메뉴 건너뛰기




Volumn 265, Issue 5, 1997, Pages 475-479

The structural link between polymerization and sickle cell disease

Author keywords

Nucleation; Pathophysiology; Polymerization

Indexed keywords

HEMOGLOBIN S;

EID: 0031556954     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0759     Document Type: Editorial
Times cited : (30)

References (21)
  • 1
    • 0024163316 scopus 로고
    • The reconstruction of helical particles with variable pitch
    • Bluemke D. A., Carragher B., Josephs R. The reconstruction of helical particles with variable pitch. Ultramicroscopy. 26:1988;255-270.
    • (1988) Ultramicroscopy , vol.26 , pp. 255-270
    • Bluemke, D.A.1    Carragher, B.2    Josephs, R.3
  • 2
    • 0028920158 scopus 로고
    • Nucleation, fiber growth and melting, and domain formation and structure in sickle cell hemoglobin gels
    • Briehl R. Nucleation, fiber growth and melting, and domain formation and structure in sickle cell hemoglobin gels. J. Mol. Biol. 245:1995;710-723.
    • (1995) J. Mol. Biol. , vol.245 , pp. 710-723
    • Briehl, R.1
  • 3
    • 0019165941 scopus 로고
    • Solid-like behaviour of unsheared sickle haemoglobin gels and the effects of shear
    • Briehl R. W. Solid-like behaviour of unsheared sickle haemoglobin gels and the effects of shear. Nature. 228:1980;622-624.
    • (1980) Nature , vol.228 , pp. 622-624
    • Briehl, R.W.1
  • 4
    • 0029995324 scopus 로고    scopus 로고
    • A 50th order reaction predicted and observed for sickle hemoglobin nucleation
    • Cao Z., Ferrone F. A. A 50th order reaction predicted and observed for sickle hemoglobin nucleation. J. Mol. Biol. 256:1996;219-222.
    • (1996) J. Mol. Biol. , vol.256 , pp. 219-222
    • Cao, Z.1    Ferrone, F.A.2
  • 5
    • 0023908075 scopus 로고
    • Structural analysis of polymers of sickle cell hemoglobin. I. Sickle hemoglobin fibers
    • Carragher B., Bluemke D. A., Gabriel B., Potel M. J., Josephs R. Structural analysis of polymers of sickle cell hemoglobin. I. sickle hemoglobin fibers. J. Mol. Biol. 199:1988;315-331.
    • (1988) J. Mol. Biol. , vol.199 , pp. 315-331
    • Carragher, B.1    Bluemke, D.A.2    Gabriel, B.3    Potel, M.J.4    Josephs, R.5
  • 6
    • 0027157440 scopus 로고
    • Double strand packing in hemoglobin S fibers
    • Cretegny I., Edelstein S. J. Double strand packing in hemoglobin S fibers. J. Mol. Biol. 230:1993;733-738.
    • (1993) J. Mol. Biol. , vol.230 , pp. 733-738
    • Cretegny, I.1    Edelstein, S.J.2
  • 7
    • 0018744120 scopus 로고
    • Three dimensional reconstruction of 14-filament fibers of hemoglobin
    • Dykes G. W., Crepeau R. H., Edelstein S. J. Three dimensional reconstruction of 14-filament fibers of hemoglobin. S. J. Mol. Biol. 130:1979;451-472.
    • (1979) S. J. Mol. Biol. , vol.130 , pp. 451-472
    • Dykes, G.W.1    Crepeau, R.H.2    Edelstein, S.J.3
  • 9
    • 0019888363 scopus 로고
    • Molecular topology in crystals and fibers of hemoglobin S
    • Edelstein S. J. Molecular topology in crystals and fibers of hemoglobin S. J. Mol. Biol. 150:1981;557-575.
    • (1981) J. Mol. Biol. , vol.150 , pp. 557-575
    • Edelstein, S.J.1
  • 11
    • 0018640810 scopus 로고
    • Oblique alignment of hemoglobin S fibers in sickled cells
    • Edelstein S. J., Crepeau R. H. Oblique alignment of hemoglobin S fibers in sickled cells. J. Mol. Biol. 134:1979;851-855.
    • (1979) J. Mol. Biol. , vol.134 , pp. 851-855
    • Edelstein, S.J.1    Crepeau, R.H.2
  • 12
    • 0020477574 scopus 로고
    • F-actin is a helix with a random variable twist
    • Egelman E. H., Francis N., DeRosier D. J. F-actin is a helix with a random variable twist. Nature. 298:1982;131-135.
    • (1982) Nature , vol.298 , pp. 131-135
    • Egelman, E.H.1    Francis, N.2    DeRosier, D.J.3
  • 13
    • 0019072559 scopus 로고
    • Kinetic studies on photolysis-induced gelation of sickle cell hemoglobin suggest a new mechanism
    • Ferrone F. A., Hofrichter J., Sunshine H., Eaton W. A. Kinetic studies on photolysis-induced gelation of sickle cell hemoglobin suggest a new mechanism. Biophys. J. 32:1980;361-377.
    • (1980) Biophys. J. , vol.32 , pp. 361-377
    • Ferrone, F.A.1    Hofrichter, J.2    Sunshine, H.3    Eaton, W.A.4
  • 14
    • 0021837479 scopus 로고
    • Kinetics of sickle hemoglobin polymerization. II. A double nucleation mechanism
    • Ferrone F. A., Hofrichter J., Eaton W. A. Kinetics of sickle hemoglobin polymerization. II. A double nucleation mechanism. J. Mol. Biol. 183:1985a;611-631.
    • (1985) J. Mol. Biol. , vol.183 , pp. 611-631
    • Ferrone, F.A.1    Hofrichter, J.2    Eaton, W.A.3
  • 15
    • 0021815445 scopus 로고
    • Kinetics of sickle hemoglobin polymerization. I. Studies using temperature-jump and laser photolysis techniques
    • Ferrone F. A., Hofrichter J., Eaton W. A. Kinetics of sickle hemoglobin polymerization. I. Studies using temperature-jump and laser photolysis techniques. J. Mol. Biol. 183:1985b;591-610.
    • (1985) J. Mol. Biol. , vol.183 , pp. 591-610
    • Ferrone, F.A.1    Hofrichter, J.2    Eaton, W.A.3
  • 16
    • 0028353621 scopus 로고
    • Cryo-electron microscopy of deoxy-sickle hemoglobin fibers
    • Lewis M. R., Gross L. J., Josephs R. Cryo-electron microscopy of deoxy-sickle hemoglobin fibers. Micr. Res. Techn. 27:1994;459-467.
    • (1994) Micr. Res. Techn. , vol.27 , pp. 459-467
    • Lewis, M.R.1    Gross, L.J.2    Josephs, R.3
  • 17
    • 0023195612 scopus 로고
    • Delay time of hemoglobin S polymeriztion prevents most cells from sickling
    • Mozzarelli A., Hofrichter J., Eaton W. A. Delay time of hemoglobin S polymeriztion prevents most cells from sickling. Science. 237:1987;500-506.
    • (1987) Science , vol.237 , pp. 500-506
    • Mozzarelli, A.1    Hofrichter, J.2    Eaton, W.A.3
  • 18
    • 0022253394 scopus 로고
    • Refined crystal structure of deoxyhemoglobin S
    • Padlan E. A., Love W. E. Refined crystal structure of deoxyhemoglobin S. J. Biol. Chem. 260:1985;8280-8291.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8280-8291
    • Padlan, E.A.1    Love, W.E.2
  • 19
    • 0025284406 scopus 로고
    • Nucleation and growth of fibres and gel formation in sickle cell haemoglobin
    • Samuel R. E., Salmon E. D., Briehl R. W. Nucleation and growth of fibres and gel formation in sickle cell haemoglobin. Nature. 345:1990;833-835.
    • (1990) Nature , vol.345 , pp. 833-835
    • Samuel, R.E.1    Salmon, E.D.2    Briehl, R.W.3
  • 20
    • 0024388204 scopus 로고
    • Intramolecular contacts within sickle hemoglobin fibers
    • Watowich S. J., Gross L. J., Josephs R. J. Intramolecular contacts within sickle hemoglobin fibers. J. Mol. Biol. 209:1989;821-828.
    • (1989) J. Mol. Biol. , vol.209 , pp. 821-828
    • Watowich, S.J.1    Gross, L.J.2    Josephs, R.J.3
  • 21
    • 0027892880 scopus 로고
    • Analysis of the intermolecular contacts within sickle hemoglobin fibers: Effect of site-specific substitutions, fiber pitch and double-strand disorder
    • Watowich S. J., Gross L. J., Josephs R. Analysis of the intermolecular contacts within sickle hemoglobin fibers: effect of site-specific substitutions, fiber pitch and double-strand disorder. J. Struct. Biol. 111:1993;161-179.
    • (1993) J. Struct. Biol. , vol.111 , pp. 161-179
    • Watowich, S.J.1    Gross, L.J.2    Josephs, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.