References of "Habraken, Yvette"
     in
Bookmark and Share    
Full Text
Peer Reviewed
See detailBinding of insertion/deletion DNA mismatches by the heterodimer of yeast mismatch repair protein MSH2 and MSH3
Habraken, Yvette ULg; Sung, Patrick; Prakash, Louise et al

in Current Biology (1996), 6(9), 1185-7

Detailed reference viewed: 4 (1 ULg)
Full Text
Peer Reviewed
See detailRAD26, the yeast homolog of human Cockayne 's syndrome group B, encodes a DNA dependent ATPase
Guzder, Sami; Habraken, Yvette ULg; Sung, Patrick et al

in Journal of Biological Chemistry (1996), 271(31), 18314-7

Detailed reference viewed: 3 (0 ULg)
Full Text
Peer Reviewed
See detailStructure-specific nuclease activity in yeast nucleotide excision repair protein RAD2
Habraken, Yvette ULg; Sung, Patrick; Prakash, Louise et al

in Journal of Biological Chemistry (1995), 270(50), 30194-8

Detailed reference viewed: 10 (0 ULg)
Full Text
Peer Reviewed
See detailReconstitution of yeast nucelotide excision repair with purified RAD proteins, replication protein A and transcription factor TFIIH
Guzder, Sami; Habraken, Yvette ULg; Sung, Patrick et al

in Journal of Biological Chemistry (1995), 270(22), 12973-6

Detailed reference viewed: 2 (0 ULg)
Full Text
Peer Reviewed
See detailA conserved 5' to 3' exonuclease activity in yeast and human nucleotide excision repair protein RAD2 and XPG
Habraken, Yvette ULg; Sung, Patrick; Prakash, Louise et al

in Journal of Biological Chemistry (1994), 269(50), 31342-5

Detailed reference viewed: 3 (0 ULg)
Peer Reviewed
See detailHolliday junction cleavage by yeast Rad1 protein
Habraken, Yvette ULg; Sung, Patrick; Prakash, Louise et al

in Nature (1994), 371

Detailed reference viewed: 7 (0 ULg)
Full Text
Peer Reviewed
See detailHuman xeroderman group G gene encodes a DNA endonuclease
Habraken, Yvette ULg; Sung, Patrick; Prakash, Louise et al

in Nucleic Acids Research (1994), 22(16), 3312-6

Detailed reference viewed: 3 (2 ULg)
Peer Reviewed
See detailYeast excision repair RAD2 encodes a single-stranded DNA endonuclease
Habraken, Yvette ULg; Sung, Partick; Prakash, Louise et al

in Nature (1993), 366

Detailed reference viewed: 4 (0 ULg)
Peer Reviewed
See detailThe formation and enzymatic repair of DNA modifications caused by haloethylnitrosoureas and related compounds
Ludlum, D.; Habraken, Yvette ULg; Carter, C. et al

in Nucleic Acids Symposium Series (1992), 105

Detailed reference viewed: 2 (0 ULg)
Full Text
Peer Reviewed
See detailEnhancement of 1,3-bis(2-chloroethyl)-1-nitrosourea resistance by gy gamma-irradiation or drug pretreatment in rat hepatoma cells
Habraken, Yvette ULg; Laval, Françoise

in Cancer Research (1991), 51(4), 499-503

Detailed reference viewed: 1 (0 ULg)
Peer Reviewed
See detailExcision of imidazole ring-opened N7-hydroxyethylguanine from chloroethylnitrosourea-treated DNA by Escherichia coli formamidopyrimidine-DNA glycolsylase
Laval, J.; Lopes, F.; Madelmont, J. et al

in IARC Scientific Publications (1991), 105

Detailed reference viewed: 2 (0 ULg)
Peer Reviewed
See detailSynthesis of high specificity tritium labelled chloroethylcyclohexylnitrosourea and its application to the study of DNA modification
Siew, E.; Habraken, Yvette ULg; Ludlum, D.

in Journal of the radiolabelled compounds and radiopharmaceuticals (1991), XXIX

Detailed reference viewed: 4 (0 ULg)
Full Text
Peer Reviewed
See detailRelease of 7-alkylguanines from N-(2-chloroethyl)-N'-cyclohexyl-N-nitrosourea-modified DNA by 3 methyladenine DNA glycosylase
Habraken, Yvette ULg; Carter, C.; Kirk, M. et al

in Cancer Research (1991), 51

Detailed reference viewed: 1 (0 ULg)
Peer Reviewed
See detailRelease of N2,3-ethanoguanine from haloethylnitrosourea-treated DNA by Escherichia coli 3-methyladenine DNA glycosylase II
Habraken, Yvette ULg; Carter, C.; Sekiguchi, M. et al

in Carcinogenesis (1991), 12(10), 1971-1973

Detailed reference viewed: 1 (0 ULg)
Peer Reviewed
See detailDevelopment of monoclonal antibodies recognizing 7-(2-hydroxyethyl)guanine and imidazole ring-opened 7-(2-hydroxyethyl)guanine.
Young, T. L.; Habraken, Yvette ULg; Ludlum, D. et al

in Carcinogenesis (1990), 11

Detailed reference viewed: 2 (0 ULg)
Peer Reviewed
See detailFormation of N2,3-ethanoguanine in DNA after in vitro treatment with the therapeutic agent, N-(2-chloroethyl)-N'-cyclohexyl-N-nitrosourea
Habraken, Yvette ULg; Carter, C.; Kirk, M. et al

in Carcinogenesis (1990), 11(2), 223-228

Detailed reference viewed: 2 (0 ULg)
Peer Reviewed
See detailRelease of the chloroethyl ethyl sulfide-modified DNA bases by bacterial 3-methyladenine DNA glycosylase I and II
Habraken, Yvette ULg; Ludlum, David

in Carcinogenesis (1989), 10(3), 489-492

Detailed reference viewed: 1 (0 ULg)
Peer Reviewed
See detailRelease of 7-alkylguanines from haloethylnitrosourea-treated DNA by E. coli 3-methyladenine-DNA glycosylase II.
Carter, C. A.; Habraken, Yvette ULg; Ludlum, David

in Biochemical and Biophysical Research Communications (1988), 155(3), 1261-5

Detailed reference viewed: 3 (2 ULg)
Full Text
Peer Reviewed
See detailFurther Purification and Characterization of the DNA 3'-Phosphatase from Rat-Liver Chromatin Which Is Also a Polynucleotide 5'-Hydroxyl Kinase
Habraken, Yvette ULg; Verly, W. G.

in European Journal of Biochemistry (1988), 171(1-2), 59-66

The DNA 3'-phosphatase activity of rat-liver chromatin has been purified. A DNA 5'-hydroxyl kinase activity comigrates at each step of purification. Both enzymes have the same molecular mass (79 kDa) and ... [more ▼]

The DNA 3'-phosphatase activity of rat-liver chromatin has been purified. A DNA 5'-hydroxyl kinase activity comigrates at each step of purification. Both enzymes have the same molecular mass (79 kDa) and the same isoelectric point (8.6). It thus seems that the two activities are born by the same protein just as with the phage T4 enzyme which is, at the same time, a 5'-hydroxyl kinase and a 3'-phosphatase. An additional argument is that ATP, which does not influence the rate of the 3'-phosphatase reaction but which is a cosubstrate of the 5'-hydroxyl kinase, protects the 3'-phosphatase activity against thermal denaturation and trypsin digestion. The two active sites must, however, be largely independent within a common support: the thermal denaturation and trypsin inactivation rates are very different for the two activities; increasing the ionic strength activates the kinase and inhibits the phosphatase; polyvalent anions inhibit the phosphatase and have little effect on the kinase. The two active sites might belong to different domains of the protein; they could not however be separated by a partial trypsin digestion. The rates of 3'-dephosphorylation and 5'-phosphorylation by the chromatin enzyme are the same in native and denatured DNA. The 3'-phosphatase has no action on 3'-monodeoxynucleotide, but it hydrolyzes the 3'-phosphate in dinucleotides. The Km of the 3'-phosphatase is 0.548 microM. The Km (5'-OH) and Km (ATP) of the 5'-hydroxyl kinase are about 3.9 microM and 0.69 microM respectively. The chromatin enzyme is unable to hydrolyze 3'-phosphoglycolate ends in DNA. [less ▲]

Detailed reference viewed: 7 (0 ULg)