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
Identification and characterization of a second 4,4′-dibenzamido-2,2′-stilbenedisulfonate (DBDS)-binding site on band 3 and its relationship with the anion/proton co-transport function
Salhany J.M., Cordes K.A., and Sloan R.L. Identification and characterization of a second 4,4′-dibenzamido-2,2′-stilbenedisulfonate (DBDS)-binding site on band 3 and its relationship with the anion/proton co-transport function. Biochem. J. 388 (2005) 343-353
Band 3 (AE1, SLC4A1)-mediated transport of stilbenedisulfonates. I: Functional identification of the proton-activated stilbenedisulfonate influx site
Salhany J.M., Cordes K.S., and Sloan R.L. Band 3 (AE1, SLC4A1)-mediated transport of stilbenedisulfonates. I: Functional identification of the proton-activated stilbenedisulfonate influx site. Blood Cell. Mol. Dis. 37 (2006) 137-148
Anion transport in red blood cells. III. Sites and sidedness in inhibition by high-affinity reversible binding of probes
Barzilay M., and Cabantchick Z.I. Anion transport in red blood cells. III. Sites and sidedness in inhibition by high-affinity reversible binding of probes. Membr. Biochem. 2 (1979) 297-322
Kinetics of conformational changes associated with inhibitor binding to the purified band 3 transporter. Direct observation of allosteric subunit interactions
Salhany J.M., Cordes K.A., and Schopfer L.M. Kinetics of conformational changes associated with inhibitor binding to the purified band 3 transporter. Direct observation of allosteric subunit interactions. Biochemistry 32 (1993) 7413-7420
Location of the stilbenedisulfonate binding site of the human erythrocyte anion-exchange system by resonance energy transfer
Rao A., Martin P., Reithmeier R.A.F., and Cantley L.C. Location of the stilbenedisulfonate binding site of the human erythrocyte anion-exchange system by resonance energy transfer. Biochemistry 18 (1979) 4505-4516
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
Salhany J.M., Sloan R.L., and Cordes K.S. 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 (2003) 1589-1602
Relocation of the disulfonic stilbene sites of AE1 (Band 3) on the basis of fluorescence energy transfer measurements
Knauf P.A., Law F.-Y., Leung T.-W.V., and Atherton S.J. Relocation of the disulfonic stilbene sites of AE1 (Band 3) on the basis of fluorescence energy transfer measurements. Biochemistry 43 (2004) 1918-11931
Differential sensitivity of stilbenedisulfonates in their reaction with band 3 HT (Pro-868 → Leu)
Salhany J.M., Schopfer L.M., Kay M.M.B., and Gamble D.N. Differential sensitivity of stilbenedisulfonates in their reaction with band 3 HT (Pro-868 → Leu). Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 1844-11848
Characterization of the stilbenedisulfonate binding site on band 3 Memphis variant II (Pro-854 → Leu)
Salhany J.M., Sloan R.L., and Schopfer L.M. Characterization of the stilbenedisulfonate binding site on band 3 Memphis variant II (Pro-854 → Leu). Biochem. J. 317 (1996) 509-514
Anion transport across the erythrocyte membrane, in situ proteolysis of band 3 protein, and crosslinkng of proteolytic fragments by 4,4′-diisothiocyanodihydrostilbene-2,2′-disulfonate
Jennings M.L., and Passow H. Anion transport across the erythrocyte membrane, in situ proteolysis of band 3 protein, and crosslinkng of proteolytic fragments by 4,4′-diisothiocyanodihydrostilbene-2,2′-disulfonate. Biochim. Biophys. Acta 554 (1979) 498-519
A structural study of the membrane domain of band 3 by tryptic digestion. Conformational change of band 3 in situ induced by alkali treatment
Kang D., Okubo K., Hamasaki N., and Kuroda H. Shimaki N. A structural study of the membrane domain of band 3 by tryptic digestion. Conformational change of band 3 in situ induced by alkali treatment. J. Biol. Chem. 267 (1992) 19211-19217