Добірка наукової літератури з теми "Mtb Rv1860"
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Статті в журналах з теми "Mtb Rv1860"
Elchennawi, Ingie, Philippe Carpentier, Christelle Caux, Marine Ponge, and Sandrine Ollagnier de Choudens. "Structural and Biochemical Characterization of Mycobacterium tuberculosis Zinc SufU-SufS Complex." Biomolecules 13, no. 5 (April 24, 2023): 732. http://dx.doi.org/10.3390/biom13050732.
Повний текст джерелаLiu, Qingyun, Junhao Zhu, Charles L. Dulberger, Sydney Stanley, Sean Wilson, Eun Seon Chung, Xin Wang, et al. "Tuberculosis treatment failure associated with evolution of antibiotic resilience." Science 378, no. 6624 (December 9, 2022): 1111–18. http://dx.doi.org/10.1126/science.abq2787.
Повний текст джерелаChoi, Seunga, Han-Gyu Choi, Yong Woo Back, Hye-Soo Park, Kang-In Lee, Sintayehu Kebede Gurmessa, Thuy An Pham, and Hwa-Jung Kim. "A Dendritic Cell-Activating Rv1876 Protein Elicits Mycobacterium Bovis BCG-Prime Effect via Th1-Immune Response." Biomolecules 11, no. 9 (September 3, 2021): 1306. http://dx.doi.org/10.3390/biom11091306.
Повний текст джерелаTripathi, Ashutosh, Kushi Anand, Mayashree Das, Ruchika Annie O’Niel, Sabarinath P. S, Chandrani Thakur, Raghunatha Reddy R. L., et al. "Mycobacterium tuberculosis requires SufT for Fe-S cluster maturation, metabolism, and survival in vivo." PLOS Pathogens 18, no. 4 (April 15, 2022): e1010475. http://dx.doi.org/10.1371/journal.ppat.1010475.
Повний текст джерелаBashiri, Ghader, Jodie M. Johnston, Genevieve L. Evans, Esther M. M. Bulloch, David C. Goldstone, Ehab N. M. Jirgis, Silke Kleinboelting, et al. "Structure and inhibition of subunit I of the anthranilate synthase complex of Mycobacterium tuberculosis and expression of the active complex." Acta Crystallographica Section D Biological Crystallography 71, no. 11 (October 31, 2015): 2297–308. http://dx.doi.org/10.1107/s1399004715017216.
Повний текст джерелаWang, Jieru, Xiaojie Zhu, Yongchong Peng, Tingting Zhu, Han Liu, Yifan Zhu, Xuekai Xiong та ін. "Mycobacterium tuberculosis YrbE3A Promotes Host Innate Immune Response by Targeting NF-κB/JNK Signaling". Microorganisms 8, № 4 (17 квітня 2020): 584. http://dx.doi.org/10.3390/microorganisms8040584.
Повний текст джерелаHandzel, Zeev T., William W. Busse, Julie B. Sedgwick, Rose Vrtis, Wai Ming Lee, E. A. B. Kelly, and James E. Gern. "Eosinophils Bind Rhinovirus and Activate Virus-Specific T Cells." Journal of Immunology 160, no. 3 (February 1, 1998): 1279–84. http://dx.doi.org/10.4049/jimmunol.160.3.1279.
Повний текст джерелаKashyap, Rajpal S., Karen M. Dobos, John T. Belisle, Hemant J. Purohit, Nitin H. Chandak, Girdhar M. Taori, and Hatim F. Daginawala. "Demonstration of Components of Antigen 85 Complex in Cerebrospinal Fluid of Tuberculous Meningitis Patients." Clinical Diagnostic Laboratory Immunology 12, no. 6 (June 2005): 752–58. http://dx.doi.org/10.1128/cdli.12.6.752-758.2005.
Повний текст джерелаGern, J. E., R. Vrtis, E. A. Kelly, E. C. Dick, and W. W. Busse. "Rhinovirus produces nonspecific activation of lymphocytes through a monocyte-dependent mechanism." Journal of Immunology 157, no. 4 (August 15, 1996): 1605–12. http://dx.doi.org/10.4049/jimmunol.157.4.1605.
Повний текст джерелаGern, J. E., E. C. Dick, W. M. Lee, S. Murray, K. Meyer, Z. T. Handzel, and W. W. Busse. "Rhinovirus enters but does not replicate inside monocytes and airway macrophages." Journal of Immunology 156, no. 2 (January 15, 1996): 621–27. http://dx.doi.org/10.4049/jimmunol.156.2.621.
Повний текст джерелаДисертації з теми "Mtb Rv1860"
Salman, Mayla. "Détection et signalisation du monoxyde de carbone chez des bactéries aérobies - Hémo-senseur RcoM-2 et réponses mycobactériennes au CO." Thesis, Université Paris-Saclay (ComUE), 2019. http://www.theses.fr/2019SACLX076.
Повний текст джерелаThe toxic gas CO can act in low quantities as signaling molecule; detected by heme-based sensor proteins.The CO-dependent transcription factor RcoM-2 has a very high affinity for CO, while being insensitive to O₂. RcoM-2 binds to DNA only when CO is bound to heme. We characterized the heme-CO interaction in full-length RcoM-2 and compared it with the isolated heme domain RcoMH-2. RcoM-2 can bind CO with lower effective affinity than RcoMH-2. CO dissociates with a 20-fold higher rate than in RcoMH-2, where CO binding is almost irreversible. A small fraction of CO can escape from the protein, thus allowing RcoM-2 to act as CO sensor. The presence of the DNA binding domain influences the binding properties of CO to heme. Identification of the precise molecular origin of the dynamic properties must await the 3D structure RcoM-2.CO detection is crucial for Mtb, the infectious agent of tuberculosis that must overcome the host's defense mechanisms, including CO. The gene cor (rv1829) has been implicated in these processes. We have shown that Cor is a highly stable dimer that is able to stoichiometrically bind a heme cofactor, suggesting a potential function as direct CO sensor. A histidine residue was identified as potential heme ligand. The internal CO dynamics is very similar to other bacterial CO sensors. Cor exhibits DNA binding activity that depends on the presence of heme and CO, which is abolished in the H70A mutant. Our studies also showed that the transcriptional regulator Rv0081, induced in response to gaz changes, can bind to the predicted regulatory region of cor. The creation of a Δcor strain in the non- pathogenic model M. smegmatis continues and will be a first step towards transcriptomic analyzes
Shobha, E. "The role of Rv1860 from M. tuberculosis in modulating the host immune response." Thesis, 2020. https://etd.iisc.ac.in/handle/2005/5083.
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