Literatura académica sobre el tema "Mtb Rv1860"
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Artículos de revistas sobre el tema "Mtb Rv1860"
Elchennawi, Ingie, Philippe Carpentier, Christelle Caux, Marine Ponge y Sandrine Ollagnier de Choudens. "Structural and Biochemical Characterization of Mycobacterium tuberculosis Zinc SufU-SufS Complex". Biomolecules 13, n.º 5 (24 de abril de 2023): 732. http://dx.doi.org/10.3390/biom13050732.
Texto completoLiu, 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, n.º 6624 (9 de diciembre de 2022): 1111–18. http://dx.doi.org/10.1126/science.abq2787.
Texto completoChoi, Seunga, Han-Gyu Choi, Yong Woo Back, Hye-Soo Park, Kang-In Lee, Sintayehu Kebede Gurmessa, Thuy An Pham y Hwa-Jung Kim. "A Dendritic Cell-Activating Rv1876 Protein Elicits Mycobacterium Bovis BCG-Prime Effect via Th1-Immune Response". Biomolecules 11, n.º 9 (3 de septiembre de 2021): 1306. http://dx.doi.org/10.3390/biom11091306.
Texto completoTripathi, 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, n.º 4 (15 de abril de 2022): e1010475. http://dx.doi.org/10.1371/journal.ppat.1010475.
Texto completoBashiri, 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, n.º 11 (31 de octubre de 2015): 2297–308. http://dx.doi.org/10.1107/s1399004715017216.
Texto completoWang, Jieru, Xiaojie Zhu, Yongchong Peng, Tingting Zhu, Han Liu, Yifan Zhu, Xuekai Xiong et al. "Mycobacterium tuberculosis YrbE3A Promotes Host Innate Immune Response by Targeting NF-κB/JNK Signaling". Microorganisms 8, n.º 4 (17 de abril de 2020): 584. http://dx.doi.org/10.3390/microorganisms8040584.
Texto completoHandzel, Zeev T., William W. Busse, Julie B. Sedgwick, Rose Vrtis, Wai Ming Lee, E. A. B. Kelly y James E. Gern. "Eosinophils Bind Rhinovirus and Activate Virus-Specific T Cells". Journal of Immunology 160, n.º 3 (1 de febrero de 1998): 1279–84. http://dx.doi.org/10.4049/jimmunol.160.3.1279.
Texto completoKashyap, Rajpal S., Karen M. Dobos, John T. Belisle, Hemant J. Purohit, Nitin H. Chandak, Girdhar M. Taori y Hatim F. Daginawala. "Demonstration of Components of Antigen 85 Complex in Cerebrospinal Fluid of Tuberculous Meningitis Patients". Clinical Diagnostic Laboratory Immunology 12, n.º 6 (junio de 2005): 752–58. http://dx.doi.org/10.1128/cdli.12.6.752-758.2005.
Texto completoGern, J. E., R. Vrtis, E. A. Kelly, E. C. Dick y W. W. Busse. "Rhinovirus produces nonspecific activation of lymphocytes through a monocyte-dependent mechanism." Journal of Immunology 157, n.º 4 (15 de agosto de 1996): 1605–12. http://dx.doi.org/10.4049/jimmunol.157.4.1605.
Texto completoGern, J. E., E. C. Dick, W. M. Lee, S. Murray, K. Meyer, Z. T. Handzel y W. W. Busse. "Rhinovirus enters but does not replicate inside monocytes and airway macrophages." Journal of Immunology 156, n.º 2 (15 de enero de 1996): 621–27. http://dx.doi.org/10.4049/jimmunol.156.2.621.
Texto completoTesis sobre el tema "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.
Texto completoThe 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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