Статті в журналах з теми "Non-OR copper binding site"
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Erales, Jenny, Brigitte Gontero, Julian Whitelegge, and Frédéric Halgand. "Mapping of a copper-binding site on the small CP12 chloroplastic protein of Chlamydomonas reinhardtii using top-down mass spectrometry and site-directed mutagenesis." Biochemical Journal 419, no. 1 (March 13, 2009): 75–86. http://dx.doi.org/10.1042/bj20082004.
Повний текст джерелаMcArdle, H. J., S. M. Gross, D. M. Danks, and A. G. Wedd. "Role of albumin's copper binding site in copper uptake by mouse hepatocytes." American Journal of Physiology-Gastrointestinal and Liver Physiology 258, no. 6 (June 1, 1990): G988—G991. http://dx.doi.org/10.1152/ajpgi.1990.258.6.g988.
Повний текст джерелаCater, Michael A., Sharon La fontaine, and Julian F. B. Mercer. "Copper binding to the N-terminal metal-binding sites or the CPC motif is not essential for copper-induced trafficking of the human Wilson protein (ATP7B)." Biochemical Journal 401, no. 1 (December 11, 2006): 143–53. http://dx.doi.org/10.1042/bj20061055.
Повний текст джерелаCalabrese, L., and M. Carbonaro. "An e.p.r. study of the non-equivalence of the copper sites of caeruloplasmin." Biochemical Journal 238, no. 1 (August 15, 1986): 291–95. http://dx.doi.org/10.1042/bj2380291.
Повний текст джерелаSinopoli, Alessandro, Antonio Magrì, Danilo Milardi, Matteo Pappalardo, Pietro Pucci, Angela Flagiello, Jeremy J. Titman, et al. "The role of copper(ii) in the aggregation of human amylin." Metallomics 6, no. 10 (2014): 1841–52. http://dx.doi.org/10.1039/c4mt00130c.
Повний текст джерелаKekez, Ivana, Mihovil Faletar, Mario Kekez, Laura Cendron, Maya Wright, Giuseppe Zanotti, and Dubravka Matković-Čalogović. "Copper Binding and Oligomerization Studies of the Metal Resistance Determinant CrdA from Helicobacter pylori." Molecules 27, no. 11 (May 24, 2022): 3387. http://dx.doi.org/10.3390/molecules27113387.
Повний текст джерелаNAKAMURA, Motoyoshi, Tasuku NAKAJIMA, Yasunori OHBA, Seigo YAMAUCHI, Byung Rho LEE, and Eiji ICHISHIMA. "Identification of copper ligands in Aspergillus oryzae tyrosinase by site-directed mutagenesis." Biochemical Journal 350, no. 2 (August 23, 2000): 537–45. http://dx.doi.org/10.1042/bj3500537.
Повний текст джерелаMaghool, Shadi, Michael T. Ryan, and Megan J. Maher. "What Role Does COA6 Play in Cytochrome C Oxidase Biogenesis: A Metallochaperone or Thiol Oxidoreductase, or Both?" International Journal of Molecular Sciences 21, no. 19 (September 23, 2020): 6983. http://dx.doi.org/10.3390/ijms21196983.
Повний текст джерелаD’Angelo, Paola, Stefano Della Longa, Alessandro Arcovito, Giordano Mancini, Andrea Zitolo, Giovanni Chillemi, Gabriele Giachin, Giuseppe Legname, and Federico Benetti. "Effects of the Pathological Q212P Mutation on Human Prion Protein Non-Octarepeat Copper-Binding Site." Biochemistry 51, no. 31 (July 27, 2012): 6068–79. http://dx.doi.org/10.1021/bi300233n.
Повний текст джерелаEakin, Catherine M., Jefferson D. Knight, Charles J. Morgan, Michael A. Gelfand та Andrew D. Miranker. "Formation of a Copper Specific Binding Site in Non-Native States of β-2-Microglobulin†". Biochemistry 41, № 34 (серпень 2002): 10646–56. http://dx.doi.org/10.1021/bi025944a.
Повний текст джерелаAttar, Narsis, Oscar A. Campos, Maria Vogelauer, Chen Cheng, Yong Xue, Stefan Schmollinger, Lukasz Salwinski, et al. "The histone H3-H4 tetramer is a copper reductase enzyme." Science 369, no. 6499 (July 2, 2020): 59–64. http://dx.doi.org/10.1126/science.aba8740.
Повний текст джерелаWatmough, Nicholas J., Sarah J. Field, Ross J. L. Hughes, and David J. Richardson. "The bacterial respiratory nitric oxide reductase." Biochemical Society Transactions 37, no. 2 (March 20, 2009): 392–99. http://dx.doi.org/10.1042/bst0370392.
Повний текст джерелаDiSpirito, Alan A., Jeremy D. Semrau, J. Colin Murrell, Warren H. Gallagher, Christopher Dennison, and Stéphane Vuilleumier. "Methanobactin and the Link between Copper and Bacterial Methane Oxidation." Microbiology and Molecular Biology Reviews 80, no. 2 (March 16, 2016): 387–409. http://dx.doi.org/10.1128/mmbr.00058-15.
Повний текст джерелаMarx, G., and M. Chevion. "Site-specific modification of albumin by free radicals. Reaction with copper(II) and ascorbate." Biochemical Journal 236, no. 2 (June 1, 1986): 397–400. http://dx.doi.org/10.1042/bj2360397.
Повний текст джерелаSOLANO, Francisco, Celia JIMÉNEZ-CERVANTES, José H. MARTÍNEZ-LIARTE, José C. GARCÍA-BORRÓN, José R. JARA, and José A. LOZANO. "Molecular mechanism for catalysis by a new zinc-enzyme, dopachrome tautomerase." Biochemical Journal 313, no. 2 (January 15, 1996): 447–53. http://dx.doi.org/10.1042/bj3130447.
Повний текст джерелаPercival, S. S., and E. D. Harris. "Regulation of Cu,Zn superoxide dismutase with copper. Caeruloplasmin maintains levels of functional enzyme activity during differentiation of K562 cells." Biochemical Journal 274, no. 1 (February 15, 1991): 153–58. http://dx.doi.org/10.1042/bj2740153.
Повний текст джерелаGiangregorio, Nicola, Annamaria Tonazzi, Lara Console, Mario Prejanò, Tiziana Marino, Nino Russo, and Cesare Indiveri. "Effect of Copper on the Mitochondrial Carnitine/Acylcarnitine Carrier Via Interaction with Cys136 and Cys155. Possible Implications in Pathophysiology." Molecules 25, no. 4 (February 13, 2020): 820. http://dx.doi.org/10.3390/molecules25040820.
Повний текст джерелаJaenicke, Elmar, Kay Büchler, Jürgen Markl, Heinz Decker, and Thomas R. M. Barends. "Cupredoxin-like domains in haemocyanins." Biochemical Journal 426, no. 3 (February 24, 2010): 373–78. http://dx.doi.org/10.1042/bj20091501.
Повний текст джерелаMartins, Lucas Sousa, Jerônimo Lameira, Hendrik G. Kruger, Cláudio Nahum Alves, and José Rogério A. Silva. "Evaluating the Performance of a Non-Bonded Cu2+ Model Including Jahn−Teller Effect into the Binding of Tyrosinase Inhibitors." International Journal of Molecular Sciences 21, no. 13 (July 6, 2020): 4783. http://dx.doi.org/10.3390/ijms21134783.
Повний текст джерелаKhalil, Abdelouahed, та Tamàs Fülöp. "A comparison of the kinetics of low-density lipoprotein oxidation induced by copper or by γ-rays: Influence of radiation dose-rate and copper concentration". Canadian Journal of Physiology and Pharmacology 79, № 2 (1 лютого 2001): 114–21. http://dx.doi.org/10.1139/y00-080.
Повний текст джерелаVarfolomeeva, Larisa A., Anastasia Yu Solovieva, Nikolai S. Shipkov, Olga G. Kulikova, Natalia I. Dergousova, Tatiana V. Rakitina, Konstantin M. Boyko, Tamara V. Tikhonova, and Vladimir O. Popov. "Probing the Role of a Conserved Phenylalanine in the Active Site of Thiocyanate Dehydrogenase." Crystals 12, no. 12 (December 8, 2022): 1787. http://dx.doi.org/10.3390/cryst12121787.
Повний текст джерелаBaek, Seung-Hun, Angela Hartsock, and James P. Shapleigh. "Agrobacterium tumefaciens C58 Uses ActR and FnrN To Control nirK and nor Expression." Journal of Bacteriology 190, no. 1 (November 2, 2007): 78–86. http://dx.doi.org/10.1128/jb.00792-07.
Повний текст джерелаBrouwer, M., T. Hoexum-Brouwer, and R. E. Cashon. "A putative glutathione-binding site in CdZn-metallothionein identified by equilibrium binding and molecular-modelling studies." Biochemical Journal 294, no. 1 (August 15, 1993): 219–25. http://dx.doi.org/10.1042/bj2940219.
Повний текст джерелаGeorgieva, Dessislava Nikolova, Stanka Stoeva, Wolfgang Voelter, and Nicolay Genov. "Viviparus ater Hemocyanin: Investigation of the Dioxygen-Binding Site and Stability of the Oxy- and Apo-Forms." Zeitschrift für Naturforschung C 56, no. 9-10 (October 1, 2001): 843–47. http://dx.doi.org/10.1515/znc-2001-9-1027.
Повний текст джерелаBoyd, Stefanie D., Morgan S. Ullrich, Jenifer S. Calvo, Fatemeh Behnia, Gabriele Meloni, and Duane D. Winkler. "Mutations in Superoxide Dismutase 1 (Sod1) Linked to Familial Amyotrophic Lateral Sclerosis Can Disrupt High-Affinity Zinc-Binding Promoted by the Copper Chaperone for Sod1 (Ccs)." Molecules 25, no. 5 (February 28, 2020): 1086. http://dx.doi.org/10.3390/molecules25051086.
Повний текст джерелаWang, Jiou, Hilda Slunt, Victoria Gonzales, David Fromholt, Michael Coonfield, Neal G. Copeland, Nancy A. Jenkins, and David R. Borchelt. "Copper-binding-site-null SOD1 causes ALS in transgenic mice: aggregates of non-native SOD1 delineate a common feature." Human Molecular Genetics 12, no. 21 (November 1, 2003): 2753–64. http://dx.doi.org/10.1093/hmg/ddg312.
Повний текст джерелаWakabayashi, Hironao, Qian Zhou, Keiji Nogami, and Philip J. Fay. "Effects of Single Point Mutations within Proposed Copper Binding Sites on Specific Activity and Inter-Chain Affinity of Factor VIII." Blood 104, no. 11 (November 16, 2004): 1730. http://dx.doi.org/10.1182/blood.v104.11.1730.1730.
Повний текст джерелаBrauchli, Sven Y., Frederik J. Malzner, Edwin C. Constable, and Catherine E. Housecroft. "Copper(i)-based dye-sensitized solar cells with sterically demanding anchoring ligands: bigger is not always better." RSC Advances 5, no. 60 (2015): 48516–25. http://dx.doi.org/10.1039/c5ra07449e.
Повний текст джерелаFaraco, Vincenza, Paola Giardina, and Giovanni Sannia. "Metal-responsive elements in Pleurotus ostreatus laccase gene promoters." Microbiology 149, no. 8 (August 1, 2003): 2155–62. http://dx.doi.org/10.1099/mic.0.26360-0.
Повний текст джерелаCATER, Michael A., John FORBES, Sharon La FONTAINE, Diane COX, and Julian F. B. MERCER. "Intracellular trafficking of the human Wilson protein: the role of the six N-terminal metal-binding sites." Biochemical Journal 380, no. 3 (June 15, 2004): 805–13. http://dx.doi.org/10.1042/bj20031804.
Повний текст джерелаJureschi, Monica, Brindusa Alina Petre, Laura Ion, Catalina Ionica Ciobanu, Ion Sandu, and Gabi Drochioiu. "Synthesis of Different Analogs of Ab(9-16) Peptide Mass spectrometric evidence for heavy metal binding." Revista de Chimie 70, no. 9 (October 15, 2019): 3348–53. http://dx.doi.org/10.37358/rc.19.9.7547.
Повний текст джерелаPirota, Valentina, Enrico Lunghi, Alessandra Benassi, Emmanuele Crespan, Mauro Freccero, and Filippo Doria. "Selective Binding and Redox-Activity on Parallel G-Quadruplexes by Pegylated Naphthalene Diimide-Copper Complexes." Molecules 26, no. 16 (August 19, 2021): 5025. http://dx.doi.org/10.3390/molecules26165025.
Повний текст джерелаPfeuffer, I., S. Klein-Hessling, A. Heinfling, S. Chuvpilo, C. Escher, T. Brabletz, B. Hentsch, H. Schwarzenbach, P. Matthias, and E. Serfling. "Octamer factors exert a dual effect on the IL-2 and IL-4 promoters." Journal of Immunology 153, no. 12 (December 15, 1994): 5572–85. http://dx.doi.org/10.4049/jimmunol.153.12.5572.
Повний текст джерелаABRAHAM, Zelda H. L., Barry E. SMITH, Barry D. HOWES, David J. LOWE, and Robert R. EADY. "pH-dependence for binding a single nitrite ion to each type-2 copper centre in the copper-containing nitrite reductase of Alcaligenes xylosoxidans." Biochemical Journal 324, no. 2 (June 1, 1997): 511–16. http://dx.doi.org/10.1042/bj3240511.
Повний текст джерелаShcheglovitov, Aleksandr, Iuliia Vitko, Roman M. Lazarenko, Peihan Orestes, Slobodan M. Todorovic, and Edward Perez-Reyes. "Molecular and biophysical basis of glutamate and trace metal modulation of voltage-gated Cav2.3 calcium channels." Journal of General Physiology 139, no. 3 (February 27, 2012): 219–34. http://dx.doi.org/10.1085/jgp.201110699.
Повний текст джерелаNaro, Fabio, Maria G. Tordi, Giorgio M. Giacometti, Francesco Tomei, Anna M. Timperio, and Lello Zolla. "Metal Binding to Pseudomonas aeruginosa Azurin: a Kinetic Investigation." Zeitschrift für Naturforschung C 55, no. 5-6 (June 1, 2000): 347–54. http://dx.doi.org/10.1515/znc-2000-5-609.
Повний текст джерелаTeodori, Laura, Marjan Omer, Anders Märcher, Mads K. Skaanning, Veronica L. Andersen, Jesper S. Nielsen, Emil Oldenburg, Yuchen Lin, Kurt V. Gothelf, and Jørgen Kjems. "Site-specific nanobody-oligonucleotide conjugation for super-resolution imaging." Journal of Biological Methods 9, no. 1 (March 1, 2022): e159. http://dx.doi.org/10.14440/jbm.2022.381.
Повний текст джерелаScala, David J., and Lee J. Kerkhof. "Diversity of Nitrous Oxide Reductase (nosZ) Genes in Continental Shelf Sediments." Applied and Environmental Microbiology 65, no. 4 (April 1, 1999): 1681–87. http://dx.doi.org/10.1128/aem.65.4.1681-1687.1999.
Повний текст джерелаAbbas, Ioana M., Marija Vranic, Holger Hoffmann, Ahmed H. El-Khatib, María Montes-Bayón, Heiko M. Möller, and Michael G. Weller. "Investigations of the Copper Peptide Hepcidin-25 by LC-MS/MS and NMR." International Journal of Molecular Sciences 19, no. 8 (August 2, 2018): 2271. http://dx.doi.org/10.3390/ijms19082271.
Повний текст джерелаSen, Kakali, Sam Horrell, Demet Kekilli, Chin W. Yong, Thomas W. Keal, Hakan Atakisi, David W. Moreau, Robert E. Thorne, Michael A. Hough, and Richard W. Strange. "Active-site protein dynamics and solvent accessibility in nativeAchromobacter cycloclastescopper nitrite reductase." IUCrJ 4, no. 4 (June 16, 2017): 495–505. http://dx.doi.org/10.1107/s2052252517007527.
Повний текст джерелаGoto, Yoshio, and Judith P. Klinman. "Binding of Dioxygen to Non-Metal Sites in Proteins: Exploration of the Importance of Binding Site Size versus Hydrophobicity in the Copper Amine Oxidase fromHansenula polymorpha†." Biochemistry 41, no. 46 (November 2002): 13637–43. http://dx.doi.org/10.1021/bi0204591.
Повний текст джерелаFrank, L. H., H. K. Cheung, and R. S. Cohen. "Identification and characterization of Drosophila female germ line transcriptional control elements." Development 114, no. 2 (February 1, 1992): 481–91. http://dx.doi.org/10.1242/dev.114.2.481.
Повний текст джерелаManiak, Halina, Michał Talma, Konrad Matyja, Anna Trusek, and Mirosław Giurg. "Synthesis and Structure-Activity Relationship Studies of Hydrazide-Hydrazones as Inhibitors of Laccase from Trametes versicolor." Molecules 25, no. 5 (March 10, 2020): 1255. http://dx.doi.org/10.3390/molecules25051255.
Повний текст джерелаOlczak, Teresa, Dabney White Dixon, and Caroline Attardo Genco. "Binding Specificity of the Porphyromonas gingivalis Heme and Hemoglobin Receptor HmuR, Gingipain K, and Gingipain R1 for Heme, Porphyrins, and Metalloporphyrins." Journal of Bacteriology 183, no. 19 (October 1, 2001): 5599–608. http://dx.doi.org/10.1128/jb.183.19.5599-5608.2001.
Повний текст джерелаBanci, Lucia, Ivano Bertini, Vito Calderone, Nunzia Della-Malva, Isabella C. Felli, Sara Neri, Anna Pavelkova, and Antonio Rosato. "Copper(I)-mediated protein–protein interactions result from suboptimal interaction surfaces." Biochemical Journal 422, no. 1 (July 29, 2009): 37–42. http://dx.doi.org/10.1042/bj20090422.
Повний текст джерелаDas, Dola, Nisha Tapryal, Shyamal K. Goswami, Paul L. Fox, and Chinmay K. Mukhopadhyay. "Regulation of ceruloplasmin in human hepatic cells by redox active copper: identification of a novel AP-1 site in the ceruloplasmin gene." Biochemical Journal 402, no. 1 (January 25, 2007): 135–41. http://dx.doi.org/10.1042/bj20060963.
Повний текст джерелаUrresti, Saioa, Alan Cartmell, Feng Liu, Paul H. Walton, and Gideon J. Davies. "Structural studies of the unusual metal-ion site of the GH124 endoglucanase from Ruminiclostridium thermocellum." Acta Crystallographica Section F Structural Biology Communications 74, no. 8 (August 1, 2018): 496–505. http://dx.doi.org/10.1107/s2053230x18006842.
Повний текст джерелаVarela-Nallar, Lorena, Enrique M. Toledo, Luis F. Larrondo, Ana L. B. Cabral, Vilma R. Martins, and Nibaldo C. Inestrosa. "Induction of cellular prion protein gene expression by copper in neurons." American Journal of Physiology-Cell Physiology 290, no. 1 (January 2006): C271—C281. http://dx.doi.org/10.1152/ajpcell.00160.2005.
Повний текст джерелаHuo, Chunheng, Tinghong Ming, Yan Wu, Hengshang Huan, Xiaoting Qiu, Chenyang Lu, Ye Li, Zhen Zhang, Jiaojiao Han, and Xiurong Su. "Structural and Biochemical Characterization of Silver/Copper Binding by Dendrorhynchus zhejiangensis Ferritin." Polymers 15, no. 5 (March 3, 2023): 1297. http://dx.doi.org/10.3390/polym15051297.
Повний текст джерелаGoumakos, William, Jean-Pierre Laussac, and Bibudhendra Sarkar. "Binding of cadmium(II) and zinc(II) to human and dog serum albumins. An equilibrium dialysis and 113Cd-NMR study." Biochemistry and Cell Biology 69, no. 12 (December 1, 1991): 809–20. http://dx.doi.org/10.1139/o91-121.
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