메뉴 건너뛰기




Volumn 1774, Issue 9, 2007, Pages 1128-1138

Aggregation and fibrillation of bovine serum albumin

Author keywords

Aggregation; Albumin; Amyloid; Fibrillation; Nucleation; Proteolysis

Indexed keywords

AMYLOID; BOVINE SERUM ALBUMIN; CONGO RED; PROTEINASE; THIOFLAVINE; TRIFLUOROETHANOL;

EID: 34548210324     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2007.06.008     Document Type: Article
Times cited : (238)

References (55)
  • 1
    • 18244365849 scopus 로고    scopus 로고
    • Protein drug stability-A formulation challenge
    • Frokjaer S., and Otzen D.E. Protein drug stability-A formulation challenge. Nat. Rev., Drug. Delivery 4 (2005) 298-306
    • (2005) Nat. Rev., Drug. Delivery , vol.4 , pp. 298-306
    • Frokjaer, S.1    Otzen, D.E.2
  • 2
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson C.M. Protein folding and misfolding. Nature 426 (2003) 884-890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 4
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • 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
    • (2003) Nature , vol.424 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddei, N.3    Ramponi, G.4    Dobson, C.M.5
  • 6
    • 27644491161 scopus 로고    scopus 로고
    • Thermodynamic analysis of the aggregation propensity of oxidized Alzheimer's beta-amyloid variants
    • Hortscansky P., Christopeit T., Schroeckh V., and Fändrich M. Thermodynamic analysis of the aggregation propensity of oxidized Alzheimer's beta-amyloid variants. Protein Sci. 14 (2005) 2915-2918
    • (2005) Protein Sci. , vol.14 , pp. 2915-2918
    • Hortscansky, P.1    Christopeit, T.2    Schroeckh, V.3    Fändrich, M.4
  • 7
    • 3342902033 scopus 로고    scopus 로고
    • Modulation of S6 fibrillation by unfolding rates and gatekeeper residues
    • Pedersen J.S., Christiansen G., and Otzen D.E. Modulation of S6 fibrillation by unfolding rates and gatekeeper residues. J. Mol. Biol. 341 (2004) 575-588
    • (2004) J. Mol. Biol. , vol.341 , pp. 575-588
    • Pedersen, J.S.1    Christiansen, G.2    Otzen, D.E.3
  • 8
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • Fändrich M., Fletcher M.A., and Dobson C.M. Amyloid fibrils from muscle myoglobin. Nature 410 (2001) 165-166
    • (2001) Nature , vol.410 , pp. 165-166
    • Fändrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 10
    • 0038386274 scopus 로고    scopus 로고
    • Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease
    • Volles M.J., and Lansbury P.T. Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease. Biochemistry 42 (2003) 7871-7878
    • (2003) Biochemistry , vol.42 , pp. 7871-7878
    • Volles, M.J.1    Lansbury, P.T.2
  • 11
    • 0035800097 scopus 로고    scopus 로고
    • Vesicle permeabilization by protofibrillar a-synuclein: Implications for the pathogenesis and treatment of Parkinson's disease
    • Volles M.J., Lee S.-J., Rochet J.-C., Shtilerman M.D., Ding T.T., Kessler J.C., and Lansbury P.T. Vesicle permeabilization by protofibrillar a-synuclein: Implications for the pathogenesis and treatment of Parkinson's disease. Biochemistry 40 (2001) 7812-7819
    • (2001) Biochemistry , vol.40 , pp. 7812-7819
    • Volles, M.J.1    Lee, S.-J.2    Rochet, J.-C.3    Shtilerman, M.D.4    Ding, T.T.5    Kessler, J.C.6    Lansbury, P.T.7
  • 12
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • Kayed R., Sokolov Y., Edmonds B., McIntire T.M., Milton S.C., Hall J.E., and Glabe C.G. Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. J. Biol. Chem. 279 (2004) 46363-46366
    • (2004) J. Biol. Chem. , vol.279 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Edmonds, B.3    McIntire, T.M.4    Milton, S.C.5    Hall, J.E.6    Glabe, C.G.7
  • 17
    • 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
    • Harper J.D., and Lansbury P.T.J. 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
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury, P.T.J.2
  • 18
    • 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
  • 20
    • 12544259221 scopus 로고    scopus 로고
    • Reversal of protein aggregation provides evidence for multiple aggregated states
    • Calamai M., Canale C., Relini A., Stefani M., Chiti F., and Dobson C.M. Reversal of protein aggregation provides evidence for multiple aggregated states. J. Mol. Biol. 346 (2005) 603-616
    • (2005) J. Mol. Biol. , vol.346 , pp. 603-616
    • Calamai, M.1    Canale, C.2    Relini, A.3    Stefani, M.4    Chiti, F.5    Dobson, C.M.6
  • 21
    • 0033062612 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin at 2.5 Å resolution
    • Sugio S., Kashima A., Mochizuki S., Noda M., and Kobayashi K. Crystal structure of human serum albumin at 2.5 Å resolution. Protein Eng. 12 (1999) 439-446
    • (1999) Protein Eng. , vol.12 , pp. 439-446
    • Sugio, S.1    Kashima, A.2    Mochizuki, S.3    Noda, M.4    Kobayashi, K.5
  • 22
    • 0025378934 scopus 로고
    • Structure and ligand binding properties of human serum albumin
    • Kragh-Hansen U. Structure and ligand binding properties of human serum albumin. Dan. Med. Bull. 37 (1990) 57-84
    • (1990) Dan. Med. Bull. , vol.37 , pp. 57-84
    • Kragh-Hansen, U.1
  • 23
    • 0043161935 scopus 로고    scopus 로고
    • Conformational changes involved in thermal aggregation processes of bovine serum albumin
    • Millitello V., Verti V., and Leone M. Conformational changes involved in thermal aggregation processes of bovine serum albumin. Biophys. Chem. 105 (2003) 133-141
    • (2003) Biophys. Chem. , vol.105 , pp. 133-141
    • Millitello, V.1    Verti, V.2    Leone, M.3
  • 24
    • 2542575542 scopus 로고    scopus 로고
    • Irreversible formation of intermediate BSA oligomers requires and induces conformational changes
    • Vaiana S.M., Emanuele A., Palma-Vittorelli M.B., and Palma M.U. Irreversible formation of intermediate BSA oligomers requires and induces conformational changes. Proteins 55 (2004) 1053-1062
    • (2004) Proteins , vol.55 , pp. 1053-1062
    • Vaiana, S.M.1    Emanuele, A.2    Palma-Vittorelli, M.B.3    Palma, M.U.4
  • 25
    • 4444344985 scopus 로고    scopus 로고
    • Heat-induced secondary structure and conformation change of bovine serum albumin investigated by Fourier Transform Infrared Spectroscopy
    • Murayama K., and Tomida M. Heat-induced secondary structure and conformation change of bovine serum albumin investigated by Fourier Transform Infrared Spectroscopy. Biochemistry 2004 (2004) 11526-11532
    • (2004) Biochemistry , vol.2004 , pp. 11526-11532
    • Murayama, K.1    Tomida, M.2
  • 26
    • 30744453243 scopus 로고    scopus 로고
    • Versatile interactions of the antimicrobial peptide Novispirin with detergents and lipids
    • Wimmer R., Andersen K., Davidsen M., Mølgaard S., Vad B., and Otzen D.E. Versatile interactions of the antimicrobial peptide Novispirin with detergents and lipids. Biochemistry 45 (2006) 481-497
    • (2006) Biochemistry , vol.45 , pp. 481-497
    • Wimmer, R.1    Andersen, K.2    Davidsen, M.3    Mølgaard, S.4    Vad, B.5    Otzen, D.E.6
  • 27
    • 20444416594 scopus 로고    scopus 로고
    • Characterization of liposomes
    • Torchilin V.P., and Weissig V. (Eds), Oxford Univ. Press, Oxford
    • Zuidam N.J., de Vrueh R., and Crommelin D.J.A. Characterization of liposomes. In: Torchilin V.P., and Weissig V. (Eds). Liposomes A Practical Approach (2003), Oxford Univ. Press, Oxford 31-78
    • (2003) Liposomes A Practical Approach , pp. 31-78
    • Zuidam, N.J.1    de Vrueh, R.2    Crommelin, D.J.A.3
  • 28
    • 0032855483 scopus 로고    scopus 로고
    • Quantifying amyloid by Congo Red spectral shift assay
    • Klunk W.E., Jacob R.F., and Mason R.P. Quantifying amyloid by Congo Red spectral shift assay. Methods Enzymol. 309 (1999) 285-305
    • (1999) Methods Enzymol. , vol.309 , pp. 285-305
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3
  • 29
    • 1642283195 scopus 로고    scopus 로고
    • Elimination of an off-pathway folding intermediate by a single point mutation
    • Mogensen J.E., Ibsen H., Lund J., and Otzen D.E. Elimination of an off-pathway folding intermediate by a single point mutation. Biochemistry 43 (2004) 3357-3367
    • (2004) Biochemistry , vol.43 , pp. 3357-3367
    • Mogensen, J.E.1    Ibsen, H.2    Lund, J.3    Otzen, D.E.4
  • 30
    • 0023375497 scopus 로고
    • Three fim genes required for the regulation of length and mediation of adhesion of Escherichia coli type 1 fimbriae
    • Klemm P., and Christiansen G. Three fim genes required for the regulation of length and mediation of adhesion of Escherichia coli type 1 fimbriae. Mol. Gen. Genet. 208 (1987) 439-445
    • (1987) Mol. Gen. Genet. , vol.208 , pp. 439-445
    • Klemm, P.1    Christiansen, G.2
  • 31
    • 0036358461 scopus 로고    scopus 로고
    • Temperature-induced formation of a non-native intermediate state of the all β-sheet protein CD2
    • Yang J.J., Yang H., Ye Y., Hopkins J., and Hastings G. Temperature-induced formation of a non-native intermediate state of the all β-sheet protein CD2. Cell Biochem. Biophys. 36 (2002) 1-18
    • (2002) Cell Biochem. Biophys. , vol.36 , pp. 1-18
    • Yang, J.J.1    Yang, H.2    Ye, Y.3    Hopkins, J.4    Hastings, G.5
  • 32
    • 22844447714 scopus 로고    scopus 로고
    • X-ray diffraction studies of amyloid structure
    • Makin O.S., and Serpell L.C. X-ray diffraction studies of amyloid structure. Methods Mol. Biol. 299 (2005) 67-80
    • (2005) Methods Mol. Biol. , vol.299 , pp. 67-80
    • Makin, O.S.1    Serpell, L.C.2
  • 34
    • 0034599720 scopus 로고    scopus 로고
    • Mutational analysis of the propensity for amyloid formation by a globular protein
    • Chiti F., Taddei N., Bucciantini M., White P., Ramponi G., and Dobson C.M. Mutational analysis of the propensity for amyloid formation by a globular protein. EMBO J. 19 (2000) 1441-1449
    • (2000) EMBO J. , vol.19 , pp. 1441-1449
    • Chiti, F.1    Taddei, N.2    Bucciantini, M.3    White, P.4    Ramponi, G.5    Dobson, C.M.6
  • 35
    • 34147108065 scopus 로고    scopus 로고
    • Alternative membrane protein conformations in alcohols
    • Otzen D.E., Sehgal P., and Nesgaard L. Alternative membrane protein conformations in alcohols. Biochemistry 46 (2007) 4348-4359
    • (2007) Biochemistry , vol.46 , pp. 4348-4359
    • Otzen, D.E.1    Sehgal, P.2    Nesgaard, L.3
  • 36
    • 0030852948 scopus 로고    scopus 로고
    • Mechanism of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction
    • Liu Y., Peterson D.A., Kimura H., and Schubert D. Mechanism of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction. J. Neurochem. 69 (1997) 581-593
    • (1997) J. Neurochem. , vol.69 , pp. 581-593
    • Liu, Y.1    Peterson, D.A.2    Kimura, H.3    Schubert, D.4
  • 37
    • 0035942997 scopus 로고    scopus 로고
    • Profile of changes in lipid bilayer structure caused by b-amyloid peptide
    • Kremer J.J., Sklansky D.J., and Murphy R.M. Profile of changes in lipid bilayer structure caused by b-amyloid peptide. Biochemistry 40 (2001) 8563-8571
    • (2001) Biochemistry , vol.40 , pp. 8563-8571
    • Kremer, J.J.1    Sklansky, D.J.2    Murphy, R.M.3
  • 40
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson C.M. Protein misfolding, evolution and disease. TIBS 24 (1999) 329-332
    • (1999) TIBS , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 41
    • 0035797795 scopus 로고    scopus 로고
    • Structural features of the Abeta amyloid fibril elucidated by limited proteolysis
    • Kheterpal I., Williams A.D., Murphy C., Bledsoe B., and Wetzel R. Structural features of the Abeta amyloid fibril elucidated by limited proteolysis. Biochemistry 40 (2001) 11757-11767
    • (2001) Biochemistry , vol.40 , pp. 11757-11767
    • Kheterpal, I.1    Williams, A.D.2    Murphy, C.3    Bledsoe, B.4    Wetzel, R.5
  • 42
    • 2142762962 scopus 로고    scopus 로고
    • Structural characterization of the fibrillar form of the yeast Saccharomyces cerevisiae prion Ure2p
    • Bousset L., Redeker V., Decottignies P., Dubois S., Le Marechal P., and Melki R. Structural characterization of the fibrillar form of the yeast Saccharomyces cerevisiae prion Ure2p. Biochemistry 43 (2004) 5022-5032
    • (2004) Biochemistry , vol.43 , pp. 5022-5032
    • Bousset, L.1    Redeker, V.2    Decottignies, P.3    Dubois, S.4    Le Marechal, P.5    Melki, R.6
  • 43
    • 27744571050 scopus 로고    scopus 로고
    • Limited proteolysis in the investigation of beta2-microglobulin amyloidogenic and fibrillar states
    • Monti M., Amoresano A., Giorgetti S., Bellotti V., and Pucci P. Limited proteolysis in the investigation of beta2-microglobulin amyloidogenic and fibrillar states. Biochim Biophys. Acta 1753 (2005) 44-50
    • (2005) Biochim Biophys. Acta , vol.1753 , pp. 44-50
    • Monti, M.1    Amoresano, A.2    Giorgetti, S.3    Bellotti, V.4    Pucci, P.5
  • 44
    • 0037077209 scopus 로고    scopus 로고
    • Conformation of beta2-microglobulin amyloid fibrils analyzed by reduction of the disulfide bond
    • Hong D.-P., Gozu M., Hasegawa K., Naiki H., and Goto Y. Conformation of beta2-microglobulin amyloid fibrils analyzed by reduction of the disulfide bond. J. Biol. Chem. 277 (2002) 21554-21560
    • (2002) J. Biol. Chem. , vol.277 , pp. 21554-21560
    • Hong, D.-P.1    Gozu, M.2    Hasegawa, K.3    Naiki, H.4    Goto, Y.5
  • 45
    • 27744523855 scopus 로고    scopus 로고
    • Towards an understanding of the structural molecular mechanism of beta2-microglobulin amyloid formation in vitro
    • Radford S.E., Gosal W.S., and Platt G.W. Towards an understanding of the structural molecular mechanism of beta2-microglobulin amyloid formation in vitro. Biochim Biophys. Acta 1753 (2005) 51-63
    • (2005) Biochim Biophys. Acta , vol.1753 , pp. 51-63
    • Radford, S.E.1    Gosal, W.S.2    Platt, G.W.3
  • 46
    • 1942473120 scopus 로고    scopus 로고
    • Transient formation of nanocrystalline structures during fibrillation of an Alzheimer-like peptide
    • Otzen D.E., and Oliveberg M. Transient formation of nanocrystalline structures during fibrillation of an Alzheimer-like peptide. Protein Sci. 13 (2004) 1417-1421
    • (2004) Protein Sci. , vol.13 , pp. 1417-1421
    • Otzen, D.E.1    Oliveberg, M.2
  • 47
    • 30744469843 scopus 로고    scopus 로고
    • Solvation-assisted pressure tuning of insulin fibrillation: from novel aggregation pathways to biotechnological applications
    • 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
    • (2006) J. Mol. Biol. , vol.356 , pp. 497-509
    • Grudzielanek, S.1    Smirnovas, V.2    Winter, R.3
  • 48
    • 28644437048 scopus 로고    scopus 로고
    • The importance of sequence diversity in the aggregation and evolution of proteins
    • Wright C.F., Teichmann S.A., Clarke J., and Dobson C.M. The importance of sequence diversity in the aggregation and evolution of proteins. Nature 438 (2005) 881
    • (2005) Nature , vol.438 , pp. 881
    • Wright, C.F.1    Teichmann, S.A.2    Clarke, J.3    Dobson, C.M.4
  • 49
    • 24644510813 scopus 로고    scopus 로고
    • Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure
    • Sambashivan S., Liu Y., Sawaya M.R., Gingery M., and Eisenberg D. Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure. Nature 437 (2005) 266-269
    • (2005) Nature , vol.437 , pp. 266-269
    • Sambashivan, S.1    Liu, Y.2    Sawaya, M.R.3    Gingery, M.4    Eisenberg, D.5
  • 50
    • 33751100148 scopus 로고    scopus 로고
    • Insights into the architecture of the Ure2p yeast protein assemblies from helical twisted fibrils
    • Ranson N., Stromer T., Bousset L., Melki R., and Serpell L.C. Insights into the architecture of the Ure2p yeast protein assemblies from helical twisted fibrils. Protein Sci. 15 (2006) 2481-2487
    • (2006) Protein Sci. , vol.15 , pp. 2481-2487
    • Ranson, N.1    Stromer, T.2    Bousset, L.3    Melki, R.4    Serpell, L.C.5
  • 51
    • 27644518721 scopus 로고    scopus 로고
    • Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR
    • Heise H., Hoyer W., Becker S., Andronesi O.C., Riedel D., and Baldus M. Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 15871-15876
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 15871-15876
    • Heise, H.1    Hoyer, W.2    Becker, S.3    Andronesi, O.C.4    Riedel, D.5    Baldus, M.6
  • 52
    • 33744937549 scopus 로고    scopus 로고
    • Sulfates dramatically stabilize a salt dependent type of glucagon fibrils
    • Pedersen J.S., Dikov D., Flink J.L., and Otzen D.E. Sulfates dramatically stabilize a salt dependent type of glucagon fibrils. Biophys. J. 90 (2006) 4181-4194
    • (2006) Biophys. J. , vol.90 , pp. 4181-4194
    • Pedersen, J.S.1    Dikov, D.2    Flink, J.L.3    Otzen, D.E.4
  • 53
    • 28944433479 scopus 로고    scopus 로고
    • The changing face of glucagon fibrillation: structural polymorphism and conformational imprinting
    • Pedersen J.S., Dikov D., Flink J.L., Hjuler H.A., Christiansen G., and Otzen D.E. The changing face of glucagon fibrillation: structural polymorphism and conformational imprinting. J. Mol. Biol. 355 (2006) 501-523
    • (2006) J. Mol. Biol. , vol.355 , pp. 501-523
    • Pedersen, J.S.1    Dikov, D.2    Flink, J.L.3    Hjuler, H.A.4    Christiansen, G.5    Otzen, D.E.6
  • 54
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • Tanaka M., Chien P., Naber N., Cooke R., and Weissman J.S. Conformational variations in an infectious protein determine prion strain differences. Nature 428 (2004) 323-328
    • (2004) Nature , vol.428 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 55
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's b-amyloid fibrils
    • Petkova A.T., Leapman R.D., Guo Z., Yau W.-M., Mattson M.P., and Tycko R. Self-propagating, molecular-level polymorphism in Alzheimer's b-amyloid fibrils. Science 307 (2005) 262-265
    • (2005) Science , vol.307 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.-M.4    Mattson, M.P.5    Tycko, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.