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Volumn 412, Issue , 2006, Pages 285-299

Nucleation: The Connections Between Equilibrium and Kinetic Behavior

(1)  Ferrone, Frank A a  

a NONE

Author keywords

[No Author keywords available]

Indexed keywords

HEMOGLOBIN;

EID: 33749597429     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(06)12017-0     Document Type: Review
Times cited : (55)

References (14)
  • 2
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    • Homogeneous nucleation in sickle hemoglobin. Stochastic measurements with a parallel method
    • Cao Z., and Ferrone F.A. Homogeneous nucleation in sickle hemoglobin. Stochastic measurements with a parallel method. Biophys. J. 72 (1997) 343-372
    • (1997) Biophys. J. , vol.72 , pp. 343-372
    • Cao, Z.1    Ferrone, F.A.2
  • 3
    • 0018744120 scopus 로고
    • Three dimensional reconstruction of 14-filament fibers of hemoglobin S
    • Dykes G.W., Crepeau R.H., and Edelstein S.J. Three dimensional reconstruction of 14-filament fibers of hemoglobin S. J. Mol. Biol. 130 (1979) 451-472
    • (1979) J. Mol. Biol. , vol.130 , pp. 451-472
    • Dykes, G.W.1    Crepeau, R.H.2    Edelstein, S.J.3
  • 4
    • 0032877134 scopus 로고    scopus 로고
    • Analysis of protein aggregation kinetics
    • Ferrone F. Analysis of protein aggregation kinetics. Methods Enzymol. 309 (1999) 256-274
    • (1999) Methods Enzymol. , vol.309 , pp. 256-274
    • Ferrone, F.1
  • 5
    • 0021837479 scopus 로고
    • Kinetics of sickle hemoglobin polymerization II: A double nucleation mechanism
    • Ferrone F.A., Hofrichter J., and Eaton W.A. Kinetics of sickle hemoglobin polymerization II: A double nucleation mechanism. J. Mol. Biol. 183 (1985) 611-631
    • (1985) J. Mol. Biol. , vol.183 , pp. 611-631
    • Ferrone, F.A.1    Hofrichter, J.2    Eaton, W.A.3
  • 6
    • 0019072559 scopus 로고
    • Kinetic studies on photolysis-induced gelation of sickle cell hemoglobin suggest a new mechanism
    • Ferrone F.A., Hofrichter J., Sunshine H., and 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
  • 7
    • 0036220417 scopus 로고    scopus 로고
    • Heterogeneous nucleation and crowding in sickle hemoglobin: An analytic approach
    • Ferrone F.A., Ivanova M., and Jasuja R. Heterogeneous nucleation and crowding in sickle hemoglobin: An analytic approach. Biophys. J. 82 (2002) 399-406
    • (2002) Biophys. J. , vol.82 , pp. 399-406
    • Ferrone, F.A.1    Ivanova, M.2    Jasuja, R.3
  • 8
    • 4544329005 scopus 로고    scopus 로고
    • Crowding and the polymerization of sickle hemoglobin
    • Ferrone F.A., and Rotter M.A. Crowding and the polymerization of sickle hemoglobin. J. Mol. Recognition 17 (2004) 497-504
    • (2004) J. Mol. Recognition , vol.17 , pp. 497-504
    • Ferrone, F.A.1    Rotter, M.A.2
  • 9
    • 0042717373 scopus 로고
    • Geometric Basis of Phase Change
    • Ginnel R. Geometric Basis of Phase Change. J. Chem. Phys. 34 (1961) 992-998
    • (1961) J. Chem. Phys. , vol.34 , pp. 992-998
    • Ginnel, R.1
  • 14
    • 0041817542 scopus 로고    scopus 로고
    • The amyloid beta peptide (Abeta(1-40)) is thermodynamically soluble at physiological concentrations
    • Sengupta P., Garai K., Sahoo B., Shi Y., Callaway D.J., and Maiti S. The amyloid beta peptide (Abeta(1-40)) is thermodynamically soluble at physiological concentrations. Biochemistry 42 (2003) 10506-10513
    • (2003) Biochemistry , vol.42 , pp. 10506-10513
    • Sengupta, P.1    Garai, K.2    Sahoo, B.3    Shi, Y.4    Callaway, D.J.5    Maiti, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.