Artykuły w czasopismach na temat „Lsr2”
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Gordon, Blair R. G., Robin Imperial, Linru Wang, William Wiley Navarre i Jun Liu. "Lsr2 of Mycobacterium Represents a Novel Class of H-NS-Like Proteins". Journal of Bacteriology 190, nr 21 (5.09.2008): 7052–59. http://dx.doi.org/10.1128/jb.00733-08.
Pełny tekst źródłaSaini, Chaman, H. K. Prasad, Rajni Rani, A. Murtaza, Namita Misra, N. P. Shanker Narayan i 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, nr 5 (27.02.2013): 673–82. http://dx.doi.org/10.1128/cvi.00762-12.
Pełny tekst źródłaPinault, Lucile, Jeong-Sun Han, Choong-Min Kang, Jimmy Franco i Donald R. Ronning. "Zafirlukast Inhibits Complexation of Lsr2 with DNA and Growth of Mycobacterium tuberculosis". Antimicrobial Agents and Chemotherapy 57, nr 5 (25.02.2013): 2134–40. http://dx.doi.org/10.1128/aac.02407-12.
Pełny tekst źródłaChen, Jeffrey M., Greg J. German, David C. Alexander, Huiping Ren, Tracy Tan i Jun Liu. "Roles of Lsr2 in Colony Morphology and Biofilm Formation of Mycobacterium smegmatis". Journal of Bacteriology 188, nr 2 (15.01.2006): 633–41. http://dx.doi.org/10.1128/jb.188.2.633-641.2006.
Pełny tekst źródłaArora, Kriti, Danelle C. Whiteford, Dalia Lau-Bonilla, Christine M. Davitt i John L. Dahl. "Inactivation of lsr2 Results in a Hypermotile Phenotype in Mycobacterium smegmatis". Journal of Bacteriology 190, nr 12 (11.04.2008): 4291–300. http://dx.doi.org/10.1128/jb.00023-08.
Pełny tekst źródłaSeo, Jeong-Woo, Ki-Hyo Jang, Soon Ah Kang, Ki-Bang Song, Eun Kyung Jang, Buem-Seek Park, Chul Ho Kim i Sang-Ki Rhee. "Molecular Characterization of the Growth Phase-Dependent Expression of the lsrA Gene, Encoding Levansucrase of Rahnella aquatilis". Journal of Bacteriology 184, nr 21 (1.11.2002): 5862–70. http://dx.doi.org/10.1128/jb.184.21.5862-5870.2002.
Pełny tekst źródłaGerges, Elias, Jean-Louis Herrmann i Frédéric Crémazy. "Lsr2 : protéine associée au nucléoïde (NAP) et facteur transcriptionnel chez les mycobactéries". médecine/sciences 40, nr 2 (luty 2024): 154–60. http://dx.doi.org/10.1051/medsci/2023218.
Pełny tekst źródłaLi, Yakun, Yuyun Wei, Xiao Guo, Xiaohui Li, Lining Lu, Lihua Hu i Zheng‐Guo He. "Insertion sequence transposition activates antimycobacteriophage immunity through an lsr2‐silenced lipid metabolism gene island". mLife 3, nr 1 (marzec 2024): 87–100. http://dx.doi.org/10.1002/mlf2.12106.
Pełny tekst źródłaNguyen, Kiet T., Kristina Piastro, Todd A. Gray i Keith M. Derbyshire. "Mycobacterial Biofilms Facilitate Horizontal DNA Transfer between Strains of Mycobacterium smegmatis". Journal of Bacteriology 192, nr 19 (30.07.2010): 5134–42. http://dx.doi.org/10.1128/jb.00650-10.
Pełny tekst źródłaDeng, Lina, Rui Wang, Guowei Wang, Mingxu Liu, Guojian Liao, Zhihua Liao i Min Chen. "Targeted isolation of sulfur-containing metabolites from Lsr2-deletion mutant strain of Streptomyces roseosporus". RSC Advances 7, nr 60 (2017): 37771–77. http://dx.doi.org/10.1039/c7ra06482a.
Pełny tekst źródłaChaduvula, Mehervani, A. Murtaza, Namita Misra, N. P. Shankar Narayan, V. Ramesh, H. K. Prasad, Rajni Rani, R. K. Chinnadurai i 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, nr 2 (5.12.2011): 742–52. http://dx.doi.org/10.1128/iai.05384-11.
Pełny tekst źródłaQu, Yuanyuan, Ci Ji Lim, Yixun R. Whang, Jun Liu i Jie Yan. "Mechanism of DNA organization by Mycobacterium tuberculosis protein Lsr2". Nucleic Acids Research 41, nr 10 (10.04.2013): 5263–72. http://dx.doi.org/10.1093/nar/gkt249.
Pełny tekst źródłaChen, Jeffrey M., Huiping Ren, James E. Shaw, Yu Jing Wang, Ming Li, Andrea S. Leung, Vanessa Tran i in. "Lsr2 of Mycobacterium tuberculosis is a DNA-bridging protein". Nucleic Acids Research 36, nr 7 (10.01.2008): 2123–35. http://dx.doi.org/10.1093/nar/gkm1162.
Pełny tekst źródłaLi, Jun, Can Attila, Liang Wang, Thomas K. Wood, James J. Valdes i 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, nr 16 (8.06.2007): 6011–20. http://dx.doi.org/10.1128/jb.00014-07.
Pełny tekst źródłaCustodio, Luiz Antonio, Alexandre Saito, Marla Karine Amarante, Thiago Cezar Fujita, Aparecida de Lourdes Perim, Ivete Conchon Costa, Ionice Felipe i Shiduca Itow Jankevicius. "Detection of Lsr2 gene of Mycobacterium leprae in nasal mucus". Brazilian Archives of Biology and Technology 55, nr 3 (czerwiec 2012): 375–80. http://dx.doi.org/10.1590/s1516-89132012000300007.
Pełny tekst źródłaYang, Wenfeng, Pengyi Li, Wei Yang, Yuxing Liu, Yulong He, Ovanes Petrosian i Aleksandr Davydenko. "Research on Robust Audio-Visual Speech Recognition Algorithms". Mathematics 11, nr 7 (5.04.2023): 1733. http://dx.doi.org/10.3390/math11071733.
Pełny tekst źródłaHa, Jung-Hye, Yumi Eo, Hee-Chul Ahn i Kyoung-Seok Ryu. "Increasing the soluble expression and crystallization of theEscherichia coliquorum-sensing protein LsrK". Acta Crystallographica Section F Structural Biology Communications 73, nr 5 (26.04.2017): 253–58. http://dx.doi.org/10.1107/s2053230x1700468x.
Pełny tekst źródłaColangeli, R., A. Haq, V. L. Arcus, E. Summers, R. S. Magliozzo, A. McBride, A. K. Mitra i in. "The multifunctional histone-like protein Lsr2 protects mycobacteria against reactive oxygen intermediates". Proceedings of the National Academy of Sciences 106, nr 11 (23.02.2009): 4414–18. http://dx.doi.org/10.1073/pnas.0810126106.
Pełny tekst źródłaAshmead, Helen M., Leonardo Negron, Kyle Webster, Vic Arcus i Juliet A. Gerrard. "Proteins as supramolecular building blocks: Nterm-Lsr2 as a new protein tecton". Biopolymers 103, nr 5 (21.02.2015): 260–70. http://dx.doi.org/10.1002/bip.22592.
Pełny tekst źródłaWang, Liang, Jun Li, John C. March, James J. Valdes i William E. Bentley. "luxS-Dependent Gene Regulation in Escherichia coli K-12 Revealed by Genomic Expression Profiling". Journal of Bacteriology 187, nr 24 (15.12.2005): 8350–60. http://dx.doi.org/10.1128/jb.187.24.8350-8360.2005.
Pełny tekst źródłaHan, Hui, Kaijie Zhang, Guoxiong Li, Ying Yu, Shuqi Shi, Caice Liang, Huanqing Niu i in. "Autoinducer-2: Its Role in Biofilm Formation and L-Threonine Production in Escherichia coli". Fermentation 9, nr 10 (19.10.2023): 916. http://dx.doi.org/10.3390/fermentation9100916.
Pełny tekst źródłaKurthkoti, Krishna, Priyanka Tare, Rakhi Paitchowdhury, Vykuntham Naga Gowthami, Maria J. Garcia, Roberto Colangeli, Dipankar Chatterji, Valakunja Nagaraja i G. Marcela Rodriguez. "The mycobacterial iron-dependent regulator IdeR induces ferritin (bfrB) by alleviating Lsr2 repression". Molecular Microbiology 98, nr 5 (18.09.2015): 864–77. http://dx.doi.org/10.1111/mmi.13166.
Pełny tekst źródłaGopal-Srivastava, Rashmi, Ales Cvekl i 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, nr 38 (20.09.1996): 23029–36. http://dx.doi.org/10.1074/jbc.271.38.23029.
Pełny tekst źródłaLiu, Jun, i Blair RG Gordon. "Targeting the global regulator Lsr2 as a novel approach for anti-tuberculosis drug development". Expert Review of Anti-infective Therapy 10, nr 9 (wrzesień 2012): 1049–53. http://dx.doi.org/10.1586/eri.12.86.
Pełny tekst źródłaBai, Yubin, Weiwei Wang, Mengyan Shi, Xiaojuan Wei, Xuzheng Zhou, Bing Li i Jiyu Zhang. "Novel Antibiofilm Inhibitor Ginkgetin as an Antibacterial Synergist against Escherichia coli". International Journal of Molecular Sciences 23, nr 15 (8.08.2022): 8809. http://dx.doi.org/10.3390/ijms23158809.
Pełny tekst źródłaPark, Kun Taek, John L. Dahl, John P. Bannantine, Raúl G. Barletta, Jongsam Ahn, Andrew J. Allen, Mary Jo Hamilton i 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, nr 6 (11.01.2008): 1687–95. http://dx.doi.org/10.1128/aem.01208-07.
Pełny tekst źródłaQin, L., A. M. Erkelens, F. Ben Bdira i R. T. Dame. "The architects of bacterial DNA bridges: a structurally and functionally conserved family of proteins". Open Biology 9, nr 12 (grudzień 2019): 190223. http://dx.doi.org/10.1098/rsob.190223.
Pełny tekst źródłaGordon, B. R. G., Y. Li, L. Wang, A. Sintsova, H. van Bakel, S. Tian, W. W. Navarre, B. Xia i 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, nr 11 (20.01.2010): 5154–59. http://dx.doi.org/10.1073/pnas.0913551107.
Pełny tekst źródłaAlqaseer, Kawther, Obolbek Turapov, Philippe Barthe, Heena Jagatia, Angélique De Visch, Christian Roumestand, Malgorzata Wegrzyn i in. "Protein kinase B controls Mycobacterium tuberculosis growth via phosphorylation of the transcriptional regulator Lsr2 at threonine 112". Molecular Microbiology 112, nr 6 (10.10.2019): 1847–62. http://dx.doi.org/10.1111/mmi.14398.
Pełny tekst źródłaDu, Yanli, Hua Zhang, Yang He, Feng Huang i 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, nr 5 (5.09.2012): 479–86. http://dx.doi.org/10.1093/jb/mvs095.
Pełny tekst źródłaDatta, Chandreyee, Rajiv Kumar Jha, Wareed Ahmed, Sohini Ganguly, Soumitra Ghosh i Valakunja Nagaraja. "Physical and functional interaction between nucleoid‐associated proteins HU and Lsr2 ofMycobacterium tuberculosis: altered DNA binding and gene regulation". Molecular Microbiology 111, nr 4 (11.02.2019): 981–94. http://dx.doi.org/10.1111/mmi.14202.
Pełny tekst źródłaSummers, Emma L., Kathrin Meindl, Isabel Usón, Alok K. Mitra, Mazdak Radjainia, Roberto Colangeli, David Alland i 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, nr 6 (13.06.2012): e38542. http://dx.doi.org/10.1371/journal.pone.0038542.
Pełny tekst źródłaColangeli, Roberto, Danica Helb, Catherine Vilchèze, Manzour Hernando Hazbón, Chee-Gun Lee, Hassan Safi, Brendan Sayers i in. "Transcriptional Regulation of Multi-Drug Tolerance and Antibiotic-Induced Responses by the Histone-Like Protein Lsr2 in M. tuberculosis". PLoS Pathogens 3, nr 6 (22.06.2007): e87. http://dx.doi.org/10.1371/journal.ppat.0030087.
Pełny tekst źródłaLuo, Li, Shi-Yi Yao, Anke Becker, Silvia Rüberg, Guan-Qiao Yu, Jia-Bi Zhu i Hai-Ping Cheng. "Two New Sinorhizobium meliloti LysR-Type Transcriptional Regulators Required for Nodulation". Journal of Bacteriology 187, nr 13 (1.07.2005): 4562–72. http://dx.doi.org/10.1128/jb.187.13.4562-4572.2005.
Pełny tekst źródłaWang, Liang, Yoshifumi Hashimoto, Chen-Yu Tsao, James J. Valdes i 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, nr 6 (15.03.2005): 2066–76. http://dx.doi.org/10.1128/jb.187.6.2066-2076.2005.
Pełny tekst źródłaRamakrishnan, S., M. B. Sukhaswami, K. M. Patil i 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, nr 3 (grudzień 1997): 605–9. http://dx.doi.org/10.1080/07391102.1997.10508970.
Pełny tekst źródłaXavier, Karina B., i Bonnie L. Bassler. "Regulation of Uptake and Processing of the Quorum-Sensing Autoinducer AI-2 in Escherichia coli". Journal of Bacteriology 187, nr 1 (1.01.2005): 238–48. http://dx.doi.org/10.1128/jb.187.1.238-248.2005.
Pełny tekst źródłaBáez-Ramírez, Estalina, Luis Querales, Carlos Andres Aranaga, Gustavo López, Elba Guerrero, Laurent Kremer, Séverine Carrère-Kremer i in. "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 (grudzień 2021): 100060. http://dx.doi.org/10.1016/j.tcsw.2021.100060.
Pełny tekst źródłaJanczarek, Monika. "The Ros/MucR Zinc-Finger Protein Family in Bacteria: Structure and Functions". International Journal of Molecular Sciences 23, nr 24 (8.12.2022): 15536. http://dx.doi.org/10.3390/ijms232415536.
Pełny tekst źródłaBruni, Gillian O., Yunci Qi, Evan Terrell, Rebecca A. Dupre i Christopher P. Mattison. "Characterization of Levan Fructan Produced by a Gluconobacter japonicus Strain Isolated from a Sugarcane Processing Facility". Microorganisms 12, nr 1 (5.01.2024): 107. http://dx.doi.org/10.3390/microorganisms12010107.
Pełny tekst źródłaYamamoto, Takanobu, Sawako Yada, Yuji Matsuda, Hirofumi Otani, Shunji Yoshikawa, Taro Sasaoka, Yu Hatano i in. "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 (20.05.2019): 1–7. http://dx.doi.org/10.1155/2019/9282876.
Pełny tekst źródłaKim, Hyun-Min, i Zifei Liu. "LSD2 Is an Epigenetic Player in Multiple Types of Cancer and Beyond". Biomolecules 14, nr 5 (3.05.2024): 553. http://dx.doi.org/10.3390/biom14050553.
Pełny tekst źródłaMarayati, Bahjat F., James F. Tucker, David A. De La Cerda, Tien-Chi Hou, Rong Chen, Tomoyasu Sugiyama, James B. Pease i Ke Zhang. "The Catalytic-Dependent and -Independent Roles of Lsd1 and Lsd2 Lysine Demethylases in Heterochromatin Formation in Schizosaccharomyces pombe". Cells 9, nr 4 (13.04.2020): 955. http://dx.doi.org/10.3390/cells9040955.
Pełny tekst źródłaXu, Yijie, Chunlan Zeng, Huiqi Wen, Qianqian Shi, Xu Zhao, Qingbin Meng, Xingzhou Li i 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, nr 5 (12.05.2023): 737. http://dx.doi.org/10.3390/ph16050737.
Pełny tekst źródłaHa, Jung-Hye, Eun-Hee Kim, Hae-Kap Cheong i Kyoung-Seok Ryu. "Crystal structures of LsrR complexed with p-AI-2 reveal distinct mechanisms". Acta Crystallographica Section A Foundations and Advances 70, a1 (5.08.2014): C580. http://dx.doi.org/10.1107/s2053273314094194.
Pełny tekst źródłaDu, Mei Hui, Min Zhao, Lei Lu, Tian Nv Wang, Tai Lun Li, Li Yan Zhao, Jun Bo Pan, Guo Fu Li i Jun Li. "Isolation and Dye Decolorization of a Bacillus subtilis Strain LS02 Exhibiting Laccase Activity". Advanced Materials Research 183-185 (styczeń 2011): 839–43. http://dx.doi.org/10.4028/www.scientific.net/amr.183-185.839.
Pełny tekst źródłaChiou, Sheng-Yuan, Chih-Kai Chao i Ya-Wun Yang. "Topography of Low Skin Resistance Points (LSRP) in Rats". American Journal of Chinese Medicine 26, nr 01 (styczeń 1998): 19–27. http://dx.doi.org/10.1142/s0192415x9800004x.
Pełny tekst źródłaShou, Yiyun, Martin Sellbom i Jin Han. "Evaluating the Construct Validity of the Levenson Self-Report Psychopathy Scale in China". Assessment 24, nr 8 (11.03.2016): 1008–23. http://dx.doi.org/10.1177/1073191116637421.
Pełny tekst źródłaMd Ghazaly, Mariam, Yeo Chin Kiat, Chong Shin Horng, Norhaslinda Hasim, Zulkeflee Abdullah i Nurdiana Nordin. "TUBULAR LINEAR SWITCHED RELUCTANCE ACTUATOR: DESIGN AND CHARACTERIZATION". Jurnal Teknologi 84, nr 5 (26.07.2022): 117–29. http://dx.doi.org/10.11113/jurnalteknologi.v84.17902.
Pełny tekst źródłaIannizzi, Claire, Elie A. Akl, Lara A. Kahale, Elena Dorando, Abina Mosunmola Aminat, James M. Barker, Joanne E. McKenzie, Neal R. Haddaway, Vanessa Piechotta i Nicole Skoetz. "Methods and guidance on conducting, reporting, publishing and appraising living systematic reviews: a scoping review protocol". F1000Research 10 (13.08.2021): 802. http://dx.doi.org/10.12688/f1000research.55108.1.
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