메뉴 건너뛰기




Volumn 7, Issue 6, 2012, Pages

Disulfide bridges remain intact while native insulin converts into amyloid fibrils

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; AMYLOID; BOVINE INSULIN; INSULIN; PHENYLALANINE; TYROSINE; DISULFIDE;

EID: 84861730624     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0036989     Document Type: Article
Times cited : (76)

References (51)
  • 1
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson CM, (2003) Protein folding and misfolding. Nature 426: 884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 2
    • 47049117171 scopus 로고    scopus 로고
    • The same primary structure of the prion protein yields two distinct self-propagating states
    • Makarava N, Baskakov IV, (2008) The same primary structure of the prion protein yields two distinct self-propagating states. J Biol Chem 283: 15988-15996.
    • (2008) J Biol Chem , vol.283 , pp. 15988-15996
    • Makarava, N.1    Baskakov, I.V.2
  • 3
    • 0033849965 scopus 로고    scopus 로고
    • Studies on the in vitro assembly of a beta 1-40: implications for the search for a beta fibril formation inhibitors
    • Goldsbury CS, Wirtz S, Muller SA, Sunderji S, Wicki P, et al. (2000) Studies on the in vitro assembly of a beta 1-40: implications for the search for a beta fibril formation inhibitors. J Struct Biol 130: 217-231.
    • (2000) J Struct Biol , vol.130 , pp. 217-231
    • Goldsbury, C.S.1    Wirtz, S.2    Muller, S.A.3    Sunderji, S.4    Wicki, P.5
  • 4
    • 84863903065 scopus 로고    scopus 로고
    • Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis
    • Lindquist SL, Kelly JW, (2011) Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis. Cold Spring Harb Perspect Biol 3: a004507.
    • (2011) Cold Spring Harb Perspect Biol , vol.3
    • Lindquist, S.L.1    Kelly, J.W.2
  • 5
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson CM, (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
  • 6
    • 79960621436 scopus 로고    scopus 로고
    • Disulfide bonds reduce the toxicity of the amyloid fibrils formed by an extracellular protein
    • Mossuto MF, Bolognesi B, Guixer B, Dhulesia A, Agostini F, et al. (2011) Disulfide bonds reduce the toxicity of the amyloid fibrils formed by an extracellular protein. Angew Chem Int Ed Engl 50: 7048-7051.
    • (2011) Angew Chem Int Ed Engl , vol.50 , pp. 7048-7051
    • Mossuto, M.F.1    Bolognesi, B.2    Guixer, B.3    Dhulesia, A.4    Agostini, F.5
  • 7
    • 70349505749 scopus 로고    scopus 로고
    • Formation mechanism of insulin fibrils and structural aspects of the insulin fibrillation process
    • Groenning M, Frokjaer S, Vestergaard B, (2009) Formation mechanism of insulin fibrils and structural aspects of the insulin fibrillation process. Curr Protein Pept Sci 10: 509-528.
    • (2009) Curr Protein Pept Sci , vol.10 , pp. 509-528
    • Groenning, M.1    Frokjaer, S.2    Vestergaard, B.3
  • 9
    • 78650982368 scopus 로고    scopus 로고
    • beta-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages
    • Liu C, Sawaya MR, Eisenberg D, (2011) beta-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages. Nat Struct Mol Biol 18: 49-55.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 49-55
    • Liu, C.1    Sawaya, M.R.2    Eisenberg, D.3
  • 10
    • 0036708005 scopus 로고    scopus 로고
    • The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR
    • Katou H, Kanno T, Hoshino M, Hagihara Y, Tanaka H, et al. (2002) The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR. Protein Sci 11: 2218-2229.
    • (2002) Protein Sci , vol.11 , pp. 2218-2229
    • Katou, H.1    Kanno, T.2    Hoshino, M.3    Hagihara, Y.4    Tanaka, H.5
  • 12
    • 1442356427 scopus 로고    scopus 로고
    • Role of disulfide bonds in the structure and activity of human insulin
    • Chang SG, Choi KD, Jang SH, Shin HC, (2003) Role of disulfide bonds in the structure and activity of human insulin. Mol Cells 16: 323-330.
    • (2003) Mol Cells , vol.16 , pp. 323-330
    • Chang, S.G.1    Choi, K.D.2    Jang, S.H.3    Shin, H.C.4
  • 13
    • 0023948509 scopus 로고
    • Insulin as an amyloid-fibril protein at sites of repeated insulin injections in a diabetic patient
    • Dische FE, Wernstedt C, Westermark GT, Westermark P, Pepys MB, 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
  • 14
    • 0023192941 scopus 로고
    • Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells
    • Westermark P, Wernstedt C, Wilander E, Hayden DW, O'Brien TD, et al. (1987) Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells. Proc Natl Acad Sci U S A 84: 3881-3885.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 3881-3885
    • Westermark, P.1    Wernstedt, C.2    Wilander, E.3    Hayden, D.W.4    O'Brien, T.D.5
  • 15
    • 67649397928 scopus 로고    scopus 로고
    • Bovine insulin filaments induced by reducing disulfide bonds show a different morphology, secondary structure, and cell toxicity from intact insulin amyloid fibrils
    • Zako T, Sakono M, Hashimoto N, Ihara M, Maeda M, (2009) Bovine insulin filaments induced by reducing disulfide bonds show a different morphology, secondary structure, and cell toxicity from intact insulin amyloid fibrils. Biophys J 96: 3331-3340.
    • (2009) Biophys J , vol.96 , pp. 3331-3340
    • Zako, T.1    Sakono, M.2    Hashimoto, N.3    Ihara, M.4    Maeda, M.5
  • 16
    • 0037082115 scopus 로고    scopus 로고
    • Redox processes of methionine relevant to beta-amyloid oxidation and Alzheimer's disease
    • Schoneich C, (2002) Redox processes of methionine relevant to beta-amyloid oxidation and Alzheimer's disease. Arch Biochem Biophys 397: 370-376.
    • (2002) Arch Biochem Biophys , vol.397 , pp. 370-376
    • Schoneich, C.1
  • 17
    • 0042347474 scopus 로고    scopus 로고
    • Three-dimensional structural interactions of insulin and its receptor
    • Yip CC, Ottensmeyer P, (2003) Three-dimensional structural interactions of insulin and its receptor. J Biol Chem 278: 27329-27332.
    • (2003) J Biol Chem , vol.278 , pp. 27329-27332
    • Yip, C.C.1    Ottensmeyer, P.2
  • 19
    • 59849109485 scopus 로고    scopus 로고
    • A universal pathway for amyloid nucleus and precursor formation for insulin
    • Nayak A, Sorci M, Krueger S, Belfort G, (2009) A universal pathway for amyloid nucleus and precursor formation for insulin. Proteins 74: 556-565.
    • (2009) Proteins , vol.74 , pp. 556-565
    • Nayak, A.1    Sorci, M.2    Krueger, S.3    Belfort, G.4
  • 20
    • 33646130171 scopus 로고    scopus 로고
    • Inhibition of insulin fibrillogenesis with targeted peptides
    • Gibson TJ, Murphy RM, (2006) Inhibition of insulin fibrillogenesis with targeted peptides. Protein Sci 15: 1133-1141.
    • (2006) Protein Sci , vol.15 , pp. 1133-1141
    • Gibson, T.J.1    Murphy, R.M.2
  • 21
    • 0035902492 scopus 로고    scopus 로고
    • Probing the mechanism of insulin fibril formation with insulin mutants
    • Nielsen L, Frokjaer S, Brange J, Uversky VN, Fink AL, (2001) Probing the mechanism of insulin fibril formation with insulin mutants. Biochemistry 40: 8397-8409.
    • (2001) Biochemistry , vol.40 , pp. 8397-8409
    • Nielsen, L.1    Frokjaer, S.2    Brange, J.3    Uversky, V.N.4    Fink, A.L.5
  • 23
    • 34249290108 scopus 로고    scopus 로고
    • Atomic structures of amyloid cross-beta spines reveal varied steric zippers
    • Sawaya MR, Sambashivan S, Nelson R, Ivanova MI, Sievers SA, et al. (2007) Atomic structures of amyloid cross-beta 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
  • 24
    • 33645240208 scopus 로고    scopus 로고
    • A systematic screen of beta(2)-microglobulin and insulin for amyloid-like segments
    • Ivanova MI, Thompson MJ, Eisenberg D, (2006) A systematic screen of beta(2)-microglobulin and insulin for amyloid-like segments. Proc Natl Acad Sci U S A 103: 4079-4082.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 4079-4082
    • Ivanova, M.I.1    Thompson, M.J.2    Eisenberg, D.3
  • 25
    • 0036242430 scopus 로고    scopus 로고
    • Mapping the core of the beta(2)-microglobulin amyloid fibril by H/D exchange
    • Hoshino M, Katou H, Hagihara Y, Hasegawa K, Naiki H, et al. (2002) Mapping the core of the beta(2)-microglobulin amyloid fibril by H/D exchange. Nat Struct Biol 9: 332-336.
    • (2002) Nat Struct Biol , vol.9 , pp. 332-336
    • Hoshino, M.1    Katou, H.2    Hagihara, Y.3    Hasegawa, K.4    Naiki, H.5
  • 26
    • 77956205734 scopus 로고    scopus 로고
    • Quantitative methods for structural characterization of proteins based on deep UV resonance Raman spectroscopy
    • Shashilov VA, Sikirzhytski V, Popova LA, Lednev IK, (2010) Quantitative methods for structural characterization of proteins based on deep UV resonance Raman spectroscopy. Methods 52: 23-37.
    • (2010) Methods , vol.52 , pp. 23-37
    • Shashilov, V.A.1    Sikirzhytski, V.2    Popova, L.A.3    Lednev, I.K.4
  • 27
    • 34548710335 scopus 로고    scopus 로고
    • Probing the cross-beta core structure of amyloid fibrils by hydrogen-deuterium exchange deep ultraviolet resonance Raman spectroscopy
    • Xu M, Shashilov V, Lednev IK, (2007) Probing the cross-beta core structure of amyloid fibrils by hydrogen-deuterium exchange deep ultraviolet resonance Raman spectroscopy. J Am Chem Soc 129: 11002-11003.
    • (2007) J Am Chem Soc , vol.129 , pp. 11002-11003
    • Xu, M.1    Shashilov, V.2    Lednev, I.K.3
  • 29
    • 0003919736 scopus 로고
    • NMR of proteins and nucleic acids
    • New York, John Wiley and Son
    • Wuthrich K, (1986) NMR of proteins and nucleic acids. New York John Wiley and Son.
    • (1986)
    • Wuthrich, K.1
  • 30
    • 0003464051 scopus 로고
    • Raman Spectroscopy in Biology: Principles and Applications
    • New York, Wiley
    • Tu AT, (1982) Raman Spectroscopy in Biology: Principles and Applications. New York Wiley.
    • (1982)
    • Tu, A.T.1
  • 31
    • 77958055499 scopus 로고    scopus 로고
    • Advanced statistical and numerical methods for spectroscopic characterization of protein structural evolution
    • Shashilov VA, Lednev IK, (2010) Advanced statistical and numerical methods for spectroscopic characterization of protein structural evolution. Chem Rev 110: 5692-5713.
    • (2010) Chem Rev , vol.110 , pp. 5692-5713
    • Shashilov, V.A.1    Lednev, I.K.2
  • 33
    • 0036304350 scopus 로고    scopus 로고
    • Insulin at pH 2: structural analysis of the conditions promoting insulin fibre formation
    • Whittingham JL, Scott DJ, Chance K, Wilson A, Finch J, et al. (2002) Insulin at pH 2: structural analysis of the conditions promoting insulin fibre formation. J Mol Biol 318: 479-490.
    • (2002) J Mol Biol , vol.318 , pp. 479-490
    • Whittingham, J.L.1    Scott, D.J.2    Chance, K.3    Wilson, A.4    Finch, J.5
  • 34
    • 4444383210 scopus 로고    scopus 로고
    • A comparison of the dynamic behavior of monomeric and dimeric insulin shows structural rearrangements in the active monomer
    • Zoete V, Meuwly M, Karplus M, (2004) A comparison of the dynamic behavior of monomeric and dimeric insulin shows structural rearrangements in the active monomer. J Mol Biol 342: 913-929.
    • (2004) J Mol Biol , vol.342 , pp. 913-929
    • Zoete, V.1    Meuwly, M.2    Karplus, M.3
  • 35
    • 32544446167 scopus 로고    scopus 로고
    • Peptide secondary structure folding reaction coordinate: correlation between uv raman amide III frequency, Psi Ramachandran angle, and hydrogen bonding
    • Mikhonin AV, Bykov SV, Myshakina NS, Asher SA, (2006) Peptide secondary structure folding reaction coordinate: correlation between uv raman amide III frequency, Psi Ramachandran angle, and hydrogen bonding. J Phys Chem B 110: 1928-1943.
    • (2006) J Phys Chem B , vol.110 , pp. 1928-1943
    • Mikhonin, A.V.1    Bykov, S.V.2    Myshakina, N.S.3    Asher, S.A.4
  • 37
    • 77956812220 scopus 로고    scopus 로고
    • Direct observation and pH control of reversed supramolecular chirality in insulin fibrils by vibrational circular dichroism
    • Kurouski D, Lombardi RA, Dukor RK, Lednev IK, Nafie LA, (2010) Direct observation and pH control of reversed supramolecular chirality in insulin fibrils by vibrational circular dichroism. Chem Commun 46: 7154-7156.
    • (2010) Chem Commun , vol.46 , pp. 7154-7156
    • Kurouski, D.1    Lombardi, R.A.2    Dukor, R.K.3    Lednev, I.K.4    Nafie, L.A.5
  • 38
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M, Saudek V, Sklenar V, (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J Biomol NMR 2: 661-665.
    • (1992) J Biomol NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 39
    • 33744991036 scopus 로고    scopus 로고
    • SideLink: automated side-chain assignment of biopolymers from NMR data by relative-hypothesis-prioritization-based simulated logic
    • Masse JE, Keller R, Pervushin K, (2006) SideLink: automated side-chain assignment of biopolymers from NMR data by relative-hypothesis-prioritization-based simulated logic. J Magn Reson 181: 45-67.
    • (2006) J Magn Reson , vol.181 , pp. 45-67
    • Masse, J.E.1    Keller, R.2    Pervushin, K.3
  • 40
    • 0025317134 scopus 로고
    • Complete sequence-specific 1 H NMR assignments for human insulin
    • Kline AD, Justice RM Jr, (1990) Complete sequence-specific 1 H NMR assignments for human insulin. Biochemistry 29: 2906-2913.
    • (1990) Biochemistry , vol.29 , pp. 2906-2913
    • Kline, A.D.1    Justice Jr., R.M.2
  • 41
    • 13844254633 scopus 로고    scopus 로고
    • Deep-UV Raman spectrometer tunable between 193 and 205 nm for structural characterization of proteins
    • Lednev IK, Ermolenkov VV, He W, Xu M, (2005) Deep-UV Raman spectrometer tunable between 193 and 205 nm for structural characterization of proteins. Anal Bioanal Chem 381: 431-437.
    • (2005) Anal Bioanal Chem , vol.381 , pp. 431-437
    • Lednev, I.K.1    Ermolenkov, V.V.2    He, W.3    Xu, M.4
  • 42
    • 34247579524 scopus 로고    scopus 로고
    • The first step of hen egg white lysozyme fibrillation, irreversible partial unfolding, is a two-state transition
    • Xu M, Shashilov V, Ermolenkov VV, Fredriksen L, Zagorevski D, Lednev IK, (2007) The first step of hen egg white lysozyme fibrillation, irreversible partial unfolding, is a two-state transition. Protein Sci 16: 815-832.
    • (2007) Protein Sci , vol.16 , pp. 815-832
    • Xu, M.1    Shashilov, V.2    Ermolenkov, V.V.3    Fredriksen, L.4    Zagorevski, D.5    Lednev, I.K.6
  • 43
  • 44
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: a package for molecular simulation and trajectory analysis
    • Lindahl E, Hess B, van der Spoel D, (2001) GROMACS 3.0: a package for molecular simulation and trajectory analysis. J Mol Model 7: 306-317.
    • (2001) J Mol Model , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    van der Spoel, D.3
  • 45
    • 4444282928 scopus 로고    scopus 로고
    • A Biomolecular Force Field Based of the Free Entahlpy of Hydration and Solvation: The GROMOCS Force-Field Parameter Sets 53A5 and 53A6
    • Oostenbrink C, Villa A, Mark AE, van Gunsteren, WF, (2004) A Biomolecular Force Field Based of the Free Entahlpy of Hydration and Solvation: The GROMOCS Force-Field Parameter Sets 53A5 and 53A6. J Comput Chem 25: 1656-1676.
    • (2004) J Comput Chem , vol.25 , pp. 1656-1676
    • Oostenbrink, C.1    Villa, A.2    Mark, A.E.3    van Gunsteren, W.F.4
  • 46
    • 84986440341 scopus 로고
    • SETTLE: An analytical version of the SHAKE and RATTLE algorithms for rigid water models
    • Miyamoto S, Kollman PA, (1992) SETTLE: An analytical version of the SHAKE and RATTLE algorithms for rigid water models. J Comput Chem 13: 952-062.
    • (1992) J Comput Chem , vol.13 , pp. 062-952
    • Miyamoto, S.1    Kollman, P.A.2
  • 48
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N•log(N) method for Ewald sums in large systems
    • Darden TA, York D, Pedersen L, (1993) Particle mesh Ewald: An N•log(N) method for Ewald sums in large systems. J Chem Phys 98: 10089-10092.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.A.1    York, D.2    Pedersen, L.3
  • 49
    • 33646439285 scopus 로고    scopus 로고
    • Force-Induced Insulin Dimer Dissoaciation: A Molecular Dynamics Study
    • Kim T, Rhee A, Yip CM, (2006) Force-Induced Insulin Dimer Dissoaciation: A Molecular Dynamics Study. J Am Chem Soc 128: 5330-5331.
    • (2006) J Am Chem Soc , vol.128 , pp. 5330-5331
    • Kim, T.1    Rhee, A.2    Yip, C.M.3
  • 50
    • 0036191007 scopus 로고    scopus 로고
    • Models@home: distributed computing in bioinformatics using a screensaver based approach
    • Krieger E, Vriend G, (2002) 18: 315-318 (2002) Models@home: distributed computing in bioinformatics using a screensaver based approach. Bioinformatics.
    • (2002) Bioinformatics , vol.18 , pp. 315-318
    • Krieger, E.1    Vriend, G.2
  • 51
    • 70350266223 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary X-ray diffraction studies of parakeet (Psittacula krameri) haemoglobin
    • Jaimohan SM, Naresh MD, Arumugam V, Mandal AB, (2009) Purification, crystallization and preliminary X-ray diffraction studies of parakeet (Psittacula krameri) haemoglobin. Acta Crystallogr Sect F Struct Biol Cryst Commun 65: 1027-1029.
    • (2009) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.65 , pp. 1027-1029
    • Jaimohan, S.M.1    Naresh, M.D.2    Arumugam, V.3    Mandal, A.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.