James M. Salhany

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Salhany JM. (2013) The oxidative denitrosylation mechanism and nitric oxide release from human fetal and adult hemoglobin, an experimentally based model simulation study. Blood Cells, Molecules & Diseases. 50: 8-19
Salhany JM. (2010) Reaction of nitrite with human fetal oxyhemoglobin: a model simulation study with implications for blood flow regulation in sickle cell disease (SCD). Blood Cells, Molecules & Diseases. 44: 111-4
Salhany JM. (2009) Kinetic evidence for modulation by glycophorin A of a conformational equilibrium between two states of band 3 (SLC4A1) bound reversibly by the competitive inhibitor DIDS. Blood Cells, Molecules & Diseases. 42: 185-91
Salhany JM. (2008) Kinetics of reaction of nitrite with deoxy hemoglobin after rapid deoxygenation or predeoxygenation by dithionite measured in solution and bound to the cytoplasmic domain of band 3 (SLC4A1). Biochemistry. 47: 6059-72
Salhany JM, Cordes KS, Sloan RL. (2006) Band 3 (AE1, SLC4A1)-mediated transport of stilbenedisulfonates. III: Role of solute and protein structure in proton-activated stilbenedisulfonate influx. Blood Cells, Molecules & Diseases. 37: 155-63
Salhany JM, Cordes KS, Sloan RL. (2006) Band 3 (AE1, SLC4A1)-mediated transport of stilbenedisulfonates. I: Functional identification of the proton-activated stilbenedisulfonate influx site. Blood Cells, Molecules & Diseases. 37: 137-48
Salhany JM, Cordes KS, Sloan RL. (2006) Band 3 (AE1, SLC4A1)-mediated transport of stilbenedisulfonates. II: Evidence for transmembrane allosteric interactions between the "primary" stilbenedisulfonate binding site and the stilbenedisulfonate efflux site. Blood Cells, Molecules & Diseases. 37: 149-54
Salhany JM, Cordes KS, Sloan RL. (2005) Identification and characterization of a second 4,4'-dibenzamido-2,2'-stilbenedisulphonate (DBDS)-binding site on band 3 and its relationship with the anion/proton co-transport function. The Biochemical Journal. 388: 343-53
Salhany JM. (2004) Slow transitions between two conformational states of band 3 (AE1) modulate divalent anion transport and DBDS binding to a second site on band 3 which is activated by lowering the pH (pK approximately 5.0). Blood Cells, Molecules & Diseases. 32: 372-8
Salhany JM, Sloan RL, Cordes KS. (2003) The carboxyl side chain of glutamate 681 interacts with a chloride binding modifier site that allosterically modulates the dimeric conformational state of band 3 (AE1). Implications for the mechanism of anion/proton cotransport. Biochemistry. 42: 1589-602