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Volumn 23, Issue 3, 2007, Pages 548-552

Protein misfolding and aggregation

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; COMPUTATIONAL METHODS; DISEASES; MATHEMATICAL MODELS;

EID: 34250376918     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp060374h     Document Type: Article
Times cited : (31)

References (43)
  • 1
    • 33645225597 scopus 로고    scopus 로고
    • Pathogenic superoxide dismutase structure, folding, aggregation and turnover
    • Hart, P. J. Pathogenic superoxide dismutase structure, folding, aggregation and turnover. Curr. Opin. Chem. Biol. 2006, 10, 131-138.
    • (2006) Curr. Opin. Chem. Biol , vol.10 , pp. 131-138
    • Hart, P.J.1
  • 2
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
    • Chi, E. Y.; Krishnan, S.; Randolph, T. W.; Carpenter, J. F. Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation. Pharm. Res. 2003, 20, 1325-1336.
    • (2003) Pharm. Res , vol.20 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 4
    • 33748041958 scopus 로고    scopus 로고
    • Effects of protein aggregates: An immunologic perspective
    • Rosenberg, A. S. Effects of protein aggregates: An immunologic perspective. Am. Assoc. Pharm. Sci. J. 2006, 8, E501-E507.
    • (2006) Am. Assoc. Pharm. Sci. J , vol.8
    • Rosenberg, A.S.1
  • 5
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F.; Dobson, C. M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 2006, 75, 333-366.
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 6
    • 0027411230 scopus 로고
    • Structure of beta-crystallite assemblies formed by Alzheimer beta-amyloid protein analogs-Analysis by X-ray diffraction
    • Inouye, H.; Fraser, P. E.; Kirschner, D. A. Structure of beta-crystallite assemblies formed by Alzheimer beta-amyloid protein analogs-Analysis by X-ray diffraction. Biophys. J. 1993, 64, 502-519.
    • (1993) Biophys. J , vol.64 , pp. 502-519
    • Inouye, H.1    Fraser, P.E.2    Kirschner, D.A.3
  • 7
    • 0031962158 scopus 로고    scopus 로고
    • Structural analysis of Alzheimer's beta(1-40) amyloid: Protofilament assembly of tubular fibrils
    • Malinchik, S. B.; Inouye, H.; Szumowski, K. E.; Kirschner, D. A. Structural analysis of Alzheimer's beta(1-40) amyloid: Protofilament assembly of tubular fibrils. Biophys. J. 1998, 74, 537-545.
    • (1998) Biophys. J , vol.74 , pp. 537-545
    • Malinchik, S.B.1    Inouye, H.2    Szumowski, K.E.3    Kirschner, D.A.4
  • 9
    • 14044278010 scopus 로고    scopus 로고
    • New model for crystalline polyglutamine assemblies and their connection with amyloid fibrils
    • Sikorski, P.; Atkins, E. New model for crystalline polyglutamine assemblies and their connection with amyloid fibrils. Biomacromolecules 2005, 6, 425-432.
    • (2005) Biomacromolecules , vol.6 , pp. 425-432
    • Sikorski, P.1    Atkins, E.2
  • 12
    • 33645995764 scopus 로고    scopus 로고
    • Recent atomic models of amyloid fibril structure
    • Nelson, R.; Eisenberg, D. Recent atomic models of amyloid fibril structure. Curr. Opin. Struct. Biol. 2006, 16, 260-265.
    • (2006) Curr. Opin. Struct. Biol , vol.16 , pp. 260-265
    • Nelson, R.1    Eisenberg, D.2
  • 13
    • 33750017513 scopus 로고    scopus 로고
    • Molecular structure of amyloid fibrils: Insights from solid-state NMR
    • Tycko, R. Molecular structure of amyloid fibrils: insights from solid-state NMR. Quart. Rev. Biophys. 2006, 39, 1-55.
    • (2006) Quart. Rev. Biophys , vol.39 , pp. 1-55
    • Tycko, R.1
  • 15
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils
    • Petkova, A. T.; Leapman, R. D.; Guo, Z. H.; Yau, W. M.; Mattson, M. P.; Tycko, R. Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science 2005, 307, 262-265.
    • (2005) Science , vol.307 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.H.3    Yau, W.M.4    Mattson, M.P.5    Tycko, R.6
  • 16
    • 2642579304 scopus 로고    scopus 로고
    • J. alcohol-induced destabilization of interferon-gamma: A study by hydrogen-deuterium isotope exchange
    • Tobler, S. A.; Holmes, S. A.; Cromwell, B. W.; Fernandez, M. E. M.; Benzyl E. J. alcohol-induced destabilization of interferon-gamma: A study by hydrogen-deuterium isotope exchange. J. Pharm. Sci. 2004, 93, 1605-1617.
    • (2004) J. Pharm. Sci , vol.93 , pp. 1605-1617
    • Tobler, S.A.1    Holmes, S.A.2    Cromwell, B.W.3    Fernandez, M.E.M.4    Benzyl, E.5
  • 17
    • 33646911952 scopus 로고    scopus 로고
    • Investigating the structural properties of amyloid-like fibrils formed in vitro from beta 2-microglobulin using limited proteolysis and electrospray ionisation mass spectrometry
    • Myers, S. L.; Thomson, N. H.; Radford, S. E.; Ashcroft, A. E. Investigating the structural properties of amyloid-like fibrils formed in vitro from beta 2-microglobulin using limited proteolysis and electrospray ionisation mass spectrometry. Rapid Commun. Mass Spectrom. 2006, 20, 1628-1636.
    • (2006) Rapid Commun. Mass Spectrom , vol.20 , pp. 1628-1636
    • Myers, S.L.1    Thomson, N.H.2    Radford, S.E.3    Ashcroft, A.E.4
  • 19
    • 33747199346 scopus 로고    scopus 로고
    • Static light scattering and small-angle neutron scattering study on aggregated recombinant gelatin in aqueous solution
    • Ramzi, A.; Sutter, M.; Hennink, W. E.; Jiskost, W. Static light scattering and small-angle neutron scattering study on aggregated recombinant gelatin in aqueous solution. J. Pharm. Sci. 2006, 95, 1703-1711.
    • (2006) J. Pharm. Sci , vol.95 , pp. 1703-1711
    • Ramzi, A.1    Sutter, M.2    Hennink, W.E.3    Jiskost, W.4
  • 21
    • 33646177852 scopus 로고    scopus 로고
    • Oligomerization and aggregation of bovine pancreatic ribonuclease A: Characteristic events observed by FTIR spectroscopy
    • Yan, Y.-B.; Zhang, J.; He, H.-W.; Zhou, H.-M. Oligomerization and aggregation of bovine pancreatic ribonuclease A: characteristic events observed by FTIR spectroscopy. Biophys. J. 2006, 90, 2525-2533.
    • (2006) Biophys. J , vol.90 , pp. 2525-2533
    • Yan, Y.-B.1    Zhang, J.2    He, H.-W.3    Zhou, H.-M.4
  • 22
    • 33644818046 scopus 로고    scopus 로고
    • Alanine scanning mutagenesis of Abeta(1-40) amyloid fibril stability
    • Williams, A. D.; Shivaprasad, S.; Wetzel, R. Alanine scanning mutagenesis of Abeta(1-40) amyloid fibril stability. J. Mol. Biol. 2006, 357, 1283-1294.
    • (2006) J. Mol. Biol , vol.357 , pp. 1283-1294
    • Williams, A.D.1    Shivaprasad, S.2    Wetzel, R.3
  • 23
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • July
    • Ross, C. A.; Poirier, M. A. Protein aggregation and neurodegenerative disease. Nat. Med. 2004, July (10 Suppl.), S10-S17.
    • (2004) Nat. Med , vol.10 , Issue.SUPPL.
    • Ross, C.A.1    Poirier, M.A.2
  • 24
    • 33646546740 scopus 로고    scopus 로고
    • Antibody response to aggregated human interferon alpha2b in wild-type and transgenic immune tolerant mice depends on type and level of aggregation
    • Hermeling S.; Schellekens, H.; Maas, C.; Gebbink, M. F. B. G.; Cronimelin, D. I. A.; Jiskoot, W. Antibody response to aggregated human interferon alpha2b in wild-type and transgenic immune tolerant mice depends on type and level of aggregation. J. Pharm. Sci. 2006, 95, 1084-1096.
    • (2006) J. Pharm. Sci , vol.95 , pp. 1084-1096
    • Hermeling, S.1    Schellekens, H.2    Maas, C.3    Gebbink, M.F.B.G.4    Cronimelin, D.I.A.5    Jiskoot, W.6
  • 25
    • 0033793872 scopus 로고    scopus 로고
    • Mechanisms of amyloidogenesis
    • Kelly, J. W. Mechanisms of amyloidogenesis. Nat. Struct. Biol. 2000, 7, 824-826.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 824-826
    • Kelly, J.W.1
  • 26
    • 0032558978 scopus 로고    scopus 로고
    • Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: Implications for wild-type, V30M, and L55P amyloid fibril formation
    • Lashuel, H. A.; Lai, Z. H.; Kelly, J. W. Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: Implications for wild-type, V30M, and L55P amyloid fibril formation. Biochemistry 1998, 37, 17851-17864.
    • (1998) Biochemistry , vol.37 , pp. 17851-17864
    • Lashuel, H.A.1    Lai, Z.H.2    Kelly, J.W.3
  • 28
    • 20544440379 scopus 로고    scopus 로고
    • Design of peptidyl compounds that affect beta-amyloid aggregation: Importance of surface tension and contex
    • Gibson, T. J.; Murphy, R. M. Design of peptidyl compounds that affect beta-amyloid aggregation: Importance of surface tension and contex. Biochemistry 2005, 44, 8898-8907.
    • (2005) Biochemistry , vol.44 , pp. 8898-8907
    • Gibson, T.J.1    Murphy, R.M.2
  • 29
    • 0142103473 scopus 로고    scopus 로고
    • Targeted control of kinetics of beta-amyloid self-association by surface tension-modifying peptides
    • Kim, J. R.; Gibson, T. J.; Murphy, R. M. Targeted control of kinetics of beta-amyloid self-association by surface tension-modifying peptides. J. Biol. Chem. 2003, 278, 40730-40735.
    • (2003) J. Biol. Chem , vol.278 , pp. 40730-40735
    • Kim, J.R.1    Gibson, T.J.2    Murphy, R.M.3
  • 30
    • 33646049045 scopus 로고    scopus 로고
    • Predicting solvent and aggregation effects of peptides using group contribution calculations
    • Kim, J. R.; Gibson, T. J.; Murphy, R. M. Predicting solvent and aggregation effects of peptides using group contribution calculations. Biotechnol. Prog. 2006, 22, 605-608.
    • (2006) Biotechnol. Prog , vol.22 , pp. 605-608
    • Kim, J.R.1    Gibson, T.J.2    Murphy, R.M.3
  • 31
    • 0026734937 scopus 로고
    • Rationalization of the effects of compatable solutes on protein stability in terms of thermodynamic nonideality
    • Winzor, C. L.; Winzor, D. J.; Paleg, L. G.; Jones, G. P.; Naidu, B. P. Rationalization of the effects of compatable solutes on protein stability in terms of thermodynamic nonideality. Arch. Biochem. Biophys. 1992, 296, 102-107.
    • (1992) Arch. Biochem. Biophys , vol.296 , pp. 102-107
    • Winzor, C.L.1    Winzor, D.J.2    Paleg, L.G.3    Jones, G.P.4    Naidu, B.P.5
  • 32
    • 0028838794 scopus 로고
    • Stabilizing effect of sucrose against irreversible denaturation of rabbit muscle lactate dehydrogenase
    • Hall, D. R.; Jacobsen, M. P.; Winzor, D. J. Stabilizing effect of sucrose against irreversible denaturation of rabbit muscle lactate dehydrogenase. Biophys. Chem. 1995, 57, 47-54.
    • (1995) Biophys. Chem , vol.57 , pp. 47-54
    • Hall, D.R.1    Jacobsen, M.P.2    Winzor, D.J.3
  • 34
    • 0242515822 scopus 로고    scopus 로고
    • Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor
    • Chi, E. Y.; Krishnan, S.; Kendrick, B. S.; Chang, B. S.; Carpenter, J. F.; Randolph, T. W. Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor. Protein Sci. 2003, 12, 903-913.
    • (2003) Protein Sci , vol.12 , pp. 903-913
    • Chi, E.Y.1    Krishnan, S.2    Kendrick, B.S.3    Chang, B.S.4    Carpenter, J.F.5    Randolph, T.W.6
  • 35
    • 0033869084 scopus 로고    scopus 로고
    • Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry
    • Nettleton, E. J.; Tito, P.; Sunde, M.; Bouchard, M.; Dobson, C. M.; Robinson, C. V. Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry. Biophys. J. 2000, 79, 1053-1065.
    • (2000) Biophys. J , vol.79 , pp. 1053-1065
    • Nettleton, E.J.1    Tito, P.2    Sunde, M.3    Bouchard, M.4    Dobson, C.M.5    Robinson, C.V.6
  • 37
    • 0032877134 scopus 로고    scopus 로고
    • Analysis of protein aggregation kinetics
    • Ferrone, F. Analysis of protein aggregation kinetics. Methods Enzymol. 1999, 309, 256-274.
    • (1999) Methods Enzymol , vol.309 , pp. 256-274
    • Ferrone, F.1
  • 38
    • 33645101164 scopus 로고    scopus 로고
    • Computational study of the fibril organization of polyglutamine repeats reveals a common motif identified in beta-helices
    • Zanuy, D.; Gunasekaran, K.; Lesk, A. M.; Nussinov, R. Computational study of the fibril organization of polyglutamine repeats reveals a common motif identified in beta-helices. J. Mol. Biol. 2006, 358, 330-345.
    • (2006) J. Mol. Biol , vol.358 , pp. 330-345
    • Zanuy, D.1    Gunasekaran, K.2    Lesk, A.M.3    Nussinov, R.4
  • 39
    • 28944435376 scopus 로고    scopus 로고
    • Characterization of two distinct beta-(2)-microglobulin unfolding intermediates that may lead to amyloid fibrils of different morphology
    • Armen, R. S.; Daggett, V. Characterization of two distinct beta-(2)-microglobulin unfolding intermediates that may lead to amyloid fibrils of different morphology. Biochemistry 2005, 44, 16098-16107.
    • (2005) Biochemistry , vol.44 , pp. 16098-16107
    • Armen, R.S.1    Daggett, V.2
  • 41
    • 15744382287 scopus 로고    scopus 로고
    • Kinetics of fibril formation by polyalanine peptides
    • Nguyen, H. D.; Hall, C. K. Kinetics of fibril formation by polyalanine peptides. J. Biol. Chem. 2005, 280, 9074-9082.
    • (2005) J. Biol. Chem , vol.280 , pp. 9074-9082
    • Nguyen, H.D.1    Hall, C.K.2
  • 42
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • Fernandez-Escamilla, A. M.; Rousseau, F.; Schymkowitz, J.; Serrano, L. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat. Biotechnol. 2004, 22, 1302-1306.
    • (2004) Nat. Biotechnol , vol.22 , pp. 1302-1306
    • Fernandez-Escamilla, A.M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 43
    • 3042584515 scopus 로고    scopus 로고
    • The role of aromaticity, exposed surface, and dipole moment in determining protein aggregatin rates
    • Tartaglia, G. G.; Cavalli, A.; Pellarin, R.; Caflisch, A. The role of aromaticity, exposed surface, and dipole moment in determining protein aggregatin rates. Protein Sci. 2004, 13, 1939-1941.
    • (2004) Protein Sci , vol.13 , pp. 1939-1941
    • Tartaglia, G.G.1    Cavalli, A.2    Pellarin, R.3    Caflisch, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.