mutM Antibody

1. expression of the bacterial DNA repair protein FPG stably protects human lung cells from the mutagenic effects of CS by improving cells' capacity to repair damaged DNA. PMID: 24498234
2. Structural and biochemical analysis of DNA helix invasion by the bacterial 8-oxoguanine DNA glycosylase MutM PMID: 23404556
3. Fpg protein seemed to be very important in the repair of ultraviolet-C induced DNA lesions. PMID: 22732937
4. structures reveal that MutM imposes the same extrusion-prone backbone conformation on the oxoG lesion irrespective of its 5'-neighbor while leaving the rest of the DNA relatively free to adjust to the particular demands of individual sequences PMID: 22465958
5. demonstrates that it is feasible to increase resistance of human TM cell to endogenous oxidative damage by FPG gene transfection PMID: 21561236
6. Over-expressed, purified and characterized two stable isotope-labeled DNA glycosylases, i.e., (15)N-labeled Escherichia coli formamidopyrimidine DNA glycosylase (Fpg) and (15)N-labeled human 8-oxoguanine-DNA glycosylase (hOGG1). PMID: 21356311
7. examination of the structural and dynamic changes that occur in solution when Fpg binds DNA PMID: 15661656
8. A base excision repair enzyme involved in the 8-oxoguanine (oxoG) repair pathway. PMID: 15979229
9. when the enzyme encounters its true substrate, 8-oxoG.C, the complex enters the productive catalytic reaction after approximately 50 ms, partitioning the substrate away from the competing dissociation process PMID: 17209553
10. The substrate specificity of two similar enzymes, MutM of E. coli and OGG1 of H. sapiens, is reported. PMID: 17536801
11. The high affinity and efficient activity of EcFpg toward the hydantoin lesions suggest that EcFpg mediates repair of the lesions in vivo. PMID: 17655276
12. Data show a lack of interaction of mutM with dnaX36 since the double dnaX36 mutM strains did not show any major changes in the frequency of G.CT.A transversions compared to the single dnaX36 strain. PMID: 18156258
13. analysis of the the driving forces that dictate Fpg enzyme efficiency and specificity, which helps to elucidate the energy landscape for lesion recognition and repair PMID: 18172202
14. Data show that processive cleavage by Fpg does not correlate with their substrate specificity and under nearly physiological salt conditions may be replaced with the distributive mode of action. PMID: 18672903

Show More

Hide All

KEGG: ecj:JW3610

STRING: 316385.ECDH10B_3817