The world’s first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.
wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
- Edit this page
- Edit alert
- Permanent link
- Send to a friend
- Your homepage
- Your articles
- Create article
- Font size
- Color scheme
- NCBI Gene
- NCBI SNP
- iHOP resource
Table of contents
- Disease relevance of sodC
- High impact information on sodC
- Chemical compound and disease context of sodC
- Biological context of sodC
- Anatomical context of sodC
- Associations of sodC with chemical compounds
- Analytical, diagnostic and therapeutic context of sodC
- Contact us
- Language [English]
- Open Access
Mycobacterium tuberculosis CDC1551
M. et al. , Piddington,
D.L. et al. , Jan,
I.S. et al. , Shi,
L. et al. , Sly,
L.M. et al. , et al.
Welcome to WikiGenes!
If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text.
Ideally this entry shall become one comprehensive and continuous article. Bulleted lists, for instance, were only used because it is impossible to automatically integrate independent facts into a continuous text.
Much of the current information on this page has been automatically compiled from Pubmed.
This precompiled information serves as a substrate and matrix to embed your contributions, but it is by no means the final word – Homo sapiens can do much better!
WikiGenes is a non-profit and open access community project – Read more .
Disease relevance of sodC
- The sodC -encoded Mycobacterium tuberculosis superoxide dismutase (SOD) shows high sequence homology to other members of the copper/zinc-containing SOD family  .
- An analysis of the sodC genes present in available databases indicates that the same signal for lipid modification is also present in the sodC gene products from other mycobacteria and Gram-positive bacteria and, uniquely, in two distinct sodC gene products from the Gram-negative bacterium Salmonella typhimurium  .
- Recombinant proteins of a full-length sodC and a truncated form lacking the putative signal peptide were overexpressed in Escherichia coli and affinity purified  .
High impact information on sodC
- In addition, the oxygen radical scavengers superoxide dismutase (SOD), catalase , mannitol , and diazabicyclooctane had no effect on the antimycobacterial activity of macrophages  .
- Concurrently, the pattern of transcription of bacterial genes underwent dramatic changes. mRNA synthesis increased for alpha-crystallin (acr), rv2626c, and rv2623 and decreased for superoxide dismutase C ( sodC ), sodA , and fibronectin-binding protein B ( fbpB )  .
- As was observed for PI 3-K inactivation, the reactive oxygen intermediate scavenger, 4-hydroxy-TEMPO, and degradative enzymes, polyethylene glycol coupled to either superoxide dismutase or catalase , also abrogated D(3)-induced antimycobacterial activity  .
- SecA2 functions in the secretion of superoxide dismutase A and in the virulence of Mycobacterium tuberculosis  .
- Evidence is also provided for an up-regulation of M. tuberculosis sodC in response to phagocytosis by human macrophages , suggesting that Cu,ZnSOD is involved in the mechanisms that facilitate mycobacterial intracellular growth  .
Chemical compound and disease context of sodC
- The hygromycin resistance vector was used to overexpress superoxide dismutase of Mycobacterium tuberculosis in M. vaccae in a form suitable for detailed structural analysis  .
Biological context of sodC
- Furthermore, the sodC mutant has enhanced susceptibility to killing by gamma interferon (IFN-gamma)-activated murine peritoneal macrophages producing oxidative burst products but is unaffected by macrophages not activated by IFN-gamma or by macrophages from respiratory burst-deficient mice  .
Anatomical context of sodC
- The infected group also exhibited significantly decreased activity of superoxide dismutase and levels of glutathione in erythrocytes  .
Associations of sodC with chemical compounds
- These included the superoxide dismutase sod A gene (TBS3), catalase-peroxidase katG gene (TBK1, TBK10), RNA polymerase beta-subunit rpo B gene (TBR5) and diaminopimelate decarboxylase lys A gene (TBL5)  .
- The strains were uniformly resistant to O2- and contained similar amounts of superoxide dismutase  .
Analytical, diagnostic and therapeutic context of sodC
- Crystallization and preliminary X-ray analysis of the superoxide dismutase from Mycobacterium tuberculosis  .
- In cases of discrepancy between the results of the COBAS AMPLICOR MTB test and culture, the medical history of the patient was reviewed, the COBAS AMPLICOR MTB test was repeated, and the gene encoding M. tuberculosis superoxide dismutase was screened using PCR (SOD-PCR)  .
- Unique features of the sodC-encoded superoxide dismutase from Mycobacterium tuberculosis, a fully functional copper-containing enzyme lacking zinc in the active site. Spagnolo, L., Törö, I., D’Orazio, M., O’Neill, P., Pedersen, J.Z., Carugo, O., Rotilio, G., Battistoni, A., Djinovic-Carugo, K. J. Biol. Chem. (2004) [ Pubmed ]
- Lipid modification of the Cu,Zn superoxide dismutase from Mycobacterium tuberculosis. D’orazio, M., Folcarelli, S., Mariani, F., Colizzi, V., Rotilio, G., Battistoni, A. Biochem. J. (2001) [ Pubmed ]
- Identification and subcellular localization of a novel Cu,Zn superoxide dismutase of Mycobacterium tuberculosis. Wu, C.H., Tsai-Wu, J.J., Huang, Y.T., Lin, C.Y., Lioua, G.G., Lee, F.J. FEBS Lett. (1998) [ Pubmed ]
- Killing of virulent Mycobacterium tuberculosis by reactive nitrogen intermediates produced by activated murine macrophages. Chan, J., Xing, Y., Magliozzo, R.S., Bloom, B.R. J. Exp. Med. (1992) [ Pubmed ]
- Expression of Th1-mediated immunity in mouse lungs induces a Mycobacterium tuberculosis transcription pattern characteristic of nonreplicating persistence. Shi, L., Jung, Y.J., Tyagi, S., Gennaro, M.L., North, R.J. Proc. Natl. Acad. Sci. U.S.A. (2003) [ Pubmed ]
- 1alpha,25-Dihydroxyvitamin D3-induced monocyte antimycobacterial activity is regulated by phosphatidylinositol 3-kinase and mediated by the NADPH-dependent phagocyte oxidase. Sly, L.M., Lopez, M., Nauseef, W.M., Reiner, N.E. J. Biol. Chem. (2001) [ Pubmed ]
- SecA2 functions in the secretion of superoxide dismutase A and in the virulence of Mycobacterium tuberculosis. Braunstein, M., Espinosa, B.J., Chan, J., Belisle, J.T., Jacobs, W.R. Mol. Microbiol. (2003) [ Pubmed ]
- Transformation of mycobacterial species using hygromycin resistance as selectable marker. Garbe, T.R., Barathi, J., Barnini, S., Zhang, Y., Abou-Zeid, C., Tang, D., Mukherjee, R., Young, D.B. Microbiology (Reading, Engl.) (1994) [ Pubmed ]
- Cu,Zn superoxide dismutase of Mycobacterium tuberculosis contributes to survival in activated macrophages that are generating an oxidative burst. Piddington, D.L., Fang, F.C., Laessig, T., Cooper, A.M., Orme, I.M., Buchmeier, N.A. Infect. Immun. (2001) [ Pubmed ]
- Protective effect of green tea extract against the erythrocytic oxidative stress injury during mycobacterium tuberculosis infection in mice. Guleria, R.S., Jain, A., Tiwari, V., Misra, M.K. Mol. Cell. Biochem. (2002) [ Pubmed ]
- A novel thiocationic liposomal formulation of antisense oligonucleotides with activity against Mycobacterium tuberculosis. Das, A.R., Dattagupta, N., Sridhar, C.N., Wu, W.K. Scand. J. Infect. Dis. (2003) [ Pubmed ]
- Virulence and resistance to superoxide, low pH and hydrogen peroxide among strains of Mycobacterium tuberculosis. Jackett, P.S., Aber, V.R., Lowrie, D.B. J. Gen. Microbiol. (1978) [ Pubmed ]
- Crystallization and preliminary X-ray analysis of the superoxide dismutase from Mycobacterium tuberculosis. Cooper, J.B., Driessen, H.P., Wood, S.P., Zhang, Y., Young, D. J. Mol. Biol. (1994) [ Pubmed ]
- Evaluation of an automatic polymerase chain reaction assay for identification of Mycobacterium tuberculosis in respiratory specimens. Jan, I.S., Hsueh, P.R., Teng, L.J., Lee, L.N., Yang, P.C., Luh, K.T. J. Formos. Med. Assoc. (1998) [ Pubmed ]