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    Your search returned 1486 results.

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    YearTitleJournalAuthorsApplication(s)
    1996Thermostable DNA Polymerases.Enzymes and Proteins from Hyperthermophilic Microorganisms, Advs.Protein ChemistryPerler, F.B., Kumar, S., and Kong, H.
    1997A New Enhancer of Position-Effect Variegation in Drosophila melanogaster Encodes a Putative RNA Helicase That Binds Chromosomes and Is Regulated by the Cell Cycle.Genetics Society of AmericaEberl, D.F., Lorenz, L.J., Melnick, M.B., Sood, V., Lasko, P., and Perrimon, N.
    1997Baculovirus-Mediated Expression and Characterization of the Full-Length Murine DNA Methyltransferase.Nuc.Acids Res.Pradhan, S., Talbot, D., Sha, M., Benner, J., Hornstra, L., Li, E., Jaenisch, R.and Roberts, R.J.
    1997Catalytic and DNA Binding Properties of PvuII Restriction Endonuclease Mutants.J.Biol.Chem.Nastri, H.G., Evans, P.D., Walker, I.H., and Riggs, P.D.
    1997Cloning and characterization of the BglII restriction-modification system reveals a possible evolutionary footprint.GeneAnton, B.P., Heiter, D.F., Benner, J.S., Hess, E.J., Greenough, L., Moran, L.S., Slatko, B.E., and Brooks, J.E.
    1997Cloning and expression of AatII restriction-modification system in Escherichia coli.GeneNwankwo, D.O., Maunus, R.E., and Xu, S.Y.
    1997Cloning of the BssHII restriction-modification system in Escherichia coli: BssHII methyltransferase contains circularly permuted cytosine-5 methyltransferase motifs.Nucl.Acids Res.Xu, S.Y., Xiao, J.P., Posfai, J., Maunus, R., and Benner, J
    1997Compilation and analysis of intein sequences.Nuc.Acids Res.Perler, F.B., Olsen, G.J., and Adam, E.
    1997Construction and characterization of a radio-iodinatable mutant of recombinant human CD4.J.Immunol.Methods Ferrer, M., Godbout, K., Sullivan, B., Austen, D., Sanderson, C., Kelley, K., Osburne, M., Harrison, S.and van Schravendijk, M.R.
    1997Crystallization and Preliminary X-ray Analysis of Restriction Endonuclease FokI Bound to DNA.FEBS Lett.Hirsch, J.A., Wah, D.A., Dorner, L.F., Schildkraut, I., Aggarwal, A.K.