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Journal of General Microbiology|March 1, 1991
Identification of four unique clones encoding 10 kDa proteins from Bacillus that cause phenotypic complementation of a phoA mutant strain of Escherichia coliJ W Lee, C W Edwards, F M Hulett
FEMS Microbiology Letters|March 5, 1998
Bacillus licheniformis MC14 alkaline phosphatase I gene with an extended COOH-terminusJ W Kim, T Peterson, G Bee, et al.
Journal of General Microbiology|August 1, 1986
Purification and characterization of the secreted alkaline phosphatase of Bacillus licheniformis MC14: identification of a possible precursorF M Hulett, K Stuckmann, D B Spencer, et al.
Gene|September 15, 1994
A pho regulon promoter induced under sporulation conditionsS M Birkey, G Sun, P J Piggot, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 1, 1985
Two alkaline phosphatase genes positioned in tandem in Bacillus licheniformis MC14 require different RNA polymerase holoenzymes for transcriptionF M Hulett, P Z Wang, M Sussman, et al.
Journal of Bacteriology|July 1, 1996
Two-component regulatory proteins ResD-ResE are required for transcriptional activation of fnr upon oxygen limitation in Bacillus subtilisM M Nakano, P Zuber, P Glaser, et al.
Gene|November 30, 1990
The Bacillus subtilis phoAIV gene: effects of in vitro inactivation on total alkaline phosphatase productionN V Kapp, C W Edwards, R S Chesnut, et al.
Journal of Bacteriology|February 1, 1977
Biochemical localization of the alkaline phosphatase of Bacillus licheniformis as a function of culture ageJ A Glynn, S D Schaffel, J M McNicholas, et al.
Molecular Microbiology|September 6, 2000
Interaction of ResD with regulatory regions of anaerobically induced genes in Bacillus subtilisM M Nakano, Y Zhu, M Lacelle, et al.
Journal of Bacteriology|May 1, 1982
Membrane-associated alkaline phosphatase from Bacillus licheniformis that requires detergent for solubilization: lactoperoxidase 125I localization and molecular weight determinationD B Spencer, J G Hansa, K V Stuckmann, et al.
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