocarbamate. Selective removal of one copper ion." Biochemical Journal 248, no. 3 (December 15, 1987): 865–70. http://dx.doi.org/10.1042/bj2480865.
Повний текст джерелаKwok, Man Long, and King Ming Chan. "Functional characterization of copper transporters zCtr1, zAtox1, zAtp7a and zAtp7b in zebrafish liver cell line ZFL." Metallomics 11, no. 9 (2019): 1532–46. http://dx.doi.org/10.1039/c9mt00159j.
Повний текст джерелаTasaki, Eisuke, Kazuya Kobayashi, Kenji Matsuura, and Yoshihito Iuchi. "Long-Lived Termite Queens Exhibit High Cu/Zn-Superoxide Dismutase Activity." Oxidative Medicine and Cellular Longevity 2018 (2018): 1–8. http://dx.doi.org/10.1155/2018/5127251.
Повний текст джерелаSong, Haiyan, Chunling Ma, Pi Liu, Chun You, Jianping Lin, and Zhiguang Zhu. "A hybrid CO2 electroreduction system mediated by enzyme-cofactor conjugates coupled with Cu nanoparticle-catalyzed cofactor regeneration." Journal of CO2 Utilization 34 (December 2019): 568–75. http://dx.doi.org/10.1016/j.jcou.2019.08.007.
Повний текст джерелаWhittaker, Mei M., and James W. Whittaker. "Cu(I)-dependent Biogenesis of the Galactose Oxidase Redox Cofactor." Journal of Biological Chemistry 278, no. 24 (April 1, 2003): 22090–101. http://dx.doi.org/10.1074/jbc.m300112200.
Повний текст джерелаYoung, Tessa R., and Zhiguang Xiao. "Principles and practice of determining metal–protein affinities." Biochemical Journal 478, no. 5 (March 10, 2021): 1085–116. http://dx.doi.org/10.1042/bcj20200838.
Повний текст джерелаChen, Guang, Jia Li, Huimin Han, Ruiying Du, and Xu Wang. "Physiological and Molecular Mechanisms of Plant Responses to Copper Stress." International Journal of Molecular Sciences 23, no. 21 (October 26, 2022): 12950. http://dx.doi.org/10.3390/ijms232112950.
Повний текст джерелаAndrei, Andreea, Yavuz Öztürk, Bahia Khalfaoui-Hassani, Juna Rauch, Dorian Marckmann, Petru-Iulian Trasnea, Fevzi Daldal, and Hans-Georg Koch. "Cu Homeostasis in Bacteria: The Ins and Outs." Membranes 10, no. 9 (September 18, 2020): 242. http://dx.doi.org/10.3390/membranes10090242.
Повний текст джерелаFukai, Tohru, Masuko Ushio-Fukai, and Jack H. Kaplan. "Copper transporters and copper chaperones: roles in cardiovascular physiology and disease." American Journal of Physiology-Cell Physiology 315, no. 2 (August 1, 2018): C186—C201. http://dx.doi.org/10.1152/ajpcell.00132.2018.
Повний текст джерелаPuig, Sergi. "Function and Regulation of the Plant COPT Family of High-Affinity Copper Transport Proteins." Advances in Botany 2014 (July 21, 2014): 1–9. http://dx.doi.org/10.1155/2014/476917.
Повний текст джерелаAndo, Yuko, Shinji Nagata, Schuichi Yanagisawa, and Tadakatsu Yoneyama. "Copper in xylem and phloem saps from rice (Oryza sativa): the effect of moderate copper concentrations in the growth medium on the accumulation of five essential metals and a speciation analysis of copper-containing compounds." Functional Plant Biology 40, no. 1 (2013): 89. http://dx.doi.org/10.1071/fp12158.
Повний текст джерелаNelson, Kyle T., та Joseph R. Prohaska. "Copper deficiency in rodents alters dopamine β-mono-oxygenase activity, mRNA and protein level". British Journal of Nutrition 102, № 1 (15 грудня 2008): 18–28. http://dx.doi.org/10.1017/s0007114508162961.
Повний текст джерелаMaiti, Biplab K., Teresa Avilés, Marta S. P. Carepo, Isabel Moura, Sofia R. Pauleta, and José J. G. Moura. "Rearrangement of Mo-Cu-S Cluster Reflects the Structural Instability of Orange Protein Cofactor." Zeitschrift für anorganische und allgemeine Chemie 639, no. 8-9 (April 9, 2013): 1361–64. http://dx.doi.org/10.1002/zaac.201300034.
Повний текст джерелаWang, Q., M. Burger, T. A. Doane, W. R. Horwath, A. R. Castillo, and F. M. Mitloehner. "Effects of inorganicv. organic copper on denitrification in agricultural soil." Advances in Animal Biosciences 4, s1 (September 2013): 42–49. http://dx.doi.org/10.1017/s2040470013000307.
Повний текст джерелаPetruzzelli, Raffaella, and Roman S. Polishchuk. "Activity and Trafficking of Copper-Transporting ATPases in Tumor Development and Defense against Platinum-Based Drugs." Cells 8, no. 9 (September 13, 2019): 1080. http://dx.doi.org/10.3390/cells8091080.
Повний текст джерелаNiccoli Asabella, Artor, Giuseppe Lucio Cascini, Corinna Altini, Domenico Paparella, Antonio Notaristefano, and Giuseppe Rubini. "The Copper Radioisotopes: A Systematic Review with Special Interest to 64Cu." BioMed Research International 2014 (2014): 1–9. http://dx.doi.org/10.1155/2014/786463.
Повний текст джерелаChen, Helen H. W., and Macus Tien Kuo. "Role of Glutathione in the Regulation of Cisplatin Resistance in Cancer Chemotherapy." Metal-Based Drugs 2010 (September 14, 2010): 1–7. http://dx.doi.org/10.1155/2010/430939.
Повний текст джерелаGuo, Y., L. Nyasae, L. T. Braiterman, and A. L. Hubbard. "NH2-terminal signals in ATP7B Cu-ATPase mediate its Cu-dependent anterograde traffic in polarized hepatic cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 289, no. 5 (November 2005): G904—G916. http://dx.doi.org/10.1152/ajpgi.00262.2005.
Повний текст джерелаSchatzman, Sabrina S., Ryan L. Peterson, Mieraf Teka, Bixi He, Diane E. Cabelli, Brendan P. Cormack, and Valeria C. Culotta. "Copper-only superoxide dismutase enzymes and iron starvation stress in Candida fungal pathogens." Journal of Biological Chemistry 295, no. 2 (December 5, 2019): 570–83. http://dx.doi.org/10.1074/jbc.ra119.011084.
Повний текст джерелаDuring, Alexandrine, Meira Fields, Charles G. Lewis та J. Cecil Smith. "Intestinal β-carotene 15,15′-dioxygenase activity is markedly enhanced in copper-deficient rats fed on high-iron diets and fructose". British Journal of Nutrition 84, № 1 (липень 2000): 117–24. http://dx.doi.org/10.1017/s0007114500001306.
Повний текст джерелаBertino, Nubia M. F., Leilson C. Grangeiro, João P. N. da Costa, Romualdo M. C. Costa, Rodolfo R. de A. Lacerda, and Victor E. de V. Gomes. "Growth, nutrient accumulation and yield of onion as a function of micronutrient fertilization." Revista Brasileira de Engenharia Agrícola e Ambiental 26, no. 2 (February 2022): 126–34. http://dx.doi.org/10.1590/1807-1929/agriambi.v26n2p126-134.
Повний текст джерелаLutsenko, Svetlana, Arnab Gupta, Jason L. Burkhead, and Vesna Zuzel. "Cellular multitasking: The dual role of human Cu-ATPases in cofactor delivery and intracellular copper balance." Archives of Biochemistry and Biophysics 476, no. 1 (August 2008): 22–32. http://dx.doi.org/10.1016/j.abb.2008.05.005.
Повний текст джерелаXu, Jia, Kaiwu He, Kaiqin Zhang, Chao Yang, Lulin Nie, Ding Dan, Jianjun Liu, Chang-E. Zhang, and Xifei Yang. "Low-Dose Copper Exposure Exacerbates Depression-Like Behavior in ApoE4 Transgenic Mice." Oxidative Medicine and Cellular Longevity 2021 (March 25, 2021): 1–20. http://dx.doi.org/10.1155/2021/6634181.
Повний текст джерелаChung, Clive Yik-Sham, Jessica M. Posimo, Sumin Lee, Tiffany Tsang, Julianne M. Davis, Donita C. Brady, and Christopher J. Chang. "Activity-based ratiometric FRET probe reveals oncogene-driven changes in labile copper pools induced by altered glutathione metabolism." Proceedings of the National Academy of Sciences 116, no. 37 (August 26, 2019): 18285–94. http://dx.doi.org/10.1073/pnas.1904610116.
Повний текст джерелаPuchkova, Ludmila V., Massimo Broggini, Elena V. Polishchuk, Ekaterina Y. Ilyechova, and Roman S. Polishchuk. "Silver Ions as a Tool for Understanding Different Aspects of Copper Metabolism." Nutrients 11, no. 6 (June 17, 2019): 1364. http://dx.doi.org/10.3390/nu11061364.
Повний текст джерелаKeith, Karen E., and Miguel A. Valvano. "Characterization of SodC, a Periplasmic Superoxide Dismutase from Burkholderia cenocepacia." Infection and Immunity 75, no. 5 (February 26, 2007): 2451–60. http://dx.doi.org/10.1128/iai.01556-06.
Повний текст джерелаFereiro, Jerry A., Xi Yu, Israel Pecht, Mordechai Sheves, Juan Carlos Cuevas, and David Cahen. "Tunneling explains efficient electron transport via protein junctions." Proceedings of the National Academy of Sciences 115, no. 20 (April 30, 2018): E4577—E4583. http://dx.doi.org/10.1073/pnas.1719867115.
Повний текст джерелаGhosh, Dibbendu, Soumen Sinhababu, Bernard D. Santarsiero, and Neal P. Mankad. "A W/Cu Synthetic Model for the Mo/Cu Cofactor of Aerobic CODH Indicates That Biochemical CO Oxidation Requires a Frustrated Lewis Acid/Base Pair." Journal of the American Chemical Society 142, no. 29 (June 29, 2020): 12635–42. http://dx.doi.org/10.1021/jacs.0c03343.
Повний текст джерелаIpsen, Johan Ø., Magnus Hallas-Møller, Søren Brander, Leila Lo Leggio, and Katja S. Johansen. "Lytic polysaccharide monooxygenases and other histidine-brace copper proteins: structure, oxygen activation and biotechnological applications." Biochemical Society Transactions 49, no. 1 (January 15, 2021): 531–40. http://dx.doi.org/10.1042/bst20201031.
Повний текст джерелаNovoa-Aponte, Lorena, Cheng Xu, Fernando C. Soncini, and José M. Argüello. "The Two-Component System CopRS Maintains Subfemtomolar Levels of Free Copper in the Periplasm of Pseudomonas aeruginosa Using a Phosphatase-Based Mechanism." mSphere 5, no. 6 (December 23, 2020): e01193-20. http://dx.doi.org/10.1128/msphere.01193-20.
Повний текст джерелаGhosh, Somdatta, Jordi Cirera, Michael A. Vance, Tetsuya Ono, Kiyoshi Fujisawa, and Edward I. Solomon. "Spectroscopic and Electronic Structure Studies of Phenolate Cu(II) Complexes: Phenolate Ring Orientation and Activation Related to Cofactor Biogenesis." Journal of the American Chemical Society 130, no. 48 (December 3, 2008): 16262–73. http://dx.doi.org/10.1021/ja8044986.
Повний текст джерелаHorn, Darryl, Hassan Al-Ali, and Antoni Barrientos. "Cmc1p Is a Conserved Mitochondrial Twin CX9C Protein Involved in Cytochrome c Oxidase Biogenesis." Molecular and Cellular Biology 28, no. 13 (April 28, 2008): 4354–64. http://dx.doi.org/10.1128/mcb.01920-07.
Повний текст джерелаAppel, Mason J., Katlyn K. Meier, Julien Lafrance-Vanasse, Hyeongtaek Lim, Chi-Lin Tsai, Britt Hedman, Keith O. Hodgson, John A. Tainer, Edward I. Solomon, and Carolyn R. Bertozzi. "Formylglycine-generating enzyme binds substrate directly at a mononuclear Cu(I) center to initiate O2activation." Proceedings of the National Academy of Sciences 116, no. 12 (March 1, 2019): 5370–75. http://dx.doi.org/10.1073/pnas.1818274116.
Повний текст джерелаCrooks, Elliot J., Brandon A. Irizarry, Martine Ziliox, Toru Kawakami, Tiffany Victor, Feng Xu, Hironobu Hojo та ін. "Copper stabilizes antiparallel β-sheet fibrils of the amyloid β40 (Aβ40)-Iowa variant". Journal of Biological Chemistry 295, № 27 (6 травня 2020): 8914–27. http://dx.doi.org/10.1074/jbc.ra119.011955.
Повний текст джерелаGadupudi, Gopi S., and King-Thom Chung. "Comparative genotoxicity of 3-hydroxyanthranilic acid and anthranilic acid in the presence of a metal cofactor Cu (II) in vitro." Mutation Research/Genetic Toxicology and Environmental Mutagenesis 726, no. 2 (December 2011): 200–208. http://dx.doi.org/10.1016/j.mrgentox.2011.09.012.
Повний текст джерелаClaros, Miguel, Alicia Casitas, and Julio Lloret-Fillol. "Visible-Light Reductive Cyclization of Nonactivated Alkyl Chlorides." Synlett 30, no. 13 (July 17, 2019): 1496–507. http://dx.doi.org/10.1055/s-0037-1611878.
Повний текст джерелаAng, Abel, Juliet M. Pullar, Margaret J. Currie, and Margreet C. M. Vissers. "Vitamin C and immune cell function in inflammation and cancer." Biochemical Society Transactions 46, no. 5 (October 9, 2018): 1147–59. http://dx.doi.org/10.1042/bst20180169.
Повний текст джерелаZahn, James A., David J. Bergmann, Jeffery M. Boyd, Ryan C. Kunz, and Alan A. DiSpirito. "Membrane-Associated Quinoprotein Formaldehyde Dehydrogenase from Methylococcus capsulatus Bath." Journal of Bacteriology 183, no. 23 (December 1, 2001): 6832–40. http://dx.doi.org/10.1128/jb.183.23.6832-6840.2001.
Повний текст джерелаHuang, Ju, Michel Nguyen, Yan Liu, Anne Robert, and Bernard Meunier. "The TDMQ Regulators of Copper Homeostasis Do Not Disturb the Activities of Cu,Zn-SOD, Tyrosinase, or the CoIII Cofactor Vitamin B12." European Journal of Inorganic Chemistry 2019, no. 10 (February 27, 2019): 1384–88. http://dx.doi.org/10.1002/ejic.201801332.
Повний текст джерелаMurakawa, Takeshi, Hideyuki Hayashi, Tomoko Sunami, Kazuo Kurihara, Taro Tamada, Ryota Kuroki, Mamoru Suzuki, Katsuyuki Tanizawa, and Toshihide Okajima. "High-resolution crystal structure of copper amine oxidase fromArthrobacter globiformis: assignment of bound diatomic molecules as O2." Acta Crystallographica Section D Biological Crystallography 69, no. 12 (November 19, 2013): 2483–94. http://dx.doi.org/10.1107/s0907444913023196.
Повний текст джерелаChillappagari, Shashi, Marcus Miethke, Hein Trip, Oscar P. Kuipers, and Mohamed A. Marahiel. "Copper Acquisition Is Mediated by YcnJ and Regulated by YcnK and CsoR in Bacillus subtilis." Journal of Bacteriology 191, no. 7 (January 23, 2009): 2362–70. http://dx.doi.org/10.1128/jb.01616-08.
Повний текст джерелаVisani, Giuseppe, Anita Manti, Laura Valentini, Barbara Canonico, Federica Loscocco, Alessandro Isidori, Elisa Gabucci, et al. "Environmental Nanoparticles Are Significantly over-Expressed in Acute Myeloid Leukemia: a Novel Pathogenetic Cofactor?" Blood 126, no. 23 (December 3, 2015): 4965. http://dx.doi.org/10.1182/blood.v126.23.4965.4965.
Повний текст джерелаBettger, William J. "Zinc and selenium, site-specific versus general antioxidation." Canadian Journal of Physiology and Pharmacology 71, no. 9 (September 1, 1993): 721–24. http://dx.doi.org/10.1139/y93-108.
Повний текст джерелаSpears, Jerry W. "139 Ruminal microbiota mineral requirements to optimize performance on different diets." Journal of Animal Science 98, Supplement_3 (November 2, 2020): 139–40. http://dx.doi.org/10.1093/jas/skaa054.243.
Повний текст джерелаCao, Shanshan, Miaomiao Wu, Shihui Xu, Xiuwen Yan, and Xiaohua Mao. "Identification of a Putative Flavin Adenine Dinucleotide-Binding Monooxygenase as a Regulator for Myxococcus xanthus Development." Journal of Bacteriology 197, no. 7 (January 20, 2015): 1185–96. http://dx.doi.org/10.1128/jb.02555-14.
Повний текст джерелаIlyechova, Ekaterina, Elisa Bonaldi, Iurii Orlov, Ekaterina Skomorokhova, Ludmila Puchkova, and Massimo Broggini. "CRISP-R/Cas9 Mediated Deletion of Copper Transport Genes CTR1 and DMT1 in NSCLC Cell Line H1299. Biological and Pharmacological Consequences." Cells 8, no. 4 (April 6, 2019): 322. http://dx.doi.org/10.3390/cells8040322.
Повний текст джерелаMasuri, Sebastiano, Petr Vaňhara, Maria Grazia Cabiddu, Lukáš Moráň, Josef Havel, Enzo Cadoni, and Tiziana Pivetta. "Copper(II) Phenanthroline-Based Complexes as Potential AntiCancer Drugs: A Walkthrough on the Mechanisms of Action." Molecules 27, no. 1 (December 22, 2021): 49. http://dx.doi.org/10.3390/molecules27010049.
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