Sand box 211: Difference between revisions

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4.↑ Karl Syson, Christopher Tomlinson, Brian R. Chapados, Jon R. Sayers, John A. Tainer, Nicholas H. Williams and Jane A. Grasby. Three Metal Ions Participate in the Reaction Catalyzed by T5 Flap Endonuclease. J Biol Chem. 2008 October 17; 283(42): 28741–28746. PMCID: PMC2568906 doi:10.1074/jbc.M801264200 [http://dx.doi.org/10.1074/jbc.M801264200]
4.↑ Karl Syson, Christopher Tomlinson, Brian R. Chapados, Jon R. Sayers, John A. Tainer, Nicholas H. Williams and Jane A. Grasby. Three Metal Ions Participate in the Reaction Catalyzed by T5 Flap Endonuclease. J Biol Chem. 2008 October 17; 283(42): 28741–28746. PMCID: PMC2568906 doi:10.1074/jbc.M801264200 [http://dx.doi.org/10.1074/jbc.M801264200]
    
    
5.↑ Dervan JJ, Feng M, Patel D, Grasby JA, Artymiuk PJ, Ceska TA, Sayers JR. Interactions of mutant and wild-type flap endonucleases with oligonucleotide substrates suggest an alternative model of DNA binding. Proc Natl Acad Sci U S A. 2002 Jun 25;99(13):8542-7 PMID: 12084915 doi:10.1073/pnas.082241699 [http.dx.doi.org/10.1073/pnas.082241699]   
5.↑ Dervan JJ, Feng M, Patel D, Grasby JA, Artymiuk PJ, Ceska TA, Sayers JR. Interactions of mutant and wild-type flap endonucleases with oligonucleotide substrates suggest an alternative model of DNA binding. Proc Natl Acad Sci U S A. 2002 Jun 25;99(13):8542-7 PMID: 12084915 doi:10.1073/pnas.082241699 [http://dx.doi.org/10.1073/pnas.082241699]   


6.↑ Pickering TJ, Garforth S, Sayers JR, Grasby JA. Variation in the steady state kinetic parameters of wild type and mutant T5 5'-3'-exonuclease with pH. Protonation of Lys-83 is critical for DNA binding. J Biol Chem. 1999 Jun 18;274(25):17711-7. PMID: 10364212 doi:10.1074/jbc.274.25.17711 [http://dx.doi.org/10.1074/jbc.274.25.17711]
6.↑ Pickering TJ, Garforth S, Sayers JR, Grasby JA. Variation in the steady state kinetic parameters of wild type and mutant T5 5'-3'-exonuclease with pH. Protonation of Lys-83 is critical for DNA binding. J Biol Chem. 1999 Jun 18;274(25):17711-7. PMID: 10364212 doi:10.1074/jbc.274.25.17711 [http://dx.doi.org/10.1074/jbc.274.25.17711]