Статті в журналах з теми "Lsr2"
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Gordon, Blair R. G., Robin Imperial, Linru Wang, William Wiley Navarre, and Jun Liu. "Lsr2 of Mycobacterium Represents a Novel Class of H-NS-Like Proteins." Journal of Bacteriology 190, no. 21 (September 5, 2008): 7052–59. http://dx.doi.org/10.1128/jb.00733-08.
Saini, Chaman, H. K. Prasad, Rajni Rani, A. Murtaza, Namita Misra, N. P. Shanker Narayan, and Indira Nath. "Lsr2 of Mycobacterium leprae and Its Synthetic Peptides Elicit Restitution of T Cell Responses in Erythema Nodosum Leprosum and Reversal Reactions in Patients with Lepromatous Leprosy." Clinical and Vaccine Immunology 20, no. 5 (February 27, 2013): 673–82. http://dx.doi.org/10.1128/cvi.00762-12.
Pinault, Lucile, Jeong-Sun Han, Choong-Min Kang, Jimmy Franco, and Donald R. Ronning. "Zafirlukast Inhibits Complexation of Lsr2 with DNA and Growth of Mycobacterium tuberculosis." Antimicrobial Agents and Chemotherapy 57, no. 5 (February 25, 2013): 2134–40. http://dx.doi.org/10.1128/aac.02407-12.
Chen, Jeffrey M., Greg J. German, David C. Alexander, Huiping Ren, Tracy Tan, and Jun Liu. "Roles of Lsr2 in Colony Morphology and Biofilm Formation of Mycobacterium smegmatis." Journal of Bacteriology 188, no. 2 (January 15, 2006): 633–41. http://dx.doi.org/10.1128/jb.188.2.633-641.2006.
Arora, Kriti, Danelle C. Whiteford, Dalia Lau-Bonilla, Christine M. Davitt, and John L. Dahl. "Inactivation of lsr2 Results in a Hypermotile Phenotype in Mycobacterium smegmatis." Journal of Bacteriology 190, no. 12 (April 11, 2008): 4291–300. http://dx.doi.org/10.1128/jb.00023-08.
Seo, Jeong-Woo, Ki-Hyo Jang, Soon Ah Kang, Ki-Bang Song, Eun Kyung Jang, Buem-Seek Park, Chul Ho Kim, and Sang-Ki Rhee. "Molecular Characterization of the Growth Phase-Dependent Expression of the lsrA Gene, Encoding Levansucrase of Rahnella aquatilis." Journal of Bacteriology 184, no. 21 (November 1, 2002): 5862–70. http://dx.doi.org/10.1128/jb.184.21.5862-5870.2002.
Gerges, Elias, Jean-Louis Herrmann, and Frédéric Crémazy. "Lsr2 : protéine associée au nucléoïde (NAP) et facteur transcriptionnel chez les mycobactéries." médecine/sciences 40, no. 2 (February 2024): 154–60. http://dx.doi.org/10.1051/medsci/2023218.
Li, Yakun, Yuyun Wei, Xiao Guo, Xiaohui Li, Lining Lu, Lihua Hu, and Zheng‐Guo He. "Insertion sequence transposition activates antimycobacteriophage immunity through an lsr2‐silenced lipid metabolism gene island." mLife 3, no. 1 (March 2024): 87–100. http://dx.doi.org/10.1002/mlf2.12106.
Nguyen, Kiet T., Kristina Piastro, Todd A. Gray, and Keith M. Derbyshire. "Mycobacterial Biofilms Facilitate Horizontal DNA Transfer between Strains of Mycobacterium smegmatis." Journal of Bacteriology 192, no. 19 (July 30, 2010): 5134–42. http://dx.doi.org/10.1128/jb.00650-10.
Deng, Lina, Rui Wang, Guowei Wang, Mingxu Liu, Guojian Liao, Zhihua Liao, and Min Chen. "Targeted isolation of sulfur-containing metabolites from Lsr2-deletion mutant strain of Streptomyces roseosporus." RSC Advances 7, no. 60 (2017): 37771–77. http://dx.doi.org/10.1039/c7ra06482a.
Chaduvula, Mehervani, A. Murtaza, Namita Misra, N. P. Shankar Narayan, V. Ramesh, H. K. Prasad, Rajni Rani, R. K. Chinnadurai, and Indira Nath. "Lsr2 Peptides of Mycobacterium leprae Show Hierarchical Responses in Lymphoproliferative Assays, with Selective Recognition by Patients with Anergic Lepromatous Leprosy." Infection and Immunity 80, no. 2 (December 5, 2011): 742–52. http://dx.doi.org/10.1128/iai.05384-11.
Qu, Yuanyuan, Ci Ji Lim, Yixun R. Whang, Jun Liu, and Jie Yan. "Mechanism of DNA organization by Mycobacterium tuberculosis protein Lsr2." Nucleic Acids Research 41, no. 10 (April 10, 2013): 5263–72. http://dx.doi.org/10.1093/nar/gkt249.
Chen, Jeffrey M., Huiping Ren, James E. Shaw, Yu Jing Wang, Ming Li, Andrea S. Leung, Vanessa Tran, et al. "Lsr2 of Mycobacterium tuberculosis is a DNA-bridging protein." Nucleic Acids Research 36, no. 7 (January 10, 2008): 2123–35. http://dx.doi.org/10.1093/nar/gkm1162.
Li, Jun, Can Attila, Liang Wang, Thomas K. Wood, James J. Valdes, and William E. Bentley. "Quorum Sensing in Escherichia coli Is Signaled by AI-2/LsrR: Effects on Small RNA and Biofilm Architecture." Journal of Bacteriology 189, no. 16 (June 8, 2007): 6011–20. http://dx.doi.org/10.1128/jb.00014-07.
Custodio, Luiz Antonio, Alexandre Saito, Marla Karine Amarante, Thiago Cezar Fujita, Aparecida de Lourdes Perim, Ivete Conchon Costa, Ionice Felipe, and Shiduca Itow Jankevicius. "Detection of Lsr2 gene of Mycobacterium leprae in nasal mucus." Brazilian Archives of Biology and Technology 55, no. 3 (June 2012): 375–80. http://dx.doi.org/10.1590/s1516-89132012000300007.
Yang, Wenfeng, Pengyi Li, Wei Yang, Yuxing Liu, Yulong He, Ovanes Petrosian, and Aleksandr Davydenko. "Research on Robust Audio-Visual Speech Recognition Algorithms." Mathematics 11, no. 7 (April 5, 2023): 1733. http://dx.doi.org/10.3390/math11071733.
Ha, Jung-Hye, Yumi Eo, Hee-Chul Ahn, and Kyoung-Seok Ryu. "Increasing the soluble expression and crystallization of theEscherichia coliquorum-sensing protein LsrK." Acta Crystallographica Section F Structural Biology Communications 73, no. 5 (April 26, 2017): 253–58. http://dx.doi.org/10.1107/s2053230x1700468x.
Colangeli, R., A. Haq, V. L. Arcus, E. Summers, R. S. Magliozzo, A. McBride, A. K. Mitra, et al. "The multifunctional histone-like protein Lsr2 protects mycobacteria against reactive oxygen intermediates." Proceedings of the National Academy of Sciences 106, no. 11 (February 23, 2009): 4414–18. http://dx.doi.org/10.1073/pnas.0810126106.
Ashmead, Helen M., Leonardo Negron, Kyle Webster, Vic Arcus, and Juliet A. Gerrard. "Proteins as supramolecular building blocks: Nterm-Lsr2 as a new protein tecton." Biopolymers 103, no. 5 (February 21, 2015): 260–70. http://dx.doi.org/10.1002/bip.22592.
Wang, Liang, Jun Li, John C. March, James J. Valdes, and William E. Bentley. "luxS-Dependent Gene Regulation in Escherichia coli K-12 Revealed by Genomic Expression Profiling." Journal of Bacteriology 187, no. 24 (December 15, 2005): 8350–60. http://dx.doi.org/10.1128/jb.187.24.8350-8360.2005.
Han, Hui, Kaijie Zhang, Guoxiong Li, Ying Yu, Shuqi Shi, Caice Liang, Huanqing Niu, et al. "Autoinducer-2: Its Role in Biofilm Formation and L-Threonine Production in Escherichia coli." Fermentation 9, no. 10 (October 19, 2023): 916. http://dx.doi.org/10.3390/fermentation9100916.
Kurthkoti, Krishna, Priyanka Tare, Rakhi Paitchowdhury, Vykuntham Naga Gowthami, Maria J. Garcia, Roberto Colangeli, Dipankar Chatterji, Valakunja Nagaraja, and G. Marcela Rodriguez. "The mycobacterial iron-dependent regulator IdeR induces ferritin (bfrB) by alleviating Lsr2 repression." Molecular Microbiology 98, no. 5 (September 18, 2015): 864–77. http://dx.doi.org/10.1111/mmi.13166.
Gopal-Srivastava, Rashmi, Ales Cvekl та Joram Piatigorsky. "Pax-6 and αB-crystallin/Small Heat Shock Protein Gene Regulation in the Murine Lens INTERACTION WITH THE LENS-SPECIFIC REGIONS, LSR1 AND LSR2". Journal of Biological Chemistry 271, № 38 (20 вересня 1996): 23029–36. http://dx.doi.org/10.1074/jbc.271.38.23029.
Liu, Jun, and Blair RG Gordon. "Targeting the global regulator Lsr2 as a novel approach for anti-tuberculosis drug development." Expert Review of Anti-infective Therapy 10, no. 9 (September 2012): 1049–53. http://dx.doi.org/10.1586/eri.12.86.
Bai, Yubin, Weiwei Wang, Mengyan Shi, Xiaojuan Wei, Xuzheng Zhou, Bing Li, and Jiyu Zhang. "Novel Antibiofilm Inhibitor Ginkgetin as an Antibacterial Synergist against Escherichia coli." International Journal of Molecular Sciences 23, no. 15 (August 8, 2022): 8809. http://dx.doi.org/10.3390/ijms23158809.
Park, Kun Taek, John L. Dahl, John P. Bannantine, Raúl G. Barletta, Jongsam Ahn, Andrew J. Allen, Mary Jo Hamilton, and William C. Davis. "Demonstration of Allelic Exchange in the Slow-Growing Bacterium Mycobacterium avium subsp. paratuberculosis, and Generation of Mutants with Deletions at the pknG, relA, and lsr2 Loci." Applied and Environmental Microbiology 74, no. 6 (January 11, 2008): 1687–95. http://dx.doi.org/10.1128/aem.01208-07.
Qin, L., A. M. Erkelens, F. Ben Bdira, and R. T. Dame. "The architects of bacterial DNA bridges: a structurally and functionally conserved family of proteins." Open Biology 9, no. 12 (December 2019): 190223. http://dx.doi.org/10.1098/rsob.190223.
Gordon, B. R. G., Y. Li, L. Wang, A. Sintsova, H. van Bakel, S. Tian, W. W. Navarre, B. Xia, and J. Liu. "Lsr2 is a nucleoid-associated protein that targets AT-rich sequences and virulence genes in Mycobacterium tuberculosis." Proceedings of the National Academy of Sciences 107, no. 11 (January 20, 2010): 5154–59. http://dx.doi.org/10.1073/pnas.0913551107.
Alqaseer, Kawther, Obolbek Turapov, Philippe Barthe, Heena Jagatia, Angélique De Visch, Christian Roumestand, Malgorzata Wegrzyn, et al. "Protein kinase B controls Mycobacterium tuberculosis growth via phosphorylation of the transcriptional regulator Lsr2 at threonine 112." Molecular Microbiology 112, no. 6 (October 10, 2019): 1847–62. http://dx.doi.org/10.1111/mmi.14398.
Du, Yanli, Hua Zhang, Yang He, Feng Huang, and Zheng-Guo He. "Mycobacterium smegmatis Lsr2 physically and functionally interacts with a new flavoprotein involved in bacterial resistance to oxidative stress." Journal of Biochemistry 152, no. 5 (September 5, 2012): 479–86. http://dx.doi.org/10.1093/jb/mvs095.
Datta, Chandreyee, Rajiv Kumar Jha, Wareed Ahmed, Sohini Ganguly, Soumitra Ghosh, and Valakunja Nagaraja. "Physical and functional interaction between nucleoid‐associated proteins HU and Lsr2 ofMycobacterium tuberculosis: altered DNA binding and gene regulation." Molecular Microbiology 111, no. 4 (February 11, 2019): 981–94. http://dx.doi.org/10.1111/mmi.14202.
Summers, Emma L., Kathrin Meindl, Isabel Usón, Alok K. Mitra, Mazdak Radjainia, Roberto Colangeli, David Alland, and Vickery L. Arcus. "The Structure of the Oligomerization Domain of Lsr2 from Mycobacterium tuberculosis Reveals a Mechanism for Chromosome Organization and Protection." PLoS ONE 7, no. 6 (June 13, 2012): e38542. http://dx.doi.org/10.1371/journal.pone.0038542.
Colangeli, Roberto, Danica Helb, Catherine Vilchèze, Manzour Hernando Hazbón, Chee-Gun Lee, Hassan Safi, Brendan Sayers, et al. "Transcriptional Regulation of Multi-Drug Tolerance and Antibiotic-Induced Responses by the Histone-Like Protein Lsr2 in M. tuberculosis." PLoS Pathogens 3, no. 6 (June 22, 2007): e87. http://dx.doi.org/10.1371/journal.ppat.0030087.
Luo, Li, Shi-Yi Yao, Anke Becker, Silvia Rüberg, Guan-Qiao Yu, Jia-Bi Zhu, and Hai-Ping Cheng. "Two New Sinorhizobium meliloti LysR-Type Transcriptional Regulators Required for Nodulation." Journal of Bacteriology 187, no. 13 (July 1, 2005): 4562–72. http://dx.doi.org/10.1128/jb.187.13.4562-4572.2005.
Wang, Liang, Yoshifumi Hashimoto, Chen-Yu Tsao, James J. Valdes, and William E. Bentley. "Cyclic AMP (cAMP) and cAMP Receptor Protein Influence both Synthesis and Uptake of Extracellular Autoinducer 2 in Escherichia coli." Journal of Bacteriology 187, no. 6 (March 15, 2005): 2066–76. http://dx.doi.org/10.1128/jb.187.6.2066-2076.2005.
Ramakrishnan, S., M. B. Sukhaswami, K. M. Patil, and C. Eswaran. "Sequence Data Analysis Reveals a Relationship Between LSR2, the Recombinant Fusion Protein Mimicing M.Leprae and VIF of Bovine Immunodeficiency Virus (BIV)." Journal of Biomolecular Structure and Dynamics 15, no. 3 (December 1997): 605–9. http://dx.doi.org/10.1080/07391102.1997.10508970.
Xavier, Karina B., and Bonnie L. Bassler. "Regulation of Uptake and Processing of the Quorum-Sensing Autoinducer AI-2 in Escherichia coli." Journal of Bacteriology 187, no. 1 (January 1, 2005): 238–48. http://dx.doi.org/10.1128/jb.187.1.238-248.2005.
Báez-Ramírez, Estalina, Luis Querales, Carlos Andres Aranaga, Gustavo López, Elba Guerrero, Laurent Kremer, Séverine Carrère-Kremer, et al. "Elimination of PknL and MSMEG_4242 in Mycobacterium smegmatis alters the character of the outer cell envelope and selects for mutations in Lsr2." Cell Surface 7 (December 2021): 100060. http://dx.doi.org/10.1016/j.tcsw.2021.100060.
Janczarek, Monika. "The Ros/MucR Zinc-Finger Protein Family in Bacteria: Structure and Functions." International Journal of Molecular Sciences 23, no. 24 (December 8, 2022): 15536. http://dx.doi.org/10.3390/ijms232415536.
Bruni, Gillian O., Yunci Qi, Evan Terrell, Rebecca A. Dupre, and Christopher P. Mattison. "Characterization of Levan Fructan Produced by a Gluconobacter japonicus Strain Isolated from a Sugarcane Processing Facility." Microorganisms 12, no. 1 (January 5, 2024): 107. http://dx.doi.org/10.3390/microorganisms12010107.
Yamamoto, Takanobu, Sawako Yada, Yuji Matsuda, Hirofumi Otani, Shunji Yoshikawa, Taro Sasaoka, Yu Hatano, et al. "A Novel Rotablator Technique (Low-Speed following High-Speed Rotational Atherectomy) Can Achieve Larger Lumen Gain: Evaluation Using Optimal Frequency Domain Imaging." Journal of Interventional Cardiology 2019 (May 20, 2019): 1–7. http://dx.doi.org/10.1155/2019/9282876.
Kim, Hyun-Min, and Zifei Liu. "LSD2 Is an Epigenetic Player in Multiple Types of Cancer and Beyond." Biomolecules 14, no. 5 (May 3, 2024): 553. http://dx.doi.org/10.3390/biom14050553.
Marayati, Bahjat F., James F. Tucker, David A. De La Cerda, Tien-Chi Hou, Rong Chen, Tomoyasu Sugiyama, James B. Pease, and Ke Zhang. "The Catalytic-Dependent and -Independent Roles of Lsd1 and Lsd2 Lysine Demethylases in Heterochromatin Formation in Schizosaccharomyces pombe." Cells 9, no. 4 (April 13, 2020): 955. http://dx.doi.org/10.3390/cells9040955.
Xu, Yijie, Chunlan Zeng, Huiqi Wen, Qianqian Shi, Xu Zhao, Qingbin Meng, Xingzhou Li, and Junhai Xiao. "Discovery of AI-2 Quorum Sensing Inhibitors Targeting the LsrK/HPr Protein–Protein Interaction Site by Molecular Dynamics Simulation, Virtual Screening, and Bioassay Evaluation." Pharmaceuticals 16, no. 5 (May 12, 2023): 737. http://dx.doi.org/10.3390/ph16050737.
Ha, Jung-Hye, Eun-Hee Kim, Hae-Kap Cheong, and Kyoung-Seok Ryu. "Crystal structures of LsrR complexed with p-AI-2 reveal distinct mechanisms." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C580. http://dx.doi.org/10.1107/s2053273314094194.
Du, Mei Hui, Min Zhao, Lei Lu, Tian Nv Wang, Tai Lun Li, Li Yan Zhao, Jun Bo Pan, Guo Fu Li, and Jun Li. "Isolation and Dye Decolorization of a Bacillus subtilis Strain LS02 Exhibiting Laccase Activity." Advanced Materials Research 183-185 (January 2011): 839–43. http://dx.doi.org/10.4028/www.scientific.net/amr.183-185.839.
Chiou, Sheng-Yuan, Chih-Kai Chao, and Ya-Wun Yang. "Topography of Low Skin Resistance Points (LSRP) in Rats." American Journal of Chinese Medicine 26, no. 01 (January 1998): 19–27. http://dx.doi.org/10.1142/s0192415x9800004x.
Shou, Yiyun, Martin Sellbom, and Jin Han. "Evaluating the Construct Validity of the Levenson Self-Report Psychopathy Scale in China." Assessment 24, no. 8 (March 11, 2016): 1008–23. http://dx.doi.org/10.1177/1073191116637421.
Md Ghazaly, Mariam, Yeo Chin Kiat, Chong Shin Horng, Norhaslinda Hasim, Zulkeflee Abdullah, and Nurdiana Nordin. "TUBULAR LINEAR SWITCHED RELUCTANCE ACTUATOR: DESIGN AND CHARACTERIZATION." Jurnal Teknologi 84, no. 5 (July 26, 2022): 117–29. http://dx.doi.org/10.11113/jurnalteknologi.v84.17902.
Iannizzi, Claire, Elie A. Akl, Lara A. Kahale, Elena Dorando, Abina Mosunmola Aminat, James M. Barker, Joanne E. McKenzie, Neal R. Haddaway, Vanessa Piechotta, and Nicole Skoetz. "Methods and guidance on conducting, reporting, publishing and appraising living systematic reviews: a scoping review protocol." F1000Research 10 (August 13, 2021): 802. http://dx.doi.org/10.12688/f1000research.55108.1.