Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Method to Extend Research in Time (MERIT) Award (R37)
Project #
1R37GM038922-01
Application #
3484877
Study Section
Microbial Physiology and Genetics Subcommittee 2 (MBC)
Project Start
1987-09-01
Project End
1992-08-31
Budget Start
1987-09-01
Budget End
1988-08-31
Support Year
1
Fiscal Year
1987
Total Cost
Indirect Cost
Name
Harvard University
Department
Type
Schools of Medicine
DUNS #
082359691
City
Boston
State
MA
Country
United States
Zip Code
02115
Gonzalez, Mark D; Akbay, Esra A; Boyd, Dana et al. (2010) Multiple interaction domains in FtsL, a protein component of the widely conserved bacterial FtsLBQ cell division complex. J Bacteriol 192:2757-68
Gonzalez, Mark D; Beckwith, Jon (2009) Divisome under construction: distinct domains of the small membrane protein FtsB are necessary for interaction with multiple cell division proteins. J Bacteriol 191:2815-25
Bardwell, J C; Lee, J O; Jander, G et al. (1993) A pathway for disulfide bond formation in vivo. Proc Natl Acad Sci U S A 90:1038-42
Martin, J L; Waksman, G; Bardwell, J C et al. (1993) Crystallization of DsbA, an Escherichia coli protein required for disulphide bond formation in vivo. J Mol Biol 230:1097-100
Bardwell, J C; McGovern, K; Beckwith, J (1991) Identification of a protein required for disulfide bond formation in vivo. Cell 67:581-9