Publications
Found 1 results
Filters: Author is X.-G. Gong [Clear All Filters]
“Evolutive and structural characterization of Nostoc commune iron-superoxide dismutase that is fit for modification”, vol. 11, pp. 3607-3617, 2012.
,
Behrend L, Henderson G and Zwacka RM (2003). Reactive oxygen species in oncogenic transformation. Biochem. Soc. Trans. 31: 1441-1444.
http://dx.doi.org/10.1042/BST0311441
PMid:14641084
Brioukhanov AL, Nesatyy VJ and Netrusov AI (2006). Purification and characterization of Fe-containing superoxide dismutase from Methanobrevibacter arboriphilus strain AZ. Biochemistry 71: 441-447.
PMid:16615865
Chen X, Kodama T, Iida T and Honda T (2007). Demonstration and characterization of manganese superoxide dismutase of Providencia alcalifaciens. Microbiol. Immunol. 51: 951-961.
PMid:17951985
Choudhary M, Jetley UK, Abash KM, Zutshi S, et al. (2007). Effect of heavy metal stress on proline, malondialdehyde, and superoxide dismutase activity in the cyanobacterium Spirulina platensis-S5. Ecotoxicol. Environ. Saf. 66: 204-209.
http://dx.doi.org/10.1016/j.ecoenv.2006.02.002
PMid:16600377
Cooper JB, McIntyre K, Badasso MO, Wood SP, et al. (1995). X-ray structure analysis of the iron-dependent superoxide dismutase from Mycobacterium tuberculosis at 2.0 Angstroms resolution reveals novel dimer-dimer interactions. J. Mol. Biol. 246: 531-544.
http://dx.doi.org/10.1006/jmbi.1994.0105
PMid:7877174
Delanian S, Martin M, Bravard A, Luccioni C, et al. (2001). Cu/Zn superoxide dismutase modulates phenotypic changes in cultured fibroblasts from human skin with chronic radiotherapy damage. Radiother. Oncol. 58: 325-331.
http://dx.doi.org/10.1016/S0167-8140(00)00332-7
Englert C, Horne M and Pfeifer F (1990). Expression of the major gas vesicle protein gene in the halophilic archaebacterium Haloferax mediterranei is modulated by salt. Mol. Gen. Genet. 222: 225-232.
http://dx.doi.org/10.1007/BF00633822
PMid:1703266
Go M and Miyazawa S (1980). Relationship between mutability, polarity and exteriority of amino acid residues in protein evolution. Int. J. Pept. Protein Res. 15: 211-224.
http://dx.doi.org/10.1111/j.1399-3011.1980.tb02570.x
PMid:7380605
Gottlieb MG, Schwanke CH, Santos AF, Jobim PF, et al. (2005). Association among oxidized LDL levels, MnSOD, apolipoprotein E polymorphisms, and cardiovascular risk factors in a south Brazilian region population. Genet. Mol. Res. 4: 691-703.
PMid:16475114
Horne M, Englert C and Pfeifer F (1988). Two genes encoding gas vacuole proteins in Halobacterium halobium. Mol. Gen. Genet. 213: 459-464.
http://dx.doi.org/10.1007/BF00339616
PMid:3185512
Hu Y, Rosen DG, Zhou Y, Feng L, et al. (2005). Mitochondrial manganese-superoxide dismutase expression in ovarian cancer: role in cell proliferation and response to oxidative stress. J. Biol. Chem. 280: 39485-39492.
http://dx.doi.org/10.1074/jbc.M503296200
PMid:16179351
Jubeh TT, Antler S, Haupt S, Barenholz Y, et al. (2005). Local prevention of oxidative stress in the intestinal epithelium of the rat by adhesive liposomes of superoxide dismutase and tempamine. Mol. Pharm. 2: 2-11.
http://dx.doi.org/10.1021/mp0499095
PMid:15804172
Kim CS, Lee CH, Shin JS, Chung YS, et al. (1997). A simple and rapid method for isolation of high quality genomic DNA from fruit trees and conifers using PVP. Nucleic Acids Res. 25: 1085-1086.
http://dx.doi.org/10.1093/nar/25.5.1085
PMid:9023124 PMCid:146538
Kopp J and Schwede T (2006). The SWISS-MODEL Repository: new features and functionalities. Nucleic Acids Res. 34: D315-D318.
http://dx.doi.org/10.1093/nar/gkj056
PMid:16381875 PMCid:1347419
Li J, Zhou K, Meng X, Wu Q, et al. (2008). Increased ROS generation and SOD activity in heteroplasmic tissues of transmitochondrial mice with A3243G mitochondrial DNA mutation. Genet. Mol. Res. 7: 1054-1062.
http://dx.doi.org/10.4238/vol7-4gmr480
PMid:19048484
Lu M, Gong X, Lu Y, Guo J, et al. (2006). Molecular cloning and functional characterization of a cell-permeable superoxide dismutase targeted to lung adenocarcinoma cells. Inhibition cell proliferation through the Akt/p27kip1 pathway. J. Biol. Chem. 281: 13620-13627.
http://dx.doi.org/10.1074/jbc.M600523200
PMid:16551617
Marklund S and Marklund G (1974). Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur. J. Biochem. 47: 469-474.
http://dx.doi.org/10.1111/j.1432-1033.1974.tb03714.x
PMid:4215654
Oyanagui Y, Sato S and Inoue M (1991). Inhibition of carrageenan-induced paw edema by superoxide dismutase that binds to heparan sulfates on vascular endothelial cells. Biochem. Pharmacol. 42: 991-995.
http://dx.doi.org/10.1016/0006-2952(91)90280-I
Parker MW and Blake CC (1988a). Crystal structure of manganese superoxide dismutase from Bacillus stearothermophilus at 2.4 A resolution. J. Mol. Biol. 199: 649-661.
http://dx.doi.org/10.1016/0022-2836(88)90308-7
Parker MW and Blake CC (1988b). Iron- and manganese-containing superoxide dismutases can be distinguished by analysis of their primary structures. FEBS Lett. 229: 377-382.
http://dx.doi.org/10.1016/0014-5793(88)81160-8
Regelsberger G, Laaha U, Dietmann D, Ruker F, et al. (2004). The iron superoxide dismutase from the filamentous cyanobacterium Nostoc PCC 7120. Localization, overexpression, and biochemical characterization. J. Biol. Chem. 279: 44384-44393.
http://dx.doi.org/10.1074/jbc.M406254200
PMid:15302891
Rengel RG, Filipovic-Grcic J, Cepelak I, Zanic-Grubisic T, et al. (2005). The effect of liposomes with superoxide dismutase on A2182 cells. Eur. J. Pharm. Biopharm. 60: 47-51.
http://dx.doi.org/10.1016/j.ejpb.2004.12.002
PMid:15848055
Schwede T, Kopp J, Guex N and Peitsch MC (2003). SWISS-MODEL: An automated protein homology-modeling server. Nucleic Acids Res. 31: 3381-3385.
http://dx.doi.org/10.1093/nar/gkg520
PMid:12824332 PMCid:168927
Seo SN, Lee JH and Kim YM (2007). Characterization of an iron- and manganese-containing superoxide dismutase from Methylobacillus sp strain SK1 DSM 8269. Mol. Cells 23: 370-378.
PMid:17646712
Shirkey B, Kovarcik DP, Wright DJ, Wilmoth G, et al. (2000). Active Fe-containing superoxide dismutase and abundant sodF mRNA in Nostoc commune (Cyanobacteria) after years of desiccation. J. Bacteriol. 182: 189-197.
http://dx.doi.org/10.1128/JB.182.1.189-197.2000
PMid:10613879 PMCid:94256
Takenaka S, Koshiya J, Okugawa S, Takata A, et al. (2011). Fe-superoxide dismutase and 2-hydroxy-1,4-benzoquinone reductase preclude the auto-oxidation step in 4-aminophenol metabolism by Burkholderia sp strain AK-5. Biodegradation 22: 1-11.
http://dx.doi.org/10.1007/s10532-010-9369-5
PMid:20480210
Tamura K, Dudley J, Nei M and Kumar S (2007). MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24: 1596-1599.
http://dx.doi.org/10.1093/molbev/msm092
PMid:17488738
Van CW, Bowler C, Villarroel R, Tsang EW, et al. (1990). Characterization of iron superoxide dismutase cDNAs from plants obtained by genetic complementation in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 87: 9903-9907.
http://dx.doi.org/10.1073/pnas.87.24.9903
Zhang Y, Zhao W, Zhang HJ, Domann FE, et al. (2002). Overexpression of copper zinc superoxide dismutase suppresses human glioma cell growth. Cancer Res. 62: 1205-1212.
PMid:11861405