메뉴 건너뛰기




Volumn 48, Issue 41, 2009, Pages 9903-9911

Real time monitoring of sickle cell hemoglobin fiber formation by UV resonance Raman spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC AMINO ACID; FIBER FORMATION; FUNCTION OF TIME; H-BOND STRENGTH; HYDROPHOBIC POCKETS; INITIAL STAGES; INTENSITY CHANGE; INTERMOLECULAR CONTACTS; LONG FIBER; MACROFIBERS; MOLECULAR INSIGHTS; MUTATION SITES; POLYMERIZATION PROCESS; PROGRESS CURVES; REAL TIME; REAL TIME MONITORING; SICKLE CELL; SIGNAL INTENSITIES; TETRAMERS; TIME POINTS; TURBIDITY MEASUREMENTS; UV-RESONANCE RAMAN SPECTROSCOPY; VIBRATIONAL MODES;

EID: 70350062719     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901352m     Document Type: Article
Times cited : (9)

References (60)
  • 1
    • 0022253394 scopus 로고
    • Refined crystal structure of deoxyhemoglobin S. II. Molecular interactions in the crystal
    • Padlan, E. A., and Love, W. E. (1985) Refined crystal structure of deoxyhemoglobin S. II. Molecular interactions in the crystal. J. Biol. Chem. 260, 8280-8291.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8280-8291
    • Padlan, E.A.1    Love, W.E.2
  • 2
    • 0031587292 scopus 로고    scopus 로고
    • The high resolution crystal structure of deoxyhemoglobin
    • Harrington, D. J., Adachi, K., and Royer, W. E., Jr. (1997) The high resolution crystal structure of deoxyhemoglobin S. J. Mol. Biol. 272, 398-407.
    • (1997) S. J. Mol. Biol. , vol.272 , pp. 398-407
    • Harrington, D.J.1    Adachi, K.2    Royer Jr., W.E.3
  • 3
    • 0032484104 scopus 로고    scopus 로고
    • Crystal structure of deoxy-human hemoglobin beta6 Glu→Trp. Implications for the structure and formation of the sickle cell fiber
    • Harrington, D. J., Adachi, K., and Royer, W. E., Jr. (1998) Crystal structure of deoxy-human hemoglobin beta6 Glu→Trp. Implications for the structure and formation of the sickle cell fiber. J. Biol. Chem. 273, 32690-32696.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32690-32696
    • Harrington, D.J.1    Adachi, K.2    Royer Jr., W.E.3
  • 4
    • 0023195612 scopus 로고
    • Delay time of hemoglobin S polymerization prevents most cells from sickling in vivo
    • Mozzarelli, A., Hofrichter, J., and Eaton, W. A. (1987) Delay time of hemoglobin S polymerization prevents most cells from sickling in vivo. Science 237, 500-506. (Pubitemid 17125918)
    • (1987) Science , vol.237 , Issue.4814 , pp. 500-506
    • Mozzarelli, A.1    Hofrichter, J.2    Eaton, W.A.3
  • 5
    • 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
  • 6
    • 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
  • 7
    • 33749597429 scopus 로고    scopus 로고
    • Nucleation: The connections between equilibrium and kinetic behavior
    • Ferrone, F. A. (2006) Nucleation: the connections between equilibrium and kinetic behavior. Methods Enzymol. 412, 285-299.
    • (2006) Methods Enzymol. , vol.412 , pp. 285-299
    • Ferrone, F.A.1
  • 8
    • 0032877134 scopus 로고    scopus 로고
    • Analysis of protein aggregation kinetics
    • Ferrone, F. (1999) Analysis of protein aggregation kinetics. Methods Enzymol. 309, 256-274.
    • (1999) Methods Enzymol. , vol.309 , pp. 256-274
    • Ferrone, F.1
  • 10
    • 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
  • 11
    • 34547700385 scopus 로고    scopus 로고
    • Two-step mechanism of homogeneous nucleation of sickle cell hemoglobin polymers
    • DOI 10.1529/biophysj.106.103705
    • Galkin, O., Pan, W., Filobelo, L., Hirsch, R. E., Nagel, R. L., and Vekilov, P. G. (2007) Two-step mechanism of homogeneous nucleation of sickle cell hemoglobin polymers. Biophys. J. 93, 902-913. (Pubitemid 47219782)
    • (2007) Biophysical Journal , vol.93 , Issue.3 , pp. 902-913
    • Galkin, O.1    Pan, W.2    Filobelo, L.3    Hirsch, R.E.4    Nagel, R.L.5    Vekilov, P.G.6
  • 12
    • 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
  • 13
    • 33846016196 scopus 로고    scopus 로고
    • Metastable mesoscopic clusters in solutions of sickle-cell hemoglobin
    • DOI 10.1529/biophysj.106.094854
    • 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. (Pubitemid 46048434)
    • (2007) Biophysical Journal , vol.92 , Issue.1 , pp. 267-277
    • Pan, W.1    Galkin, O.2    Filobelo, L.3    Nagel, R.L.4    Vekilov, P.G.5
  • 15
    • 0038194523 scopus 로고    scopus 로고
    • Conformational changes in FmetHbS probed with UV resonance Raman and fluorescence spectroscopic methods
    • Sokolov, L., and Mukerji, I. (1998) Conformational changes in FmetHbS probed with UV resonance Raman and fluorescence spectroscopic methods. J. Phys. Chem. B 102, 8314-8319.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 8314-8319
    • Sokolov, L.1    Mukerji, I.2
  • 16
    • 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., and Josephs, R. (1988) Structural analysis of polymers of sickle cell hemoglobin. I. Sickle hemoglobin fibers. J. Mol. Biol. 199, 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
  • 17
    • 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., and Josephs, R. (1993) Analysis of the intermolecular contacts within sickle hemoglobin fibers: effect of site-specific substitutions, fiber pitch, and double-strand disorder. J. Struct. Biol. 111, 161-179.
    • (1993) J. Struct. Biol. , vol.111 , pp. 161-179
    • Watowich, S.J.1    Gross, L.J.2    Josephs, R.3
  • 18
    • 0031962235 scopus 로고    scopus 로고
    • Analysis of the stability of hemoglobin S double strands
    • Mu, X. Q., Makowski, L., and Magdoff-Fairchild, B. (1998) Analysis of the stability of hemoglobin S double strands. Biophys. J. 74, 655-668. (Pubitemid 28041794)
    • (1998) Biophysical Journal , vol.74 , Issue.1 , pp. 655-668
    • Mu, X.-Q.1    Makowski, L.2    Magdoff-Fairchild, B.3
  • 19
    • 0038397419 scopus 로고    scopus 로고
    • Twisted protein aggregates and disease: The stability of sickle hemoglobin fibers
    • Turner, M. S., Briehl, R. W., Ferrone, F. A., and Josephs, R. (2003) Twisted protein aggregates and disease: the stability of sickle hemoglobin fibers. Phys. Rev. Lett. 90, 128101-128107.
    • (2003) Phys. Rev. Lett. , vol.90 , pp. 128101-128107
    • Turner, M.S.1    Briehl, R.W.2    Ferrone, F.A.3    Josephs, R.4
  • 20
    • 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
  • 21
    • 0028920158 scopus 로고
    • Nucleation, fiber growth and melting, and domain formation and structure in sickle cell hemoglobin fibers
    • Briehl, R. W. (1995) Nucleation, fiber growth and melting, and domain formation and structure in sickle cell hemoglobin fibers. J. Mol. Biol. 245, 710-723.
    • (1995) J. Mol. Biol. , vol.245 , pp. 710-723
    • Briehl, R.W.1
  • 22
    • 0028044585 scopus 로고
    • Fragility and structure of hemoglobin S fibers and their consequences for geleation kinetics and rheology
    • Briehl, R. W., and Guzman, A. E. (1994) Fragility and structure of hemoglobin S fibers and their consequences for geleation kinetics and rheology. Blood 83, 573-579.
    • (1994) Blood , vol.83 , pp. 573-579
    • Briehl, R.W.1    Guzman, A.E.2
  • 24
    • 35548963401 scopus 로고    scopus 로고
    • Enthalpic and entropic stages in alpha-helical peptide unfolding, from laser T-jump/UV Raman spectroscopy
    • Balakrishnan, G., Hu, Y., Bender, G. M., Getahun, Z., DeGrado, W. F., and Spiro, T. G. (2007) Enthalpic and entropic stages in alpha-helical peptide unfolding, from laser T-jump/UV Raman spectroscopy. J. Am. Chem. Soc. 129, 12801-12808.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 12801-12808
    • Balakrishnan, G.1    Hu, Y.2    Bender, G.M.3    Getahun, Z.4    DeGrado, W.F.5    Spiro, T.G.6
  • 26
    • 0034812787 scopus 로고    scopus 로고
    • Transient UV Raman spectroscopy finds no crossing barrier between the peptide alpha-helix and fully random coil conformation
    • Lednev, I. K., Karnoup, A. S., Sparrow, M. C., and Asher, S. A. (2001) Transient UV Raman spectroscopy finds no crossing barrier between the peptide alpha-helix and fully random coil conformation. J. Am. Chem. Soc. 123, 2388-2392.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 2388-2392
    • Lednev, I.K.1    Karnoup, A.S.2    Sparrow, M.C.3    Asher, S.A.4
  • 27
    • 0032478198 scopus 로고    scopus 로고
    • Uv resonance raman-selective amide vibrational enhancement: Quantitative methodology for determining protein secondary structure
    • DOI 10.1021/bi971160z
    • Chi, Z., Chen, X. G., Holtz, J. S., and Asher, S. A. (1998) UV resonance Raman-selective amide vibrational enhancement: quantitative methodology for determining protein secondary structure. Biochemistry 37, 2854-2864. (Pubitemid 28145738)
    • (1998) Biochemistry , vol.37 , Issue.9 , pp. 2854-2864
    • Chi, Z.1    Chen, X.G.2    Holtz, J.S.W.3    Asher, S.A.4
  • 28
    • 33746603928 scopus 로고    scopus 로고
    • 10-helical peptide reveals a rough energy landscape
    • DOI 10.1021/bi060858m
    • Ahmed, Z., and Asher, S. A. (2006) UV resonance Raman investigation of a 3(10)-helical peptide reveals a rough energy landscape. Biochemistry 45, 9068-9073. (Pubitemid 44156369)
    • (2006) Biochemistry , vol.45 , Issue.30 , pp. 9068-9073
    • Ahmed, Z.1    Asher, S.A.2
  • 29
    • 0028308524 scopus 로고
    • Time-resolved resonance Raman spectroscopy as probe of structure, dynamics, and reactivity in hemoglobin
    • DOI 10.1016/0076-6879(94)32049-7
    • Friedman, J. M. (1994) Time-resolved resonance Raman spectroscopy as probe of structure, dynamics, and reactivity in hemoglobin. Methods Enzymol. 232, 205-231. (Pubitemid 24177502)
    • (1994) Methods in Enzymology , vol.232 , pp. 205-231
    • Friedman, J.M.1
  • 30
    • 21344452300 scopus 로고    scopus 로고
    • Proteins in motion: Resonance Raman spectroscopy as a probe of functional intermediates
    • Samuni, U., and Friedman, J. M. (2005) Proteins in motion: resonance Raman spectroscopy as a probe of functional intermediates. Methods Mol. Biol. 305, 287-300.
    • (2005) Methods Mol. Biol. , vol.305 , pp. 287-300
    • Samuni, U.1    Friedman, J.M.2
  • 31
    • 3042660617 scopus 로고    scopus 로고
    • Hemoglobin site-mutants reveal dynamical role of interhelical H-bonds in the allosteric pathway: Time-resolved UV resonance Raman evidence for intradimer coupling
    • Balakrishnan, G., Tsai, C. H., Wu, Q., Case, M. A., Pevsner, A., McLendon, G. L., Ho, C., and Spiro, T. G. (2004) Hemoglobin site-mutants reveal dynamical role of interhelical H-bonds in the allosteric pathway: time-resolved UV resonance Raman evidence for intradimer coupling. J. Mol. Biol. 340, 857-868.
    • (2004) J. Mol. Biol. , vol.340 , pp. 857-868
    • Balakrishnan, G.1    Tsai, C.H.2    Wu, Q.3    Case, M.A.4    Pevsner, A.5    McLendon, G.L.6    Ho, C.7    Spiro, T.G.8
  • 32
    • 0033653524 scopus 로고    scopus 로고
    • Kinetics of hemoglobin allostery from time-resolved UV resonance Raman spectroscopy: Effect of a chemical cross link
    • Zhao, X., Balakrishnan, G., Moore, E. G., and Spiro, T. G. (2000) Kinetics of hemoglobin allostery from time-resolved UV resonance Raman spectroscopy: effect of a chemical cross link. J. Raman Spectrosc. 31, 349-352.
    • (2000) J. Raman Spectrosc. , vol.31 , pp. 349-352
    • Zhao, X.1    Balakrishnan, G.2    Moore, E.G.3    Spiro, T.G.4
  • 33
    • 0000967751 scopus 로고
    • Hemoglobin R to T structural dynamics from simultaneous monitoring of tyrosine and tryptophan time-resolved UV resonance Raman signals
    • Rodgers, K. R., Su, C., Subramaniam, S., and Spiro, T. (1992) Hemoglobin R to T structural dynamics from simultaneous monitoring of tyrosine and tryptophan time-resolved UV resonance Raman signals. J. Am. Chem. Soc. 114, 3697-3709.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 3697-3709
    • Rodgers, K.R.1    Su, C.2    Subramaniam, S.3    Spiro, T.4
  • 34
    • 6444222269 scopus 로고    scopus 로고
    • Time-resolved resonance Raman study of Hb a with 220 nm excitation: Probing phenylalanine
    • Kneipp, J., Balakrishnan, G., and Spiro, T. G. (2004) Time-resolved resonance Raman study of Hb A with 220 nm excitation: probing phenylalanine. J. Phys. Chem. B 108, 15919-15927.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 15919-15927
    • Kneipp, J.1    Balakrishnan, G.2    Spiro, T.G.3
  • 35
    • 0036296098 scopus 로고    scopus 로고
    • Time-resolved resonance Raman study on ultrafast structural relaxation and vibrational cooling of photodissociated carbonmonoxy myoglobin
    • DOI 10.1002/bip.10096
    • Kitagawa, T., Haruta, N., and Mizutani, Y. (2002) Time-resolved resonance Raman study on ultrafast structural relaxation and vibrational cooling of photodissociated carbonmonoxy myoglobin. Biopolymers 67, 207-213. (Pubitemid 34712510)
    • (2002) Biopolymers - Biospectroscopy Section , vol.67 , Issue.4-5 , pp. 207-213
    • Kitagawa, T.1    Haruta, N.2    Mizutani, Y.3
  • 36
    • 0028799067 scopus 로고
    • Hemoglobin allostery: Resonance Raman spectroscopy of kinetic intermediates
    • Jayaraman, V., Rodgers, K. R., Mukerji, I., and Spiro, T. G. (1995) Hemoglobin allostery: resonance Raman spectroscopy of kinetic intermediates. Science 269, 1843-1848.
    • (1995) Science , vol.269 , pp. 1843-1848
    • Jayaraman, V.1    Rodgers, K.R.2    Mukerji, I.3    Spiro, T.G.4
  • 37
    • 33947312669 scopus 로고    scopus 로고
    • The role of beta 93 Cys in the inhibition of Hb S fiber formation
    • Knee, K. M., Roden, C. K., Flory, M. R., and Mukerji, I. (2007) The role of beta 93 Cys in the inhibition of Hb S fiber formation. Biophys. Chem. 127, 181-193.
    • (2007) Biophys. Chem. , vol.127 , pp. 181-193
    • Knee, K.M.1    Roden, C.K.2    Flory, M.R.3    Mukerji, I.4
  • 38
    • 0034319649 scopus 로고    scopus 로고
    • Structure of sickle cell hemoglobin fibers probed with UV resonance Raman spectroscopy
    • Sokolov, L., and Mukerji, I. (2000) Structure of sickle cell hemoglobin fibers probed with UV resonance Raman spectroscopy. J. Phys. Chem. B 104, 10835-10843.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 10835-10843
    • Sokolov, L.1    Mukerji, I.2
  • 39
    • 34247579524 scopus 로고    scopus 로고
    • The first step of hen egg white lysozyme fibrillation, irreversible partial unfolding, is a two-state transition
    • DOI 10.1110/ps.062639307
    • Xu, M., Shashilov, V. A., Ermolenkov, V. V., Fredriksen, L., Zagorevski, D., and Lednev, I. K. (2007) The first step of hen egg white lysozyme fibrillation, irreversible partial unfolding, is a two-state transition. Protein Sci. 16, 815-832. (Pubitemid 46683187)
    • (2007) Protein Science , vol.16 , Issue.5 , pp. 815-832
    • Xu, M.1    Shashilov, V.A.2    Ermolenkov, V.V.3    Fredriksen, L.4    Zagorevski, D.5    Lednev, I.K.6
  • 40
    • 34250172716 scopus 로고    scopus 로고
    • Probing a fibrillation nucleus directly by deep ultraviolet Raman spectroscopy
    • Shashilov, V., Xu, M., Ermolenkov, V. V., Fredriksen, L., and Lednev, I. K. (2007) Probing a fibrillation nucleus directly by deep ultraviolet Raman spectroscopy. J. Am. Chem. Soc. 129, 6972-6973.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 6972-6973
    • Shashilov, V.1    Xu, M.2    Ermolenkov, V.V.3    Fredriksen, L.4    Lednev, I.K.5
  • 41
    • 3042521090 scopus 로고    scopus 로고
    • Time-resolved absorption and UV resonance Raman spectra reveal stepwise formation of T quaternary contacts in the allosteric pathway of hemoglobin
    • Balakrishnan, G., Case, M. A., Pevsner, A., Zhao, X., Tengroth, C., McLendon, G. L., and Spiro, T. G. (2004) Time-resolved absorption and UV resonance Raman spectra reveal stepwise formation of T quaternary contacts in the allosteric pathway of hemoglobin. J. Mol. Biol. 340, 843-856.
    • (2004) J. Mol. Biol. , vol.340 , pp. 843-856
    • Balakrishnan, G.1    Case, M.A.2    Pevsner, A.3    Zhao, X.4    Tengroth, C.5    McLendon, G.L.6    Spiro, T.G.7
  • 43
    • 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
  • 44
    • 0018679997 scopus 로고
    • Nucleation-controlled aggregation of deoxyhemoglobin S. Possible difference in the size of nuclei in different phosphate concentrations
    • Adachi, K., and Asakura, T. (1979) Nucleation-controlled aggregation of deoxyhemoglobin S. Possible difference in the size of nuclei in different phosphate concentrations. J. Biol. Chem. 254, 7765-7771.
    • (1979) J. Biol. Chem. , vol.254 , pp. 7765-7771
    • Adachi, K.1    Asakura, T.2
  • 45
    • 0020397654 scopus 로고
    • Kinetics of the polymerization of hemoglobin in high and low phosphate buffers
    • Adachi, K., and Asakura, T. (1982) Kinetics of the polymerization of hemoglobin in high and low phosphate buffers. Blood Cells 8, 213-224. (Pubitemid 13203931)
    • (1982) Blood Cells , vol.8 , Issue.2 , pp. 213-224
    • Adachi, K.1    Asakura, T.2
  • 48
    • 0034044670 scopus 로고    scopus 로고
    • Solubility of fluoromethemoglobin S: Effect of phosphate and temperature on polymerization
    • Yohe, M. E., Sheffield, K. M., and Mukerji, I. (2000) Solubility of fluoromethemoglobin S: effect of phosphate and temperature on polymerization. Biophys. J. 78, 3218-3226. (Pubitemid 30396950)
    • (2000) Biophysical Journal , vol.78 , Issue.6 , pp. 3218-3226
    • Yohe, M.E.1    Sheffield, K.M.2    Mukerji, I.3
  • 49
    • 10044231883 scopus 로고    scopus 로고
    • Aggregation of normal and sickle hemoglobin in high concentration phosphate buffer
    • DOI 10.1529/biophysj.104.046482
    • Chen, K., Ballas, S. K., Hantgan, R. R., and Kim-Shapiro, D. B. (2004) Aggregation of normal and sickle hemoglobin in high concentration phosphate buffer. Biophys. J. 87, 4113-4121. (Pubitemid 39602915)
    • (2004) Biophysical Journal , vol.87 , Issue.6 , pp. 4113-4121
    • Chen, K.1    Ballas, S.K.2    Hantgan, R.R.3    Kim-Shapiro, D.B.4
  • 50
    • 10244252826 scopus 로고    scopus 로고
    • Polymerization and sickle cell disease: A molecular view
    • DOI 10.1080/10739680490278312
    • Ferrone, F. A. (2004) Polymerization and sickle cell disease: a molecular view. Microcirculation 11, 115-128. (Pubitemid 39619074)
    • (2004) Microcirculation , vol.11 , Issue.2 , pp. 115-128
    • Ferrone, F.A.1
  • 51
    • 20144376843 scopus 로고    scopus 로고
    • Intersubunit interactions associated with Tyr42 alpha stabilize the quaternary-T tetramer but are not major quaternary constraints in deoxyhemoglobin
    • DOI 10.1021/bi0484670
    • Kavanaugh, J. S., Rogers, P. H., Arnone, A., Hui, H. L., Wierzba, A., DeYoung, A., Kwiatkowski, L. D., Noble, R. W., Juszczak, L. J., Peterson, E. S., and Friedman, J. M. (2005) Intersubunit interactions associated with Tyr42 alpha stabilize the quaternary-T tetramer but are not major quaternary constraints in deoxyhemoglobin. Biochemistry 44, 3806-3820. (Pubitemid 40358033)
    • (2005) Biochemistry , vol.44 , Issue.10 , pp. 3806-3820
    • Kavanaugh, J.S.1    Rogers, P.H.2    Arnone, A.3    Hui, H.L.4    Wierzba, A.5    Deyoung, A.6    Kwiatkowski, L.D.7    Noble, R.W.8    Juszczak, L.J.9    Peterson, E.S.10    Friedman, J.M.11
  • 52
    • 0033604830 scopus 로고    scopus 로고
    • Quaternary structure sensitive tyrosine residues in human hemoglobin: UV resonance Raman studies of mutants at α140, β35 and β145 tyrosine
    • Nagai, M., Wajcman, H., Lahary, A., Nakatsukasa, T., Nagatomo, S., and Kitagawa, T. (1999) Quaternary structure sensitive tyrosine residues in human hemoglobin: UV resonance Raman studies of mutants at α140, β35 and β145 tyrosine. Biochemistry 38, 1243-1251.
    • (1999) Biochemistry , vol.38 , pp. 1243-1251
    • Nagai, M.1    Wajcman, H.2    Lahary, A.3    Nakatsukasa, T.4    Nagatomo, S.5    Kitagawa, T.6
  • 53
    • 0019157117 scopus 로고
    • Proton longitudinal relaxation investigation of histidyl residues of normal human adult and sickle deoxyhemoglobin: Evidence for the existence of pregelation aggregates in sickle deoxyhemoglobin solutions
    • Russu, I. M., and Ho, C. (1980) Proton longitudinal relaxation investigation of histidyl residues of normal human adult and sickle deoxyhemoglobin: evidence for the existence of pregelation aggregates in sickle deoxyhemoglobin solutions. Proc. Natl. Acad. Sci. U.S.A. 77, 6577-6581.
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 6577-6581
    • Russu, I.M.1    Ho, C.2
  • 54
    • 1542375225 scopus 로고    scopus 로고
    • Liquid-Liquid Phase Separation in Hemoglobins: Distinct Aggregation Mechanisms of the β6 Mutants
    • Chen, Q., Vekilov, P. G., Nagel, R. L., and Hirsch, R. E. (2004) Liquid-liquid phase separation in hemoglobins: distinct aggregation mechanisms of the β6 mutants. Biophys. J. 86, 1702-1712. (Pubitemid 38295605)
    • (2004) Biophysical Journal , vol.86 , Issue.3 , pp. 1702-1712
    • Chen, Q.1    Vekilov, P.G.2    Nagel, R.L.3    Hirsch, R.E.4
  • 55
    • 0018627161 scopus 로고
    • Gelation of deoxyhemoglobin a in concentrated phosphate buffer
    • Adachi, K., and Asakura, T. (1979) Gelation of deoxyhemoglobin A in concentrated phosphate buffer. J. Biol. Chem. 254, 12273-12276.
    • (1979) J. Biol. Chem. , vol.254 , pp. 12273-12276
    • Adachi, K.1    Asakura, T.2
  • 56
    • 0027281288 scopus 로고
    • On the formation and crystallization of sickle hemoglobin macrofibers
    • McDade, W. A., and Josephs, R. (1993) On the formation and crystallization of sickle hemoglobin macrofibers. J. Struct. Biol. 110, 90-97.
    • (1993) J. Struct. Biol. , vol.110 , pp. 90-97
    • McDade, W.A.1    Josephs, R.2
  • 57
    • 0023885041 scopus 로고
    • Structural analysis of polymers of sickle cell hemoglobin. III. Fibers within fascicles
    • Carragher, B., Bluemke, D. A., Becker, M., McDade, W. A., Potel, M. J., and Josephs, R. (1988) Structural analysis of polymers of sickle cell hemoglobin. III. Fibers within fascicles. J. Mol. Biol. 199, 383-388.
    • (1988) J. Mol. Biol. , vol.199 , pp. 383-388
    • Carragher, B.1    Bluemke, D.A.2    Becker, M.3    McDade, W.A.4    Potel, M.J.5    Josephs, R.6
  • 58
    • 0024388204 scopus 로고
    • Intermolecular contacts within sickle hemoglobin fibers
    • Watowich, S. J., Gross, L. J., and Josephs, R. (1989) Intermolecular contacts within sickle hemoglobin fibers. J. Mol. Biol. 209, 821-828.
    • (1989) J. Mol. Biol. , vol.209 , pp. 821-828
    • Watowich, S.J.1    Gross, L.J.2    Josephs, R.3
  • 60
    • 0028881772 scopus 로고
    • Carbon monoxide religation kinetics to hemoglobin S polymers following ligand photolysis
    • Shapiro, D. B., Esquerra, R. M., Goldbeck, R. A., Ballas, S. K., Mohandas, N., and Kliger, D. S. (1995) Carbon monoxide religation kinetics to hemoglobin S polymers following ligand photolysis. J. Biol. Chem. 270, 26078-26085.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26078-26085
    • Shapiro, D.B.1    Esquerra, R.M.2    Goldbeck, R.A.3    Ballas, S.K.4    Mohandas, N.5    Kliger, D.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.