Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
3R01GM048157-01S1
Application #
3307634
Study Section
Physical Biochemistry Study Section (PB)
Project Start
1992-08-01
Project End
1997-07-31
Budget Start
1992-08-01
Budget End
1993-07-31
Support Year
1
Fiscal Year
1993
Total Cost
Indirect Cost
Name
Wayne State University
Department
Type
Schools of Medicine
DUNS #
City
Detroit
State
MI
Country
United States
Zip Code
48202
Clark, Greg W; Ackerman, Sharon H; Tillier, Elisabeth R et al. (2014) Multidimensional mutual information methods for the analysis of covariation in multiple sequence alignments. BMC Bioinformatics 15:157
Ackerman, Sharon H; Gatti, Domenico L (2013) Biapenem inactivation by B2 metallo ?-lactamases: energy landscape of the hydrolysis reaction. PLoS One 8:e55136
Ackerman, Sharon H; Tillier, Elisabeth R; Gatti, Domenico L (2012) Accurate simulation and detection of coevolution signals in multiple sequence alignments. PLoS One 7:e47108
Kucharczyk, Roza; Ezkurdia, Nahia; Couplan, Elodie et al. (2010) Consequences of the pathogenic T9176C mutation of human mitochondrial DNA on yeast mitochondrial ATP synthase. Biochim Biophys Acta 1797:1105-12
Meulemans, Ann; Seneca, Sara; Pribyl, Thomas et al. (2010) Defining the pathogenesis of the human Atp12p W94R mutation using a Saccharomyces cerevisiae yeast model. J Biol Chem 285:4099-109
Hinton, Ayana; Gatti, Domenico L; Ackerman, Sharon H (2004) The molecular chaperone, Atp12p, from Homo sapiens. In vitro studies with purified wild type and mutant (E240K) proteins. J Biol Chem 279:9016-22
Hinton, Ayana; Zuiderweg, Erik R P; Ackerman, Sharon H (2003) A purified subfragment of yeast Atp11p retains full molecular chaperone activity. J Biol Chem 278:34110-3
White, M; Ackerman, S H (1995) Bacterial production and characterization of ATP11, a yeast protein required for mitochondrial F1-ATPase assembly. Arch Biochem Biophys 319:299-304