Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM043756-14
Application #
6746929
Study Section
Microbial Physiology and Genetics Subcommittee 2 (MBC)
Program Officer
Wolfe, Paul B
Project Start
1990-12-01
Project End
2006-12-31
Budget Start
2004-01-01
Budget End
2004-12-31
Support Year
14
Fiscal Year
2004
Total Cost
$556,868
Indirect Cost
Name
Public Health Research Institute
Department
Type
DUNS #
City
Newark
State
NJ
Country
United States
Zip Code
07103
Mann, Jessica M; Carabetta, Valerie J; Cristea, Ileana M et al. (2013) Complex formation and processing of the minor transformation pilins of Bacillus subtilis. Mol Microbiol 90:1201-15
Mirouze, Nicolas; Dubnau, David (2013) Chance and Necessity in Bacillus subtilis Development. Microbiol Spectr 1:
Briley Jr, Kenneth; Dorsey-Oresto, Angella; Prepiak, Peter et al. (2011) The secretion ATPase ComGA is required for the binding and transport of transforming DNA. Mol Microbiol 81:818-30
Briley Jr, Kenneth; Prepiak, Peter; Dias, Miguel J et al. (2011) Maf acts downstream of ComGA to arrest cell division in competent cells of B. subtilis. Mol Microbiol 81:23-39
Burton, Briana; Dubnau, David (2010) Membrane-associated DNA transport machines. Cold Spring Harb Perspect Biol 2:a000406
Dubnau, David (2010) Swim or chill: lifestyles of a bacillus. Genes Dev 24:735-7
Johnsen, P J; Dubnau, D; Levin, B R (2009) Episodic selection and the maintenance of competence and natural transformation in Bacillus subtilis. Genetics 181:1521-33
Kramer, Naomi; Hahn, Jeanette; Dubnau, David (2007) Multiple interactions among the competence proteins of Bacillus subtilis. Mol Microbiol 65:454-64
Chen, Ines; Provvedi, Roberta; Dubnau, David (2006) A macromolecular complex formed by a pilin-like protein in competent Bacillus subtilis. J Biol Chem 281:21720-7
Draskovic, Irena; Dubnau, David (2005) Biogenesis of a putative channel protein, ComEC, required for DNA uptake: membrane topology, oligomerization and formation of disulphide bonds. Mol Microbiol 55:881-96

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