We believe that basic research and the cultivation of scientific knowledge is critical for us to stay connected with our customers and to drive scientific breakthroughs. At NEB, over 30 labs participate in research projects, which are aided by post-doctoral fellows and students in Masters and Ph.D. programs. NEB researchers have authored or co-authored over 1,200 publications (as of 1/19) many of which are in peer-reviewed journals. Further, NEB products have been used successfully in numerous publications by scientists throughout the world.
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Your search returned 2144 results.
|1994||Structure of PvuII endonuclease with cognate DNA.||EMBO J.||Cheng, X., Balendiran, K., Schildkraut, I., and Anderson, J.E.|
|1994||REBASE - restriction enzymes and methylases||Nucl.Acids.Res.||Roberts, R.J.and Macelis, D.|
|1994||Protein splicing: an analysis of the branched intermediate and its resolution by succinimide formation.||EMBO J.||Xu, M.Q., Comb, D.G., Paulus, H., Noren, C.J., Shao, Y., and Perler, F.B.|
|1994||Organization and sequence of the HpaII restriction-modification system and adjacent genes.||Gene||Kulakauskas, S., Barsomian, J.M., Lubys, A., Roberts, R.J., and Wilson, G.G.|
|1994||Ligand-induced conformational states of the cytosine-specific DNA methyltransferase M.HgaI-2.||J.Mol.Biol.||Baldwin, G.S., Kelly, S.M., Price, N.C., Wilson, G.G., Connolly, B.A., Artymiuk, P.J., and Hornby, D.P.|
|1994||Hhal Methyltransferase Flips its Target Base Out of the DNA Helix.||Cell||Klimasauskas, S., Kumar, S., Roberts, R.J., and Cheng, X.|
|1994||Restriction and modification. In: Molecular Biology of Bacteriophage T4||American Society for Microbiology, Washington, D.C.||Carlson, K., Raleigh, E.A. and Hattman, S.|
|1994||An amazing distortion in DNA induced by a methyltransferase (Nobel lecture)||Angew.Chem.Int.Ed.Engl.||Roberts, R.J.|
|1994||An analysis of the humoral immune response of dogs following vaccination with irradiated infective larvae of Dirofilaria immitis.||Parasite Immunol.||Mejia, J.S., and Carlow, C.K.S.|
|1994||Three-dimensional structure of the adenine-specific DNA methyltransferase M.Taq I in complex with the cofactor S-adenosylmethionine.||Proc.Natl.Acad.Sci.USA||Labahn, J., Granzin, J., Schluckebier, G., Robinson, D.P., Jack, W.E., Schildkraut, I., and Saenger, W.|