메뉴 건너뛰기




Volumn 107, Issue 1, 2014, Pages 197-207

Sulfate anion delays the self-assembly of human insulin by modifying the aggregation pathway

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; INSULIN; PROTEIN AGGREGATE; SULFATE;

EID: 84904002015     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2014.05.030     Document Type: Article
Times cited : (23)

References (67)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • F. Chiti, and C.M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 84875939276 scopus 로고    scopus 로고
    • The self-assembly, aggregation and phase transitions of food protein systems in one, two and three dimensions
    • R. Mezzenga, and P. Fischer The self-assembly, aggregation and phase transitions of food protein systems in one, two and three dimensions Rep. Prog. Phys. 76 2013 046601
    • (2013) Rep. Prog. Phys. , vol.76 , pp. 046601
    • Mezzenga, R.1    Fischer, P.2
  • 3
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
    • E.Y. Chi, and S. Krishnan J.F. Carpenter Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation Pharm. Res. 20 2003 1325 1336
    • (2003) Pharm. Res. , vol.20 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Carpenter, J.F.3
  • 4
    • 0037421836 scopus 로고    scopus 로고
    • Kinetics of irreversible protein aggregation: Analysis of extended Lumry-Eyring models and implications for predicting protein shelf life
    • C.J. Roberts Kinetics of irreversible protein aggregation: analysis of extended Lumry-Eyring models and implications for predicting protein shelf life J. Phys. Chem. B 107 2003 1194 1207
    • (2003) J. Phys. Chem. B , vol.107 , pp. 1194-1207
    • Roberts, C.J.1
  • 5
    • 78650088238 scopus 로고    scopus 로고
    • Designer self-assembling peptide materials for diverse applications
    • C.A.E. Hauser, and S. Zhang Designer self-assembling peptide materials for diverse applications Macromol. Symp. 295 2010 30 48
    • (2010) Macromol. Symp. , vol.295 , pp. 30-48
    • Hauser, C.A.E.1    Zhang, S.2
  • 6
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • F. Chiti, and M. Stefani C.M. Dobson 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    Dobson, C.M.3
  • 7
    • 0034718157 scopus 로고    scopus 로고
    • Alzheimer's amyloid fibrils: Structure and assembly
    • L.C. Serpell Alzheimer's amyloid fibrils: structure and assembly Biochim. Biophys. Acta 1502 2000 16 30
    • (2000) Biochim. Biophys. Acta , vol.1502 , pp. 16-30
    • Serpell, L.C.1
  • 8
    • 77955230701 scopus 로고    scopus 로고
    • Understanding amyloid aggregation by statistical analysis of atomic force microscopy images
    • J. Adamcik, and J.-M. Jung R. Mezzenga Understanding amyloid aggregation by statistical analysis of atomic force microscopy images Nat. Nanotechnol. 5 2010 423 428
    • (2010) Nat. Nanotechnol. , vol.5 , pp. 423-428
    • Adamcik, J.1    Jung, J.-M.2    Mezzenga, R.3
  • 9
    • 72149118250 scopus 로고    scopus 로고
    • An analytical solution to the kinetics of breakable filament assembly
    • T.P.J. Knowles, and C.A. Waudby C.M. Dobson An analytical solution to the kinetics of breakable filament assembly Science 326 2009 1533 1537
    • (2009) Science , vol.326 , pp. 1533-1537
    • Knowles, T.P.J.1    Waudby, C.A.2    Dobson, C.M.3
  • 10
    • 84863981137 scopus 로고    scopus 로고
    • From macroscopic measurements to microscopic mechanisms of protein aggregation
    • S.I.A. Cohen, and M. Vendruscolo T.P.J. Knowles From macroscopic measurements to microscopic mechanisms of protein aggregation J. Mol. Biol. 421 2012 160 171
    • (2012) J. Mol. Biol. , vol.421 , pp. 160-171
    • Cohen, S.I.A.1    Vendruscolo, M.2    Knowles, T.P.J.3
  • 11
    • 0035957228 scopus 로고    scopus 로고
    • Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates
    • R. Khurana, and J.R. Gillespie A.L. Fink Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates Biochemistry 40 2001 3525 3535
    • (2001) Biochemistry , vol.40 , pp. 3525-3535
    • Khurana, R.1    Gillespie, J.R.2    Fink, A.L.3
  • 12
    • 0036468090 scopus 로고    scopus 로고
    • Aggregation, gelation and phase separation of heat denatured globular proteins
    • D.J. Durand, C. Gimel, and T. Nicolai Aggregation, gelation and phase separation of heat denatured globular proteins Physica A: Stat. Mech. Appl. 304 2002 253 265
    • (2002) Physica A: Stat. Mech. Appl. , vol.304 , pp. 253-265
    • Durand, D.J.1    Gimel, C.2    Nicolai, T.3
  • 13
    • 84862693132 scopus 로고    scopus 로고
    • Population balance modeling of antibodies aggregation kinetics
    • P. Arosio, and S. Rima M. Morbidelli Population balance modeling of antibodies aggregation kinetics J. Phys. Chem. B 116 2012 7066 7075
    • (2012) J. Phys. Chem. B , vol.116 , pp. 7066-7075
    • Arosio, P.1    Rima, S.2    Morbidelli, M.3
  • 16
    • 84862867185 scopus 로고    scopus 로고
    • Why continuum electrostatics theories cannot explain biological structure, polyelectrolytes or ionic strength effects in ion-protein interactions
    • K.D. Collins Why continuum electrostatics theories cannot explain biological structure, polyelectrolytes or ionic strength effects in ion-protein interactions Biophys. Chem. 167 2012 43 59
    • (2012) Biophys. Chem. , vol.167 , pp. 43-59
    • Collins, K.D.1
  • 17
    • 0021755248 scopus 로고
    • Mechanism of protein salting in and salting out by divalent cation salts: Balance between hydration and salt binding
    • T. Arakawa, and S.N. Timasheff Mechanism of protein salting in and salting out by divalent cation salts: balance between hydration and salt binding Biochemistry 23 1984 5912 5923
    • (1984) Biochemistry , vol.23 , pp. 5912-5923
    • Arakawa, T.1    Timasheff, S.N.2
  • 18
    • 2142700029 scopus 로고    scopus 로고
    • Protein interactions and association: An open challenge for colloid science
    • R. Piazza Protein interactions and association: an open challenge for colloid science Curr. Opin. Colloid Interface Sci. 8 2004 515 522
    • (2004) Curr. Opin. Colloid Interface Sci. , vol.8 , pp. 515-522
    • Piazza, R.1
  • 19
    • 84855445083 scopus 로고    scopus 로고
    • Inhibiting, promoting, and preserving stability of functional protein fibrils
    • O.G. Jones, and R. Mezzenga Inhibiting, promoting, and preserving stability of functional protein fibrils Soft Matter 8 2012 876 895
    • (2012) Soft Matter , vol.8 , pp. 876-895
    • Jones, O.G.1    Mezzenga, R.2
  • 20
    • 84874885410 scopus 로고    scopus 로고
    • Electrostatic effects in filamentous protein aggregation
    • A.K. Buell, and P. Hung T.P. Knowles Electrostatic effects in filamentous protein aggregation Biophys. J. 104 2013 1116 1126
    • (2013) Biophys. J. , vol.104 , pp. 1116-1126
    • Buell, A.K.1    Hung, P.2    Knowles, T.P.3
  • 21
    • 84855976504 scopus 로고    scopus 로고
    • Studying salt effects on protein stability using ribonuclease t1 as a model system
    • D.L. Beauchamp, and M. Khajehpour Studying salt effects on protein stability using ribonuclease t1 as a model system Biophys. Chem. 161 2012 29 38
    • (2012) Biophys. Chem. , vol.161 , pp. 29-38
    • Beauchamp, D.L.1    Khajehpour, M.2
  • 22
    • 84863009479 scopus 로고    scopus 로고
    • On the role of salt type and concentration on the stability behavior of a monoclonal antibody solution
    • P. Arosio, and B. Jaquet M. Morbidelli On the role of salt type and concentration on the stability behavior of a monoclonal antibody solution Biophys. Chem. 168-169 2012 19 27
    • (2012) Biophys. Chem. , vol.168-169 , pp. 19-27
    • Arosio, P.1    Jaquet, B.2    Morbidelli, M.3
  • 23
    • 84863353690 scopus 로고    scopus 로고
    • Stability and gelation behavior of bovine serum albumin pre-aggregates in the presence of calcium chloride
    • H. Wu, and P. Arosio M. Morbidelli Stability and gelation behavior of bovine serum albumin pre-aggregates in the presence of calcium chloride Phys. Chem. Chem. Phys. 14 2012 4906 4916
    • (2012) Phys. Chem. Chem. Phys. , vol.14 , pp. 4906-4916
    • Wu, H.1    Arosio, P.2    Morbidelli, M.3
  • 24
    • 11844256958 scopus 로고    scopus 로고
    • On the restabilization of protein-covered latex colloids at high ionic strengths
    • H. Huang, M. Manciu, and E. Ruckenstein On the restabilization of protein-covered latex colloids at high ionic strengths Langmuir 21 2005 94 99
    • (2005) Langmuir , vol.21 , pp. 94-99
    • Huang, H.1    Manciu, M.2    Ruckenstein, E.3
  • 25
    • 0043065429 scopus 로고    scopus 로고
    • Molecular mechanisms of Fe2+-induced β-lactoglobulin cold gelation
    • G.E. Remondetto, and M. Subirade Molecular mechanisms of Fe2+-induced β-lactoglobulin cold gelation Biopolymers 69 2003 461 469
    • (2003) Biopolymers , vol.69 , pp. 461-469
    • Remondetto, G.E.1    Subirade, M.2
  • 26
    • 35148899284 scopus 로고    scopus 로고
    • Effect of different salt ions on the propensity of aggregation and on the structure of Alzheimer's abeta(1-40) amyloid fibrils
    • K. Klement, and K. Wieligmann M. Fändrich Effect of different salt ions on the propensity of aggregation and on the structure of Alzheimer's abeta(1-40) amyloid fibrils J. Mol. Biol. 373 2007 1321 1333
    • (2007) J. Mol. Biol. , vol.373 , pp. 1321-1333
    • Klement, K.1    Wieligmann, K.2    Fändrich, M.3
  • 27
    • 1542533563 scopus 로고    scopus 로고
    • Role of protein-water interactions and electrostatics in α-synuclein fibril formation
    • L.A. Munishkina, and J. Henriques A.L. Fink Role of protein-water interactions and electrostatics in α-synuclein fibril formation Biochemistry 43 2004 3289 3300
    • (2004) Biochemistry , vol.43 , pp. 3289-3300
    • Munishkina, L.A.1    Henriques, J.2    Fink, A.L.3
  • 28
    • 84868159835 scopus 로고    scopus 로고
    • Ionic strength effects on amyloid formation by amylin are a complicated interplay among Debye screening, ion selectivity, and Hofmeister effects
    • P.J. Marek, and V. Patsalo D.P. Raleigh Ionic strength effects on amyloid formation by amylin are a complicated interplay among Debye screening, ion selectivity, and Hofmeister effects Biochemistry 51 2012 8478 8490
    • (2012) Biochemistry , vol.51 , pp. 8478-8490
    • Marek, P.J.1    Patsalo, V.2    Raleigh, D.P.3
  • 29
    • 75149188405 scopus 로고    scopus 로고
    • The Hofmeister effect on amyloid formation using yeast prion protein
    • V. Yeh, and J.M. Broering A.S. Bommarius The Hofmeister effect on amyloid formation using yeast prion protein Protein Sci. 19 2010 47 56
    • (2010) Protein Sci. , vol.19 , pp. 47-56
    • Yeh, V.1    Broering, J.M.2    Bommarius, A.S.3
  • 30
    • 84869083333 scopus 로고    scopus 로고
    • Salt anions promote the conversion of HypF-N into amyloid-like oligomers and modulate the structure of the oligomers and the monomeric precursor state
    • S. Campioni, and B. Mannini F. Chiti Salt anions promote the conversion of HypF-N into amyloid-like oligomers and modulate the structure of the oligomers and the monomeric precursor state J. Mol. Biol. 424 2012 132 149
    • (2012) J. Mol. Biol. , vol.424 , pp. 132-149
    • Campioni, S.1    Mannini, B.2    Chiti, F.3
  • 31
    • 0022147096 scopus 로고
    • The Hofmeister effect and the behavior of water at interfaces
    • K.D. Collins, and M.W. Washabaugh The Hofmeister effect and the behavior of water at interfaces Q. Rev. Biophys. 18 1985 323 422
    • (1985) Q. Rev. Biophys. , vol.18 , pp. 323-422
    • Collins, K.D.1    Washabaugh, M.W.2
  • 33
    • 0017623134 scopus 로고
    • Salt effect on hydrophobic interactions in precipitation and chromatography of proteins: An interpretation of the lyotropic series
    • W. Melander, and C. Horváth Salt effect on hydrophobic interactions in precipitation and chromatography of proteins: an interpretation of the lyotropic series Arch. Biochem. Biophys. 183 1977 200 215
    • (1977) Arch. Biochem. Biophys. , vol.183 , pp. 200-215
    • Melander, W.1    Horváth, C.2
  • 34
    • 84863269470 scopus 로고    scopus 로고
    • In vitro aggregation behavior of a non-amyloidogenic lambda light chain dimer deriving from U266 multiple myeloma cells
    • P. Arosio, and M. Owczarz M. Morbidelli In vitro aggregation behavior of a non-amyloidogenic lambda light chain dimer deriving from U266 multiple myeloma cells Plos One 7 2012 e33372
    • (2012) Plos One , vol.7 , pp. 33372
    • Arosio, P.1    Owczarz, M.2    Morbidelli, M.3
  • 35
    • 33745698477 scopus 로고    scopus 로고
    • The effects of sodium sulfate, glycosaminoglycans, and Congo red on the structure, stability, and amyloid formation of an immunoglobulin light-chain protein
    • R.W. McLaughlin, and J.K. De Stigter M. Ramirez-Alvarado The effects of sodium sulfate, glycosaminoglycans, and Congo red on the structure, stability, and amyloid formation of an immunoglobulin light-chain protein Protein Sci. 15 2006 1710 1722
    • (2006) Protein Sci. , vol.15 , pp. 1710-1722
    • McLaughlin, R.W.1    De Stigter, J.K.2    Ramirez-Alvarado, M.3
  • 36
    • 33744937549 scopus 로고    scopus 로고
    • Sulfates dramatically stabilize a salt-dependent type of glucagon fibrils
    • J.S. Pedersen, and J.M. Flink D.E. Otzen 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    Flink, J.M.2    Otzen, D.E.3
  • 37
    • 0036081128 scopus 로고    scopus 로고
    • Sulfate anion stabilization of native ribonuclease A both by anion binding and by the Hofmeister effect
    • C.H.I. Ramos, and R.L. Baldwin Sulfate anion stabilization of native ribonuclease A both by anion binding and by the Hofmeister effect Protein Sci. 11 2002 1771 1778
    • (2002) Protein Sci. , vol.11 , pp. 1771-1778
    • Ramos, C.H.I.1    Baldwin, R.L.2
  • 38
    • 0036304350 scopus 로고    scopus 로고
    • Insulin at pH 2: Structural analysis of the conditions promoting insulin fibre formation
    • J.L. Whittingham, and D.J. Scott G. Guy Dodson Insulin at pH 2: structural analysis of the conditions promoting insulin fibre formation J. Mol. Biol. 318 2002 479 490
    • (2002) J. Mol. Biol. , vol.318 , pp. 479-490
    • Whittingham, J.L.1    Scott, D.J.2    Guy Dodson, G.3
  • 39
    • 33749593513 scopus 로고    scopus 로고
    • Anion effect on the nanostructure of a metal ion binding self-assembling peptide
    • H. Yang, and M. Pritzker P. Chen Anion effect on the nanostructure of a metal ion binding self-assembling peptide Langmuir 22 2006 8553 8562
    • (2006) Langmuir , vol.22 , pp. 8553-8562
    • Yang, H.1    Pritzker, M.2    Chen, P.3
  • 40
    • 77949886084 scopus 로고    scopus 로고
    • Effects of hydrophobicity and anions on self-assembly of the peptide EMK16-II
    • D. Zou, and Z. Tie P. Chen Effects of hydrophobicity and anions on self-assembly of the peptide EMK16-II Biopolymers 93 2010 318 329
    • (2010) Biopolymers , vol.93 , pp. 318-329
    • Zou, D.1    Tie, Z.2    Chen, P.3
  • 41
    • 84860766011 scopus 로고    scopus 로고
    • Rapid oligomer formation of human muscle acylphosphatase induced by heparan sulfate
    • S1-S2
    • N. Motamedi-Shad, and T. Garfagnini F. Chiti Rapid oligomer formation of human muscle acylphosphatase induced by heparan sulfate Nat. Struct. Mol. Biol. 19 2012 547 554 S1-S2
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 547-554
    • Motamedi-Shad, N.1    Garfagnini, T.2    Chiti, F.3
  • 42
    • 34447503337 scopus 로고    scopus 로고
    • Specific glycosaminoglycans promote unseeded amyloid formation from beta2-microglobulin under physiological conditions
    • A.J. Borysik, and I.J. Morten E.W. Hewitt Specific glycosaminoglycans promote unseeded amyloid formation from beta2-microglobulin under physiological conditions Kidney Int. 72 2007 174 181
    • (2007) Kidney Int. , vol.72 , pp. 174-181
    • Borysik, A.J.1    Morten, I.J.2    Hewitt, E.W.3
  • 43
    • 0037022186 scopus 로고    scopus 로고
    • Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from α-synuclein in vitro
    • J.A. Cohlberg, and J. Li A.L. Fink Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from α-synuclein in vitro Biochemistry 41 2002 1502 1511
    • (2002) Biochemistry , vol.41 , pp. 1502-1511
    • Cohlberg, J.A.1    Li, J.2    Fink, A.L.3
  • 44
    • 79851492876 scopus 로고    scopus 로고
    • Sulfated glycosaminoglycans accelerate transthyretin amyloidogenesis by quaternary structural conversion
    • S. Bourgault, and J.P. Solomon J.W. Kelly Sulfated glycosaminoglycans accelerate transthyretin amyloidogenesis by quaternary structural conversion Biochemistry 50 2011 1001 1015
    • (2011) Biochemistry , vol.50 , pp. 1001-1015
    • Bourgault, S.1    Solomon, J.P.2    Kelly, J.W.3
  • 45
    • 84861111636 scopus 로고    scopus 로고
    • Effect of heparin on protein aggregation: Inhibition versus promotion
    • Y. Xu, and D. Seeman P.L. Dubin Effect of heparin on protein aggregation: inhibition versus promotion Biomacromolecules 13 2012 1642 1651
    • (2012) Biomacromolecules , vol.13 , pp. 1642-1651
    • Xu, Y.1    Seeman, D.2    Dubin, P.L.3
  • 46
    • 84872849919 scopus 로고    scopus 로고
    • Amyloid formation in heterogeneous environments: Islet amyloid polypeptide glycosaminoglycan interactions
    • H. Wang, P. Cao, and D.P. Raleigh Amyloid formation in heterogeneous environments: islet amyloid polypeptide glycosaminoglycan interactions J. Mol. Biol. 425 2013 492 505
    • (2013) J. Mol. Biol. , vol.425 , pp. 492-505
    • Wang, H.1    Cao, P.2    Raleigh, D.P.3
  • 47
    • 28844482969 scopus 로고    scopus 로고
    • The kinetic behavior of insulin fibrillation is determined by heterogeneous nucleation pathways
    • F. Librizzi, and C. Rischel The kinetic behavior of insulin fibrillation is determined by heterogeneous nucleation pathways Protein Sci. 14 2005 3129 3134
    • (2005) Protein Sci. , vol.14 , pp. 3129-3134
    • Librizzi, F.1    Rischel, C.2
  • 49
    • 52649110660 scopus 로고    scopus 로고
    • Suppression of insulin aggregation by heparin
    • K. Giger, and R.P. Vanam P.L. Dubin Suppression of insulin aggregation by heparin Biomacromolecules 9 2008 2338 2344
    • (2008) Biomacromolecules , vol.9 , pp. 2338-2344
    • Giger, K.1    Vanam, R.P.2    Dubin, P.L.3
  • 50
    • 0033777523 scopus 로고    scopus 로고
    • Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy
    • M. Bouchard, and J. Zurdo C.V. Robinson Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy Protein Sci. 9 2000 1960 1967
    • (2000) Protein Sci. , vol.9 , pp. 1960-1967
    • Bouchard, M.1    Zurdo, J.2    Robinson, C.V.3
  • 51
    • 43049164334 scopus 로고    scopus 로고
    • Secondary nucleation and accessible surface in insulin amyloid fibril formation
    • V. Foderà, and F. Librizzi M. Leone Secondary nucleation and accessible surface in insulin amyloid fibril formation J. Phys. Chem. B 112 2008 3853 3858
    • (2008) J. Phys. Chem. B , vol.112 , pp. 3853-3858
    • Foderà, V.1    Librizzi, F.2    Leone, M.3
  • 52
    • 34247862247 scopus 로고    scopus 로고
    • A three-stage kinetic model of amyloid fibrillation
    • C.C. Lee, and A. Nayak G.J. McRae A three-stage kinetic model of amyloid fibrillation Biophys. J. 92 2007 3448 3458
    • (2007) Biophys. J. , vol.92 , pp. 3448-3458
    • Lee, C.C.1    Nayak, A.2    McRae, G.J.3
  • 53
    • 84878689786 scopus 로고    scopus 로고
    • Mechanistic and environmental control of the prevalence and lifetime of amyloid oligomers
    • R.J. Morris, and K. Eden C.E. Macphee Mechanistic and environmental control of the prevalence and lifetime of amyloid oligomers Nat. Commun. 4 2013 1 18
    • (2013) Nat. Commun. , vol.4 , pp. 1-18
    • Morris, R.J.1    Eden, K.2    MacPhee, C.E.3
  • 54
    • 0141483330 scopus 로고    scopus 로고
    • Partially folded intermediates in insulin fibrillation
    • A. Ahmad, and I.S. Millett A.L. Fink Partially folded intermediates in insulin fibrillation Biochemistry 42 2003 11404 11416
    • (2003) Biochemistry , vol.42 , pp. 11404-11416
    • Ahmad, A.1    Millett, I.S.2    Fink, A.L.3
  • 55
    • 2442715309 scopus 로고    scopus 로고
    • Mechanism of insulin fibrillation: The structure of insulin under amyloidogenic conditions resembles a protein-folding intermediate
    • Q.X. Hua, and M.A. Weiss Mechanism of insulin fibrillation: the structure of insulin under amyloidogenic conditions resembles a protein-folding intermediate J. Biol. Chem. 279 2004 21449 21460
    • (2004) J. Biol. Chem. , vol.279 , pp. 21449-21460
    • Hua, Q.X.1    Weiss, M.A.2
  • 56
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism
    • L. Nielsen, and R. Khurana A.L. Fink Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism Biochemistry 40 2001 6036 6046
    • (2001) Biochemistry , vol.40 , pp. 6036-6046
    • Nielsen, L.1    Khurana, R.2    Fink, A.L.3
  • 57
    • 68149099439 scopus 로고    scopus 로고
    • Self-organization pathways and spatial heterogeneity in insulin amyloid fibril formation
    • V. Foderà, and S. Cataldo M. Leone Self-organization pathways and spatial heterogeneity in insulin amyloid fibril formation J. Phys. Chem. B 113 2009 10830 10837
    • (2009) J. Phys. Chem. B , vol.113 , pp. 10830-10837
    • Foderà, V.1    Cataldo, S.2    Leone, M.3
  • 58
    • 33846283349 scopus 로고    scopus 로고
    • Kinetics of different processes in human insulin amyloid formation
    • M. Manno, and E.F. Craparo P.L. San Biagio Kinetics of different processes in human insulin amyloid formation J. Mol. Biol. 366 2007 258 274
    • (2007) J. Mol. Biol. , vol.366 , pp. 258-274
    • Manno, M.1    Craparo, E.F.2    San Biagio, P.L.3
  • 59
    • 34249028643 scopus 로고    scopus 로고
    • A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils
    • B. Vestergaard, and M. Groenning D.I. Svergun A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils PLoS Biol. 5 2007 e134
    • (2007) PLoS Biol. , vol.5 , pp. 134
    • Vestergaard, B.1    Groenning, M.2    Svergun, D.I.3
  • 60
    • 17144426174 scopus 로고    scopus 로고
    • Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy
    • R. Jansen, W. Dzwolak, and R. Winter Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy Biophys. J. 88 2005 1344 1353
    • (2005) Biophys. J. , vol.88 , pp. 1344-1353
    • Jansen, R.1    Dzwolak, W.2    Winter, R.3
  • 61
    • 33646199155 scopus 로고    scopus 로고
    • Early events in insulin fibrillization studied by time-lapse atomic force microscopy
    • A. Podestà, and G. Tiana M. Manno Early events in insulin fibrillization studied by time-lapse atomic force microscopy Biophys. J. 90 2006 589 597
    • (2006) Biophys. J. , vol.90 , pp. 589-597
    • Podestà, A.1    Tiana, G.2    Manno, M.3
  • 62
    • 40849130157 scopus 로고    scopus 로고
    • Surface-enhanced nucleation of insulin amyloid fibrillation
    • A. Nayak, A.K. Dutta, and G. Belfort Surface-enhanced nucleation of insulin amyloid fibrillation Biochem. Biophys. Res. Commun. 369 2008 303 307
    • (2008) Biochem. Biophys. Res. Commun. , vol.369 , pp. 303-307
    • Nayak, A.1    Dutta, A.K.2    Belfort, G.3
  • 63
    • 0026004620 scopus 로고
    • Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces
    • V. Sluzky, and J.A. Tamada R. Langer Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces Proc. Natl. Acad. Sci. USA 88 1991 9377 9381
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9377-9381
    • Sluzky, V.1    Tamada, J.A.2    Langer, R.3
  • 64
    • 77952320068 scopus 로고    scopus 로고
    • Molecular mechanism of Thioflavin-T binding to amyloid fibrils
    • M. Biancalana, and S. Koide Molecular mechanism of Thioflavin-T binding to amyloid fibrils Biochim. Biophys. Acta 1804 2010 1405 1412
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 1405-1412
    • Biancalana, M.1    Koide, S.2
  • 65
    • 33746648618 scopus 로고    scopus 로고
    • Fibrillation of human insulin A and B chains
    • D.P. Hong, A. Ahmad, and A.L. Fink Fibrillation of human insulin A and B chains Biochemistry 45 2006 9342 9353
    • (2006) Biochemistry , vol.45 , pp. 9342-9353
    • Hong, D.P.1    Ahmad, A.2    Fink, A.L.3
  • 67
    • 0026673537 scopus 로고
    • Effects of sulfate ions on Alzheimer beta/A4 peptide assemblies: Implications for amyloid fibril-proteoglycan interactions
    • P.E. Fraser, and J.T. Nguyen D.A. Kirschner Effects of sulfate ions on Alzheimer beta/A4 peptide assemblies: implications for amyloid fibril-proteoglycan interactions J. Neurochem. 59 1992 1531 1540
    • (1992) J. Neurochem. , vol.59 , pp. 1531-1540
    • Fraser, P.E.1    Nguyen, J.T.2    Kirschner, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.