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Volumn 97, Issue 12, 2009, Pages 3187-3195

Molecular modeling of the misfolded insulin subunit and amyloid fibril

Author keywords

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Indexed keywords

SOLENOIDEA;

EID: 73449140121     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.09.042     Document Type: Article
Times cited : (30)

References (48)
  • 1
    • 0035237310 scopus 로고    scopus 로고
    • Protein folding and its links with human disease
    • Dobson, C. M. 2001. Protein folding and its links with human disease. Biochem. Soc. Symp. 68:1-26.
    • (2001) Biochem. Soc. Symp , vol.68 , pp. 1-26
    • Dobson, C.M.1
  • 3
    • 34547875005 scopus 로고    scopus 로고
    • Structural analyses of fibrinogen amyloid fibrils
    • Serpell, L. C., M. Benson, J. J. Liepnieks, and P. E. Fraser. 2007. Structural analyses of fibrinogen amyloid fibrils. Amyloid. 14:199-203.
    • (2007) Amyloid , vol.14 , pp. 199-203
    • Serpell, L.C.1    Benson, M.2    Liepnieks, J.J.3    Fraser, P.E.4
  • 4
    • 0034716942 scopus 로고    scopus 로고
    • Direct visualisation of the b-sheet structure of synthetic Alzheimer's amyloid
    • Serpell, L. C., and J. M. Smith. 2000. Direct visualisation of the b-sheet structure of synthetic Alzheimer's amyloid. J. Mol. Biol. 299:225 - 231.
    • (2000) J. Mol. Biol , vol.299 , pp. 225-231
    • Serpell, L.C.1    Smith, J.M.2
  • 6
    • 0041343061 scopus 로고    scopus 로고
    • A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy
    • Khurana, R., C. Ionescu-Zanetti, M. Pope, J. Li, L. Nielson, et al. 2003. A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy. Biophys. J. 85:1135 -1144.
    • (2003) Biophys. J , vol.85 , pp. 1135-1144
    • Khurana, R.1    Ionescu-Zanetti, C.2    Pope, M.3    Li, J.4    Nielson, L.5
  • 7
    • 0042847751 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
    • Jimenez, J. L., J. I. Guijarro, E. Orlova, J. Zurdo, C. M. Dobson, et al. 1999. Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J. 18:815 - 821.
    • (1999) EMBO J , vol.18 , pp. 815-821
    • Jimenez, J.L.1    Guijarro, J.I.2    Orlova, E.3    Zurdo, J.4    Dobson, C.M.5
  • 9
    • 0033777523 scopus 로고    scopus 로고
    • Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy
    • Bouchard, M., J. Zurdo, E. J. Nettleton, C. M. Dobson, and C. V. Robinson. 2000. Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy. Protein Sci. 9:1960-1967.
    • (2000) Protein Sci , vol.9 , pp. 1960-1967
    • Bouchard, M.1    Zurdo, J.2    Nettleton, E.J.3    Dobson, C.M.4    Robinson, C.V.5
  • 10
    • 20444440728 scopus 로고    scopus 로고
    • Structure of the cross-β spine of amyloid-like fibrils
    • Nelson, R., M. R. Sawaya, M. Balbirnie, A. O. Madsen, C. Riekel, et al. 2005. Structure of the cross-β spine of amyloid-like fibrils. Nature. 435:773-778.
    • (2005) Nature , vol.435 , pp. 773-778
    • Nelson, R.1    Sawaya, M.R.2    Balbirnie, M.3    Madsen, A.O.4    Riekel, C.5
  • 11
    • 34249290108 scopus 로고    scopus 로고
    • Atomic structures of amyloid cross-β spines reveal varied steric zippers
    • Sawaya, M. R., S. Sambashivan, R. Nelson, M. I. Ivanova, S. A. Sievers, et al. 2007. Atomic structures of amyloid cross-β spines reveal varied steric zippers. Nature. 447:453-457.
    • (2007) Nature , vol.447 , pp. 453-457
    • Sawaya, M.R.1    Sambashivan, S.2    Nelson, R.3    Ivanova, M.I.4    Sievers, S.A.5
  • 13
    • 40849120669 scopus 로고    scopus 로고
    • Amyloid fibrils of the HET-s(218-289) prion form a β solenoid with a triangular hydrophobic core
    • Wasmer, C., A. Lange, H. Van Melckebeke, A. B. Siemer, R. Riek, et al. 2008. Amyloid fibrils of the HET-s(218-289) prion form a β solenoid with a triangular hydrophobic core. Science. 319:1523-1526.
    • (2008) Science , vol.319 , pp. 1523-1526
    • Wasmer, C.1    Lange, A.2    Van Melckebeke, H.3    Siemer, A.B.4    Riek, R.5
  • 14
    • 44949250850 scopus 로고    scopus 로고
    • Paired β-sheet structure of an Ab(1-40) amyloid fibril revealed by electron microscopy
    • Sachse, C., M. Fandrich, and N. Grigorieff. 2008. Paired β-sheet structure of an Ab(1-40) amyloid fibril revealed by electron microscopy. Proc. Natl. Acad. Sci. USA. 105:7462-7466.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 7462-7466
    • Sachse, C.1    Fandrich, M.2    Grigorieff, N.3
  • 15
    • 33845661120 scopus 로고    scopus 로고
    • β-rolls, β-helices, and other β-solenoid proteins
    • Kajava, A. V., and A. C. Steven. 2006. β-rolls, β-helices, and other β-solenoid proteins. Adv. Protein Chem. 73:55-96.
    • (2006) Adv. Protein Chem , vol.73 , pp. 55-96
    • Kajava, A.V.1    Steven, A.C.2
  • 16
    • 0035543109 scopus 로고    scopus 로고
    • The architecture of parallel β-helices and related folds
    • Jenkins, J., and R. Pickersgill. 2001. The architecture of parallel β-helices and related folds. Prog. Biophys. Mol. Biol. 77:111-175.
    • (2001) Prog. Biophys. Mol. Biol , vol.77 , pp. 111-175
    • Jenkins, J.1    Pickersgill, R.2
  • 17
    • 0037168655 scopus 로고    scopus 로고
    • A structural model for Alzheimer's b-amyloid fibrils based on experimental constraints from solid state NMR
    • Petkova, A. T., Y. Ishii, J. J. Balbach, O. N. Antzutkin, R. D. Leapman, et al. 2002. A structural model for Alzheimer's b-amyloid fibrils based on experimental constraints from solid state NMR. Proc. Natl. Acad. Sci. USA. 99:16742-16747.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16742-16747
    • Petkova, A.T.1    Ishii, Y.2    Balbach, J.J.3    Antzutkin, O.N.4    Leapman, R.D.5
  • 20
    • 0023948509 scopus 로고
    • Insulin as an amyloid-fibril protein at sites of repeated insulin injections in a diabetic patient
    • Dische, F. E., C. Wernstedt, G. T. Westermark, P. Westermark, M. B. Pepys, et al. 1988. Insulin as an amyloid-fibril protein at sites of repeated insulin injections in a diabetic patient. Diabetologia. 31:158-161.
    • (1988) Diabetologia , vol.31 , pp. 158-161
    • Dische, F.E.1    Wernstedt, C.2    Westermark, G.T.3    Westermark, P.4    Pepys, M.B.5
  • 21
    • 33745285736 scopus 로고    scopus 로고
    • The component polypeptide chains of bovine insulin nucleate or inhibit aggregation of the parent protein in a conformationdependent manner
    • Devlin, G. L., T. P. Knowles, A. Squires, M. G. McCammon, S. L. Gras, et al. 2006. The component polypeptide chains of bovine insulin nucleate or inhibit aggregation of the parent protein in a conformationdependent manner. J. Mol. Biol. 360:497-509.
    • (2006) J. Mol. Biol , vol.360 , pp. 497-509
    • Devlin, G.L.1    Knowles, T.P.2    Squires, A.3    McCammon, M.G.4    Gras, S.L.5
  • 23
    • 33846321921 scopus 로고
    • Assay of insulin in vitro by fibril elongation and precipitation
    • Waugh, D. F., R. E. Thompson, and R. J. Weimer. 1950. Assay of insulin in vitro by fibril elongation and precipitation. J. Biol. Chem. 185:85-95.
    • (1950) J. Biol. Chem , vol.185 , pp. 85-95
    • Waugh, D.F.1    Thompson, R.E.2    Weimer, R.J.3
  • 24
    • 0015517217 scopus 로고
    • Cross- protein structures. I. Insulin fibrils
    • Burke, M. J., and M. A. Rougvie. 1972. Cross- protein structures. I. Insulin fibrils. Biochemistry. 11:2435-2439.
    • (1972) Biochemistry , vol.11 , pp. 2435-2439
    • Burke, M.J.1    Rougvie, M.A.2
  • 25
    • 2442715309 scopus 로고    scopus 로고
    • Mechanism of insulin fibrillation: The structure of insulin under amyloidogenic conditions resembles a protein-folding intermediate
    • Hua, Q. X., and M. A. Weiss. 2004. Mechanism of insulin fibrillation: the structure of insulin under amyloidogenic conditions resembles a protein-folding intermediate. J. Biol. Chem. 279:21449-21460.
    • (2004) J. Biol. Chem , vol.279 , pp. 21449-21460
    • Hua, Q.X.1    Weiss, M.A.2
  • 26
    • 34249028643 scopus 로고    scopus 로고
    • A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils
    • Vestergaard, B., M. Groenning, M. Roessle, J. S. Kastrup, M. van de Weert, et al. 2007. A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils. PLoS Biol. 5:e134.
    • (2007) PLoS Biol , vol.5
    • Vestergaard, B.1    Groenning, M.2    Roessle, M.3    Kastrup, J.S.4    van de Weert, M.5
  • 27
    • 0033869084 scopus 로고    scopus 로고
    • Characterization of the oligomeric states of insulin in selfassembly and amyloid fibril formation by mass spectrometry
    • Nettleton, E. J., P. Tito, M. Sunde, M. Bouchard, C. M. Dobson, et al. 2000. Characterization of the oligomeric states of insulin in selfassembly and amyloid fibril formation by mass spectrometry. Biophys. J. 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
  • 28
    • 30044446633 scopus 로고    scopus 로고
    • Early events in the fibrillation of monomeric insulin
    • Ahmad, A., V. N. Uversky, D. Hong, and A. L. Fink. 2005. Early events in the fibrillation of monomeric insulin. J. Biol. Chem. 280:42669-42675.
    • (2005) J. Biol. Chem , vol.280 , pp. 42669-42675
    • Ahmad, A.1    Uversky, V.N.2    Hong, D.3    Fink, A.L.4
  • 29
    • 17144426174 scopus 로고    scopus 로고
    • Amyloidogenic selfassembly of insulin aggregates probed by high resolution atomic force microscopy
    • Jansen, R., W. Dzwolak, and R. Winter. 2005. Amyloidogenic selfassembly 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
  • 31
    • 0001751804 scopus 로고    scopus 로고
    • Parametrization of aliphatic CHn united atoms of GROMOS96 force field
    • Daura, X., A. E. Mark, and W. F. Van Gunsteren. 1998. Parametrization of aliphatic CHn united atoms of GROMOS96 force field. J. Comput. Chem. 19:535-547.
    • (1998) J. Comput. Chem , vol.19 , pp. 535-547
    • Daura, X.1    Mark, A.E.2    Van Gunsteren, W.F.3
  • 32
    • 33745620145 scopus 로고    scopus 로고
    • Two-rung model of a left-handed b-helix for prions explains species barrier and strain variation in transmissible spongiform encephalopathies
    • Langedijk, J. P., G. Fuentes, R. Boshuizen, and A. M. Bonvin. 2006. Two-rung model of a left-handed b-helix for prions explains species barrier and strain variation in transmissible spongiform encephalopathies. J. Mol. Biol. 360:907-920.
    • (2006) J. Mol. Biol , vol.360 , pp. 907-920
    • Langedijk, J.P.1    Fuentes, G.2    Boshuizen, R.3    Bonvin, A.M.4
  • 33
    • 50849106747 scopus 로고    scopus 로고
    • Analysis of the sequence and structural features of the left-handed b-helical fold
    • Choi, J. H., C. Govaerts, B. C. May, and F. E. Cohen. 2008. Analysis of the sequence and structural features of the left-handed b-helical fold. Proteins. 73:150-160.
    • (2008) Proteins , vol.73 , pp. 150-160
    • Choi, J.H.1    Govaerts, C.2    May, B.C.3    Cohen, F.E.4
  • 34
    • 85031334301 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 35
    • 85031334241 scopus 로고    scopus 로고
    • Borovinskiy, A. 2006. DISORDER (http://fibernet.vanderbilt.edu/software/ disorder).
    • Borovinskiy, A. 2006. DISORDER (http://fibernet.vanderbilt.edu/software/ disorder).
  • 37
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three-dimensional structure
    • Bowie, J. U., R. Luthy, and D. Eisenberg. 1991. A method to identify protein sequences that fold into a known three-dimensional structure. Science. 253:164-170.
    • (1991) Science , vol.253 , pp. 164-170
    • Bowie, J.U.1    Luthy, R.2    Eisenberg, D.3
  • 38
    • 33646076466 scopus 로고    scopus 로고
    • Standard conformations of b-arches in b-solenoid proteins
    • Hennetin, J., B. Jullian, A. C. Steven, and A. V. Kajava. 2006. Standard conformations of b-arches in b-solenoid proteins. J. Mol. Biol. 358:1094-1105.
    • (2006) J. Mol. Biol , vol.358 , pp. 1094-1105
    • Hennetin, J.1    Jullian, B.2    Steven, A.C.3    Kajava, A.V.4
  • 39
    • 0030907673 scopus 로고    scopus 로고
    • A model of insulin fibrils derived from the x-ray crystal structure of a monomeric insulin (despentapeptide insulin)
    • Brange, J., G. G. Dodson, D. J. Edwards, P. H. Holden, and J. L. Whittingham. 1997. A model of insulin fibrils derived from the x-ray crystal structure of a monomeric insulin (despentapeptide insulin). Proteins. 27:507-516.
    • (1997) Proteins , vol.27 , pp. 507-516
    • Brange, J.1    Dodson, G.G.2    Edwards, D.J.3    Holden, P.H.4    Whittingham, J.L.5
  • 40
    • 29244479548 scopus 로고    scopus 로고
    • Independent heterologous fibrillation of insulin and its B-chain peptide
    • Hong, D. P., and A. L. Fink. 2005. Independent heterologous fibrillation of insulin and its B-chain peptide. Biochemistry. 44:16701-16709.
    • (2005) Biochemistry , vol.44 , pp. 16701-16709
    • Hong, D.P.1    Fink, A.L.2
  • 41
    • 33746648618 scopus 로고    scopus 로고
    • Fibrillation of human insulin A and B chains
    • Hong, D. P., A. Ahmad, and A. L. Fink. 2006. Fibrillation of human insulin A and B chains. Biochemistry. 45:9342-9353.
    • (2006) Biochemistry , vol.45 , pp. 9342-9353
    • Hong, D.P.1    Ahmad, A.2    Fink, A.L.3
  • 42
    • 33748660053 scopus 로고    scopus 로고
    • Structure-specific effects of protein topology on cross-b assembly: Studies of insulin fibrillation
    • Huang, K., N. C. Maiti, N. B. Phillips, P. R. Carey, and M. A. Weiss. 2006. Structure-specific effects of protein topology on cross-b assembly: studies of insulin fibrillation. Biochemistry. 45:10278-10293.
    • (2006) Biochemistry , vol.45 , pp. 10278-10293
    • Huang, K.1    Maiti, N.C.2    Phillips, N.B.3    Carey, P.R.4    Weiss, M.A.5
  • 44
    • 33745815094 scopus 로고    scopus 로고
    • De novo tubular nanostructure design based on self-assembly of b-helical protein motifs
    • Haspel, N., D. Zanuy, C. Aleman, H. Wolfson, and R. Nussinov. 2006. De novo tubular nanostructure design based on self-assembly of b-helical protein motifs. Structure. 14:1137-1148.
    • (2006) Structure , vol.14 , pp. 1137-1148
    • Haspel, N.1    Zanuy, D.2    Aleman, C.3    Wolfson, H.4    Nussinov, R.5
  • 45
    • 33846850446 scopus 로고    scopus 로고
    • Nanostructure design using protein building blocks enhanced by conformationally constrained synthetic residues
    • Zheng, J., D. Zanuy, N. Haspel, C. J. Tsai, C. Aleman, et al. 2007. Nanostructure design using protein building blocks enhanced by conformationally constrained synthetic residues. Biochemistry. 46:1205-1218.
    • (2007) Biochemistry , vol.46 , pp. 1205-1218
    • Zheng, J.1    Zanuy, D.2    Haspel, N.3    Tsai, C.J.4    Aleman, C.5
  • 46
    • 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
  • 47
    • 34548615995 scopus 로고    scopus 로고
    • The structural basis of yeast prion strain variants
    • Toyama, B. H., M. J. Kelly, J. D. Gross, and J. S. Weissman. 2007. The structural basis of yeast prion strain variants. Nature. 449:233-237.
    • (2007) Nature , vol.449 , pp. 233-237
    • Toyama, B.H.1    Kelly, M.J.2    Gross, J.D.3    Weissman, J.S.4


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