M3i

@article{,

title = {[Estimation of DNA methylation level in nonendometrial uterus malignancies]},

author = { A. Popiela and M. S. Gabrys and J. Rabczynski and M. Panszczyk and G. Keith and W. Baranowski},

year  = {2002},

date = {2002-01-01},

journal = {Ginekol Pol},

volume = {73},

number = {11},

pages = {962-5},

abstract = {OBJECTIVES: Rebuilding of genome structure leads to many pathological states including neoplastic malignancies. Rebuilding often occurs as a process caused by disturbances in gene silencing mechanism. DNA methylation pattern is one of the most important mechanisms connected to gene's silencing. Estimation of DNA methylation level in nonendometrial uterine neoplastic tissues compared to normal endometrial samples was the aim of this study. DESIGN: It was to be shown, that changes in methylation rate in promotory regions could lead to carcinogenesis in particular cell. Authors describe an analysis of DNA methylation level in nonendometrial neoplastic uterine tissues compared to DNA methylation level in normal endometrium. MATERIALS AND METHODS: Tissue samples from 9 women with tumor mixtus mesodermalis were collected. 12 samples were normal endometrium-control group. DNA was isolated from tissues and than we performed an estimation of DNA methylation levels. Than we performed a statistical analysis of results. RESULTS: The median DNA methylation level was significantly higher in neoplastic tissues than in normal endometrium. CONCLUSIONS: Authors conclude, that DNA methylation level is higher in neoplastic tissues, but does not correlate with clinical stage of the disease.},

note = {0017-0011 

Journal Article},

keywords = {*DNA, 80, Abstract, Age, Aged, and, Case-Control, English, Expression, Factors, Female, Gene, Human, Mesodermal/genetics/*metabolism, Methylation, Middle, Mixed, Neoplasms/genetics/*metabolism, Neoplastic, over, Regulation, silencing, Studies, tumor, Uterine},

pubstate = {published},

tppubtype = {article}

}

@article{,

title = {Polypurine tract formation by Ty1 RNase H},

author = { M. Wilhelm and O. Uzun and E. H. Mules and A. Gabriel and F. X. Wilhelm},

year  = {2001},

date = {2001-01-01},

journal = {J Biol Chem},

volume = {276},

number = {50},

pages = {47695-701},

abstract = {To better understand the mechanism by which Ty1 RNase H creates the polypurine tract (PPT) primer, we have demonstrated the polymerase-dependent hydrolytic activity of Ty1 reverse transcriptase (RT) during minus-strand synthesis. Using RNase H and polymerase mutants of the recombinant Ty1 RT protein, we show that the two domains of Ty1 RT can act independently of one another. Our results indicate that RNA/DNA substrates containing a short RNA PPT, which serve as primers for plus-strand DNA synthesis, are relatively resistant to RNase H cleavage. RNA substrates with a correct 5' end but with 3' end extending beyond the plus-strand initiation site were cleaved specifically to generate the correct 3' end of the PPT. Using long RNA/DNA duplexes containing the PPT, we show that Ty1 RT is able to make specific internal cleavages that could generate the plus-strand primer with correct 5' and 3' ends. Long RNA/DNA duplexes with mutations in the PPT or in a U-rich region upstream of the PPT, which abolish plus-strand initiation in vivo, were not cleaved specifically at the 5' end of the PPT. Our work demonstrates that the in vitro enzyme can recapitulate key processes that control proper replication in vivo.},

note = {0021-9258 

Journal Article},

keywords = {*Purines, *Retroelements, Base, Binding, Calf, Data, DNA, DNA/metabolism, Factors, Gov't, H, Hydrolysis, Molecular, Mutation, Non-U.S., P.H.S., Polymerase/*chemistry/*metabolism, Primers/pharmacology, Protein, Proteins/metabolism, Recombinant, Ribonuclease, RNA-Directed, RNA/metabolism, Sequence, Sites, Support, Thymus/*chemistry/*genetics/metabolism, time, U.S.},

pubstate = {published},

tppubtype = {article}

}