Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
Research Project (R01)
Project #
3R01DK019185-14S1
Application #
3226287
Study Section
Physiology Study Section (PHY)
Project Start
1976-06-01
Project End
1993-11-30
Budget Start
1990-12-01
Budget End
1991-11-30
Support Year
14
Fiscal Year
1992
Total Cost
Indirect Cost
Name
State University New York Stony Brook
Department
Type
Schools of Medicine
DUNS #
804878247
City
Stony Brook
State
NY
Country
United States
Zip Code
11794
Martin, Dwight W (2005) Structure-function relationships in the NA+,K+-pump. Semin Nephrol 25:282-91
Rice, W J; Young, H S; Martin, D W et al. (2001) Structure of Na+,K+-ATPase at 11-A resolution: comparison with Ca2+-ATPase in E1 and E2 states. Biophys J 80:2187-97
Martin, D W; Sachs, J R (2000) Ligands presumed to label high affinity and low affinity ATP binding sites do not interact in an (alpha beta)2 diprotomer in duck nasal gland Na+,K+-ATPase, nor Do the sites coexist in native enzyme. J Biol Chem 275:24512-7
Martin, D W; Marecek, J; Scarlata, S et al. (2000) Alphabeta protomers of Na+,K+-ATPase from microsomes of duck salt gland are mostly monomeric: formation of higher oligomers does not modify molecular activity. Proc Natl Acad Sci U S A 97:3195-200
Martin, D W; Sachs, J R (1999) Preparation of Na+,K+-ATPase with near maximal specific activity and phosphorylation capacity: evidence that the reaction mechanism involves all of the sites. Biochemistry 38:7485-97
Sachs, J R; Martin, D W (1999) Role of polyamine structure in inhibition of K+-Cl- cotransport in human red cell ghosts. J Physiol 520 Pt 3:723-35
Martin, D W; Jesty, J (1995) Calcium stimulation of procoagulant activity in human erythrocytes. ATP dependence and the effects of modifiers of stimulation and recovery. J Biol Chem 270:10468-74
Sachs, J R (1994) The role of (alpha beta) protomer interaction in determining functional characteristics of red cell Na,K-ATPase. Biochim Biophys Acta 1193:199-211
Sachs, J R (1994) Soluble polycations and cationic amphiphiles inhibit volume-sensitive K-Cl cotransport in human red cell ghosts. Am J Physiol 266:C997-1005
Sachs, J R; Martin, D W (1993) The role of ATP in swelling-stimulated K-Cl cotransport in human red cell ghosts. Phosphorylation-dephosphorylation events are not in the signal transduction pathway. J Gen Physiol 102:551-73

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