Martin, Dwight W (2005) Structure-function relationships in the NA+,K+-pump. Semin Nephrol 25:282-91
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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
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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
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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
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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
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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
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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
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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
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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
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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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