메뉴 건너뛰기




Volumn 90, Issue 11, 2006, Pages 4181-4194

Sulfates dramatically stabilize a salt-dependent type of glucagon fibrils

Author keywords

[No Author keywords available]

Indexed keywords

ACID; ANION; CATION; CHLORIDE; GLUCAGON; INORGANIC SALT; OLIGOMER; SODIUM CHLORIDE; SULFATE;

EID: 33744937549     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.070912     Document Type: Article
Times cited : (94)

References (64)
  • 1
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett, J. T., and P. T. Lansbury, Jr. 1993. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell. 73:1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 4
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson, C. M. 1999. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24:329-332.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 5
    • 0038612852 scopus 로고    scopus 로고
    • Amyloid as a natural product
    • Kelly, J. W., and W. E. Balch. 2003. Amyloid as a natural product. J. Cell Biol. 161:461-462.
    • (2003) J. Cell Biol. , vol.161 , pp. 461-462
    • Kelly, J.W.1    Balch, W.E.2
  • 6
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen, C. B. 1973. Principles that govern the folding of protein chains. Science. 181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 8
    • 1642633056 scopus 로고    scopus 로고
    • Conformational variations in an infectious protein determine prion strain differences
    • Tanaka, M., P. Chien, N. Naber, R. Cooke, and J. S. Weissman. 2004. Conformational variations in an infectious protein determine prion strain differences. Nature. 428:323-328.
    • (2004) Nature , vol.428 , pp. 323-328
    • Tanaka, M.1    Chien, P.2    Naber, N.3    Cooke, R.4    Weissman, J.S.5
  • 9
    • 0028800177 scopus 로고
    • Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin
    • Bauer, H. H., U. Aebi, M. Haner, R. Hermann, M. Muller, and H. P. Merkle. 1995. Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin. J. Struct. Biol. 115:1-15.
    • (1995) J. Struct. Biol. , vol.115 , pp. 1-15
    • Bauer, H.H.1    Aebi, U.2    Haner, M.3    Hermann, R.4    Muller, M.5    Merkle, H.P.6
  • 13
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils
    • Petkova, A. T., R. D. Leapman, Z. Guo, W. M. Yau, M. P. Mattson, and R. Tycko. 2005. Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science. 307:262-265.
    • (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
  • 14
    • 3042665537 scopus 로고    scopus 로고
    • Insulin forms amyloid in a strain-dependent manner: An FT-IR spectroscopic study
    • Dzwolak, W., V. Smirnovas, R. Jansen, and R. Winter. 2004. Insulin forms amyloid in a strain-dependent manner: an FT-IR spectroscopic study. Protein Sci. 13:1927-1932.
    • (2004) Protein Sci. , vol.13 , pp. 1927-1932
    • Dzwolak, W.1    Smirnovas, V.2    Jansen, R.3    Winter, R.4
  • 15
    • 28944433479 scopus 로고    scopus 로고
    • The changing face of glucagon fibrillation: Structural polymorphism and conformational imprinting
    • Pedersen, J. S., D. Dikov, J. L. Flink, H. A. Hjuler, G. Christiansen, and D. E. Otzen. 2006. The changing face of glucagon fibrillation: structural polymorphism and conformational imprinting. J. Mol. Biol. 355:501-523.
    • (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
  • 16
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: The importance of being unfolded
    • Uversky, V. N., and A. L. Fink. 2004. Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim. Biophys. Acta. 1698:131-153.
    • (2004) Biochim. Biophys. Acta , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 17
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism
    • Nielsen, L., R. Khurana, A. Coats, S. Frokjaer, J. Brange, S. Vyas, V. N. Uversky, and A. L. Fink. 2001. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry. 40:6036-6046.
    • (2001) Biochemistry , vol.40 , 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
  • 18
    • 13444269021 scopus 로고    scopus 로고
    • Critical balance of electrostatic and hydrophobic interactions is required for beta 2-microglobulin amyloid fibril growth and stability
    • Raman, B., E. Chatani, M. Kihara, T. Ban, M. Sakai, K. Hasegawa, H. Naiki, M. Rao Ch, and Y. Goto. 2005. Critical balance of electrostatic and hydrophobic interactions is required for beta 2-microglobulin amyloid fibril growth and stability. Biochemistry. 44:1288-1299.
    • (2005) Biochemistry , vol.44 , pp. 1288-1299
    • Raman, B.1    Chatani, E.2    Kihara, M.3    Ban, T.4    Sakai, M.5    Hasegawa, K.6    Naiki, H.7    Rao Ch, M.8    Goto, Y.9
  • 19
    • 1542533563 scopus 로고    scopus 로고
    • Role of protein-water interactions and electrostatics in α-synuclein fibril formation
    • Munishkina, L. A., J. Henriques, V. N. Uversky, and A. L. Fink. 2004. Role of protein-water interactions and electrostatics in α-synuclein fibril formation. Biochemistry. 43:3289-3300.
    • (2004) Biochemistry , vol.43 , pp. 3289-3300
    • Munishkina, L.A.1    Henriques, J.2    Uversky, V.N.3    Fink, A.L.4
  • 20
    • 3342902033 scopus 로고    scopus 로고
    • Modulation of S6 fibrillation by unfolding rates and gatekeeper residues
    • Pedersen, J. S., G. Christensen, and D. E. Otzen. 2004. Modulation of S6 fibrillation by unfolding rates and gatekeeper residues. J. Mol. Biol. 341:575-588.
    • (2004) J. Mol. Biol. , vol.341 , pp. 575-588
    • Pedersen, J.S.1    Christensen, G.2    Otzen, D.E.3
  • 21
    • 0024969402 scopus 로고
    • Relative effectiveness of various ions on the solubility and crystal growth of lysozyme
    • Ries-Kautt, M. M., and A. F. Ducruix. 1989. Relative effectiveness of various ions on the solubility and crystal growth of lysozyme. J. Biol. Chem. 264:745-748.
    • (1989) J. Biol. Chem. , vol.264 , pp. 745-748
    • Ries-Kautt, M.M.1    Ducruix, A.F.2
  • 22
    • 0037137253 scopus 로고    scopus 로고
    • Protein hydration, thermodynamic binding, and preferential hydration
    • Timasheff, S. N. 2002. Protein hydration, thermodynamic binding, and preferential hydration. Biochemistry. 41:13473-13482.
    • (2002) Biochemistry , vol.41 , pp. 13473-13482
    • Timasheff, S.N.1
  • 23
    • 0027327488 scopus 로고
    • Aluminum, iron, and zinc ions promote aggregation of physiological concentrations of β-amyloid peptide
    • Mantyh, P. W., J. R. Ghilardi, S. Rogers, E. DeMaster, C. J. Allen, E. R. Stimson, and J. E. Maggio. 1993. Aluminum, iron, and zinc ions promote aggregation of physiological concentrations of β-amyloid peptide. J. Neurochem. 61:1171-1174.
    • (1993) J. Neurochem. , vol.61 , pp. 1171-1174
    • Mantyh, P.W.1    Ghilardi, J.R.2    Rogers, S.3    DeMaster, E.4    Allen, C.J.5    Stimson, E.R.6    Maggio, J.E.7
  • 24
    • 12144282992 scopus 로고    scopus 로고
    • Trace metal contamination initiates the apparent auto-aggregation, amyloidosis, and oligomerization of Alzheimer's Aβ peptides
    • Huang, X., C. S. Atwood, R. D. Moir, M. A. Hartshorn, R. E. Tanzi, and A. I. Bush. 2004. Trace metal contamination initiates the apparent auto-aggregation, amyloidosis, and oligomerization of Alzheimer's Aβ peptides. J. Biol. Inorg. Chem. 9:954-960.
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 954-960
    • Huang, X.1    Atwood, C.S.2    Moir, R.D.3    Hartshorn, M.A.4    Tanzi, R.E.5    Bush, A.I.6
  • 25
    • 0026673537 scopus 로고
    • Effects of sulfate ions on Alzheimer β/A4 peptide assemblies: Implications for amyloid fibril-proteoglycan interactions
    • Fraser, P. E., J. T. Nguyen, D. T. Chin, and D. A. Kirschner. 1992. Effects of sulfate ions on Alzheimer β/A4 peptide assemblies: implications for amyloid fibril-proteoglycan interactions. J. Neurochem. 59:1531-1540.
    • (1992) J. Neurochem. , vol.59 , pp. 1531-1540
    • Fraser, P.E.1    Nguyen, J.T.2    Chin, D.T.3    Kirschner, D.A.4
  • 26
    • 16744366300 scopus 로고    scopus 로고
    • 'In vitro' amyloid fibril formation from transthyretin: The influence of ions and the amyloidogenicity of TTR variants
    • Bonifacio, M. J., Y. Sakaki, and M. J. Saraiva. 1996. 'In vitro' amyloid fibril formation from transthyretin: the influence of ions and the amyloidogenicity of TTR variants. Biochim. Biophys. Acta. 1316:35-42.
    • (1996) Biochim. Biophys. Acta , vol.1316 , pp. 35-42
    • Bonifacio, M.J.1    Sakaki, Y.2    Saraiva, M.J.3
  • 27
    • 0023128689 scopus 로고
    • Sulfated glycosaminoglycans: A common constituent of all amyloids?
    • Snow, A. D., J. Willmer, and R. Kisilevsky. 1987. Sulfated glycosaminoglycans: a common constituent of all amyloids? Lab. Invest. 56:120-123.
    • (1987) Lab. Invest. , vol.56 , pp. 120-123
    • Snow, A.D.1    Willmer, J.2    Kisilevsky, R.3
  • 28
    • 0025074920 scopus 로고
    • Influence of sulphate ions on the structure of AA amyloid fibrils
    • Wong, S., and R. Kisilevsky. 1990. Influence of sulphate ions on the structure of AA amyloid fibrils. Scand. J. Immunol. 32:225-232.
    • (1990) Scand. J. Immunol. , vol.32 , pp. 225-232
    • Wong, S.1    Kisilevsky, R.2
  • 29
    • 0029907548 scopus 로고    scopus 로고
    • Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
    • Goedert, M., R. Jakes, M. G. Spillantini, M. Hasegawa, M. J. Smith, and R. A. Crowther. 1996. Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans. Nature. 383:550-553.
    • (1996) Nature , vol.383 , pp. 550-553
    • Goedert, M.1    Jakes, R.2    Spillantini, M.G.3    Hasegawa, M.4    Smith, M.J.5    Crowther, R.A.6
  • 30
    • 0029796168 scopus 로고    scopus 로고
    • Polymerization of τ into filaments in the presence of heparin: The minimal sequence required for τ-τ interaction
    • Perez, M., J. M. Valpuesta, M. Medina, E. Montejo de Garcini, and J. Avila. 1996. Polymerization of τ into filaments in the presence of heparin: the minimal sequence required for τ-τ interaction. J. Neurochem. 67:1183-1190.
    • (1996) J. Neurochem. , vol.67 , pp. 1183-1190
    • Perez, M.1    Valpuesta, J.M.2    Medina, M.3    Montejo De Garcini, E.4    Avila, J.5
  • 31
    • 0030590911 scopus 로고    scopus 로고
    • RNA stimulates aggregation of microtubule-associated protein τ into Alzheimer-like paired helical filaments
    • Kampers, T., P. Friedhoff, J. Biernat, E. M. Mandelkow, and E. Mandelkow. 1996. RNA stimulates aggregation of microtubule-associated protein τ into Alzheimer-like paired helical filaments. FEBS Lett. 399:344-349.
    • (1996) FEBS Lett. , vol.399 , pp. 344-349
    • Kampers, T.1    Friedhoff, P.2    Biernat, J.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 32
    • 0345306656 scopus 로고    scopus 로고
    • Rapid anionic micelle-mediated α-synuclein fibrillization in vitro
    • Necula, M., C. N. Chirita, and J. Kuret. 2003. Rapid anionic micelle-mediated α-synuclein fibrillization in vitro. J. Biol. Chem. 278:46674-46680.
    • (2003) J. Biol. Chem. , vol.278 , pp. 46674-46680
    • Necula, M.1    Chirita, C.N.2    Kuret, J.3
  • 34
    • 0014599351 scopus 로고
    • Formation and structure of gels and fibrils from glucagon
    • Beaven, G. H., W. B. Gratzer, and H. G. Davies. 1969. Formation and structure of gels and fibrils from glucagon. Eur. J. Biochem. 11:37-42.
    • (1969) Eur. J. Biochem. , vol.11 , pp. 37-42
    • Beaven, G.H.1    Gratzer, W.B.2    Davies, H.G.3
  • 35
    • 0016329537 scopus 로고
    • β-Pleated sheet fibrils. A comparison of native amyloid with synthetic protein fibrils
    • Glenner, G. G., E. D. Eanes, H. A. Bladen, R. P. Linke, and J. D. Termine. 1974. β-Pleated sheet fibrils. A comparison of native amyloid with synthetic protein fibrils. J. Histochem. Cytochem. 22:1141-1158.
    • (1974) J. Histochem. Cytochem. , vol.22 , pp. 1141-1158
    • Glenner, G.G.1    Eanes, E.D.2    Bladen, H.A.3    Linke, R.P.4    Termine, J.D.5
  • 36
    • 0017700305 scopus 로고
    • Conformational transitions of glucagon in solution: The α to β transition
    • Moran, E. C., P. Y. Chou, and G. D. Fasman. 1977. Conformational transitions of glucagon in solution: the α to β transition. Biochem. Biophys. Res. Commun. 77:1300-1306.
    • (1977) Biochem. Biophys. Res. Commun. , vol.77 , pp. 1300-1306
    • Moran, E.C.1    Chou, P.Y.2    Fasman, G.D.3
  • 37
    • 0034255443 scopus 로고    scopus 로고
    • A new method for the determination of stability parameters of proteins from their heat-induced denaturation curves
    • Yadav, S., and F. Ahmad. 2000. A new method for the determination of stability parameters of proteins from their heat-induced denaturation curves. Anal. Biochem. 283:207-213.
    • (2000) Anal. Biochem. , vol.283 , pp. 207-213
    • Yadav, S.1    Ahmad, F.2
  • 39
    • 0029792830 scopus 로고    scopus 로고
    • How Hofmeister ion interactions affect protein stability
    • Baldwin, R. L. 1996. How Hofmeister ion interactions affect protein stability. Biophys. J. 71:2056-2063.
    • (1996) Biophys. J. , vol.71 , pp. 2056-2063
    • Baldwin, R.L.1
  • 40
    • 0001891876 scopus 로고
    • Anion chromatography with low-conductivity eluents. II
    • Gjerde, D. T., G. Schmuckler, and J. S. Fritz. 1980. Anion chromatography with low-conductivity eluents. II. J. Chromatogr. 187:35-45.
    • (1980) J. Chromatogr. , vol.187 , pp. 35-45
    • Gjerde, D.T.1    Schmuckler, G.2    Fritz, J.S.3
  • 41
    • 0040346675 scopus 로고
    • Studies on ion-exchange resins. XIII. selectivity coefficients of quaternary Base Anion-exchange Resins Toward Univalent Anions
    • Gregor, H. P., J. Belle, and R. A. Marcus. 1955. Studies on ion-exchange resins. XIII. selectivity coefficients of quaternary Base Anion-exchange Resins Toward Univalent Anions. J. Am. Chem. Soc. 77:2713-2719.
    • (1955) J. Am. Chem. Soc. , vol.77 , pp. 2713-2719
    • Gregor, H.P.1    Belle, J.2    Marcus, R.A.3
  • 42
    • 0033526429 scopus 로고    scopus 로고
    • Effect of ion binding on protein transport through ultrafiltration membranes
    • Menon, M. K., and A. L. Zydney. 1999. Effect of ion binding on protein transport through ultrafiltration membranes. Biotechnol. Bioeng. 63:298-307.
    • (1999) Biotechnol. Bioeng. , vol.63 , pp. 298-307
    • Menon, M.K.1    Zydney, A.L.2
  • 43
    • 0025195499 scopus 로고
    • Mechanism of acid-induced folding of proteins
    • Goto, Y., N. Takahashi, and A. L. Fink. 1990. Mechanism of acid-induced folding of proteins. Biochemistry. 29:3480-3488.
    • (1990) Biochemistry , vol.29 , pp. 3480-3488
    • Goto, Y.1    Takahashi, N.2    Fink, A.L.3
  • 44
    • 0019991540 scopus 로고
    • Cation-induced conformational change in glucagon
    • Epand, R. M. 1982. Cation-induced conformational change in glucagon. Mol. Pharmacol. 22:105-108.
    • (1982) Mol. Pharmacol. , vol.22 , pp. 105-108
    • Epand, R.M.1
  • 46
    • 17144426174 scopus 로고    scopus 로고
    • Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy
    • Jansen, R., W. Dzwolak, and R. Winter. 2005. Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy. Biophys. J. 88:1344-1353.
    • (2005) Biophys. J. , vol.88 , pp. 1344-1353
    • Jansen, R.1    Dzwolak, W.2    Winter, R.3
  • 47
    • 0032879778 scopus 로고    scopus 로고
    • Analysis of protein structure by solution optical spectroscopy
    • Colon, W. 1999. Analysis of protein structure by solution optical spectroscopy. Methods Enzymol. 309:605-632.
    • (1999) Methods Enzymol. , vol.309 , pp. 605-632
    • Colon, W.1
  • 48
    • 0037302324 scopus 로고    scopus 로고
    • Structural composition of βI- and βII-proteins
    • Sreerama, N., and R. W. Woody. 2003. Structural composition of βI- and βII-proteins. Protein Sci. 12:384-388.
    • (2003) Protein Sci. , vol.12 , pp. 384-388
    • Sreerama, N.1    Woody, R.W.2
  • 50
    • 0019310670 scopus 로고
    • Helical conformation of glucagon in surfactant solutions
    • Wu, C. S., and J. T. Yang. 1980. Helical conformation of glucagon in surfactant solutions. Biochemistry. 19:2117-2122.
    • (1980) Biochemistry , vol.19 , pp. 2117-2122
    • Wu, C.S.1    Yang, J.T.2
  • 51
    • 0032831759 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy in analysis of protein deposits
    • Seshadri, S., R. Khurana, and A. L. Fink. 1999. Fourier transform infrared spectroscopy in analysis of protein deposits. Methods Enzymol. 309:559-576.
    • (1999) Methods Enzymol. , vol.309 , pp. 559-576
    • Seshadri, S.1    Khurana, R.2    Fink, A.L.3
  • 52
    • 9344243513 scopus 로고    scopus 로고
    • FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils
    • Zandomeneghi, G., M. R. Krebs, M. G. McCammon, and M. Fandrich. 2004. FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils. Protein Sci. 13:3314-3321.
    • (2004) Protein Sci. , vol.13 , pp. 3314-3321
    • Zandomeneghi, G.1    Krebs, M.R.2    McCammon, M.G.3    Fandrich, M.4
  • 53
    • 0014155571 scopus 로고
    • Infrared study of poly-L-proline in aqueous solution
    • Swenson, C. A., and R. Formanek. 1967. Infrared study of poly-L-proline in aqueous solution. J. Phys. Chem. 71:4073-4077.
    • (1967) J. Phys. Chem. , vol.71 , pp. 4073-4077
    • Swenson, C.A.1    Formanek, R.2
  • 54
    • 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
  • 56
    • 20444403757 scopus 로고    scopus 로고
    • Prediction of "aggregation-prone" and "aggregation- susceptible" regions in proteins associated with neurodegenerative diseases
    • Pawar, A. P., K. F. Dubay, J. Zurdo, F. Chiti, M. Vendruscolo, and C. M. Dobson. 2005. Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases. J. Mol. Biol. 350:379-392.
    • (2005) J. Mol. Biol. , vol.350 , pp. 379-392
    • Pawar, A.P.1    Dubay, K.F.2    Zurdo, J.3    Chiti, F.4    Vendruscolo, M.5    Dobson, C.M.6
  • 58
    • 0017857175 scopus 로고
    • Effects of Hofmeister salts on the self-association of glucagon
    • Formisano, S., M. L. Johnson, and H. Edelhoch. 1978. Effects of Hofmeister salts on the self-association of glucagon. Biochemistry. 17:1468-1473.
    • (1978) Biochemistry , vol.17 , pp. 1468-1473
    • Formisano, S.1    Johnson, M.L.2    Edelhoch, H.3
  • 59
    • 28944438938 scopus 로고
    • Proton nuclear magnetic resonance study of glucagon
    • Patel, D. J. 1970. Proton nuclear magnetic resonance study of glucagon. Macromolecules. 3:448-449.
    • (1970) Macromolecules , vol.3 , pp. 448-449
    • Patel, D.J.1
  • 60
    • 8844247180 scopus 로고    scopus 로고
    • Mechanism of prion propagation: Amyloid growth occurs by monomer addition
    • Collins, S. R., A. Douglass, R. D. Vale, and J. S. Weissman. 2004. Mechanism of prion propagation: amyloid growth occurs by monomer addition. PLoS Biol. 2:e321.
    • (2004) PLoS Biol. , vol.2
    • Collins, S.R.1    Douglass, A.2    Vale, R.D.3    Weissman, J.S.4
  • 61
    • 0026351184 scopus 로고
    • Role of electrostatic repulsion in the acidic molten globule of cytochrome c
    • Goto, Y., and S. Nishikiori. 1991. Role of electrostatic repulsion in the acidic molten globule of cytochrome c. J. Mol. Biol. 222:679-686.
    • (1991) J. Mol. Biol. , vol.222 , pp. 679-686
    • Goto, Y.1    Nishikiori, S.2
  • 62
    • 0036081128 scopus 로고    scopus 로고
    • Sulfate anion stabilization of native ribonuclease a both by anion binding and by the Hofmeister effect
    • Ramos, C. H., and R. L. Baldwin. 2002. Sulfate anion stabilization of native ribonuclease A both by anion binding and by the Hofmeister effect. Protein Sci. 11:1771-1778.
    • (2002) Protein Sci. , vol.11 , pp. 1771-1778
    • Ramos, C.H.1    Baldwin, R.L.2
  • 63
    • 0023767031 scopus 로고
    • The potential significance of sulphated glycosaminoglycans as a common constituent of all amyloids: Or, perhaps amyloid is not a misnomer
    • Kisilevsky, R., and A. Snow. 1988. The potential significance of sulphated glycosaminoglycans as a common constituent of all amyloids: or, perhaps amyloid is not a misnomer. Med. Hypotheses. 26:231-236.
    • (1988) Med. Hypotheses , vol.26 , pp. 231-236
    • Kisilevsky, R.1    Snow, A.2
  • 64
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of α-synuclein secondary structure upon binding to synthetic membranes
    • Davidson, W. S., A. Jonas, D. F. Clayton, and J. M. George. 1998. Stabilization of α-synuclein secondary structure upon binding to synthetic membranes. J. Biol. Chem. 273:9443-9449.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.