메뉴 건너뛰기




Volumn 411, Issue 1, 2011, Pages 275-285

Amyloid fibrillation kinetics: Insight from atomistic nucleation theory

Author keywords

amyloid fibrils; homogeneous nucleation; nucleation rate; nucleus size; protein aggregation

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN[1-40]; BETA 2 MICROGLOBULIN;

EID: 79960698583     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.05.032     Document Type: Article
Times cited : (34)

References (64)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • Chiti F., and Dobson C.M. Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366 (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 34547316314 scopus 로고    scopus 로고
    • Self-assembled peptide nanostructures: The design of molecular building blocks and their technological utilization
    • Gazit E. Self-assembled peptide nanostructures: the design of molecular building blocks and their technological utilization Chem. Soc. Rev. 36 2007 1263 1269
    • (2007) Chem. Soc. Rev. , vol.36 , pp. 1263-1269
    • Gazit, E.1
  • 4
    • 40849120669 scopus 로고    scopus 로고
    • Amyloid fibrils of the HET-s(218-289) prion form a β solenoid with a triangular hydrophobic core
    • DOI 10.1126/science.1151839
    • Wasmer C., Lange A., Van Melckebeke H., Siemer A.B., Riek R., and Meier B.H. Amyloid fibrils of the HET-s(218-289) prion form a β solenoid with a triangular hydrophobic core Science 319 2008 1523 1526 (Pubitemid 351398180)
    • (2008) Science , vol.319 , Issue.5869 , pp. 1523-1526
    • Wasmer, C.1    Lange, A.2    Van Melckebeke, H.3    Siemer, A.B.4    Riek, R.5    Meier, B.H.6
  • 5
    • 0016369152 scopus 로고
    • Kinetics and mechanism of deoxyhemoglobin S gelation: A new approach to understanding sickle cell disease
    • Hofrichter J., Ross P.D., and Eaton W.A. Kinetics and mechanism of deoxyhemoglobin S gelation: a new approach to understanding sickle cell disease Proc. Natl Acad. Sci. USA 71 1974 4864 4868
    • (1974) Proc. Natl Acad. Sci. USA , vol.71 , pp. 4864-4868
    • Hofrichter, J.1    Ross, P.D.2    Eaton, W.A.3
  • 6
    • 0021815445 scopus 로고
    • Kinetics of sickle hemoglobin polymerization. I. Studies using temperature-jump and laser photolysis techniques
    • DOI 10.1016/0022-2836(85)90174-3
    • Ferrone F.A., Hofrichter J., and Eaton W.A. Kinetics of sickle hemoglobin polymerization. I. Studies using temperature-jump and laser photolysis techniques J. Mol. Biol. 183 1985 591 610 (Pubitemid 15036850)
    • (1985) Journal of Molecular Biology , vol.183 , Issue.4 , pp. 591-610
    • Ferrone, F.A.1    Hofrichter, J.2    Eaton, W.A.3
  • 7
    • 0021837479 scopus 로고
    • Kinetics of sickle hemoglobin polymerization. II. A double nucleation mechanism
    • DOI 10.1016/0022-2836(85)90175-5
    • 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 (Pubitemid 15036851)
    • (1985) Journal of Molecular Biology , vol.183 , Issue.4 , pp. 611-631
    • Ferrone, F.A.1    Hofrichter, J.2    Eaton, W.A.3
  • 8
    • 0023042358 scopus 로고
    • Kinetics of sickle hemoglobin polymerization. III. Nucleation rates determined from stochastic fluctuations in polymerization progress curves
    • Hofrichter J. Kinetics of sickle hemoglobin polymerization. III. Nucleation rates determined from stochastic fluctuations in polymerization progress curves J. Mol. Biol. 189 1986 553 571
    • (1986) J. Mol. Biol. , vol.189 , pp. 553-571
    • Hofrichter, J.1
  • 9
    • 0027195933 scopus 로고
    • Seeding 'one-dimensional crystallization' of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • DOI 10.1016/0092-8674(93)90635-4
    • Jarrett J.T., and Lansbury P.T. Jr Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73 1993 1055 1058 (Pubitemid 23180480)
    • (1993) Cell , vol.73 , Issue.6 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 12
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • DOI 10.1146/annurev.biochem.66.1.385
    • Harper J.D., and Lansbury P.T. Jr Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins Annu. Rev. Biochem. 66 1997 385 407 (Pubitemid 27274662)
    • (1997) Annual Review of Biochemistry , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 13
    • 1642434114 scopus 로고    scopus 로고
    • Mechanisms of Homogeneous Nucleation of Polymers of Sickle Cell Anemia Hemoglobin in Deoxy State
    • DOI 10.1016/j.jmb.2003.12.019
    • Galkin O., and Vekilov P.G. Mechanisms of homogeneous nucleation of polymers of sickle cell anemia hemoglobin in deoxy state J. Mol. Biol. 336 2004 43 59 (Pubitemid 38111176)
    • (2004) Journal of Molecular Biology , vol.336 , Issue.1 , pp. 43-59
    • Galkin, O.1    Vekilov, P.G.2
  • 14
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated conformational conversion and the replication of conformational information by a prion determinant
    • DOI 10.1126/science.289.5483.1317
    • Serio T.R., Cashikar A.G., Kowal A.S., Sawicki G.J., Moslehi J.J., and Serpell L. Nucleated conformational conversion and the replication of conformational information by a prion determinant Science 289 2000 1317 1321 (Pubitemid 30656041)
    • (2000) Science , vol.289 , Issue.5483 , pp. 1317-1321
    • Serio, T.R.1    Cashikar, A.G.2    Kowal, A.S.3    Sawicki, G.J.4    Moslehi, J.J.5    Serpell, L.6    Arnsdorf, M.F.7    Lindquist, S.L.8
  • 16
    • 15744382287 scopus 로고    scopus 로고
    • Kinetics of fibril formation by polyalanine peptides
    • DOI 10.1074/jbc.M407338200
    • Nguyen H.D., and Hall C.K. Kinetics of fibril formation by polyalanine peptides J. Biol. Chem. 280 2005 9074 9082 (Pubitemid 40409601)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.10 , pp. 9074-9082
    • Nguyen, H.D.1    Hall, C.K.2
  • 17
    • 33244456166 scopus 로고    scopus 로고
    • Spontaneous fibril formation by polyalanines; discontinuous molecular dynamics simulations
    • DOI 10.1021/ja0539140
    • Nguyen H.D., and Hall C.K. Spontaneous fibril formation by polyalanines; discontinuous molecular dynamics simulations J. Am. Chem. Soc. 128 2006 1890 1901 (Pubitemid 43277329)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.6 , pp. 1890-1901
    • Nguyen, H.D.1    Hall, C.K.2
  • 18
    • 33749597429 scopus 로고    scopus 로고
    • Nucleation: The Connections Between Equilibrium and Kinetic Behavior
    • DOI 10.1016/S0076-6879(06)12017-0, PII S0076687906120170
    • Ferrone F.A. Nucleation: the connections between equilibrium and kinetic behavior Methods Enzymol. 412 2006 285 299 (Pubitemid 44548586)
    • (2006) Methods in Enzymology , vol.412 , pp. 285-299
    • Ferrone, F.A.1
  • 19
    • 33751513333 scopus 로고    scopus 로고
    • The Kinetics of Nucleation and Growth of Sickle Cell Hemoglobin Fibers
    • DOI 10.1016/j.jmb.2006.10.001, PII S002228360601326X
    • Galkin O., Nagel R.L., and Vekilov P.G. The kinetics of nucleation and growth of sickle cell hemoglobin fibers J. Mol. Biol. 365 2007 425 439 (Pubitemid 44838716)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.2 , pp. 425-439
    • Galkin, O.1    Nagel, R.L.2    Vekilov, P.G.3
  • 21
    • 62549097355 scopus 로고    scopus 로고
    • Characterization of the nucleation barriers for protein aggregation and amyloid formation
    • Auer S., Dobson C.M., and Vendruscolo M. Characterization of the nucleation barriers for protein aggregation and amyloid formation HFSP J. 1 2007 137 146
    • (2007) HFSP J. , vol.1 , pp. 137-146
    • Auer, S.1    Dobson, C.M.2    Vendruscolo, M.3
  • 22
    • 58049115628 scopus 로고    scopus 로고
    • Self-templated nucleation in peptide and protein aggregation
    • Auer S., Dobson C.M., Vendruscolo M., and Maritan A. Self-templated nucleation in peptide and protein aggregation Phys. Rev. Lett. 101 2008 258101
    • (2008) Phys. Rev. Lett. , vol.101 , pp. 258101
    • Auer, S.1    Dobson, C.M.2    Vendruscolo, M.3    Maritan, A.4
  • 23
    • 48249092311 scopus 로고    scopus 로고
    • Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly
    • Xue W.F., Homans S.W., and Radford S.E. Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly Proc. Natl Acad. Sci. USA 105 2008 8926 8931
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 8926-8931
    • Xue, W.F.1    Homans, S.W.2    Radford, S.E.3
  • 24
    • 38849136693 scopus 로고    scopus 로고
    • Quasihomogeneous nucleation of amyloid beta yields numerical bounds for the critical radius, the surface tension, and the free energy barrier for nucleus formation
    • Garai K., Sahoo B., Sengupta P., and Maiti S. Quasihomogeneous nucleation of amyloid beta yields numerical bounds for the critical radius, the surface tension, and the free energy barrier for nucleus formation J. Chem. Phys. 128 2008 045102
    • (2008) J. Chem. Phys. , vol.128 , pp. 045102
    • Garai, K.1    Sahoo, B.2    Sengupta, P.3    Maiti, S.4
  • 25
    • 58749109622 scopus 로고    scopus 로고
    • Simulations of nucleation and elongation of amyloid fibrils
    • Zhang J., and Muthukumar M. Simulations of nucleation and elongation of amyloid fibrils J. Chem. Phys. 130 2009 035102 035117
    • (2009) J. Chem. Phys. , vol.130 , pp. 035102-035117
    • Zhang, J.1    Muthukumar, M.2
  • 26
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism
    • DOI 10.1021/bi002555c
    • Nielsen L., Khurana R., Coats A., Frokjaer S., Brange J., and Vyas S. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism Biochemistry 40 2001 6036 6046 (Pubitemid 32466306)
    • (2001) Biochemistry , vol.40 , Issue.20 , pp. 6036-6046
    • Nielsen, L.1    Khurana, R.2    Coats, A.3    Frokjaer, S.4    Brange, J.5    Vyas, S.6    Uversky, V.N.7    Fink, A.L.8
  • 28
    • 0037453298 scopus 로고    scopus 로고
    • Relationship between stability of folding intermediates and amyloid formation for the yeast prion Ure2p: A quantitative analysis of the effects of pH and buffer system
    • DOI 10.1016/S0022-2836(03)00249-3
    • Zhu L., Zhang X.J., Wang L.Y., Zhou J.M., and Perrett S. Relationship between stability of folding intermediates and amyloid formation for the yeast prion Ure2p: a quantitative analysis of the effects of pH and buffer system J. Mol. Biol. 328 2003 235 254 (Pubitemid 36390293)
    • (2003) Journal of Molecular Biology , vol.328 , Issue.1 , pp. 235-254
    • Zhu, L.1    Zhang, X.-J.2    Wang, L.-Y.3    Zhou, J.-M.4    Perrett, S.5
  • 30
    • 23644450224 scopus 로고    scopus 로고
    • Mutagenic analysis of the nucleation propensity of oxidized Alzheimer's β-amyloid peptide
    • DOI 10.1110/ps.051470405
    • Christopeit T., Hortschansky P., Schroeckh V., Gührs K., Zandomeneghi G., and Fändrich M. Mutagenic analysis of the nucleation propensity of oxidized Alzheimer's β-amyloid peptide Protein Sci. 14 2005 2125 2131 (Pubitemid 41132378)
    • (2005) Protein Science , vol.14 , Issue.8 , pp. 2125-2131
    • Christopeit, T.1    Hortschansky, P.2    Schroeckh, V.3    Guhrs, K.4    Zandomeneghi, G.5    Fandrich, M.6
  • 31
    • 22244439242 scopus 로고    scopus 로고
    • The aggregation kinetics of Alzheimer's β-amyloid peptide is controlled by stochastic nucleation
    • DOI 10.1110/ps.041266605
    • Hortschansky P., Schroeckh V., Christopeit T., Zandomeneghi G., and Fandrich M. The aggregation kinetics of Alzheimer's β-amyloid peptide is controlled by stochastic nucleation Protein Sci. 14 2005 1753 1759 (Pubitemid 40994145)
    • (2005) Protein Science , vol.14 , Issue.7 , pp. 1753-1759
    • Hortschansky, P.1    Schroeckh, V.2    Christopeit, T.3    Zandomeneghi, G.4    Fandrich, M.5
  • 32
    • 33846005437 scopus 로고    scopus 로고
    • Absolute Correlation between Lag Time and Growth Rate in the Spontaneous Formation of Several Amyloid-like Aggregates and Fibrils
    • DOI 10.1016/j.jmb.2006.11.009, PII S0022283606015385
    • Fändrich M. Absolute correlation between lag time and growth rate in the spontaneous formation of several amyloid-like aggregates and fibrils J. Mol. Biol. 365 2007 1266 1270 (Pubitemid 46048846)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.5 , pp. 1266-1270
    • Fandrich, M.1
  • 33
    • 33744937549 scopus 로고    scopus 로고
    • Sulfates dramatically stabilize a salt-dependent type of glucagon fibrils
    • DOI 10.1529/biophysj.105.070912
    • Pedersen J.S., Flink J.M., Dikov D., and Otzen D.E. Sulfates dramatically stabilize a salt-dependent type of glucagon fibrils Biophys. J. 90 2006 4181 4194 (Pubitemid 43846132)
    • (2006) Biophysical Journal , vol.90 , Issue.11 , pp. 4181-4194
    • Pedersen, J.S.1    Flink, J.M.2    Dikov, D.3    Otzen, D.E.4
  • 34
    • 30744469843 scopus 로고    scopus 로고
    • Solvation-assisted pressure tuning of insulin fibrillation: From novel aggregation pathways to biotechnological applications
    • DOI 10.1016/j.jmb.2005.11.075, PII S0022283605015111
    • Grudzielanek S., Smirnovas V., and Winter R. Solvation-assisted pressure tuning of insulin fibrillation: from novel aggregation pathways to biotechnological applications J. Mol. Biol. 356 2006 497 509 (Pubitemid 43099986)
    • (2006) Journal of Molecular Biology , vol.356 , Issue.2 , pp. 497-509
    • Grudzielanek, S.1    Smirnovas, V.2    Winter, R.3
  • 35
    • 65849165676 scopus 로고    scopus 로고
    • Competition between intramolecular and intermolecular interactions in an amyloid-forming protein
    • Routledge K.E., Tartaglia G.G., Platt G.W., Vendruscolo M., and Radford S.E. Competition between intramolecular and intermolecular interactions in an amyloid-forming protein J. Mol. Biol. 389 2009 776 786
    • (2009) J. Mol. Biol. , vol.389 , pp. 776-786
    • Routledge, K.E.1    Tartaglia, G.G.2    Platt, G.W.3    Vendruscolo, M.4    Radford, S.E.5
  • 37
    • 77951676986 scopus 로고    scopus 로고
    • Amyloid β-protein aggregation produces highly reproducible kinetic data and occurs by a two-phase process
    • Hellstrand E., Boland B., Walsh D.M., and Linse S. Amyloid β-protein aggregation produces highly reproducible kinetic data and occurs by a two-phase process ACS Chem. Neurosci. 1 2009 13 18
    • (2009) ACS Chem. Neurosci. , vol.1 , pp. 13-18
    • Hellstrand, E.1    Boland, B.2    Walsh, D.M.3    Linse, S.4
  • 38
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • DOI 10.1038/nature01891
    • Chiti F., Stefani M., Taddei N., Ramponi G., and Dobson C.M. Rationalization of the effects of mutations on peptide and protein aggregation rates Nature 424 2003 805 808 (Pubitemid 37021713)
    • (2003) Nature , vol.424 , Issue.6950 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddel, N.3    Ramponi, G.4    Dobson, C.M.5
  • 39
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • DOI 10.1038/nbt1012
    • Fernandez-Escamilla A.M., Rousseau F., Schymkowitz J., and Serrano L. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins Nat. Biotechnol. 22 2004 1302 1306 (Pubitemid 39336784)
    • (2004) Nature Biotechnology , vol.22 , Issue.10 , pp. 1302-1306
    • Fernandez-Escamilla, A.-M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 40
    • 33845978790 scopus 로고    scopus 로고
    • Insight into the structure of amyloid fibrils from the analysis of globular proteins
    • Trovato A., Chiti F., Maritan A., and Seno F. Insight into the structure of amyloid fibrils from the analysis of globular proteins PLoS Comput. Biol. 2 2006 e170
    • (2006) PLoS Comput. Biol. , vol.2 , pp. 170
    • Trovato, A.1    Chiti, F.2    Maritan, A.3    Seno, F.4
  • 42
    • 3342963982 scopus 로고    scopus 로고
    • Detecting hidden sequence propensity for amyloid fibril formation
    • DOI 10.1110/ps.04790604
    • Yoon S., and Welsh W.J. Detecting hidden sequence propensity for amyloid fibril formation Protein Sci. 13 2004 2149 2160 (Pubitemid 38989619)
    • (2004) Protein Science , vol.13 , Issue.8 , pp. 2149-2160
    • Yoon, S.1    Welsh, W.J.2
  • 43
    • 33748525884 scopus 로고    scopus 로고
    • Computational models for the prediction of polypeptide aggregation propensity
    • DOI 10.1016/j.cbpa.2006.07.009, PII S1367593106001104, Analytical Techniques/Mechanisms
    • Caflisch A. Computational models for the prediction of polypeptide aggregation propensity Curr. Opin. Chem. Biol. 10 2006 437 444 (Pubitemid 44375058)
    • (2006) Current Opinion in Chemical Biology , vol.10 , Issue.5 , pp. 437-444
    • Caflisch, A.1
  • 45
    • 77955792312 scopus 로고    scopus 로고
    • Insight into the correlation between lag time and aggregation rate in the kinetics of protein aggregation
    • Auer S., and Kashchiev D. Insight into the correlation between lag time and aggregation rate in the kinetics of protein aggregation Proteins 78 2010 2412 2416
    • (2010) Proteins , vol.78 , pp. 2412-2416
    • Auer, S.1    Kashchiev, D.2
  • 46
    • 77953556011 scopus 로고    scopus 로고
    • Nucleation of amyloid fibrils
    • Kashchiev D., and Auer S. Nucleation of amyloid fibrils J. Chem. Phys. 132 2010 215101
    • (2010) J. Chem. Phys. , vol.132 , pp. 215101
    • Kashchiev, D.1    Auer, S.2
  • 47
    • 78650335625 scopus 로고    scopus 로고
    • Atomistic theory of amyloid fibril nucleation
    • Cabriolu R., Kashchiev D., and Auer S. Atomistic theory of amyloid fibril nucleation J. Chem. Phys. 133 2010 225101 225112
    • (2010) J. Chem. Phys. , vol.133 , pp. 225101-225112
    • Cabriolu, R.1    Kashchiev, D.2    Auer, S.3
  • 51
    • 2942748436 scopus 로고    scopus 로고
    • Oligomeric assembly of native-like precursors precedes amyloid formation by β-2 microglobulin
    • DOI 10.1021/bi049792q
    • Eakin C.M., Attenello F.J., Morgan C.J., and Miranker A.D. Oligomeric assembly of native-like precursors precedes amyloid formation by β-2 microglobulin Biochemistry 43 2004 7808 7815 (Pubitemid 38787688)
    • (2004) Biochemistry , vol.43 , Issue.24 , pp. 7808-7815
    • Eakin, C.M.1    Attenello, F.J.2    Morgan, C.J.3    Miranker, A.D.4
  • 53
    • 33644813233 scopus 로고    scopus 로고
    • A native to amyloidogenic transition regulated by a backbone trigger
    • DOI 10.1038/nsmb1068, PII N1068
    • Eakin C.M., Berman A.J., and Miranker A.D. A native to amyloidogenic transition regulated by a backbone trigger Nat. Struct. Mol. Biol. 13 2006 202 208 (Pubitemid 43348505)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.3 , pp. 202-208
    • Eakin, C.M.1    Berman, A.J.2    Miranker, A.D.3
  • 54
    • 77952759080 scopus 로고    scopus 로고
    • Stacked sets of parallel, in-register beta-strands of beta-2-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling
    • Ladner C.L., Chen M., Smith D.P., Platt G.W., Radford S.E., and Langen R. Stacked sets of parallel, in-register beta-strands of beta-2-microglobulin in amyloid fibrils revealed by site-directed spin labeling and chemical labeling J. Biol. Chem. 285 2010 17137 17147
    • (2010) J. Biol. Chem. , vol.285 , pp. 17137-17147
    • Ladner, C.L.1    Chen, M.2    Smith, D.P.3    Platt, G.W.4    Radford, S.E.5    Langen, R.6
  • 55
    • 78650982368 scopus 로고    scopus 로고
    • 2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages
    • 2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages Nat. Struct. Mol. Biol. 18 2011 49 55
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 49-55
    • Liu, C.1    Sawaya, M.R.2    Eisenberg, D.3
  • 56
    • 55349095013 scopus 로고    scopus 로고
    • Toward a better description of the nucleation rate of crystals and crystalline monolayers
    • Kashchiev D. Toward a better description of the nucleation rate of crystals and crystalline monolayers J. Chem. Phys. 129 2008 164701
    • (2008) J. Chem. Phys. , vol.129 , pp. 164701
    • Kashchiev, D.1
  • 57
    • 0021828928 scopus 로고
    • Hydrogen bonding and biological specificity analysed by protein engineering
    • DOI 10.1038/314235a0
    • Fersht A.R., Shi J.P., Knill-Jones J., Lowe D.M., Wilkinson A.J., and Blow D.M. Hydrogen bonding and biological specificity analysed by protein engineering Nature 314 1985 235 238 (Pubitemid 15076511)
    • (1985) Nature , vol.314 , Issue.6008 , pp. 235-238
    • Fersht, A.R.1    Shi, J.P.2    Knill-Jones, J.3
  • 58
    • 36749114484 scopus 로고
    • On the relation between nucleation work, nucleus size, and nucleation rate
    • Kashchiev D. On the relation between nucleation work, nucleus size, and nucleation rate J. Chem. Phys. 76 1982 5098 5102
    • (1982) J. Chem. Phys. , vol.76 , pp. 5098-5102
    • Kashchiev, D.1
  • 60
    • 77649240855 scopus 로고    scopus 로고
    • Identifying the amylome, proteins capable of forming amyloid-like fibrils
    • Goldschmidt L., Teng P.K., Riek R., and Eisenberg D. Identifying the amylome, proteins capable of forming amyloid-like fibrils Proc. Natl Acad. Sci. USA 107 2010 3487 3492
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 3487-3492
    • Goldschmidt, L.1    Teng, P.K.2    Riek, R.3    Eisenberg, D.4
  • 63
    • 0029376152 scopus 로고
    • The interaction energy between two protein molecules related to physical properties of their solution and their crystals and implications for crystal growth
    • Haas C., and Drenth J. The interaction energy between two protein molecules related to physical properties of their solution and their crystals and implications for crystal growth J. Cryst. Growth 154 1995 126 135
    • (1995) J. Cryst. Growth , vol.154 , pp. 126-135
    • Haas, C.1    Drenth, J.2
  • 64
    • 77951290266 scopus 로고    scopus 로고
    • Phase diagram of α-helical and β-sheet forming peptides
    • Auer S., and Kashchiev D. Phase diagram of α-helical and β-sheet forming peptides Phys. Rev. Lett. 104 2010 168105
    • (2010) Phys. Rev. Lett. , vol.104 , pp. 168105
    • Auer, S.1    Kashchiev, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.