Noncovalent modification of deoxyhemoglobin S solubility and erythrocyte sickling. Waterman MR, Yamaoka K, Dahm L, Taylor J, Cottam GL (1974) Proc Natl Acad Sci U S A 71: 2222-5 Functional studies on hemoglobin opossum. Conclusions drawn regarding the role of the distal histidine. Sharma VS, John ME, Waterman MR (1982) J Biol Chem 257: 11887-92 Structural basis for the conformational states of nitrosyl hemoglobins M Saskatoon and M Milwaukee. Influence of distal histidine residues on proximal histidine-iron bonds. John ME, Waterman MR (1980) J Biol Chem 255: 4501-6 Structural characteristics of nitrosyl hemoglobins and their relation to ESR spectra. John ME, Waterman MR (1979) FEBS Lett 106: 219-22 The gelation of deoxyhemoglobin S in erythrocytes as detected by transverse water proton relazation measurements. Cottam GL, Valentine KM, Yamaoka K, Waterman MR (1974) Arch Biochem Biophys 162: 487-92 Effect of pH, carbamylation and other hemoglobins on deoxyhemoglobin S aggregation inside intact erythrocytes as detected by proton relaxation rate measurements. Chuang AH, Waterman MR, Yamaoka K, Cottam L (1975) Arch Biochem Biophys 167: 145-50 Evaluation of the water environments in deoxygenated sickle cells by longitudinal and transverse water proton relaxation rates. Thompson BC, Waterman MR, Cottam GL (1975) Arch Biochem Biophys 166: 193-200 Reversible solubility of deoxyhemoglobin S. Cottam GL, Waterman MR (1973) Biochem Biophys Res Commun 54: 1157-63 Spin-label studies at F9(93)beta of deoxyhemoglobin S aggregation. Yamaoka K, Cottam GL, Waterman MR (1974) Biochem Biophys Res Commun 58: 1058-65 Hemoglobin Hofu (beta 126 Val is replaced by Glu) in a black American. Russo FM, John ME, Waterman MR, Simon LM, Sheehan RG (1979) Hemoglobin 3: 83-6
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