Статті в журналах з теми "Oxidoreductases, X-Ray Crystallography"
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Ознайомтеся з топ-28 статей у журналах для дослідження на тему "Oxidoreductases, X-Ray Crystallography".
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Gibson, Marcus I., Percival Yang-Ting Chen, Aileen C. Johnson, Elizabeth Pierce, Mehmet Can, Stephen W. Ragsdale, and Catherine L. Drennan. "One-carbon chemistry of oxalate oxidoreductase captured by X-ray crystallography." Proceedings of the National Academy of Sciences 113, no. 2 (December 28, 2015): 320–25. http://dx.doi.org/10.1073/pnas.1518537113.
Повний текст джерелаZhang, Yanfei, Maia M. Cherney, Matthew Solomonson, Jianshe Liu, Michael N. G. James, and Joel H. Weiner. "Preliminary X-ray crystallographic analysis of sulfide:quinone oxidoreductase fromAcidithiobacillus ferrooxidans." Acta Crystallographica Section F Structural Biology and Crystallization Communications 65, no. 8 (July 30, 2009): 839–42. http://dx.doi.org/10.1107/s1744309109027535.
Повний текст джерелаBarber, James. "Photosystem II: the engine of life." Quarterly Reviews of Biophysics 36, no. 1 (January 27, 2003): 71–89. http://dx.doi.org/10.1017/s0033583502003839.
Повний текст джерелаPanicker, Lata, Hari Sharan Misra, and Subhash Chandra Bihani. "Purification, crystallization and preliminary crystallographic investigation of FrnE, a disulfide oxidoreductase fromDeinococcus radiodurans." Acta Crystallographica Section F Structural Biology Communications 70, no. 11 (October 25, 2014): 1540–42. http://dx.doi.org/10.1107/s2053230x14020330.
Повний текст джерелаIGARASHI, Noriyuki. "X-ray Crystallographic Structure of the Novel Multipleheme Enzyme, Hydroxylamine Oxidoreductase from Nitrosomonas Europaea." Nihon Kessho Gakkaishi 41, no. 5 (1999): 283–92. http://dx.doi.org/10.5940/jcrsj.41.283.
Повний текст джерелаCherrier, Mickaël V., Xavier Vernède, Daphna Fenel, Lydie Martin, Benoit Arragain, Emmanuelle Neumann, Juan C. Fontecilla-Camps, Guy Schoehn, and Yvain Nicolet. "Oxygen-Sensitive Metalloprotein Structure Determination by Cryo-Electron Microscopy." Biomolecules 12, no. 3 (March 12, 2022): 441. http://dx.doi.org/10.3390/biom12030441.
Повний текст джерелаMano, Jun’ichi, Hye-Jin Yoon, Kozi Asada, Elena Babiychuk, Dirk Inzé та Bunzo Mikami. "Crystallization and preliminary X-ray crystallographic analysis of NADPH: azodicarbonyl/quinone oxidoreductase, a plant ζ-crystallin". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1480, № 1-2 (липень 2000): 374–76. http://dx.doi.org/10.1016/s0167-4838(00)00073-x.
Повний текст джерелаKmita, Katarzyna, Christophe Wirth, Judith Warnau, Sergio Guerrero-Castillo, Carola Hunte, Gerhard Hummer, Ville R. I. Kaila, Klaus Zwicker, Ulrich Brandt, and Volker Zickermann. "Accessory NUMM (NDUFS6) subunit harbors a Zn-binding site and is essential for biogenesis of mitochondrial complex I." Proceedings of the National Academy of Sciences 112, no. 18 (April 20, 2015): 5685–90. http://dx.doi.org/10.1073/pnas.1424353112.
Повний текст джерелаOtrelo-Cardoso, Ana, Márcia da Silva Correia, Viola Schwuchow, Dmitri Svergun, Maria Romão, Silke Leimkühler, and Teresa Santos-Silva. "Structural Data on the Periplasmic Aldehyde Oxidoreductase PaoABC from Escherichia coli: SAXS and Preliminary X-ray Crystallography Analysis." International Journal of Molecular Sciences 15, no. 2 (January 31, 2014): 2223–36. http://dx.doi.org/10.3390/ijms15022223.
Повний текст джерелаTu, Shih-Long, Nathan C. Rockwell, J. Clark Lagarias, and Andrew J. Fisher. "Insight into the Radical Mechanism of Phycocyanobilin−Ferredoxin Oxidoreductase (PcyA) Revealed by X-ray Crystallography and Biochemical Measurements†." Biochemistry 46, no. 6 (February 2007): 1484–94. http://dx.doi.org/10.1021/bi062038f.
Повний текст джерелаMaher, Megan J., Anuradha S. Herath, Saumya R. Udagedara, David A. Dougan, and Kaye N. Truscott. "Crystal structure of bacterial succinate:quinone oxidoreductase flavoprotein SdhA in complex with its assembly factor SdhE." Proceedings of the National Academy of Sciences 115, no. 12 (March 7, 2018): 2982–87. http://dx.doi.org/10.1073/pnas.1800195115.
Повний текст джерелаCedervall, Peder E., Alan B. Hooper, and Carrie M. Wilmot. "Crystallization and preliminary X-ray crystallographic analysis of a new crystal form of hydroxylamine oxidoreductase fromNitrosomonas europaea." Acta Crystallographica Section F Structural Biology and Crystallization Communications 65, no. 12 (November 27, 2009): 1296–98. http://dx.doi.org/10.1107/s1744309109046119.
Повний текст джерелаKim, Min-Kyu, Young Jun An, Chang-Sook Jeong, and Sun-Shin Cha. "Crystallization and preliminary X-ray crystallographic analysis of the putative NADP(H)-dependent oxidoreductase YncB fromVibrio vulnificus." Acta Crystallographica Section F Structural Biology and Crystallization Communications 68, no. 9 (August 31, 2012): 1098–101. http://dx.doi.org/10.1107/s1744309112030527.
Повний текст джерелаHou, Hai, Ruiying Li, Xiaoyan Wang, Zhen Yuan, Xuemeng Liu, Zhenmin Chen, and Xiaoling Xu. "Crystallographic analysis of a novel aldo-keto reductase fromThermotoga maritimain complex with NADP+." Acta Crystallographica Section F Structural Biology Communications 71, no. 7 (June 27, 2015): 847–55. http://dx.doi.org/10.1107/s2053230x15009735.
Повний текст джерелаCheng, Zhong, Yao Li, Chun Sui, Xiaobo Sun, and Yong Xie. "Synthesis, purification and crystallographic studies of the C-terminal sterol carrier protein type 2 (SCP-2) domain of human hydroxysteroid dehydrogenase-like protein 2." Acta Crystallographica Section F Structural Biology Communications 71, no. 7 (June 27, 2015): 901–5. http://dx.doi.org/10.1107/s2053230x15008559.
Повний текст джерелаBuey, Rubén M., Juan B. Arellano, Luis López-Maury, Sergio Galindo-Trigo, Adrián Velázquez-Campoy, José L. Revuelta, José M. de Pereda, et al. "Unprecedented pathway of reducing equivalents in a diflavin-linked disulfide oxidoreductase." Proceedings of the National Academy of Sciences 114, no. 48 (November 13, 2017): 12725–30. http://dx.doi.org/10.1073/pnas.1713698114.
Повний текст джерелаRosário, Ana Lúcia, Filipa V. Sena, Ana P. Batista, Tânia F. Oliveira, Diogo Athayde, Manuela M. Pereira, José A. Brito, and Margarida Archer. "Expression, purification, crystallization and preliminary X-ray diffraction analysis of a type II NADH:quinone oxidoreductase from the human pathogenStaphylococcus aureus." Acta Crystallographica Section F Structural Biology Communications 71, no. 4 (March 28, 2015): 477–82. http://dx.doi.org/10.1107/s2053230x15005178.
Повний текст джерелаChicano, Tadeo Moreno, Lea Dietrich, Naomi M. de Almeida, Mohd Akram, Elisabeth Hartmann, Franziska Leidreiter, Daniel Leopoldus, et al. "Structural and functional characterization of the intracellular filament-forming nitrite oxidoreductase multiprotein complex." Nature Microbiology 6, no. 9 (July 15, 2021): 1129–39. http://dx.doi.org/10.1038/s41564-021-00934-8.
Повний текст джерелаLee, Kitaik, Kwon Joo Yeo, Sae Hae Choi, Eun Hye Lee, Bo Keun Kim, Sulhee Kim, Hae-Kap Cheong, et al. "Monothiol and dithiol glutaredoxin-1 from Clostridium oremlandii: identification of domain-swapped structures by NMR, X-ray crystallography and HDX mass spectrometry." IUCrJ 7, no. 6 (September 19, 2020): 1019–27. http://dx.doi.org/10.1107/s2052252520011598.
Повний текст джерелаCapper, Michael, Paul O'Neill, Giancarlo Biagini, Samar Hasnain, and Svetlana Antonyuk. "Overcoming drug-resistant malaria through rational drug design in cytochrome bc1." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C806. http://dx.doi.org/10.1107/s2053273314091931.
Повний текст джерелаHausrath, Andrew C., Nicholas A. Ramirez, Alan T. Ly, and Megan M. McEvoy. "The bacterial copper resistance protein CopG contains a cysteine-bridged tetranuclear copper cluster." Journal of Biological Chemistry 295, no. 32 (June 22, 2020): 11364–76. http://dx.doi.org/10.1074/jbc.ra120.013907.
Повний текст джерелаWinski, Shannon L., Margarita Faig, Mario A. Bianchet, David Siegel, Elizabeth Swann, Kim Fung, Mark W. Duncan, Christopher J. Moody, L. Mario Amzel, and David Ross. "Characterization of a Mechanism-Based Inhibitor of NAD(P)H:Quinone Oxidoreductase 1 by Biochemical, X-ray Crystallographic, and Mass Spectrometric Approaches†." Biochemistry 40, no. 50 (December 2001): 15135–42. http://dx.doi.org/10.1021/bi011324i.
Повний текст джерелаZhu, Jiapeng, Martin S. King, Minmin Yu, Liron Klipcan, Andrew G. W. Leslie та Judy Hirst. "Structure of subcomplex Iβ of mammalian respiratory complex I leads to new supernumerary subunit assignments". Proceedings of the National Academy of Sciences 112, № 39 (14 вересня 2015): 12087–92. http://dx.doi.org/10.1073/pnas.1510577112.
Повний текст джерелаKANEMURA, Shingo, Kenji INABA, and Masaki OKUMURA. "Crystallographic and Small Angle X-ray Scattering Analyses Provide New Mechanistic Insight into the Protein Quality Control System by the ER-Resident Oxidoreductases and their Upstream Enzymes." Nihon Kessho Gakkaishi 64, no. 3 (August 31, 2022): 209–10. http://dx.doi.org/10.5940/jcrsj.64.209.
Повний текст джерелаFarheen, Jabeen, and Simeen Mansoor. "Anti-stress phytohormones impact on proteome profile of green gram (Vigna radiata) under salt toxicity." World Journal of Biology and Biotechnology 5, no. 2 (April 30, 2020): 17. http://dx.doi.org/10.33865/wjb.005.02.0213.
Повний текст джерелаWang, Yung-Lin, Chin-Yuan Chang, Ning-Shian Hsu, I.-Wen Lo, Kuan-Hung Lin, Chun-Liang Chen, Chi-Fon Chang, et al. "N-Formimidoylation/-iminoacetylation modification in aminoglycosides requires FAD-dependent and ligand-protein NOS bridge dual chemistry." Nature Communications 14, no. 1 (May 3, 2023). http://dx.doi.org/10.1038/s41467-023-38218-w.
Повний текст джерелаGalemou Yoga, Etienne, Jonathan Schiller, and Volker Zickermann. "Ubiquinone Binding and Reduction by Complex I—Open Questions and Mechanistic Implications." Frontiers in Chemistry 9 (April 30, 2021). http://dx.doi.org/10.3389/fchem.2021.672851.
Повний текст джерелаSiegel, Sara D., Brendan R. Amer, Chenggang Wu, Michael R. Sawaya, Jason E. Gosschalk, Robert T. Clubb, and Hung Ton-That. "Structure and Mechanism of LcpA, a Phosphotransferase That Mediates Glycosylation of a Gram-Positive Bacterial Cell Wall-Anchored Protein." mBio 10, no. 1 (February 19, 2019). http://dx.doi.org/10.1128/mbio.01580-18.
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