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Volumn 47, Issue 19, 2008, Pages 5441-5449

Role of the β4Thr-β73Asp hydrogen bond in HbS polymer and domain formation from multinucleate-containing clusters

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL GROWTH; CRYSTALLINE MATERIALS; NUCLEATION; ORGANIC POLYMERS; SYNTHETIC FIBERS;

EID: 43249097894     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800149u     Document Type: Article
Times cited : (5)

References (30)
  • 2
    • 0025276708 scopus 로고
    • Sickle cell hemoglobin polymerization
    • Eaton, W. A., and Hofrichter, J. (1990) Sickle cell hemoglobin polymerization. Adv. Protein Chem. 40, 63-279.
    • (1990) Adv. Protein Chem , vol.40 , pp. 63-279
    • Eaton, W.A.1    Hofrichter, J.2
  • 3
    • 0018744120 scopus 로고
    • Three-dimensional reconstruction of the 14-filament fibers of hemoglobin S
    • Dykes, G. W., Crepeau, R. H., and Edelstein, S. J. (1979) Three-dimensional reconstruction of the 14-filament fibers of hemoglobin S. J. Mol. Biol. 130, 451-472.
    • (1979) J. Mol. Biol , vol.130 , pp. 451-472
    • Dykes, G.W.1    Crepeau, R.H.2    Edelstein, S.J.3
  • 4
    • 0022260102 scopus 로고    scopus 로고
    • Padlan, E. A., and Love, W. E. (1985) Refined crystal structure of deoxyhemoglobin S. I. Restrained least-squares refinement at 3.0-Å resolution. J. Biol. Chem. 260, 8272-8279.
    • Padlan, E. A., and Love, W. E. (1985) Refined crystal structure of deoxyhemoglobin S. I. Restrained least-squares refinement at 3.0-Å resolution. J. Biol. Chem. 260, 8272-8279.
  • 5
    • 0031587292 scopus 로고    scopus 로고
    • The high resolution crystal structure of deoxyhemoglobin S
    • Harrington, D. J., Adachi, K., and Royer, W. E. (1997) The high resolution crystal structure of deoxyhemoglobin S. J. Mol. Biol. 272, 398-407.
    • (1997) J. Mol. Biol , vol.272 , pp. 398-407
    • Harrington, D.J.1    Adachi, K.2    Royer, W.E.3
  • 7
    • 0037461365 scopus 로고    scopus 로고
    • Effects of different β73 amino acids on formation of 14-stranded fibers of Hb S versus double-stranded crystals of Hb C-Harlem
    • Adachi, K., Ding, M., Wehrli, S., Reddy, K. S., Surrey, S., and Horiuchi, K. (2003) Effects of different β73 amino acids on formation of 14-stranded fibers of Hb S versus double-stranded crystals of Hb C-Harlem. Biochemistry 42, 4476-4484.
    • (2003) Biochemistry , vol.42 , pp. 4476-4484
    • Adachi, K.1    Ding, M.2    Wehrli, S.3    Reddy, K.S.4    Surrey, S.5    Horiuchi, K.6
  • 8
    • 0021815445 scopus 로고
    • Kinetics of sickle hemoglobin polymerization. I. Studies using temperature-jump and laser photolysis techniques
    • Ferrone, F. A., Hofrichter, J., and Eaton, W. A. (1985) Kinetics of sickle hemoglobin polymerization. I. Studies using temperature-jump and laser photolysis techniques. J. Mol. Biol. 183, 591-610.
    • (1985) J. Mol. Biol , vol.183 , pp. 591-610
    • Ferrone, F.A.1    Hofrichter, J.2    Eaton, W.A.3
  • 9
    • 0021837479 scopus 로고
    • Kinetics of sickle hemoglobin polymerization. II. A double nucleation mechanism
    • Ferrone, F. A., Hofrichter, J., and Eaton, W. A. (1985) Kinetics of sickle hemoglobin polymerization. II. A double nucleation mechanism. J. Mol. Biol. 183, 611-631.
    • (1985) J. Mol. Biol , vol.183 , pp. 611-631
    • Ferrone, F.A.1    Hofrichter, J.2    Eaton, W.A.3
  • 10
    • 0029008481 scopus 로고
    • The biophysics of sickle cell hydroxyurea therapy
    • Eaton, W. A., and Hofrichter, J. (1995) The biophysics of sickle cell hydroxyurea therapy. Science 268, 1142-1143.
    • (1995) Science , vol.268 , pp. 1142-1143
    • Eaton, W.A.1    Hofrichter, J.2
  • 11
    • 0036220417 scopus 로고    scopus 로고
    • Heterogeneous nucleation and crowding in sickle hemoglobin: An analytic approach
    • Ferrone, F. A., Ivanova, M., and Jasuja, R. (2002) Heterogeneous nucleation and crowding in sickle hemoglobin: An analytic approach. Biophys. J. 82, 399-406.
    • (2002) Biophys. J , vol.82 , pp. 399-406
    • Ferrone, F.A.1    Ivanova, M.2    Jasuja, R.3
  • 12
    • 0014709419 scopus 로고
    • The fine structure of cell-free sickled hemoglobin
    • White, J. G., and Heagan, B. (1970) The fine structure of cell-free sickled hemoglobin. Am. J. Pathol. 58, 1-17.
    • (1970) Am. J. Pathol , vol.58 , pp. 1-17
    • White, J.G.1    Heagan, B.2
  • 13
    • 0015711638 scopus 로고
    • Structure of hemoglobin S fibers: Optical determination of the molecular orientation in sickled erythrocytes
    • Hofrichter, J., Hendricker, D. G., and Eaton, W. A. (1973) Structure of hemoglobin S fibers: Optical determination of the molecular orientation in sickled erythrocytes. Proc. Natl. Acad. Sci. U.S.A. 70, 3604-3608.
    • (1973) Proc. Natl. Acad. Sci. U.S.A , vol.70 , pp. 3604-3608
    • Hofrichter, J.1    Hendricker, D.G.2    Eaton, W.A.3
  • 14
    • 0025284406 scopus 로고
    • Nucleation and growth of fibres and gel formation in sickle cell haemoglobin
    • Samuel, R. E., Salmon, E. D., and Briehl, R. W. (1990) Nucleation and growth of fibres and gel formation in sickle cell haemoglobin. Nature 345, 833-835.
    • (1990) Nature , vol.345 , pp. 833-835
    • Samuel, R.E.1    Salmon, E.D.2    Briehl, R.W.3
  • 15
    • 0028920158 scopus 로고
    • Nucleation, fiber growth and melting, and domain formation and structure in sickle cell hemoglobin gels
    • Briehl, R. W. (1995) Nucleation, fiber growth and melting, and domain formation and structure in sickle cell hemoglobin gels. J. Mol. Biol. 245, 710-723.
    • (1995) J. Mol. Biol , vol.245 , pp. 710-723
    • Briehl, R.W.1
  • 16
    • 1642434114 scopus 로고    scopus 로고
    • Mechanisms of homogeneous nucleation of polymers of sickle cell anemia hemoglobin in deoxy state
    • Galkin, O., and Vekilov, P. G. (2004) Mechanisms of homogeneous nucleation of polymers of sickle cell anemia hemoglobin in deoxy state. J. Mol. Biol. 336, 43-59.
    • (2004) J. Mol. Biol , vol.336 , pp. 43-59
    • Galkin, O.1    Vekilov, P.G.2
  • 17
    • 33751513333 scopus 로고    scopus 로고
    • The kinetics of nucleation and growth of sickle cell hemoglobin fibers
    • Galkin, O., Nagel, R. L., and Vekilov, P. G. (2007) The kinetics of nucleation and growth of sickle cell hemoglobin fibers. J. Mol. Biol. 365, 425-439.
    • (2007) J. Mol. Biol , vol.365 , pp. 425-439
    • Galkin, O.1    Nagel, R.L.2    Vekilov, P.G.3
  • 18
    • 34848813177 scopus 로고    scopus 로고
    • Sickle-cell haemoglobin polymerization: Is it the primary pathogenic event of sickle-cell anaemia?
    • Vekilov, P. G. (2007) Sickle-cell haemoglobin polymerization: Is it the primary pathogenic event of sickle-cell anaemia? Br. J. Haematol. 139, 173-184.
    • (2007) Br. J. Haematol , vol.139 , pp. 173-184
    • Vekilov, P.G.1
  • 19
    • 0019214043 scopus 로고
    • Polymerization of deoxyhemoglobin CHarlem (β6Glu replaced by Val, β73Asp replaced by Asn). The effect of β73 asparagine on the gelation and crystallization of hemoglobin
    • Adachi, K., and Asakura, T. (1980) Polymerization of deoxyhemoglobin CHarlem (β6Glu replaced by Val, β73Asp replaced by Asn). The effect of β73 asparagine on the gelation and crystallization of hemoglobin. J. Mol. Biol. 144, 467-480.
    • (1980) J. Mol. Biol , vol.144 , pp. 467-480
    • Adachi, K.1    Asakura, T.2
  • 21
    • 33745863152 scopus 로고    scopus 로고
    • Inhibition of hemoglobin S polymerization in vitro by a novel 15-mer EF-helix β73 histidine-containing peptide
    • Akbar, M. G., Tamura, Y., Ding, M., Ding, H., Rosenblatt, M. M., Reddy, K. S., Surrey, S., and Adachi, K. (2006) Inhibition of hemoglobin S polymerization in vitro by a novel 15-mer EF-helix β73 histidine-containing peptide. Biochemistry 45, 8358-8367.
    • (2006) Biochemistry , vol.45 , pp. 8358-8367
    • Akbar, M.G.1    Tamura, Y.2    Ding, M.3    Ding, H.4    Rosenblatt, M.M.5    Reddy, K.S.6    Surrey, S.7    Adachi, K.8
  • 22
    • 0030841343 scopus 로고    scopus 로고
    • Conformational disease
    • Carrell, R. W., and Lomas, D. A. (1997) Conformational disease. Lancet 350, 134-138.
    • (1997) Lancet , vol.350 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 23
    • 0033793872 scopus 로고    scopus 로고
    • Mechanisms of amyloidogenesis
    • Kelly, J. W. (2000) Mechanisms of amyloidogenesis. Nat. Struct. Biol. 7, 824-826.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 824-826
    • Kelly, J.W.1
  • 24
    • 0033621165 scopus 로고    scopus 로고
    • Amyloid diseases: Abnormal protein aggregation in neurodegeneration
    • Koo, E. H., Lansbury, P. T., Jr., and Kelly, J. W. (1999) Amyloid diseases: Abnormal protein aggregation in neurodegeneration. Proc. Natl. Acad. Sci. U.S.A. 96, 9989-9990.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 9989-9990
    • Koo, E.H.1    Lansbury Jr., P.T.2    Kelly, J.W.3
  • 26
    • 0027451963 scopus 로고
    • Effects of β6 aromatic amino acids on polymerization and solubility of recombinant hemoglobins made in yeast
    • Adachi, K., Konitzer, P., Kim, J., Welch, N., and Surrey, S. (1993) Effects of β6 aromatic amino acids on polymerization and solubility of recombinant hemoglobins made in yeast. J. Biol. Chem. 268, 21650-21656.
    • (1993) J. Biol. Chem , vol.268 , pp. 21650-21656
    • Adachi, K.1    Konitzer, P.2    Kim, J.3    Welch, N.4    Surrey, S.5
  • 27
    • 0033763140 scopus 로고    scopus 로고
    • Polymerization of deoxy-sickle cell hemoglobin in high-phosphate buffer
    • Wang, Z., Kishchenko, G., Chen, Y., and Josephs, R. (2000) Polymerization of deoxy-sickle cell hemoglobin in high-phosphate buffer. J. Struct. Biol. 131, 197-209.
    • (2000) J. Struct. Biol , vol.131 , pp. 197-209
    • Wang, Z.1    Kishchenko, G.2    Chen, Y.3    Josephs, R.4
  • 28
    • 33846016196 scopus 로고    scopus 로고
    • Metastable mesoscopic clusters in solutions of sickle-cell hemoglobin
    • Pan, W., Galkin, O., Filobelo, L., Nagel, R. L., and Vekilov, P. G. (2007) Metastable mesoscopic clusters in solutions of sickle-cell hemoglobin. Biophys. J. 92, 267-277.
    • (2007) Biophys. J , vol.92 , pp. 267-277
    • Pan, W.1    Galkin, O.2    Filobelo, L.3    Nagel, R.L.4    Vekilov, P.G.5
  • 29


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.