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Volumn 23, Issue 1, 2007, Pages 246-254

Insights into the conformational changes of several human lysozyme variants associated with hereditary systemic amyloidosis

Author keywords

[No Author keywords available]

Indexed keywords

COMPUTER SIMULATION; CONFORMATIONS; DISEASES; ETHANOL; HYDROGEN BONDS; HYDROPHOBICITY; MOLECULAR DYNAMICS;

EID: 33847160348     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp060264a     Document Type: Conference Paper
Times cited : (5)

References (60)
  • 1
    • 0030841343 scopus 로고    scopus 로고
    • Conformational disease
    • Carrell, R. W.; Lomas, D. A. Conformational disease. Lancet 1997, 350, 134-138.
    • (1997) Lancet , vol.350 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 2
    • 1642417648 scopus 로고    scopus 로고
    • Amyloid fibrils from the viewpoint of protein folding
    • Ohnishia, S.; Takanob, K. Amyloid fibrils from the viewpoint of protein folding. Cell. Mol. Life Sci. 2004, 61, 511-524.
    • (2004) Cell. Mol. Life Sci , vol.61 , pp. 511-524
    • Ohnishia, S.1    Takanob, K.2
  • 3
    • 0042709605 scopus 로고    scopus 로고
    • Molecular mechanisms of amyloidosis
    • Merlini, G.; Bellotti, V. Molecular mechanisms of amyloidosis. N. Engl. J. Med. 2003, 349, 583-596.
    • (2003) N. Engl. J. Med , vol.349 , pp. 583-596
    • Merlini, G.1    Bellotti, V.2
  • 4
    • 0030004644 scopus 로고    scopus 로고
    • The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate which can self-assemble into amyloid
    • Lai, Z.; Colon, W.; Kelly, J. W. The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate which can self-assemble into amyloid. Biochemistry 1996, 35, 6470-6482.
    • (1996) Biochemistry , vol.35 , pp. 6470-6482
    • Lai, Z.1    Colon, W.2    Kelly, J.W.3
  • 5
    • 0030572683 scopus 로고    scopus 로고
    • For protein misassembly, it's the 'I' decade
    • Wetzel, R. For protein misassembly, it's the 'I' decade. Cell 1996, 86, 699-702.
    • (1996) Cell , vol.86 , pp. 699-702
    • Wetzel, R.1
  • 10
    • 0018025443 scopus 로고
    • Human lysozyme (origin and distribution in health and disease)
    • Reitamo, S.; Klockars, M.; Adinolfi, M.; Osserman, E. F. Human lysozyme (origin and distribution in health and disease). Ric. Clin. Lab. 1987, 138, 211-231.
    • (1987) Ric. Clin. Lab , vol.138 , pp. 211-231
    • Reitamo, S.1    Klockars, M.2    Adinolfi, M.3    Osserman, E.F.4
  • 11
    • 21244468176 scopus 로고    scopus 로고
    • Lysozyme: A paradigmatic molecule for the investigation of protein structure, function and misfolding
    • Merlini, G.; Bellotti, V. Lysozyme: a paradigmatic molecule for the investigation of protein structure, function and misfolding. Clin. Chim. Acta 2005, 357, 168-172.
    • (2005) Clin. Chim. Acta , vol.357 , pp. 168-172
    • Merlini, G.1    Bellotti, V.2
  • 12
    • 0019816864 scopus 로고
    • Refinement of human lysozyme at 1.5 Å resolution analysis of non-bonded and hydrogen-bond interactions
    • Artymiuk, P. J.; Blake, C. C. F. Refinement of human lysozyme at 1.5 Å resolution analysis of non-bonded and hydrogen-bond interactions. J. Mol. Biol. 1981, 152, 737-762.
    • (1981) J. Mol. Biol , vol.152 , pp. 737-762
    • Artymiuk, P.J.1    Blake, C.C.F.2
  • 13
    • 0027506498 scopus 로고    scopus 로고
    • Pepys, M. B.; Hawkins, P. N.; Booth, D. R.; Vigushin, D. M.; Tennent, G. A.; Soutar, A. K.; feestT. G.; Zalin, A. M.; HsuanJ. J. Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature 1993, 362, 553-557.
    • Pepys, M. B.; Hawkins, P. N.; Booth, D. R.; Vigushin, D. M.; Tennent, G. A.; Soutar, A. K.; feestT. G.; Zalin, A. M.; HsuanJ. J. Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature 1993, 362, 553-557.
  • 16
    • 0032444658 scopus 로고    scopus 로고
    • cosolvents come of age. Recent studies with peptides and proteins
    • Buck, M. Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins. Q. Rev. Biophys. 1998, 3, 297-355.
    • (1998) Q. Rev. Biophys , vol.3 , pp. 297-355
    • Buck, M.T.1
  • 17
    • 0033595582 scopus 로고    scopus 로고
    • Clustering of fluorine-substituted alcohols as a factor responsible for their marked effects on proteins and peptides
    • Hong, D.-P.; Hoshino, M.; Kuboi, R.; Goto, Y. Clustering of fluorine-substituted alcohols as a factor responsible for their marked effects on proteins and peptides. J. Am. Chem. Soc. 1999, 121, 8427-8433.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 8427-8433
    • Hong, D.-P.1    Hoshino, M.2    Kuboi, R.3    Goto, Y.4
  • 18
    • 0033019392 scopus 로고    scopus 로고
    • Alcohol-induced denaturation of beta-lactoglobulin: A close correlation to the alcohol-induced alpha-helix formation of melittin
    • Hirota-Nakaoka, N.; Goto, Y. Alcohol-induced denaturation of beta-lactoglobulin: a close correlation to the alcohol-induced alpha-helix formation of melittin. Bioorg. Med. Chem. 1999, 7, 67-73.
    • (1999) Bioorg. Med. Chem , vol.7 , pp. 67-73
    • Hirota-Nakaoka, N.1    Goto, Y.2
  • 19
    • 0034005357 scopus 로고    scopus 로고
    • Amyloid protofilament formation of hen egg lysozyme in highly concentrated ethanol solution
    • Goda, S.; Takano, K.; Yamagat, Y.; Nagata, R.; Akutsu, H.; Maki, S.; Namba, K.; Yutani, K. Amyloid protofilament formation of hen egg lysozyme in highly concentrated ethanol solution. Protein Sci. 2000, 9, 369-375.
    • (2000) Protein Sci , vol.9 , pp. 369-375
    • Goda, S.1    Takano, K.2    Yamagat, Y.3    Nagata, R.4    Akutsu, H.5    Maki, S.6    Namba, K.7    Yutani, K.8
  • 21
    • 0025278448 scopus 로고    scopus 로고
    • Westermark, P.; Sletten, K.; Johansson, B.; Cornwell, G. G. 3rd. Fibril in senile systemic amyloidosis is derived from normal transthyretin. Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 2843-2845.
    • Westermark, P.; Sletten, K.; Johansson, B.; Cornwell, G. G. 3rd. Fibril in senile systemic amyloidosis is derived from normal transthyretin. Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 2843-2845.
  • 22
    • 0036775896 scopus 로고    scopus 로고
    • Elongation in a beta-structure promotes amyloid-like fibril formation of human lysozyme
    • Goda, S.; Takano, K.; Yamagata, Y.; Maki, S.; Namba, K.; Yutani, K. Elongation in a beta-structure promotes amyloid-like fibril formation of human lysozyme. J. Biochem. (Tokyo) 2002, 4, 655-661.
    • (2002) J. Biochem. (Tokyo) , vol.4 , pp. 655-661
    • Goda, S.1    Takano, K.2    Yamagata, Y.3    Maki, S.4    Namba, K.5    Yutani, K.6
  • 23
    • 0038647638 scopus 로고    scopus 로고
    • The effects of solvent and temperature on the structural integrity of monomeric melittin by molecular dynamics simulations
    • Liu, H.-L.; Hsu, C-M. The effects of solvent and temperature on the structural integrity of monomeric melittin by molecular dynamics simulations. Chem. Phys. Lett. 2003, 375, 119-125.
    • (2003) Chem. Phys. Lett , vol.375 , pp. 119-125
    • Liu, H.-L.1    Hsu, C.-M.2
  • 24
    • 0037058670 scopus 로고    scopus 로고
    • The predicted unfolding order of the β-strands in the starch binding domain from Aspergillus niger glucoamylase
    • Liu, H.-L.; Wang, W.-C. The predicted unfolding order of the β-strands in the starch binding domain from Aspergillus niger glucoamylase. Chem. Phys. Lett. 2003, 366, 284-290.
    • (2003) Chem. Phys. Lett , vol.366 , pp. 284-290
    • Liu, H.-L.1    Wang, W.-C.2
  • 25
    • 0037387089 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the unfolding of the starch binding domain from Aspergillus niger glucoamylase
    • Liu, H.-L.; Wang, W.-C. Molecular dynamics simulations of the unfolding of the starch binding domain from Aspergillus niger glucoamylase. J. Biomol. Struct. Dyn. 2003, 20, 615-622.
    • (2003) J. Biomol. Struct. Dyn , vol.20 , pp. 615-622
    • Liu, H.-L.1    Wang, W.-C.2
  • 26
    • 0141873352 scopus 로고    scopus 로고
    • Predicted unfolding order of the 13 α-helices in the catalytic domain of glucoamylase from Aspergillus awamori var. X100 by molecular dynamics simulations
    • Liu, H.-L.; Wang, W.-C. Predicted unfolding order of the 13 α-helices in the catalytic domain of glucoamylase from Aspergillus awamori var. X100 by molecular dynamics simulations. Biotechnol. Prog. 2003, 19, 1583-1590.
    • (2003) Biotechnol. Prog , vol.19 , pp. 1583-1590
    • Liu, H.-L.1    Wang, W.-C.2
  • 27
    • 0037320744 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the unfolding mechanism of the catalytic domain from Aspergillus awamori var. X100 glucoamylase
    • Liu, H.-L.; Wang, W.-C.; Hsu, C.-M. Molecular dynamics simulations of the unfolding mechanism of the catalytic domain from Aspergillus awamori var. X100 glucoamylase. J. Biomol. Struct Dyn. 2003, 20, 567-574.
    • (2003) J. Biomol. Struct Dyn , vol.20 , pp. 567-574
    • Liu, H.-L.1    Wang, W.-C.2    Hsu, C.-M.3
  • 28
    • 4143088346 scopus 로고    scopus 로고
    • Molecular dynamics simulations to investigate the temperature effect on the main proteinases from various coronaviruses
    • Liu, H.-L.; Lin, J.-C.; Hsieh, W.-C.; Chen, C.-W.; Su, Y.-C. Molecular dynamics simulations to investigate the temperature effect on the main proteinases from various coronaviruses. J. Biomol. Struct. Dyn. 2004, 22, 65-77.
    • (2004) J. Biomol. Struct. Dyn , vol.22 , pp. 65-77
    • Liu, H.-L.1    Lin, J.-C.2    Hsieh, W.-C.3    Chen, C.-W.4    Su, Y.-C.5
  • 29
    • 21044445789 scopus 로고    scopus 로고
    • Molecular dynamics simulations to investigate the thermal unfolding behaviors of N-carbamyl-D-amino acid amidohydrolase
    • Liu, H.-L.; Hsieh, W.-C. Molecular dynamics simulations to investigate the thermal unfolding behaviors of N-carbamyl-D-amino acid amidohydrolase. J. Chin. Inst. Chem. Eng. 2005, 36, 185-194.
    • (2005) J. Chin. Inst. Chem. Eng , vol.36 , pp. 185-194
    • Liu, H.-L.1    Hsieh, W.-C.2
  • 30
    • 32344444190 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the tetramerization domain of Shaker and Kv1.1 potassium channels
    • Chen, C.-W.; Lin, J.-C.; Liu, H.-L. Molecular dynamics simulations of the tetramerization domain of Shaker and Kv1.1 potassium channels. J. Chin. Inst. Chem. Eng. 2005, 36, 649-660.
    • (2005) J. Chin. Inst. Chem. Eng , vol.36 , pp. 649-660
    • Chen, C.-W.1    Lin, J.-C.2    Liu, H.-L.3
  • 31
    • 33845329531 scopus 로고    scopus 로고
    • Structural analysis of human lysozyme using molecular dynamics simulations
    • Liu, H.-L.; Wu, Y.-C.; Zhao, J.-H.; Fang, H.-W.; Ho, Y. Structural analysis of human lysozyme using molecular dynamics simulations. J. Biomol. Struct. Dyn. 2006, 24, 229-238.
    • (2006) J. Biomol. Struct. Dyn , vol.24 , pp. 229-238
    • Liu, H.-L.1    Wu, Y.-C.2    Zhao, J.-H.3    Fang, H.-W.4    Ho, Y.5
  • 33
    • 33847153725 scopus 로고    scopus 로고
    • The effects of salt and pH on the spermatozoa agglutinating activity of carp ovum cystatin by molecular dynamics simulations
    • Su, Y.-C.; Liu, H.-L. The effects of salt and pH on the spermatozoa agglutinating activity of carp ovum cystatin by molecular dynamics simulations. J. Chin. Chem. Soc. 2006, 53, 713-720.
    • (2006) J. Chin. Chem. Soc , vol.53 , pp. 713-720
    • Su, Y.-C.1    Liu, H.-L.2
  • 34
    • 33344454916 scopus 로고    scopus 로고
    • The effects of various alcohols on the stability of melittin: A molecular dynamics study
    • Liu, H.-L.; Hsu, C.-M. The effects of various alcohols on the stability of melittin: A molecular dynamics study. J. Chin. Chem. Soc. 2003, 50, 1235-1240.
    • (2003) J. Chin. Chem. Soc , vol.50 , pp. 1235-1240
    • Liu, H.-L.1    Hsu, C.-M.2
  • 35
    • 2942748486 scopus 로고    scopus 로고
    • Molecular dynamics simulations to determine the effect of supercritical carbon dioxide on the structural integrity of hen egg white lysozyme
    • Liu, H.-L.; Hsieh, W.-C.; Liu, H-S. Molecular dynamics simulations to determine the effect of supercritical carbon dioxide on the structural integrity of hen egg white lysozyme. Biotechnol. Prog. 2004, 20, 930-938.
    • (2004) Biotechnol. Prog , vol.20 , pp. 930-938
    • Liu, H.-L.1    Hsieh, W.-C.2    Liu, H.-S.3
  • 36
    • 33344463350 scopus 로고    scopus 로고
    • The effects of various alcohols on the structural stability of melittin, TH-10Aox, and Tc1 by molecular dynamics simulations
    • Zhao, J.-H.; Liu, H.-L. The effects of various alcohols on the structural stability of melittin, TH-10Aox, and Tc1 by molecular dynamics simulations. Chem. Phys. Lett. 2006, 420, 235-240.
    • (2006) Chem. Phys. Lett , vol.420 , pp. 235-240
    • Zhao, J.-H.1    Liu, H.-L.2
  • 37
    • 0036968512 scopus 로고    scopus 로고
    • Increasing temperature accelerates protein unfolding without changing the pathway of unfolding
    • Day, R.; Bennion, B.; Ham, S.; Daggett, V. Increasing temperature accelerates protein unfolding without changing the pathway of unfolding. J. Mol. Biol. 2002, 322, 189-203.
    • (2002) J. Mol. Biol , vol.322 , pp. 189-203
    • Day, R.1    Bennion, B.2    Ham, S.3    Daggett, V.4
  • 38
    • 0032080288 scopus 로고    scopus 로고
    • Derivation of class II force fields. VI. Carbohydrate compounds and anomeric effects
    • Hwang, M. J.; Ni, X.; Waldman, M.; Ewig, C. S.; Hagler, A. T. Derivation of class II force fields. VI. Carbohydrate compounds and anomeric effects. Biopolymers 1998, 45, 435-468.
    • (1998) Biopolymers , vol.45 , pp. 435-468
    • Hwang, M.J.1    Ni, X.2    Waldman, M.3    Ewig, C.S.4    Hagler, A.T.5
  • 40
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W.; Sander, C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983, 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 41
    • 0347753598 scopus 로고    scopus 로고
    • Energetics of protein thermodynamic cooperativity: Contributions of local and nonlocal interactions
    • Knott, M.; Kaya, H.; Chan, H. S. Energetics of protein thermodynamic cooperativity: contributions of local and nonlocal interactions. Polymer 2004, 45, 623-632.
    • (2004) Polymer , vol.45 , pp. 623-632
    • Knott, M.1    Kaya, H.2    Chan, H.S.3
  • 43
    • 0037381819 scopus 로고    scopus 로고
    • Simulations of human lysozyme: Probing the conformations triggering amyloidosis
    • Moraitakis, G.; Goodfellow, J. M. Simulations of human lysozyme: probing the conformations triggering amyloidosis. Biophys. J. 2003, 84, 2149-2158.
    • (2003) Biophys. J , vol.84 , pp. 2149-2158
    • Moraitakis, G.1    Goodfellow, J.M.2
  • 44
    • 0033516512 scopus 로고    scopus 로고
    • Analysis methods for comparison of multiple molecular dynamics trajectories: Applications to protein unfolding pathways and denatured ensembles
    • Kazmirski, S. L.; Li, A.; Daggett, V. Analysis methods for comparison of multiple molecular dynamics trajectories: applications to protein unfolding pathways and denatured ensembles. J. Mol. Biol. 1999, 290, 283-304.
    • (1999) J. Mol. Biol , vol.290 , pp. 283-304
    • Kazmirski, S.L.1    Li, A.2    Daggett, V.3
  • 46
    • 0033580657 scopus 로고    scopus 로고
    • Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants
    • Canet, D.; Sunde, M.; Last, A. M.; Miranker, A.; Spencer, A.; Robinson, C. V.; Dobson, C. M. Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants. Biochemistry 1999, 38, 6419-6427.
    • (1999) Biochemistry , vol.38 , pp. 6419-6427
    • Canet, D.1    Sunde, M.2    Last, A.M.3    Miranker, A.4    Spencer, A.5    Robinson, C.V.6    Dobson, C.M.7
  • 47
    • 0032484148 scopus 로고    scopus 로고
    • Non-native interactions in protein folding intermediates: Molecular dynamics simulations of hen lysozyme
    • Kazmirski, S. L.; Daggett, V. Non-native interactions in protein folding intermediates: molecular dynamics simulations of hen lysozyme. J. Mol. Biol. 1998, 284, 793-806.
    • (1998) J. Mol. Biol , vol.284 , pp. 793-806
    • Kazmirski, S.L.1    Daggett, V.2
  • 48
    • 0030727330 scopus 로고    scopus 로고
    • Modelling protein unfolding: Hen egg-white lysozyme
    • Williams, M. A.; Thornton, J. M.; Goodfellow, J. M. Modelling protein unfolding: hen egg-white lysozyme. Protein Eng. 1997, 10, 895-903.
    • (1997) Protein Eng , vol.10 , pp. 895-903
    • Williams, M.A.1    Thornton, J.M.2    Goodfellow, J.M.3
  • 49
    • 0032579189 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the unfolding of barnase: Characterization of the major intermediate
    • Li, A.; Daggett, V. Molecular dynamics simulation of the unfolding of barnase: characterization of the major intermediate. J. Mol. Biol. 1998, 275, 677-694.
    • (1998) J. Mol. Biol , vol.275 , pp. 677-694
    • Li, A.1    Daggett, V.2
  • 51
    • 0028926875 scopus 로고
    • Computational approaches to study protein unfolding: Hen egg white lysozyme as a case study
    • Hünenberger, P. H.; Mark, A. E.; van Gunsteren, W. F. Computational approaches to study protein unfolding: hen egg white lysozyme as a case study. Proteins: Struct. Funct. Genet. 1995, 21, 196-213.
    • (1995) Proteins: Struct. Funct. Genet , vol.21 , pp. 196-213
    • Hünenberger, P.H.1    Mark, A.E.2    van Gunsteren, W.F.3
  • 52
    • 0034308141 scopus 로고    scopus 로고
    • Unfolding of hen egg lysozyme by molecular dynamics simulations at 300 K: Insight into the role of the interdomain interface
    • Gilquin, B.; Guilbert, C.; Perahia, D. Unfolding of hen egg lysozyme by molecular dynamics simulations at 300 K: insight into the role of the interdomain interface. Proteins: Struct. Funct. Genet. 2000, 41, 58-74.
    • (2000) Proteins: Struct. Funct. Genet , vol.41 , pp. 58-74
    • Gilquin, B.1    Guilbert, C.2    Perahia, D.3
  • 53
    • 0034599720 scopus 로고    scopus 로고
    • Mutational analysis of the propensity for amyloid formation by a globular protein
    • Chili, F.; Taddei, N.; Bucciantini, M.; White, P.; Ramponi, G.; Dobson, C. M. Mutational analysis of the propensity for amyloid formation by a globular protein. EMBO J. 2000, 19, 1441-1449.
    • (2000) EMBO J , vol.19 , pp. 1441-1449
    • Chili, F.1    Taddei, N.2    Bucciantini, M.3    White, P.4    Ramponi, G.5    Dobson, C.M.6
  • 55
    • 0025679019 scopus 로고    scopus 로고
    • Tobias, D. J.; Sneddon, S. P.; Brooks, C. L. 3rd. Reverse turns in blocked dipeptides are intrinsically unstable in water. J. Mol. Biol. 1990, 216, 783-796.
    • Tobias, D. J.; Sneddon, S. P.; Brooks, C. L. 3rd. Reverse turns in blocked dipeptides are intrinsically unstable in water. J. Mol. Biol. 1990, 216, 783-796.
  • 57
    • 0026743136 scopus 로고
    • Folding of peptide fragments comprising the complete sequence of proteins models for initiation of protein folding. II. Plastocyanin
    • Dyson, H. J.; Sayre, J. R.; Merutka, G.; Shin, H. C.; Lerner, R. A.; Wright, P. E. Folding of peptide fragments comprising the complete sequence of proteins models for initiation of protein folding. II. Plastocyanin. J. Mol. Biol. 1992, 226, 819-835.
    • (1992) J. Mol. Biol , vol.226 , pp. 819-835
    • Dyson, H.J.1    Sayre, J.R.2    Merutka, G.3    Shin, H.C.4    Lerner, R.A.5    Wright, P.E.6
  • 58
    • 0025784650 scopus 로고
    • Dynamic Monte Carlo simulations of a new lattice model of globular protein folding, structure and dynamics
    • Skolnick, J.; Kolinski, A. Dynamic Monte Carlo simulations of a new lattice model of globular protein folding, structure and dynamics. J. Mol. Biol. 1991, 221, 499-531.
    • (1991) J. Mol. Biol , vol.221 , pp. 499-531
    • Skolnick, J.1    Kolinski, A.2
  • 59
    • 0030596522 scopus 로고    scopus 로고
    • Free energy determinants of secondary structure formation: III. Beta-turns and their role in protein folding
    • Yang, A. S.; Hitz, B.; Honig, B. Free energy determinants of secondary structure formation: III. Beta-turns and their role in protein folding. J. Mol. Biol. 1996, 259, 873-882.
    • (1996) J. Mol. Biol , vol.259 , pp. 873-882
    • Yang, A.S.1    Hitz, B.2    Honig, B.3


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