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2. 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 JM, Sloan RL, Cordes KS. Biochemistry; 2003 Feb 18; 42(6):1589-602. PubMed ID: 12578372 [Abstract] [Full Text] [Related]
3. Erythrocyte band 3 protein: evidence for multiple membrane-crossing segments in the 17 000-dalton chymotryptic fragment. Jennings ML, Nicknish JS. Biochemistry; 1984 Dec 18; 23(26):6432-6. PubMed ID: 6529560 [Abstract] [Full Text] [Related]
5. Identification of the eosinyl-5-maleimide reaction site on the human erythrocyte anion-exchange protein: overlap with the reaction sites of other chemical probes. Cobb CE, Beth AH. Biochemistry; 1990 Sep 11; 29(36):8283-90. PubMed ID: 1701324 [Abstract] [Full Text] [Related]
6. Anion-proton cotransport through the human red blood cell band 3 protein. Role of glutamate 681. Jennings ML, Smith JS. J Biol Chem; 1992 Jul 15; 267(20):13964-71. PubMed ID: 1352774 [Abstract] [Full Text] [Related]
7. Localization of a site of intermolecular cross-linking in human red blood cell band 3 protein. Jennings ML, Nicknish JS. J Biol Chem; 1985 May 10; 260(9):5472-9. PubMed ID: 3988763 [Abstract] [Full Text] [Related]
9. Allosteric effects in stilbenedisulfonate binding to band 3 protein (AE1). Salhany JM. Cell Mol Biol (Noisy-le-grand); 1996 Nov 10; 42(7):1065-96. PubMed ID: 8960781 [Abstract] [Full Text] [Related]
10. Conformational change of band 3 protein induced by diethyl pyrocarbonate modification in human erythrocyte ghosts. Izuhara K, Okubo K, Hamasaki N. Biochemistry; 1989 May 30; 28(11):4725-8. PubMed ID: 2765508 [Abstract] [Full Text] [Related]
13. Reductive methylation of the two 4,4'-diisothiocyanodihydrostilbene-2,2'-disulfonate-binding lysine residues of band 3, the human erythrocyte anion transport protein. Jennings ML. J Biol Chem; 1982 Jul 10; 257(13):7554-9. PubMed ID: 6806279 [Abstract] [Full Text] [Related]
15. The kinetics of intramolecular cross-linking of the band 3 protein in the red blood cell membrane by 4,4'-diisothiocyano dihydrostilbene-2,2'-disulfonic acid (H2DIDS). Kampmann L, Lepke S, Fasold H, Fritzsch G, Passow H. J Membr Biol; 1982 Jul 10; 70(3):199-216. PubMed ID: 7186941 [Abstract] [Full Text] [Related]
18. Anion transport across the erythrocyte membrane, in situ proteolysis of band 3 protein, and cross-linking of proteolytic fragments by 4,4'-diisothiocyano dihydrostilbene-2,2'-disulfonate. Jennings ML, Passow H. Biochim Biophys Acta; 1979 Jul 05; 554(2):498-519. PubMed ID: 486455 [Abstract] [Full Text] [Related]
19. Synthesis and characterization of a novel spin-labeled affinity probe of human erythrocyte band 3: characteristics of the stilbenedisulfonate binding site. Scothorn DJ, Wojcicki WE, Hustedt EJ, Beth AH, Cobb CE. Biochemistry; 1996 May 28; 35(21):6931-43. PubMed ID: 8639645 [Abstract] [Full Text] [Related]
20. In situ cross-linking of human erythrocyte band 3 by bis(sulfosuccinimidyl)suberate. Evidence for ligand modulation of two alternate quaternary forms: covalent band 3 dimers and noncovalent tetramers formed by the association of two covalent dimers. Salhany JM, Sloan RL, Cordes KA. J Biol Chem; 1990 Oct 15; 265(29):17688-93. PubMed ID: 2211656 [Abstract] [Full Text] [Related] Page: [Next] [New Search]