Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
First Independent Research Support & Transition (FIRST) Awards (R29)
Project #
5R29DK044322-04
Application #
2143714
Study Section
Physical Biochemistry Study Section (PB)
Project Start
1993-02-01
Project End
1998-01-31
Budget Start
1996-02-01
Budget End
1997-01-31
Support Year
4
Fiscal Year
1996
Total Cost
Indirect Cost
Name
University of Rochester
Department
Pharmacology
Type
Schools of Dentistry
DUNS #
208469486
City
Rochester
State
NY
Country
United States
Zip Code
14627
Krueger, J K; Gallagher, S C; Zhi, G et al. (2001) Activation of myosin light chain kinase requires translocation of bound calmodulin. J Biol Chem 276:4535-8
Persechini, A; Yano, K; Stemmer, P M (2000) Ca(2+) binding and energy coupling in the calmodulin-myosin light chain kinase complex. J Biol Chem 275:4199-204
Persechini, A; Cronk, B (1999) The relationship between the free concentrations of Ca2+ and Ca2+-calmodulin in intact cells. J Biol Chem 274:6827-30
Romoser, V A; Hinkle, P M; Persechini, A (1997) Detection in living cells of Ca2+-dependent changes in the fluorescence emission of an indicator composed of two green fluorescent protein variants linked by a calmodulin-binding sequence. A new class of fluorescent indicators. J Biol Chem 272:13270-4
Persechini, A; Lynch, J A; Romoser, V A (1997) Novel fluorescent indicator proteins for monitoring free intracellular Ca2+. Cell Calcium 22:209-16
Persechini, A; Gansz, K J; Paresi, R J (1996) Activation of myosin light chain kinase and nitric oxide synthase activities by engineered calmodulins with duplicated or exchanged EF hand pairs. Biochemistry 35:224-8
Persechini, A; White, H D; Gansz, K J (1996) Different mechanisms for Ca2+ dissociation from complexes of calmodulin with nitric oxide synthase or myosin light chain kinase. J Biol Chem 271:62-7
Persechini, A; Stemmer, P M; Ohashi, I (1996) Localization of unique functional determinants in the calmodulin lobes to individual EF hands. J Biol Chem 271:32217-25
Kataoka, M; Persechini, A; Tokunaga, F et al. (1996) The linker of calmodulin lacking Glu84 is elongated in solution, although it is bent in the crystal. Proteins 25:335-41
Persechini, A; Gansz, K J; Paresi, R J (1996) A role in enzyme activation for the N-terminal leader sequence in calmodulin. J Biol Chem 271:19279-82

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