Статті в журналах з теми "Azurin protein"
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Yamada, Tohru, Masatoshi Goto, Vasu Punj, Olga Zaborina, Kazuhide Kimbara, T. K. Das Gupta, and A. M. Chakrabarty. "The Bacterial Redox Protein Azurin Induces Apoptosis in J774 Macrophages through Complex Formation and Stabilization of the Tumor Suppressor Protein p53." Infection and Immunity 70, no. 12 (December 2002): 7054–62. http://dx.doi.org/10.1128/iai.70.12.7054-7062.2002.
Повний текст джерелаAslam, Shakira, Hafiz Muzzammel Rehman, Muhammad Zeeshan Sarwar, Ajaz Ahmad, Nadeem Ahmed, Muhammad Imran Amirzada, Hafiz Muhammad Rehman, Humaira Yasmin, Tariq Nadeem, and Hamid Bashir. "Computational Modeling, High-Level Soluble Expression and In Vitro Cytotoxicity Assessment of Recombinant Pseudomonas aeruginosa Azurin: A Promising Anti-Cancer Therapeutic Candidate." Pharmaceutics 15, no. 7 (June 26, 2023): 1825. http://dx.doi.org/10.3390/pharmaceutics15071825.
Повний текст джерелаValli S, Abiraami, and Mythili T. "BIOINFORMATIC STUDY OF AN ANTITUMOR PROTEIN, AZURIN." Asian Journal of Pharmaceutical and Clinical Research 11, no. 6 (June 7, 2018): 169. http://dx.doi.org/10.22159/ajpcr.2018.v11i6.23339.
Повний текст джерелаSignorelli, Sara, Salvatore Cannistraro, and Anna Rita Bizzarri. "Raman Evidence of p53-DBD Disorder Decrease upon Interaction with the Anticancer Protein Azurin." International Journal of Molecular Sciences 20, no. 12 (June 24, 2019): 3078. http://dx.doi.org/10.3390/ijms20123078.
Повний текст джерелаNaguleswaran, Arunasalam, Arsenio M. Fialho, Anita Chaudhari, Chang Soo Hong, Ananda M. Chakrabarty, and William J. Sullivan. "Azurin-Like Protein Blocks Invasion of Toxoplasma gondii through Potential Interactions with Parasite Surface Antigen SAG1." Antimicrobial Agents and Chemotherapy 52, no. 2 (December 10, 2007): 402–8. http://dx.doi.org/10.1128/aac.01005-07.
Повний текст джерелаGammuto, Leandro, Carolina Chiellini, Marta Iozzo, Renato Fani, and Giulio Petroni. "The Azurin Coding Gene: Origin and Phylogenetic Distribution." Microorganisms 10, no. 1 (December 22, 2021): 9. http://dx.doi.org/10.3390/microorganisms10010009.
Повний текст джерелаAmbler, R. P., and J. Tobari. "Two distinct azurins function in the electron-transport chain of the obligate methylotroph Methylomonas J." Biochemical Journal 261, no. 2 (July 15, 1989): 495–99. http://dx.doi.org/10.1042/bj2610495.
Повний текст джерелаFialho, Arsenio M., Prabhakar Salunkhe, Sunil Manna, Sidharth Mahali, and Ananda M. Chakrabarty. "Glioblastoma Multiforme: Novel Therapeutic Approaches." ISRN Neurology 2012 (February 8, 2012): 1–10. http://dx.doi.org/10.5402/2012/642345.
Повний текст джерелаKretchmer, Joshua S., Nicholas Boekelheide, Jeffrey J. Warren, Jay R. Winkler, Harry B. Gray, and Thomas F. Miller. "Fluctuating hydrogen-bond networks govern anomalous electron transfer kinetics in a blue copper protein." Proceedings of the National Academy of Sciences 115, no. 24 (May 29, 2018): 6129–34. http://dx.doi.org/10.1073/pnas.1805719115.
Повний текст джерелаOrtega, Vilhena, Zotti, Díez-Pérez, Cuevas, and Pérez. "Tuning Structure and Dynamics of Blue Copper Azurin Junctions via Single Amino-Acid Mutations." Biomolecules 9, no. 10 (October 15, 2019): 611. http://dx.doi.org/10.3390/biom9100611.
Повний текст джерелаKarlsson, B. Göran, Margareta Nordling, Torbjörn Pascher, Li-Chu Tsai, Lennart Sjölin, and Lennart G. Lundberg. "Cassette mutagenesis of Met121 in azurin from Pseudomonas aeruginosa." "Protein Engineering, Design and Selection" 4, no. 3 (1991): 343–49. http://dx.doi.org/10.1093/protein/4.3.343.
Повний текст джерелаPunj, Vasu, Rachna Sharma, Olga Zaborina, and A. M. Chakrabarty. "Energy-Generating Enzymes of Burkholderia cepacia and Their Interactions with Macrophages." Journal of Bacteriology 185, no. 10 (May 15, 2003): 3167–78. http://dx.doi.org/10.1128/jb.185.10.3167-3178.2003.
Повний текст джерелаNguyen, Chuong, and Van Duy Nguyen. "Discovery of Azurin-Like Anticancer Bacteriocins from Human Gut Microbiome through Homology Modeling and Molecular Docking against the Tumor Suppressor p53." BioMed Research International 2016 (2016): 1–12. http://dx.doi.org/10.1155/2016/8490482.
Повний текст джерелаYamada, T., R. Mehta, D. Majumdar, A. M. Chakrabarty, and T. K. Das Gupta. "Azurin, highly potent and selective anticancer agent for breast cancer." Journal of Clinical Oncology 24, no. 18_suppl (June 20, 2006): 13106. http://dx.doi.org/10.1200/jco.2006.24.18_suppl.13106.
Повний текст джерелаGhasemi-Dehkordi, Payam, Abbas Doosti, and Mohammad-Saeid Jami. "The effects of pBudCE4.1-azurin-MAM-A recombinant vector on IL-2, IL-6, IL-7, and IL-10 expressions in laboratory mice." Journal of Shahrekord University of Medical Sciences 22, no. 1 (February 28, 2020): 38–45. http://dx.doi.org/10.34172/jsums.2020.07.
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 джерелаPradhan, Biswajit, Christopher Engelhard, Sebastiaan Van Mulken, Xueyan Miao, Gerard W. Canters, and Michel Orrit. "Single electron transfer events and dynamical heterogeneity in the small protein azurin from Pseudomonas aeruginosa." Chemical Science 11, no. 3 (2020): 763–71. http://dx.doi.org/10.1039/c9sc05405g.
Повний текст джерелаHo, Man Yi, Sarah A. Goodchild, Pedro Estrela, Daping Chu, and Piero Migliorato. "Switching of electrochemical characteristics of redox protein upon specific biomolecular interactions." Analyst 139, no. 23 (2014): 6118–21. http://dx.doi.org/10.1039/c4an01591f.
Повний текст джерелаSharma, Mukesh Kumar. "Annotated protein network analysis linking oral diseases." Bioinformation 18, no. 8 (August 31, 2022): 724–29. http://dx.doi.org/10.6026/97320630018724.
Повний текст джерелаde Jongh, Thyra E., Miguel Prudencio, Marcellus Ubbink, and Gerard W. Canters. "Modelling protein-protein electron transfer in cross-linked dimers of azurin." Journal of Inorganic Biochemistry 96, no. 1 (July 2003): 161. http://dx.doi.org/10.1016/s0162-0134(03)80663-3.
Повний текст джерелаTrinh, Dinh Kha, Thi Thao Nguyen, Thi Huyen La, Thi Thu Huyen Nguyen, and Thi Tuyen Do. "Cloning, expression and anticancer activity of azurin from Pseudomonas aeruginosa VTCC-B-657." Research Journal of Biotechnology 18, no. 1 (December 15, 2022): 1–6. http://dx.doi.org/10.25303/1801rjbt01006.
Повний текст джерелаM. Fialho, Arsenio, Nuno Bernardes, and Ananda M Chakrabarty. "Exploring the anticancer potential of the bacterial protein azurin." AIMS Microbiology 2, no. 3 (2016): 292–303. http://dx.doi.org/10.3934/microbiol.2016.3.292.
Повний текст джерелаYagati, Ajay Kumar, Sang-Uk Kim, Junhong Min, and Jeong-Woo Choi. "Multi-bit biomemory consisting of recombinant protein variants, azurin." Biosensors and Bioelectronics 24, no. 5 (January 2009): 1503–7. http://dx.doi.org/10.1016/j.bios.2008.07.080.
Повний текст джерелаKim, Sang-Uk, Ajay Kumar Yagati, Junhong Min, and Jeong-Woo Choi. "Nanoscale protein-based memory device composed of recombinant azurin." Biomaterials 31, no. 6 (February 2010): 1293–98. http://dx.doi.org/10.1016/j.biomaterials.2009.10.032.
Повний текст джерелаYamada, T., M. Goto, V. Punj, O. Zaborina, M. L. Chen, K. Kimbara, D. Majumdar, E. Cunningham, T. K. Das Gupta, and A. M. Chakrabarty. "Bacterial redox protein azurin, tumor suppressor protein p53, and regression of cancer." Proceedings of the National Academy of Sciences 99, no. 22 (October 22, 2002): 14098–103. http://dx.doi.org/10.1073/pnas.222539699.
Повний текст джерелаZhang, Yunlei, Youming Zhang, Liqiu Xia, Xiangli Zhang, Xuezhi Ding, Fu Yan, and Feng Wu. "Escherichia coli Nissle 1917 Targets and Restrains Mouse B16 Melanoma and 4T1 Breast Tumors through Expression of Azurin Protein." Applied and Environmental Microbiology 78, no. 21 (August 24, 2012): 7603–10. http://dx.doi.org/10.1128/aem.01390-12.
Повний текст джерелаLawton, S. A., and C. Anthony. "The role of blue copper proteins in the oxidation of methylamine by an obligate methylotroph." Biochemical Journal 228, no. 3 (June 15, 1985): 719–26. http://dx.doi.org/10.1042/bj2280719.
Повний текст джерелаGao, Meng, Jingjing Zhou, Zhengding Su, and Yongqi Huang. "Bacterial cupredoxin azurin hijacks cellular signaling networks: Protein-protein interactions and cancer therapy." Protein Science 26, no. 12 (October 27, 2017): 2334–41. http://dx.doi.org/10.1002/pro.3310.
Повний текст джерелаWitharana, Chamindri, and RanmuniBhagya Lakshani Dharmawickreme. "Bacterial protein azurin and tumour suppressor p53 in cancer regression." Advances in Human Biology 11, no. 2 (2021): 147. http://dx.doi.org/10.4103/aihb.aihb_69_20.
Повний текст джерелаWebb, M. Adam, and Glen R. Loppnow. "Protein Tuning of Excited-State Charge-Transfer Dynamics in Azurin." Journal of Physical Chemistry B 102, no. 44 (October 1998): 8923–29. http://dx.doi.org/10.1021/jp982316n.
Повний текст джерелаKofman, V., O. Farver, I. Pecht, and D. Goldfarb. "Two-Dimensional Pulsed EPR Spectroscopy of the Copper Protein Azurin." Journal of the American Chemical Society 118, no. 5 (January 1996): 1201–6. http://dx.doi.org/10.1021/ja952704s.
Повний текст джерелаKarlsson, B. Göran, Torbjörn Pascher, Margareta Nordling, Rolf H. A. Arvidsson, and Lennart G. Lundberg. "Expression of the blue copper protein azurin fromPseudomonas aeruginosainEscherichia coli." FEBS Letters 246, no. 1-2 (March 27, 1989): 211–17. http://dx.doi.org/10.1016/0014-5793(89)80285-6.
Повний текст джерелаApiyo, David, and Pernilla Wittung-Stafshede. "Unique complex between bacterial azurin and tumor-suppressor protein p53." Biochemical and Biophysical Research Communications 332, no. 4 (July 2005): 965–68. http://dx.doi.org/10.1016/j.bbrc.2005.05.038.
Повний текст джерелаChoi, Jeong-Woo, Byung-Keun Oh, Young Jun Kim, and Junhong Min. "Protein-based biomemory device consisting of the cysteine-modified azurin." Applied Physics Letters 91, no. 26 (December 24, 2007): 263902. http://dx.doi.org/10.1063/1.2828046.
Повний текст джерелаSato, M., H. Watanabe, and T. Kohzuma. "Studies on the crystal growth of blue copper protein azurin I and azurin II from Alcaligenes xylosoxidans NCIMB 11015." Seibutsu Butsuri 41, supplement (2001): S157. http://dx.doi.org/10.2142/biophys.41.s157_1.
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 джерелаRomero-Muñiz, Carlos, María Ortega, Jose Guilherme Vilhena, Rubén Pérez, Juan Carlos Cuevas, and Linda A. Zotti. "The Role of Metal Ions in the Electron Transport through Azurin-Based Junctions." Applied Sciences 11, no. 9 (April 21, 2021): 3732. http://dx.doi.org/10.3390/app11093732.
Повний текст джерелаFaham, Salem, Michael W. Day, William B. Connick, Brian R. Crane, Angel J. Di Bilio, William P. Schaefer, Douglas C. Rees, and Harry B. Gray. "Structures of ruthenium-modified Pseudomonas aeruginosa azurin and [Ru(2,2′-bipyridine)2(imidazole)2]SO4·10H2O." Acta Crystallographica Section D Biological Crystallography 55, no. 2 (February 1, 1999): 379–85. http://dx.doi.org/10.1107/s0907444998010464.
Повний текст джерелаYANG, D., X. MIAO, Z. YE, J. FENG, R. XU, X. HUANG, and F. GE. "Bacterial redox protein azurin induce apoptosis in human osteosarcoma U2OS cells." Pharmacological Research 52, no. 5 (November 2005): 413–21. http://dx.doi.org/10.1016/j.phrs.2005.06.002.
Повний текст джерелаAinscough, Eric W., Alistair G. Bingham, Andrew M. Brodie, Walther R. Ellis, Harry B. Gray, Thomas M. Loehr, Jeffrey E. Plowman, Gillian E. Norris, and Edward N. Baker. "Spectrochemical studies on the blue copper protein azurin from Alcaligenes denitrificans." Biochemistry 26, no. 1 (January 13, 1987): 71–82. http://dx.doi.org/10.1021/bi00375a011.
Повний текст джерелаWittung-Stafshede, Pernilla. "Role of Cofactors in Folding of the Blue-Copper Protein Azurin." Inorganic Chemistry 43, no. 25 (December 2004): 7926–33. http://dx.doi.org/10.1021/ic049398g.
Повний текст джерелаDelfino, Ines, and Salvatore Cannistraro. "Optical investigation of the electron transfer protein azurin–gold nanoparticle system." Biophysical Chemistry 139, no. 1 (January 2009): 1–7. http://dx.doi.org/10.1016/j.bpc.2008.09.016.
Повний текст джерелаCoremans, J. W. A., M. van Gastel, O. G. Poluektov, E. J. J. Groenen, T. den Blaauwen, G. van Pouderoyen, G. W. Canters, H. Nar, C. Hammann, and A. Messerschmidt. "An ENDOR and ESEEM study of the blue copper protein azurin." Chemical Physics Letters 235, no. 3-4 (March 1995): 202–10. http://dx.doi.org/10.1016/0009-2614(95)00114-j.
Повний текст джерелаVenkat, Anurag Setty, Stefano Corni, and Rosa Di Felice. "Electronic Coupling Between Azurin and Gold at Different Protein/Substrate Orientations." Small 3, no. 8 (August 3, 2007): 1431–37. http://dx.doi.org/10.1002/smll.200700001.
Повний текст джерелаLiu, Jing, Katlyn K. Meier, Shiliang Tian, Jun-long Zhang, Hongchao Guo, Charles E. Schulz, Howard Robinson, Mark J. Nilges, Eckard Münck, and Yi Lu. "Redesigning the Blue Copper Azurin into a Redox-Active Mononuclear Nonheme Iron Protein: Preparation and Study of Fe(II)-M121E Azurin." Journal of the American Chemical Society 136, no. 35 (August 22, 2014): 12337–44. http://dx.doi.org/10.1021/ja505410u.
Повний текст джерелаSereena, M., and Denoj Sebastian. "Molecular Detection of Azurin: A Powerful Anticancer Protein from Native Pseudomonas Isolates." Journal of Advances in Medical and Pharmaceutical Sciences 5, no. 1 (January 10, 2016): 1–7. http://dx.doi.org/10.9734/jamps/2016/20557.
Повний текст джерелаBelhadj, Mahfoud, John M. Jean, Richard A. Friesner, John Schoonover, and William H. Woodruff. "Theoretical analysis of resonance Raman spectra from the blue copper protein azurin." Journal of Physical Chemistry 94, no. 5 (March 1990): 2160–66. http://dx.doi.org/10.1021/j100368a078.
Повний текст джерелаFriis, E. P., J. E. T. Andersen, L. L. Madsen, P. Møller, and J. Ulstrup. "In situ STM and AFM of the copper protein Pseudomonas aeruginosa azurin." Journal of Electroanalytical Chemistry 431, no. 1 (June 1997): 35–38. http://dx.doi.org/10.1016/s0022-0728(97)00178-2.
Повний текст джерелаPompa, P. P., A. Bramanti, G. Maruccio, L. L. del Mercato, R. Cingolani, and R. Rinaldi. "Ageing of solid-state protein films: Behavior of azurin at ambient conditions." Chemical Physics Letters 404, no. 1-3 (March 2005): 59–62. http://dx.doi.org/10.1016/j.cplett.2005.01.076.
Повний текст джерелаPaydarnia, Nafiseh, Shahryar Khoshtinat Nikkhoi, Azita Fakhravar, Mohsen Mehdiabdol, Hedieh Heydarzadeh, and Saeed Ranjbar. "Synergistic effect of granzyme B-azurin fusion protein on breast cancer cells." Molecular Biology Reports 46, no. 3 (April 1, 2019): 3129–40. http://dx.doi.org/10.1007/s11033-019-04767-x.
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