Статті в журналах з теми "CYP101C1"
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Sarkar, Md Raihan, and Stephen G. Bell. "Complementary and selective oxidation of hydrocarbon derivatives by two cytochrome P450 enzymes of the same family." Catalysis Science & Technology 10, no. 17 (2020): 5983–95. http://dx.doi.org/10.1039/d0cy01040e.
Повний текст джерелаHussain, Haitham A., and John M. Ward. "Enhanced Heterologous Expression of Two Streptomyces griseolus Cytochrome P450s and Streptomyces coelicolor Ferredoxin Reductase as Potentially Efficient Hydroxylation Catalysts." Applied and Environmental Microbiology 69, no. 1 (January 2003): 373–82. http://dx.doi.org/10.1128/aem.69.1.373-382.2003.
Повний текст джерелаYang, Wen, Stephen G. Bell, Hui Wang, Weihong Zhou, Mark Bartlam, Luet-Lok Wong, and Zihe Rao. "The structure of CYP101D2 unveils a potential path for substrate entry into the active site." Biochemical Journal 433, no. 1 (December 15, 2010): 85–93. http://dx.doi.org/10.1042/bj20101017.
Повний текст джерелаUnterweger, Birgit, Dieter M. Bulach, Judith Scoble, David J. Midgley, Paul Greenfield, Dena Lyras, Priscilla Johanesen, and Geoffrey J. Dumsday. "CYP101J2, CYP101J3, and CYP101J4, 1,8-Cineole-Hydroxylating Cytochrome P450 Monooxygenases from Sphingobium yanoikuyae Strain B2." Applied and Environmental Microbiology 82, no. 22 (September 2, 2016): 6507–17. http://dx.doi.org/10.1128/aem.02067-16.
Повний текст джерелаMa, Ming, Stephen G. Bell, Wen Yang, Yiming Hao, Nicholas H. Rees, Mark Bartlam, Weihong Zhou, Luet-Lok Wong, and Zihe Rao. "Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444." ChemBioChem 12, no. 1 (December 10, 2010): 88–99. http://dx.doi.org/10.1002/cbic.201000537.
Повний текст джерелаShumyantseva, V. V., A. V. Kuzikov, R. A. Masamrekh, Y. Khatri, M. G. Zavialova, R. Bernhardt, and A. I. Archakov. "Direct electrochemistry of CYP109C1, CYP109C2 and CYP109D1 from Sorangium cellulosum So ce56." Electrochimica Acta 192 (February 2016): 72–79. http://dx.doi.org/10.1016/j.electacta.2016.01.162.
Повний текст джерелаAmaya, José A., Dipanwita Batabyal, and Thomas L. Poulos. "Proton Relay Network in the Bacterial P450s: CYP101A1 and CYP101D1." Biochemistry 59, no. 31 (June 23, 2020): 2896–902. http://dx.doi.org/10.1021/acs.biochem.0c00329.
Повний текст джерелаLamb, David C., Li Lei, Bin Zhao, Hang Yuan, Colin J. Jackson, Andrew G. S. Warrilow, Tove Skaug, et al. "Streptomyces coelicolor A3(2) CYP102 Protein, a Novel Fatty Acid Hydroxylase Encoded as a Heme Domain without an N-Terminal Redox Partner." Applied and Environmental Microbiology 76, no. 6 (January 22, 2010): 1975–80. http://dx.doi.org/10.1128/aem.03000-09.
Повний текст джерелаSubedi, Pradeep, Hackwon Do, Jun Hyuck Lee, and Tae-Jin Oh. "Crystal Structure and Biochemical Analysis of a Cytochrome P450 CYP101D5 from Sphingomonas echinoides." International Journal of Molecular Sciences 23, no. 21 (November 1, 2022): 13317. http://dx.doi.org/10.3390/ijms232113317.
Повний текст джерелаDezvarei, Shaghayegh, Joel H. Z. Lee, and Stephen G. Bell. "Stereoselective hydroxylation of isophorone by variants of the cytochromes P450 CYP102A1 and CYP101A1." Enzyme and Microbial Technology 111 (April 2018): 29–37. http://dx.doi.org/10.1016/j.enzmictec.2018.01.002.
Повний текст джерелаUeno, Motoi, Midori Yamashita, Michizane Hashimoto, Motohiro Hino, and Akihiko Fujie. "Oxidative activities of heterologously expressed CYP107B1 and CYP105D1 in whole-cell biotransformation using Streptomyces lividans TK24." Journal of Bioscience and Bioengineering 100, no. 5 (November 2005): 567–72. http://dx.doi.org/10.1263/jbb.100.567.
Повний текст джерелаKan, Jie, Tao Peng, Tongwang Huang, Guangming Xiong, and Zhong Hu. "NarL, a Novel Repressor for CYP108j1 Expression during PAHs Degradation in Rhodococcus sp. P14." International Journal of Molecular Sciences 21, no. 3 (February 1, 2020): 983. http://dx.doi.org/10.3390/ijms21030983.
Повний текст джерелаHall, Emma A., and Stephen G. Bell. "The efficient and selective biocatalytic oxidation of norisoprenoid and aromatic substrates by CYP101B1 from Novosphingobium aromaticivorans DSM12444." RSC Advances 5, no. 8 (2015): 5762–73. http://dx.doi.org/10.1039/c4ra14010a.
Повний текст джерелаHall, Emma A., Md Raihan Sarkar, and Stephen G. Bell. "The selective oxidation of substituted aromatic hydrocarbons and the observation of uncoupling via redox cycling during naphthalene oxidation by the CYP101B1 system." Catalysis Science & Technology 7, no. 7 (2017): 1537–48. http://dx.doi.org/10.1039/c7cy00088j.
Повний текст джерелаSarkar, Md Raihan, Samrat Dasgupta, Simon M. Pyke, and Stephen G. Bell. "Selective biocatalytic hydroxylation of unactivated methylene C–H bonds in cyclic alkyl substrates." Chemical Communications 55, no. 34 (2019): 5029–32. http://dx.doi.org/10.1039/c9cc02060h.
Повний текст джерелаSu, Min, Sumita Chakraborty, Yoichi Osawa, and Haoming Zhang. "Cryo-EM reveals the architecture of the dimeric cytochrome P450 CYP102A1 enzyme and conformational changes required for redox partner recognition." Journal of Biological Chemistry 295, no. 6 (January 3, 2020): 1637–45. http://dx.doi.org/10.1074/jbc.ra119.011305.
Повний текст джерелаPark, Chan Mi, Hyun Seo Park, Gun Su Cha, Ki Deok Park, and Chul-Ho Yun. "Regioselective Hydroxylation of Rhododendrol by CYP102A1 and Tyrosinase." Catalysts 10, no. 10 (September 25, 2020): 1114. http://dx.doi.org/10.3390/catal10101114.
Повний текст джерелаIvanov, Yu D., N. S. Bukharina, P. A. Frantsuzov, T. O. Pleshakova, N. V. Krohin, S. L. Kanashenko, and A. I. Archakov. "Oligomeric state investigation of flavocytochrome CYP102A1 using afm with standard and supersharp probes." Biomeditsinskaya Khimiya 59, no. 4 (2013): 378–87. http://dx.doi.org/10.18097/pbmc20135904378.
Повний текст джерелаNguyen, Ngoc Anh, Ngoc Tan Cao, Thi Huong Ha Nguyen, Jung-Hwan Ji, Gun Su Cha, Hyung-Sik Kang, and Chul-Ho Yun. "Enzymatic Production of 3-OH Phlorizin, a Possible Bioactive Polyphenol from Apples, by Bacillus megaterium CYP102A1 via Regioselective Hydroxylation." Antioxidants 10, no. 8 (August 23, 2021): 1327. http://dx.doi.org/10.3390/antiox10081327.
Повний текст джерелаXu, Lian-Hua, Shinya Fushinobu, Haruo Ikeda, Takayoshi Wakagi, and Hirofumi Shoun. "Crystal Structures of Cytochrome P450 105P1 from Streptomyces avermitilis: Conformational Flexibility and Histidine Ligation State." Journal of Bacteriology 191, no. 4 (December 12, 2008): 1211–19. http://dx.doi.org/10.1128/jb.01276-08.
Повний текст джерелаSyed, Khajamohiddin, Aleksey Porollo, Ying Wai Lam, Paul E. Grimmett, and Jagjit S. Yadav. "CYP63A2, a Catalytically Versatile Fungal P450 Monooxygenase Capable of Oxidizing Higher-Molecular-Weight Polycyclic Aromatic Hydrocarbons, Alkylphenols, and Alkanes." Applied and Environmental Microbiology 79, no. 8 (February 15, 2013): 2692–702. http://dx.doi.org/10.1128/aem.03767-12.
Повний текст джерелаKaderbhai, Mustak A., Cynthia C. Ugochukwu, Steven L. Kelly, and David C. Lamb. "Export of Cytochrome P450 105D1 to the Periplasmic Space of Escherichia coli." Applied and Environmental Microbiology 67, no. 5 (May 1, 2001): 2136–38. http://dx.doi.org/10.1128/aem.67.5.2136-2138.2001.
Повний текст джерелаTakita, Teisuke, Hiro Sakuma, Ren Ohashi, Somaye Nilouyal, Sho Nemoto, Moeka Wada, Yuya Yogo, et al. "Comparison of the stability of CYP105A1 and its variants engineered for production of active forms of vitamin D." Bioscience, Biotechnology, and Biochemistry 86, no. 4 (February 4, 2022): 444–54. http://dx.doi.org/10.1093/bbb/zbac019.
Повний текст джерелаFaletrov, Y. V., V. O. Maliugin, N. S. Frolova, and V. M. Shkumatov. "<i>In silico</i> evaluation of new affine interactions of methylcoumarin with cytochromes P450." Proceedings of the National Academy of Sciences of Belarus, Chemical Series 58, no. 2 (June 8, 2022): 186–90. http://dx.doi.org/10.29235/1561-8331-2022-58-2-186-190.
Повний текст джерелаNguyen, Thi, Soo-Jin Yeom, and Chul-Ho Yun. "Production of a Human Metabolite of Atorvastatin by Bacterial CYP102A1 Peroxygenase." Applied Sciences 11, no. 2 (January 10, 2021): 603. http://dx.doi.org/10.3390/app11020603.
Повний текст джерелаNguyen, Thi Huong Ha, Soo-Jin Yeom, and Chul-Ho Yun. "Production of a Human Metabolite of Atorvastatin by Bacterial CYP102A1 Peroxygenase." Applied Sciences 11, no. 2 (January 10, 2021): 603. http://dx.doi.org/10.3390/app11020603.
Повний текст джерелаFollmer, Alec H., Mavish Mahomed, David B. Goodin, and Thomas L. Poulos. "Substrate-Dependent Allosteric Regulation in Cytochrome P450cam (CYP101A1)." Journal of the American Chemical Society 140, no. 47 (October 30, 2018): 16222–28. http://dx.doi.org/10.1021/jacs.8b09441.
Повний текст джерелаWhitehouse, Christopher J. C., Stephen G. Bell, and Luet-Lok Wong. "P450BM3(CYP102A1): connecting the dots." Chem. Soc. Rev. 41, no. 3 (2012): 1218–60. http://dx.doi.org/10.1039/c1cs15192d.
Повний текст джерелаZhang, Aili, Ting Zhang, Emma A. Hall, Sean Hutchinson, Max J. Cryle, Luet-Lok Wong, Weihong Zhou, and Stephen G. Bell. "The crystal structure of the versatile cytochrome P450 enzyme CYP109B1 from Bacillus subtilis." Molecular BioSystems 11, no. 3 (2015): 869–81. http://dx.doi.org/10.1039/c4mb00665h.
Повний текст джерелаBatabyal, Dipanwita, and Thomas L. Poulos. "Effect of redox partner binding on CYP101D1 conformational dynamics." Journal of Inorganic Biochemistry 183 (June 2018): 179–83. http://dx.doi.org/10.1016/j.jinorgbio.2018.02.013.
Повний текст джерелаCao, Ngoc Tan, Ngoc Anh Nguyen, Chan Mi Park, Gun Su Cha, Ki Deok Park, and Chul-Ho Yun. "A Novel Statin Compound from Monacolin J Produced Using CYP102A1-Catalyzed Regioselective C-Hydroxylation." Pharmaceuticals 14, no. 10 (September 26, 2021): 981. http://dx.doi.org/10.3390/ph14100981.
Повний текст джерелаIvanov, Yuri D., Amir Taldaev, Andrey V. Lisitsa, Elena A. Ponomarenko, and Alexander I. Archakov. "Prediction of Monomeric and Dimeric Structures of CYP102A1 Using AlphaFold2 and AlphaFold Multimer and Assessment of Point Mutation Effect on the Efficiency of Intra- and Interprotein Electron Transfer." Molecules 27, no. 4 (February 18, 2022): 1386. http://dx.doi.org/10.3390/molecules27041386.
Повний текст джерелаIvanov, Yuri D., Natalia S. Bukharina, Pavel A. Frantsuzov, Tatyana O. Pleshakova, Sergey L. Kanashenko, Natalia V. Medvedeva, Viktoriya V. Argentova, Viktor G. Zgoda, Andrew W. Munro, and Alexander I. Archakov. "AFM study of cytochrome CYP102A1 oligomeric state." Soft Matter 8, no. 17 (2012): 4602. http://dx.doi.org/10.1039/c2sm07333a.
Повний текст джерелаWhitehouse, Christopher J C., Stephen G Bell, and Luet-Lok Wong. "Desaturation of Alkylbenzenes by Cytochrome P450BM3(CYP102A1)." Chemistry - A European Journal 14, no. 35 (December 8, 2008): 10905–8. http://dx.doi.org/10.1002/chem.200801927.
Повний текст джерелаWhitehouse, Christopher J. C., Nicholas H. Rees, Stephen G. Bell, and Luet-Lok Wong. "Dearomatisation of o-Xylene by P450BM3 (CYP102A1)." Chemistry - A European Journal 17, no. 24 (April 26, 2011): 6862–68. http://dx.doi.org/10.1002/chem.201002465.
Повний текст джерелаWhitehouse, Christopher J. C., Stephen G. Bell, and Luet-Lok Wong. "ChemInform Abstract: P450BM3(CYP102A1): Connecting the Dots." ChemInform 43, no. 17 (March 29, 2012): no. http://dx.doi.org/10.1002/chin.201217268.
Повний текст джерелаBatabyal, Dipanwita, Huiying Li, and Thomas L. Poulos. "Synergistic Effects of Mutations in Cytochrome P450cam Designed To Mimic CYP101D1." Biochemistry 52, no. 32 (July 31, 2013): 5396–402. http://dx.doi.org/10.1021/bi400676d.
Повний текст джерелаNikolaeva, V. M., V. V. Fokina, A. A. Shutov, A. V. Kazantsev, N. I. Strizhov, and M. V. Donova. "Construction and Functional Analysis of Mycolicibacterium smegmatis Recombinant Strains Carrying the Genes of Bacillary Cytochromes CYP106A1 and CYP106A2." Biotekhnologiya 37, no. 6 (2021): 34–47. http://dx.doi.org/10.21519/0234-2758-2021-37-6-34-47.
Повний текст джерелаAhsan, Md, Mahesh Patil, Hyunwoo Jeon, Sihyong Sung, Taeowan Chung та Hyungdon Yun. "Biosynthesis of Nylon 12 Monomer, ω-Aminododecanoic Acid Using Artificial Self-Sufficient P450, AlkJ and ω-TA". Catalysts 8, № 9 (18 вересня 2018): 400. http://dx.doi.org/10.3390/catal8090400.
Повний текст джерелаNguyen, Thi Huong Ha, Su-Min Woo, Ngoc Anh Nguyen, Gun-Su Cha, Soo-Jin Yeom, Hyung-Sik Kang, and Chul-Ho Yun. "Regioselective Hydroxylation of Naringin Dihydrochalcone to Produce Neoeriocitrin Dihydrochalcone by CYP102A1 (BM3) Mutants." Catalysts 10, no. 8 (July 23, 2020): 823. http://dx.doi.org/10.3390/catal10080823.
Повний текст джерелаBalaraman, Priyadarshini, and Erika Plettner. "Chemotaxis by Pseudomonas putida (ATCC 17453) towards camphor involves cytochrome P450cam (CYP101A1)." Biochimica et Biophysica Acta (BBA) - General Subjects 1863, no. 2 (February 2019): 304–12. http://dx.doi.org/10.1016/j.bbagen.2018.10.018.
Повний текст джерелаCryle, Max J., and James J. De Voss. "Carbon–carbon bond cleavage by cytochrome P450BioI(CYP107H1)." Chem. Commun., no. 1 (2004): 86–87. http://dx.doi.org/10.1039/b311652b.
Повний текст джерелаSyntrivanis, Leonidas-Dimitrios, Luet Lok Wong, and Jeremy Robertson. "Hydroxylation of Eleuthoside Synthetic Intermediates by P450BM3 (CYP102A1)." European Journal of Organic Chemistry 2018, no. 45 (November 14, 2018): 6369–78. http://dx.doi.org/10.1002/ejoc.201801206.
Повний текст джерелаMaurer, Steffen C, Katja Kühnel, Leonard A Kaysser, Sabine Eiben, Rolf D Schmid, and Vlada B Urlacher. "Catalytic Hydroxylation in Biphasic Systems using CYP102A1 Mutants." Advanced Synthesis & Catalysis 347, no. 7-8 (June 2005): 1090–98. http://dx.doi.org/10.1002/adsc.200505044.
Повний текст джерелаIvanov, Yu D., K. A. Malsagova, S. G. Vesnin, V. Yu Tatur, N. D. Ivanova, and V. S. Ziborov. "The Registration of a Biomaser-Like Effect in an Enzyme System with an RTM Sensor." Journal of Sensors 2019 (August 21, 2019): 1–11. http://dx.doi.org/10.1155/2019/7608512.
Повний текст джерелаChang, Yan-Tyng, and Gilda H. Loew. "Construction and evaluation of a three-dimensional structure of cytochrome P450choP enzyme (CYP105C1)." "Protein Engineering, Design and Selection" 9, no. 9 (1996): 755–66. http://dx.doi.org/10.1093/protein/9.9.755.
Повний текст джерелаKolesanova, Ekaterina F., Sergey A. Kozin, Andrey B. Rumyantsev, Christiane Jung, Gaston Hui Bon Hoa, and Alexander I. Archakov. "Epitope Mapping of Cytochrome P450cam (CYP101)." Archives of Biochemistry and Biophysics 341, no. 2 (May 1997): 229–37. http://dx.doi.org/10.1006/abbi.1997.9934.
Повний текст джерелаRoh, Changhyun, Kwon-Young Choi, Bishnu Prasad Pandey, and Byung-Gee Kim. "Hydroxylation of daidzein by CYP107H1 from Bacillus subtilis 168." Journal of Molecular Catalysis B: Enzymatic 59, no. 4 (August 2009): 248–53. http://dx.doi.org/10.1016/j.molcatb.2008.07.005.
Повний текст джерелаKim, Vitchan, Young-Ran Lim, Inho Lee, Jong-ha Lee, Sangjun Han, Tan-Viet Pham, Harim Kim, Rowoon Lee, Lin-Woo Kang, and Donghak Kim. "Structural insights into CYP107G1 from rapamycin-producing Streptomyces rapamycinicus." Archives of Biochemistry and Biophysics 692 (October 2020): 108544. http://dx.doi.org/10.1016/j.abb.2020.108544.
Повний текст джерелаShen, Chen, Wanli Zhao, Xuming Liu, and Jihua Liu. "Enzyme-catalyzed regio-selective demethylation of papaverine by CYP105D1." Biotechnology Letters 41, no. 1 (November 21, 2018): 171–80. http://dx.doi.org/10.1007/s10529-018-2626-0.
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