Статті в журналах з теми "M. tuberculosis argininosuccinate lyase"
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Paul, Anju, Archita Mishra, Avadhesha Surolia, and Mamannamana Vijayan. "Structural studies on M. tuberculosis argininosuccinate lyase and its liganded complex: Insights into catalytic mechanism." IUBMB Life 71, no. 5 (January 7, 2019): 643–52. http://dx.doi.org/10.1002/iub.2000.
Повний текст джерелаChen, Xiaobo, Jiayue Chen, Wei Zhang, Huiying Wang, Xiang Liu, Weihong Zhou, Haitao Yang, and Zihe Rao. "Crystal structure and biochemical study on argininosuccinate lyase from Mycobacterium tuberculosis." Biochemical and Biophysical Research Communications 510, no. 1 (February 2019): 116–21. http://dx.doi.org/10.1016/j.bbrc.2019.01.061.
Повний текст джерелаSalapatek, Anne Marie F., Yu-Fang Wang, Yu-Kang Mao, Masataka Mori, and Edwin E. Daniel. "Myogenic NOS in canine lower esophageal sphincter: enzyme activation, substrate recycling, and product actions." American Journal of Physiology-Cell Physiology 274, no. 4 (April 1, 1998): C1145—C1157. http://dx.doi.org/10.1152/ajpcell.1998.274.4.c1145.
Повний текст джерелаChung, Sai-Fung, Chi-Fai Kim, Ho-Yin Chow, Hiu-Chi Chong, Suet-Ying Tam, Yun-Chung Leung, and Wai-Hung Lo. "Recombinant Bacillus caldovelox Arginase Mutant (BCA-M) Induces Apoptosis, Autophagy, Cell Cycle Arrest and Growth Inhibition in Human Cervical Cancer Cells." International Journal of Molecular Sciences 21, no. 20 (October 9, 2020): 7445. http://dx.doi.org/10.3390/ijms21207445.
Повний текст джерелаPaul, A., A. Mishra, A. Surolia, and M. Vijayan. "Cloning, expression, purification, crystallization and preliminary X-ray studies of argininosuccinate lyase (Rv1659) fromMycobacterium tuberculosis." Acta Crystallographica Section F Structural Biology and Crystallization Communications 69, no. 12 (November 29, 2013): 1422–24. http://dx.doi.org/10.1107/s1744309113031138.
Повний текст джерелаLee, H. J., S. H. Chiou та G. G. Chang. "Inactivation of the endogenous argininosuccinate lyase activity of duck δ-crystallin by modification of an essential histidine residue with diethyl pyrocarbonate". Biochemical Journal 293, № 2 (15 липня 1993): 537–44. http://dx.doi.org/10.1042/bj2930537.
Повний текст джерелаHöner Zu Bentrup, Kerstin, Andras Miczak, Dana L. Swenson, and David G. Russell. "Characterization of Activity and Expression of Isocitrate Lyase in Mycobacterium avium andMycobacterium tuberculosis." Journal of Bacteriology 181, no. 23 (December 1, 1999): 7161–67. http://dx.doi.org/10.1128/jb.181.23.7161-7167.1999.
Повний текст джерелаMishra, Archita, and Avadhesha Surolia. "Biochemical characterization of argininosuccinate lyase fromM. tuberculosis: significance of a c-terminal cysteine in catalysis and thermal stability." IUBMB Life 69, no. 11 (October 16, 2017): 896–907. http://dx.doi.org/10.1002/iub.1683.
Повний текст джерелаDuan, Changyuan, Qihua Jiang, Xue Jiang, Hongwei Zeng, Qiaomin Wu, Yang Yu, and Xiaolan Yang. "Discovery of a Novel Inhibitor Structure of Mycobacterium tuberculosis Isocitrate Lyase." Molecules 27, no. 8 (April 11, 2022): 2447. http://dx.doi.org/10.3390/molecules27082447.
Повний текст джерелаLee, Yie-Vern, Habibah A. Wahab, and Yee Siew Choong. "Potential Inhibitors for Isocitrate Lyase ofMycobacterium tuberculosisand Non-M. tuberculosis: A Summary." BioMed Research International 2015 (2015): 1–20. http://dx.doi.org/10.1155/2015/895453.
Повний текст джерелаGouzy, Alexandre, Claire Healy, Katherine A. Black, Kyu Y. Rhee, and Sabine Ehrt. "Growth of Mycobacterium tuberculosis at acidic pH depends on lipid assimilation and is accompanied by reduced GAPDH activity." Proceedings of the National Academy of Sciences 118, no. 32 (August 2, 2021): e2024571118. http://dx.doi.org/10.1073/pnas.2024571118.
Повний текст джерелаMicklinghoff, Julia C., Katrin J. Breitinger, Mascha Schmidt, Robert Geffers, Bernhard J. Eikmanns, and Franz-Christoph Bange. "Role of the Transcriptional Regulator RamB (Rv0465c) in the Control of the Glyoxylate Cycle in Mycobacterium tuberculosis." Journal of Bacteriology 191, no. 23 (September 18, 2009): 7260–69. http://dx.doi.org/10.1128/jb.01009-09.
Повний текст джерелаChanda, Anesha, Sanjib Kalita, Awdhesh Kumar Mishra, Liza Changkakoti, Janayita Biswa Sarma, Kunal Biswas, Debashree Kakati, et al. "Identification of Concomitant Inhibitors against Glutamine Synthetase and Isocitrate Lyase in Mycobacterium tuberculosis from Natural Sources." BioMed Research International 2022 (October 3, 2022): 1–14. http://dx.doi.org/10.1155/2022/4661491.
Повний текст джерелаSavvi, Suzana, Digby F. Warner, Bavesh D. Kana, John D. McKinney, Valerie Mizrahi, and Stephanie S. Dawes. "Functional Characterization of a Vitamin B12-Dependent Methylmalonyl Pathway in Mycobacterium tuberculosis: Implications for Propionate Metabolism during Growth on Fatty Acids." Journal of Bacteriology 190, no. 11 (March 28, 2008): 3886–95. http://dx.doi.org/10.1128/jb.01767-07.
Повний текст джерелаHarrison, Anthony J., Minmin Yu, Therés Gårdenborg, Martin Middleditch, Rochelle J. Ramsay, Edward N. Baker, and J. Shaun Lott. "The Structure of MbtI from Mycobacterium tuberculosis, the First Enzyme in the Biosynthesis of the Siderophore Mycobactin, Reveals It To Be a Salicylate Synthase." Journal of Bacteriology 188, no. 17 (September 1, 2006): 6081–91. http://dx.doi.org/10.1128/jb.00338-06.
Повний текст джерелаWalsh, P. "Subcellular localization and biochemical properties of the enzymes of carbamoyl phosphate and urea synthesis in the batrachoidid fishes Opsanus beta, Opsanus tau and Porichthys notatus." Journal of Experimental Biology 198, no. 3 (March 1, 1995): 755–66. http://dx.doi.org/10.1242/jeb.198.3.755.
Повний текст джерелаWang, Xiao-Ming, Changlong Lu, Karine Soetaert, Catherine S'Heeren, Priska Peirs, Marie-Antoinette Lanéelle, Philippe Lefèvre, et al. "Biochemical and immunological characterization of a cpn60.1 knockout mutant of Mycobacterium bovis BCG." Microbiology 157, no. 4 (April 1, 2011): 1205–19. http://dx.doi.org/10.1099/mic.0.045120-0.
Повний текст джерелаIbeji, Collins U., Nor Amirah Mohd Salleh, Jia Siang Sum, Angela Chiew Wen Ch’ng, Theam Soon Lim, and Yee Siew Choong. "Demystifying the catalytic pathway of Mycobacterium tuberculosis isocitrate lyase." Scientific Reports 10, no. 1 (November 3, 2020). http://dx.doi.org/10.1038/s41598-020-75799-8.
Повний текст джерелаKo, Eon-Min, Ju-Yeon Kim, Sujin Lee, Suhkmann Kim, Jihwan Hwang, and Jeong-Il Oh. "Regulation of the icl1 gene encoding the major isocitrate lyase in Mycobacterium smegmatis." Journal of Bacteriology, September 13, 2021. http://dx.doi.org/10.1128/jb.00402-21.
Повний текст джерелаHavis, Spencer, Abiodun Bodunrin, Jonathan Rangel, Rene Zimmerer, Jesse Murphy, Jacob D. Storey, Thinh D. Duong, et al. "A Universal Stress Protein That Controls Bacterial Stress Survival in Micrococcus luteus." Journal of Bacteriology 201, no. 24 (September 23, 2019). http://dx.doi.org/10.1128/jb.00497-19.
Повний текст джерелаPuniya, Bhanwar Lal, Deepika Kulshreshtha, Inna Mittal, Ahmed Mobeen, and Srinivasan Ramachandran. "Integration of Metabolic Modeling with Gene Co-expression Reveals Transcriptionally Programmed Reactions Explaining Robustness in Mycobacterium tuberculosis." Scientific Reports 6, no. 1 (March 22, 2016). http://dx.doi.org/10.1038/srep23440.
Повний текст джерелаSharma, Shweta, Rupesh Chikhale, Nivedita Shinde, A. M. Khan, and Vivek Kumar Gupta. "Targeting dormant phenotype acquired mycobacteria using natural products by exploring its important targets: In vitro and in silico studies." Frontiers in Cellular and Infection Microbiology 13 (March 24, 2023). http://dx.doi.org/10.3389/fcimb.2023.1111997.
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