Publications

Publications

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YearTitleJournalAuthorsApplication(s)
2007Acetamide selection of Kluyveromyces lactis cells transformed with an integrative vector leads to high frequency formation of multicopy strainsAppl. Environ. Microbiol.Read, J.D., Colussi, P.A., Ganatra, M.B. and Taron, C.H.
2007Acetamide Selection of Kluyveromyces lactis Cells Transformed with an Integrative Vector Leads to High Frequency Formation of Multicopy Strains.Appl.Environ.Microbiol.Read, J.D., Colussi, P.A., Ganatra, M.B.and Taron, C.H.
1984Acetylcholinesterase secreted by intestinal nematodes: a reinterpretation of its putative role of "biochemical holdfast."Trans.Royal Soc Trop.Med.and Hyg.Philipp, M.
1990AciI, a unique restriction endonuclease from Arthrobacter citreus which recognizes 5' CCGC3'.Nucl.Acids Res.Polisson, C., and Morgan, R.D.
2015Activation and enhancement of Fredericamycin A production in deepsea-derived Streptomyces somaliensis SCSIO ZH66 by using ribosome engineering and response surface methodology.Microb Cell FactYonghe Zhang, Huiming Huang, Shanshan Xu, Bo Wang, Jianhua Ju, Huarong Tan, Wenli LiHigh-Fidelity PCR
2010Activation of DNA Cleavage by Oligomerization of DNA Bound SgrAI.BiochemistryPark, C.K., Stiteler, A.P., Shah, S., Ghare, M.I., Bitinaite, J.and Horton, N.C.
1996Activation of glycosylasparaginase.Formation of Active N-Terminal Threonine by Intramolecular Autoproteolysis.J.Biol.Chem.Guan, C., Cui, T., Rao, V., Liao, W., Benner, J., Lin, C.L., and Comb, D.
1995Active site and oligosaccharide recognition residues of peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F.J.Biol.Chem.Kuhn, P., Guan, C., Cui, T., Tarentino, A.L., Plummer, T.H.J., and Van Roey, P.
1998Active site mutants of a cyclosporin A-insensitive cyclophilin from Brugia malayi: effect on catalysis and drug binding.Mol.Biochem.Parasitol.Ma, D.and Carlow, C.K.S.
2011Activity, specificity and structure of I-Bth03051: a representative of a new homing endonuclease familyTaylor, G.K., Heiter, D.F., Pietrokovski, S. and Stoddard, B.L.