Academic literature on the topic 'Mycobacterium smegmatis'

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Journal articles on the topic "Mycobacterium smegmatis"

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Chauhan, Priyanka, Santhe Amber van der Meulen, João Miguel Simões Caetano, Hojjat Ghasemi Goojani, Dennis Botman, Rob van Spanning, Holger Lill, and Dirk Bald. "Response of Mycobacterium smegmatis to the Cytochrome bcc Inhibitor Q203." International Journal of Molecular Sciences 23, no. 18 (September 7, 2022): 10331. http://dx.doi.org/10.3390/ijms231810331.

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For the design of next-generation tuberculosis chemotherapy, insight into bacterial defence against drugs is required. Currently, targeting respiration has attracted strong attention for combatting drug-resistant mycobacteria. Q203 (telacebec), an inhibitor of the cytochrome bcc complex in the mycobacterial respiratory chain, is currently evaluated in phase-2 clinical trials. Q203 has bacteriostatic activity against M. tuberculosis, which can be converted to bactericidal activity by concurrently inhibiting an alternative branch of the mycobacterial respiratory chain, cytochrome bd. In contrast, non-tuberculous mycobacteria, such as Mycobacterium smegmatis, show only very little sensitivity to Q203. In this report, we investigated factors that M. smegmatis employs to adapt to Q203 in the presence or absence of a functional cytochrome bd, especially regarding its terminal oxidases. In the presence of a functional cytochrome bd, M. smegmatis responds to Q203 by increasing the expression of cytochrome bcc as well as of cytochrome bd, whereas a M. smegmatisbd-KO strain adapted to Q203 by increasing the expression of cytochrome bcc. Interestingly, single-cell studies revealed cell-to-cell variability in drug adaptation. We also investigated the role of a putative second cytochrome bd isoform postulated for M. smegmatis. Although this putative isoform showed differential expression in response to Q203 in the M. smegmatisbd-KO strain, it did not display functional features similar to the characterised cytochrome bd variant.
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Converse, Scott E., and Jeffery S. Cox. "A Protein Secretion Pathway Critical for Mycobacterium tuberculosis Virulence Is Conserved and Functional in Mycobacterium smegmatis." Journal of Bacteriology 187, no. 4 (February 15, 2005): 1238–45. http://dx.doi.org/10.1128/jb.187.4.1238-1245.2005.

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ABSTRACT The Snm protein secretion system is a critical determinant of Mycobacterium tuberculosis virulence. However, genes encoding components of this pathway are conserved among all mycobacteria, including the nonpathogenic saprophyte Mycobacterium smegmatis. We show that the Snm system is operational in M. smegmatis and that secretion of its homologous ESAT-6 and CFP-10 substrates is regulated by growth conditions. Importantly, we show that Snm secretion in M. smegmatis requires genes that are homologous to those required for secretion in M. tuberculosis. Using a gene knockout strategy in M. smegmatis, we have also discovered four new gene products that are essential for Snm secretion, including the serine protease mycosin 1. Despite the evolutionary distance between M. smegmatis and M. tuberculosis, the M. smegmatis Snm system can secrete the M. tuberculosis ESAT-6 and CFP-10 proteins, suggesting that substrate recognition is also conserved between the two species. M. smegmatis, therefore, represents a powerful system to study the multicomponent Snm secretory machine and to understand the role of this conserved system in mycobacterial biology.
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Payton, Mark, Roy Auty, Rupika Delgoda, Martin Everett, and Edith Sim. "Cloning and Characterization of Arylamine N -Acetyltransferase Genes from Mycobacterium smegmatis and Mycobacterium tuberculosis: Increased Expression Results in Isoniazid Resistance." Journal of Bacteriology 181, no. 4 (February 15, 1999): 1343–47. http://dx.doi.org/10.1128/jb.181.4.1343-1347.1999.

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ABSTRACT Arylamine N-acetyltransferases (NATs) are found in many eukaryotic organisms, including humans, and have previously been identified in the prokaryote Salmonella typhimurium. NATs from many sources acetylate the antitubercular drug isoniazid and so inactivate it. nat genes were cloned fromMycobacterium smegmatis and Mycobacterium tuberculosis, and expressed in Escherichia coli andM. smegmatis. The induced M. smegmatis NAT catalyzes the acetylation of isoniazid. A monospecific antiserum raised against pure NAT from S. typhimurium recognizes NAT fromM. smegmatis and cross-reacts with recombinant NAT fromM. tuberculosis. Overexpression of mycobacterialnat genes in E. coli results in predominantly insoluble recombinant protein; however, with M. smegmatisas the host using the vector pACE-1, NAT proteins from M. tuberculosis and M. smegmatis are soluble. M. smegmatis transformants induced to express the M. tuberculosis nat gene in culture demonstrated a threefold higher resistance to isoniazid. We propose that NAT in mycobacteria could have a role in acetylating, and hence inactivating, isoniazid.
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Pandey, N., K. Singh, F. Ahmad, and R. Sharma. "Characterization of biofilm formation by Mycobacterium smegmatis during different environmental stress conditions: An in-vitro study." Journal of Environmental Biology 43, no. 6 (November 15, 2022): 771–78. http://dx.doi.org/10.22438/jeb/43/6/mrn-4081.

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Aim: In-vitro characterisation of biofilm produced by Mycobacterium smegmatis (M. smegmatis), a surrogate model for biofilm production by Mycobacteria, and to evaluate the impact of different environmental stress on mycobacterial growth and biofilm formation. Methodology: M. smegmatis biofilms were studied using tissue culture plate and tube adherence methods. Confocal Laser scanning microscopy (CLSM) and scanning electron microscopy (SEM) were used to study the 3D structure and surface morphology, respectively. Additionally, the effect of different environmental stress, such as the absence of essential ions, exposure to harsh environmental conditions, such as acidic environment or oxidative stress, on mycobacterial biofilm formation and mycobacterial growth was assessed. Results: All the exposures, except for carbon supplemented media had a detrimental effect on the number of viable counts and on biofilm formation by mycobacteria (p<0.001). Growth in low pH and oxidative stress was found to be maximum showing reduction by 98% when compared with control. Interpretation: Our findings present various environmental conditions that profoundly affect biofilm formation and thus, may find practical implications in future as effective mycobacterial control strategies having attributes of mycobacterial growth as well as biofilm inhibition. Key words: Biofilm, Environmental stress, Multi-drug resistance, Mycobacterium
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Guo, Ming, Zhonghe Sun, and Ying Zhang. "Mycobacterium smegmatis Has Two Pyrazinamidase Enzymes, PncA and PzaA." Journal of Bacteriology 182, no. 13 (July 1, 2000): 3881–84. http://dx.doi.org/10.1128/jb.182.13.3881-3884.2000.

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ABSTRACT The Mycobacterium smegmatis pncA gene, encoding nicotinamidase/pyrazinamidase, was identified. While it was similar to counterparts from other mycobacteria, the M. smegmatis PncA had little homology to the other M. smegmatispyrazinamidase/nicotinamidase, encoded by the pzaA gene. Transformation of Mycobacterium bovis strain BCG withM. smegmatis pncA or pzaA conferred susceptibility to pyrazinamide.
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Arthur, Patrick K., Vincent Amarh, Precious Cramer, Gloria B. Arkaifie, Ethel J. S. Blessie, Mohammed-Sherrif Fuseini, Isaac Carilo, Rebecca Yeboah, Leonard Asare, and Brian D. Robertson. "Characterization of Two New Multidrug-Resistant Strains of Mycobacterium smegmatis: Tools for Routine In Vitro Screening of Novel Anti-Mycobacterial Agents." Antibiotics 8, no. 1 (January 2, 2019): 4. http://dx.doi.org/10.3390/antibiotics8010004.

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Mycobacterium tuberculosis is a pathogen of global public health concern. This threat is exacerbated by the emergence of multidrug-resistant and extremely-drug-resistant strains of the pathogen. We have obtained two distinct clones of multidrug-resistant Mycobacterium smegmatis after gradual exposure of Mycobacterium smegmatis mc2 155 to increasing concentrations of erythromycin. The resulting resistant strains of Mycobacterium smegmatis exhibited robust viability in the presence of high concentrations of erythromycin and were found to be resistant to a wide range of other antimicrobials. They also displayed a unique growth phenotype in comparison to the parental drug-susceptible Mycobacterium smegmatis mc2 155, and a distinct colony morphology in the presence of cholesterol. We propose that these two multidrug-resistant clones of Mycobacterium smegmatis could be used as model organisms at the inceptive phase of routine in vitro screening of novel antimicrobial agents targeted against multidrug-resistant Mycobacterial tuberculosis.
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Burguière, Adeline, Paul G. Hitchen, Lynn G. Dover, Anne Dell, and Gurdyal S. Besra. "Altered expression profile of mycobacterial surface glycopeptidolipids following treatment with the antifungal azole inhibitors econazole and clotrimazole." Microbiology 151, no. 6 (June 1, 2005): 2087–95. http://dx.doi.org/10.1099/mic.0.27938-0.

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The azole antifungal drugs econazole and clotrimazole are known cytochrome P450 enzyme inhibitors. This study shows that these drugs are potent inhibitors of mycobacterial growth and are more effective against Mycobacterium smegmatis than isoniazid and ethionamide, two established anti-mycobacterial drugs. Several non-tuberculous mycobacteria, including the pathogenic members of the Mycobacterium avium–intracellulare complex (MAC) and the fast-growing saprophytic organism M. smegmatis, produce an array of serovar-specific (ss) and non-serovar-specific (ns) glycopeptidolipids (GPLs). GPL biosynthesis has been investigated for several years but has still not been fully elucidated. The authors demonstrate here that econazole and clotrimazole inhibit GPL biosynthesis in M. smegmatis. In particular, clotrimazole inhibits all four types of nsGPLs found in M. smegmatis, suggesting an early and common target within their biosynthetic pathway. Altogether, the data suggest that an azole-specific target, most likely a cytochrome P450, may be involved in the hydroxylation of the N-acyl chain in GPL biosynthesis. Azole antifungal drugs and potential derivatives could represent an interesting new range of anti-mycobacterial drugs, especially against opportunistic human pathogens including MAC, M. scrofulaceum, M. peregrinum, M. chelonae and M. abscessus.
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Cai, Xiaoying, Lei Liu, Chunhong Qiu, Chongzheng Wen, Yao He, Yanxiang Cui, Siyu Li, et al. "Identification and architecture of a putative secretion tube across mycobacterial outer envelope." Science Advances 7, no. 34 (August 2021): eabg5656. http://dx.doi.org/10.1126/sciadv.abg5656.

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Tuberculosis-causing mycobacteria have thick cell-wall and capsule layers that are formed from complex structures. Protein secretion across these barriers depends on a specialized protein secretion system, but none has been reported. We show that Mycobacterium tuberculosis Rv3705c and its homologous MSMEG_6251 in Mycobacterium smegmatis are tube-forming proteins in the mycobacterial envelope (TiME). Crystallographic and cryo-EM structures of these two proteins show that both proteins form rotationally symmetric rings. Two layers of TiME rings pack together in a tail-to-tail manner into a ring-shaped complex, which, in turn, stacks together to form tubes. M. smegmatis TiME was detected mainly in the cell wall and capsule. Knocking out the TiME gene markedly decreased the amount of secreted protein in the M. smegmatis culture medium, and expression of this gene in knocked-out strain partially restored the level of secreted protein. Our structure and functional data thus suggest that TiME forms a protein transport tube across the mycobacterial outer envelope.
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Grigorov, Artem S., Yulia V. Skvortsova, Oksana S. Bychenko, Leonid V. Aseev, Ludmila S. Koledinskaya, Irina V. Boni, and Tatyana L. Azhikina. "Dynamic Transcriptional Landscape of Mycobacterium smegmatis under Cold Stress." International Journal of Molecular Sciences 24, no. 16 (August 11, 2023): 12706. http://dx.doi.org/10.3390/ijms241612706.

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Bacterial adaptation to cold stress requires wide transcriptional reprogramming. However, the knowledge of molecular mechanisms underlying the cold stress response of mycobacteria is limited. We conducted comparative transcriptomic analysis of Mycobacterium smegmatis subjected to cold shock. The growth of M. smegmatis cultivated at 37oC was arrested just after exposure to cold (acclimation phase) but later (by 24 h) was resumed at a much slower rate (adaptation phase). Transcriptomic analyses revealed distinct gene expression patterns corresponding to the two phases. During the acclimation phase, differential expression was observed for genes associated with cell wall remodeling, starvation response, and osmotic pressure stress, in parallel with global changes in the expression of transcription factors and the downregulation of ribosomal genes, suggesting an energy-saving strategy to support survival. At the adaptation phase, the expression profiles were recovered, indicating restoration of the processes repressed earlier. Comparison of transcriptional responses in M. smegmatis with those in other bacteria revealed unique adaptation strategies developed by mycobacteria. Our findings shed light on the molecular mechanisms underlying M. smegmatis survival under cold stress. Further research should clarify whether the discovered transcriptional mechanisms exist in other mycobacterial species, including pathogenic Mycobacterium tuberculosis, which could be important for transmission control.
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Wolschendorf, Frank, Maysa Mahfoud, and Michael Niederweis. "Porins Are Required for Uptake of Phosphates by Mycobacterium smegmatis." Journal of Bacteriology 189, no. 6 (January 5, 2007): 2435–42. http://dx.doi.org/10.1128/jb.01600-06.

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ABSTRACT Phosphorus is an essential nutrient, but how phosphates cross the mycobacterial cell wall is unknown. Phosphatase activity in whole cells of Mycobacterium smegmatis was significantly lower than that in lysed cells, indicating that access to the substrate was restricted. The loss of the outer membrane (OM) porin MspA also reduced the phosphatase activity in whole cells compared to that in lysed cells. A similar result was obtained for M. smegmatis that overexpressed endogenous alkaline phosphatase, indicating that PhoA is not a surface protein, contrary to a previous report. The uptake of phosphate by a mutant lacking the porins MspA and MspC was twofold lower than that by wild-type M. smegmatis. Strikingly, the loss of these porins resulted in a severe growth defect of M. smegmatis on low-phosphate plates. We concluded that the OM of M. smegmatis represents a permeability barrier for phosphates and that Msp porins are the only OM channels for the diffusion of phosphate in M. smegmatis. However, phosphate diffusion through Msp pores is rather inefficient as shown by the 10-fold lower permeability of M. smegmatis for phosphate compared to that for glucose. This is likely due to the negative charges in the constriction zone of Msp porins. The phosphatase activity in whole cells of Mycobacterium bovis BCG was significantly less than that in lysed cells, indicating a similar uptake pathway for phosphates in slow-growing mycobacteria. However, porins that could mediate the diffusion of phosphates across the OM of M. bovis BCG and Mycobacterium tuberculosis are unknown.
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Dissertations / Theses on the topic "Mycobacterium smegmatis"

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Vorwieger, Stefan [Verfasser], and Dirk [Akademischer Betreuer] Wagner. "Efflux-Inhibition bei Mycobacterium smegmatis und Mycobacterium avium." Freiburg : Universität, 2012. http://d-nb.info/1123467102/34.

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Mahenthiralingam, Eshwar. "The amidase promotor of Mycobacterium smegmatis." Thesis, Open University, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.278899.

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Bruell, Christian M. "Mechanism of protein synthesis in Mycobacterium smegmatis /." Zürich : ETH, 2008. http://e-collection.ethbib.ethz.ch/show?type=diss&nr=17733.

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Trower, Carolyn Joy 1975. "A preliminary investigation of a sialidase activity associated with M. smegmatis." Monash University, Dept. of Medicinal Chemistry, 2003. http://arrow.monash.edu.au/hdl/1959.1/7646.

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Smeulders, Maria Jeanne. "The stationary phase survival response of Mycobacterium smegmatis." Thesis, Imperial College London, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.287866.

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Sikder, Mahmudul Hasan. "Characterisation of the Mycobacterium smegmatis transcriptional regulator MSMEG_5424." Thesis, Royal Veterinary College (University of London), 2013. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.618297.

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Rao, Tara. "Analysis of the multiple chaperonins of Mycobacterium smegmatis." Thesis, University of Birmingham, 2010. http://etheses.bham.ac.uk//id/eprint/1006/.

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Although most bacteria contain a single gene for the essential oligomeric chaperonin Cpn60, many contain two or more cpn60 genes. The non-pathogenic Mycobacterium smegmatis has three cpn60 homologues, while the pathogenic Mycobacterium tuberculosis has two. This study is a functional characterisation of the chaperonins of M. smegmatis. Expression of cpn60.1, cpn60.2 and cpn10, but not cpn60.3, was found to be induced under stress conditions, particularly heat shock. Studies of the cpn10-cpn60.1 operon concluded that transcription is from a single promoter, with a subsequent post-transcriptional cleavage of the mRNA between the two genes. Cpn60.1 in M. smegmatis is required for biofilm maturation. Using this assay, we intended to test various Cpn60 homologues for their ability to function in M. smegmatis. Preliminary results obtained revealed that only the M. tuberculosis Cpn60.1 can fully complement for loss of the M. smegmatis Cpn60.1. While E. coli GroEL and Cpn60.3 appear to only partially complement, Cpn60.2 shows no complementing ability. Cpn60.2 expresses well and complements for loss of the E. coli Cpn60 homologue GroEL even at higher temperatures (42°C). Using native gels and analytical ultracentrifugation, purified Cpn60.2 did not oligomerise under normal conditions, however in the presence of nucleotide and high concentrations of salt, the formation of large oligomers was observed. Neither Cpn60.1 nor Cpn60.3 complemented for loss of GroEL.
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Ogwang, Sam. "Intrinsic Antifolate Resistance in Mycobacterium smegmatis." Case Western Reserve University School of Graduate Studies / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=case1270147885.

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Berger, Sven. "Expression der Poren bildenden Hämolysine Listeriolysin und TlyA in Mycobacterium smegmatis." [S.l. : s.n.], 2002. http://deposit.ddb.de/cgi-bin/dokserv?idn=964920824.

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Faller, Michael. "Kristallstruktur eines mycobacteriellen Porins." [S.l. : s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=972775730.

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Book chapters on the topic "Mycobacterium smegmatis"

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Majumdar, Gaurav, Rendani Mbau, Vinayak Singh, Digby F. Warner, Marte Singsås Dragset, and Raju Mukherjee. "Genome-Wide Transposon Mutagenesis in Mycobacterium tuberculosis and Mycobacterium smegmatis." In Methods in Molecular Biology, 321–35. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-6472-7_21.

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Bhatt, Apoorva, and William R. Jacobs. "Gene Essentiality Testing in Mycobacterium smegmatis Using Specialized Transduction." In Methods in Molecular Biology, 325–36. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-207-6_22.

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Clark, Ryan R., Todd A. Gray, and Keith M. Derbyshire. "Quantifying and Characterizing Distributive Conjugal Transfer in Mycobacterium smegmatis." In Horizontal Gene Transfer, 123–34. New York, NY: Springer US, 2019. http://dx.doi.org/10.1007/978-1-4939-9877-7_9.

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Bloch, Konrad. "Control Mechanisms for Fatty Acid Synthesis in Mycobacterium Smegmatis." In Advances in Enzymology - and Related Areas of Molecular Biology, 1–84. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470122907.ch1.

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García-Fernández, Julia, Igor Martínez, Lorena Fernández-Cabezón, Carmen Felpeto-Santero, José-Luis García, and Beatriz Galán. "Bioconversion of Phytosterols into Androstadienedione by Mycobacterium smegmatis CECT 8331." In Microbial Steroids, 211–25. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7183-1_15.

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Chelliah, Ramachandran, and Deog-Hwan Oh. "Screening of Actinobacterial Cultures for Antimycobacterial Activity Using Mycobacterium smegmatis." In Methods in Actinobacteriology, 391–93. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-1728-1_47.

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Conference papers on the topic "Mycobacterium smegmatis"

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SYAHPUTRA, GITA. "Anti-mycobacterial activity of methanol plants extract to against Mycobacterium bovis and Mycobacterium smegmatis." In Seminar Nasional Masyarakat Biodiversitas Indonesia. Masyarakat Biodiversitas Indonesia, 2016. http://dx.doi.org/10.13057/psnmbi/m020211.

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Morita, Yasu S., Svetozar Kovacevic, Helen Billman-Jacobe, and Malcolm J. McConville. "RECONSTITUTION OF PHOSPHATIDYLINOSITOL MANNOSIDE BIOSYNTHESIS IN MYCOBACTERIUM SMEGMATIS." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.453.

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Bruce-Micah, R., U. Gamm, D. Hüttenberger, J. Cullum, and H. J. Foth. "Photodynamic inactivation of the models Mycobacterium phlei and Mycobacterium smegmatis in vitro." In European Conference on Biomedical Optics. Washington, D.C.: OSA, 2009. http://dx.doi.org/10.1364/ecbo.2009.7373_1l.

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Bruce-Micah, R., U. Gamm, D. Hüttenberger, J. Cullum, and H. J. Foth. "Photodynamic inactivation of the models Mycobacterium phlei and Mycobacterium smegmatis in vitro." In European Conferences on Biomedical Optics, edited by Ronald Sroka and Lothar D. Lilge. SPIE, 2009. http://dx.doi.org/10.1117/12.831872.

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Patterson, John H., Dharshini Jeevarajah, Helen Billman-Jacobe, and Malcolm J. McConville. "DELETION OF PHOSPHOMANNOSE ISOMERASE IN MYCOBACTERIUM SMEGMATIS REVEALS ESSENTIAL MANNOSE CONTAINING GLYCOCONJUGATES." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.399.

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Карпов, М. В., Н. И. Стрижов, А. А. Шутов, and М. В. Донова. "Биоконверсия холестерина в прогестерон рекомбинантными штаммами Mycobacterium smegmatis mc2155 с делециями в генах окисления стероидного ядра." In VI Пущинская школа-конференция «Биохимия, физиология и биосферная роль микроорганизмов». ИД «Вода: химия и экология», 2019. http://dx.doi.org/10.18334/ibpm2019.200-201.

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Карпов, М. В., Н. И. Стрижов, А. А. Шутов, and М. В. Донова. "Биоконверсия холестерина в прогестерон рекомбинантными штаммами Mycobacterium smegmatis mc2155 с делециями в генах окисления стероидного ядра." In VI Пущинская школа-конференция «Биохимия, физиология и биосферная роль микроорганизмов». ИД «Вода: химия и экология», 2019. http://dx.doi.org/10.18334/ibpm2019_200-201.

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Pereira, Victor, Marcos Schwarz, and Leila Lima. "Use of a theophylline responsive riboswitch for translational control applied to the expression of secreted heterologous proteins in Mycobacterium smegmatis." In International Symposium on Immunobiological. Instituto de Tecnologia em Imunobiológicos, 2021. http://dx.doi.org/10.35259/isi.2021_46598.

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