Literatura académica sobre el tema "C-di-AMP synthase"
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Artículos de revistas sobre el tema "C-di-AMP synthase"
Zheng, Yue, Jie Zhou, Stefan M. Cooper, Clement Opoku-Temeng, Amanda Moreira De Brito y Herman O. Sintim. "Structure–activity relationship studies of c-di-AMP synthase inhibitor, bromophenol-thiohydantoin". Tetrahedron 72, n.º 25 (junio de 2016): 3554–58. http://dx.doi.org/10.1016/j.tet.2015.10.073.
Texto completoOpoku-Temeng, Clement y Herman O. Sintim. "Potent inhibition of cyclic diadenylate monophosphate cyclase by the antiparasitic drug, suramin". Chemical Communications 52, n.º 19 (2016): 3754–57. http://dx.doi.org/10.1039/c5cc10446g.
Texto completoZheng, Yue, Jie Zhou, David A. Sayre y Herman O. Sintim. "Identification of bromophenol thiohydantoin as an inhibitor of DisA, a c-di-AMP synthase, from a 1000 compound library, using the coralyne assay". Chem. Commun. 50, n.º 76 (2014): 11234–37. http://dx.doi.org/10.1039/c4cc02916j.
Texto completoVoronkov, Andrey y Dmitry Pozdnyakov. "Endothelotropic Activity of 4-Hydroxy-3,5-Di-Tret-Butylcinnamic Acid in the Conditions of Experimental Cerebral Ischemia". Research Results in Pharmacology 4, n.º 2 (19 de julio de 2018): 1–10. http://dx.doi.org/10.3897/rrpharmacology.4.26519.
Texto completoOpoku-Temeng, Clement, Neetu Dayal, Jacob Miller y Herman O. Sintim. "Hydroxybenzylidene-indolinones, c-di-AMP synthase inhibitors, have antibacterial and anti-biofilm activities and also re-sensitize resistant bacteria to methicillin and vancomycin". RSC Advances 7, n.º 14 (2017): 8288–94. http://dx.doi.org/10.1039/c6ra28443d.
Texto completoSchmidt, Andrew J., Dmitri A. Ryjenkov y Mark Gomelsky. "The Ubiquitous Protein Domain EAL Is a Cyclic Diguanylate-Specific Phosphodiesterase: Enzymatically Active and Inactive EAL Domains". Journal of Bacteriology 187, n.º 14 (julio de 2005): 4774–81. http://dx.doi.org/10.1128/jb.187.14.4774-4781.2005.
Texto completoLi, Haotian, Tingting Li, Wenjin Zou, Minghui Ni, Qiao Hu, Xiuxiu Qiu, Zhiming Yao et al. "IPA-3: An Inhibitor of Diadenylate Cyclase of Streptococcus suis with Potent Antimicrobial Activity". Antibiotics 11, n.º 3 (21 de marzo de 2022): 418. http://dx.doi.org/10.3390/antibiotics11030418.
Texto completoBhat, Aaqib M., Bhopal C. Mohapatra, Insha Mushtaq, Sukanya Chakraborty, Samikshan Dutta, Sameer Mirza, Matthew D. Storck et al. "Abstract 2411: Di-ganglioside GD2 expression and role in promoting tumorigenicity in prostate cancer". Cancer Research 82, n.º 12_Supplement (15 de junio de 2022): 2411. http://dx.doi.org/10.1158/1538-7445.am2022-2411.
Texto completoWu, Yongxia, Chih-Hang Anthony Tang, Corey Mealer, David Bastian, Mohammed Hanief Sofi, Linlu Tian, Steven Douglas Schutt et al. "Sting Negatively Regulates Allogeneic T-Cell Responses By Constraining Antigen-Presenting Cell Function". Blood 136, Supplement 1 (5 de noviembre de 2020): 37–38. http://dx.doi.org/10.1182/blood-2020-139860.
Texto completoRaineri, Alice, Rachele Campagnari, Roberto Dal Toso, Stefano Copetti, Macarena Gomez-Lira y Marta Menegazzi. "3,5-Dicaffeoylquinic Acid Lowers 3T3-L1 Mitotic Clonal Expansion and Adipocyte Differentiation by Enhancing Heme Oxygenase-1 Expression". Molecules 26, n.º 16 (19 de agosto de 2021): 5027. http://dx.doi.org/10.3390/molecules26165027.
Texto completoTesis sobre el tema "C-di-AMP synthase"
Gautam, Sudhanshu. "Homeostasis of cyclic-di-AMP in Mycobacterium smegmatis: Functional and structural contributions of c-di-AMP synthase (MsDisA) and hydrolase (MsPDE)". Thesis, 2022. https://etd.iisc.ac.in/handle/2005/5866.
Texto completoKang, Mai-Wun y 康邁文. "Biochemical and structural studies of DacA and LSm14A﹐a c-di-AMP synthetase and a DNA sensor﹐respectively". Thesis, 2013. http://ndltd.ncl.edu.tw/handle/87227591505057743267.
Texto completo國立中興大學
生物化學研究所
102
【Theme one】 Recently, it was found that cyclic diadenosine monophosphate (c-di-AMP), which is one of the cyclic nucleotide second messengers, can exist in Bacillus subtilis (Bsu), in charge of adjusting spore formation and cell wall metabolism. The c-di-AMP concentration in Bacillus subtilis is chiefly adjusted by diadenylate cyclases (DAC) and phosphodiesterases (PDE). It is synthesized from two molecules of ATP by diadenylyl cyclase (DAC) enzymes which have a DGA-domain or RHR- domain, and is degraded to pApA by PDE, which have a DHH-domain or DHHA-domain. The research aim is to study the structure and the function of DAC protein in Bacillus subtilis str. 168 (BsuDacA). Currently, the crystal structure was determined to a resolution of 2.85A. We further used Differential Scanning Calorimetry (DSC) detect the interaction between the DAC domain BsuDacA(105-268) protein and ATP. From the result, the Tm of BsuDacA(105-268) in its apo-form and ATP-binding form are shown to be 45℃ and 50℃, respectively. The result indicate that ATP bind with BsuDacA to stabilize its conformation. Enzyme Kinetic assay indicates that BsuDacA(105-268) exhibits a Vmax and Km of 2.13 umol min-1 and 56.97 uM, respectively. To sum up, BsuDacA(105-268) can interact with ATP, and synthesize c-di-AMP to potentially assist cell wall formation. 【Theme two】 Pattern recognition receptors (PRRs) are essential for detecting invading Pathogens via the Pathogen-Associated Molecular Patterns (PAMPs). PRRs are located in the membrane or endosome, and can be regarded as the sensor of extracellular nucleic acid. The research aim is to study the structure and the function of the mammalian cytoplasm protein LSm14A. According to provious results, hLSm14A firstly detects virus DNA or RNA. Then P-bodies will interact with RIG-1/VISA/MITA proteins, initiate the releasing of IFNs and then launch the immune responses, such as immunity, and inflammatory responses. Though the 3D structures of N-terminal LSm domain of hLSm14A has been discovered, the structure of C-terminal (including DFDF domain and FFD/TFG/RGG domain) remained unknown. Thus, little is know about how foreign DNA or RNA of virus interact with hLSm14A protein. To obtain more information about the interaction between hLSm14A and virus DNA or RNA, we have constructed the hLSm14A clone by total gene synthesis and expressed the hLSm14A(261-463) protein fragment. Currently, wa have obtained the hLSm14A(261-463) crystal. But due to the poor crystal quality, we were unable to collect good diffraction data to determine its structure. From the gel-filtration data, hLSm14A(261-463) was found to exist as a mixture of tetramer and monomer in solution, which may lead to the imperfect protein crystals. It may be necessary to study hLSm14A protein in different lengh to get a better crystal quality to determine its structure.