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Volumn 105, Issue 5, 2013, Pages 1227-1235

Effect of proline mutations on the monomer conformations of amylin

Author keywords

[No Author keywords available]

Indexed keywords

AMYLIN; MUTANT PROTEIN; PRAMLINTIDE; PROLINE;

EID: 84883609138     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.07.029     Document Type: Article
Times cited : (47)

References (74)
  • 1
    • 79954535899 scopus 로고    scopus 로고
    • Islet amyloid polypeptide, islet amyloid, and diabetes mellitus
    • P. Westermark, A. Andersson, and G.T. Westermark Islet amyloid polypeptide, islet amyloid, and diabetes mellitus Physiol. Rev. 91 2011 795 826
    • (2011) Physiol. Rev. , vol.91 , pp. 795-826
    • Westermark, P.1    Andersson, A.2    Westermark, G.T.3
  • 2
    • 67650325176 scopus 로고    scopus 로고
    • The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: Insights from type II diabetes
    • J.A. Hebda, and A.D. Miranker The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: insights from type II diabetes Annu. Rev. Biophys 38 2009 125 152
    • (2009) Annu. Rev. Biophys , vol.38 , pp. 125-152
    • Hebda, J.A.1    Miranker, A.D.2
  • 3
    • 84873527000 scopus 로고    scopus 로고
    • Aggregation of islet amyloid polypeptide: From physical chemistry to cell biology
    • P. Cao, A. Abedini, and D.P. Raleigh Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology Curr. Opin. Struct. Biol. 23 2013 82 89
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 82-89
    • Cao, P.1    Abedini, A.2    Raleigh, D.P.3
  • 4
    • 0000845316 scopus 로고
    • Hyalinization of the islet of Langerhans in diabetes mellitus
    • E.T. Bell Hyalinization of the islet of Langerhans in diabetes mellitus Diabetes 1 1952 341 344
    • (1952) Diabetes , vol.1 , pp. 341-344
    • Bell, E.T.1
  • 5
    • 0023189095 scopus 로고
    • Islet amyloid formed from diabetes-associated peptide may be pathogenic in type-2 diabetes
    • A. Clark, and G.J. Cooper R.C. Turner Islet amyloid formed from diabetes-associated peptide may be pathogenic in type-2 diabetes Lancet 2 1987 231 234
    • (1987) Lancet , vol.2 , pp. 231-234
    • Clark, A.1    Cooper, G.J.2    Turner, R.C.3
  • 6
    • 0024213009 scopus 로고
    • Islet amyloid, increased A-cells, reduced B-cells and exocrine fibrosis: Quantitative changes in the pancreas in type 2 diabetes
    • A. Clark, and C.A. Wells R.C. Turner Islet amyloid, increased A-cells, reduced B-cells and exocrine fibrosis: quantitative changes in the pancreas in type 2 diabetes Diabetes Res. 9 1988 151 159
    • (1988) Diabetes Res. , vol.9 , pp. 151-159
    • Clark, A.1    Wells, C.A.2    Turner, R.C.3
  • 7
    • 0028303844 scopus 로고
    • Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus
    • A. Lorenzo, and B. Razzaboni B.A. Yankner Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus Nature 368 1994 756 760
    • (1994) Nature , vol.368 , pp. 756-760
    • Lorenzo, A.1    Razzaboni, B.2    Yankner, B.A.3
  • 8
    • 0015884138 scopus 로고
    • The pancreatic islet cells in insular amyloidosis in human diabetic and non-diabetic adults
    • P. Westermark, and L. Grimelius The pancreatic islet cells in insular amyloidosis in human diabetic and non-diabetic adults Acta Pathol. Microbiol. Scand. [A] 81 1973 291 300
    • (1973) Acta Pathol. Microbiol. Scand. [A] , vol.81 , pp. 291-300
    • Westermark, P.1    Grimelius, L.2
  • 9
    • 0018146301 scopus 로고
    • The influence of amyloid deposits on the islet volume in maturity onset diabetes mellitus
    • P. Westermark, and E. Wilander The influence of amyloid deposits on the islet volume in maturity onset diabetes mellitus Diabetologia 15 1978 417 421
    • (1978) Diabetologia , vol.15 , pp. 417-421
    • Westermark, P.1    Wilander, E.2
  • 10
    • 0030025653 scopus 로고    scopus 로고
    • Effects of β cell granule components on human islet amyloid polypeptide fibril formation
    • P. Westermark, and Z.C. Li D.F. Steiner Effects of β cell granule components on human islet amyloid polypeptide fibril formation FEBS Lett. 379 1996 203 206
    • (1996) FEBS Lett. , vol.379 , pp. 203-206
    • Westermark, P.1    Li, Z.C.2    Steiner, D.F.3
  • 11
    • 0018130887 scopus 로고
    • Insular amyloidosis and diabetes mellitus in Macaca nigra
    • C.F. Howard Jr. Insular amyloidosis and diabetes mellitus in Macaca nigra Diabetes 27 1978 357 364
    • (1978) Diabetes , vol.27 , pp. 357-364
    • Howard, Jr.C.F.1
  • 12
    • 0019795815 scopus 로고
    • Feline insular amyloid: Association with diabetes mellitus
    • B.L. Yano, D.W. Hayden, and K.H. Johnson Feline insular amyloid: association with diabetes mellitus Vet. Pathol. 18 1981 621 627
    • (1981) Vet. Pathol. , vol.18 , pp. 621-627
    • Yano, B.L.1    Hayden, D.W.2    Johnson, K.H.3
  • 14
    • 0024400674 scopus 로고
    • Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species
    • C. Betsholtz, and L. Christmansson P. Westermark Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species FEBS Lett. 251 1989 261 264
    • (1989) FEBS Lett. , vol.251 , pp. 261-264
    • Betsholtz, C.1    Christmansson, L.2    Westermark, P.3
  • 15
    • 0037470589 scopus 로고    scopus 로고
    • Full-length rat amylin forms fibrils following substitution of single residues from human amylin
    • J. Green, and C. Goldsbury U. Aebi Full-length rat amylin forms fibrils following substitution of single residues from human amylin J. Mol. Biol. 326 2003 1147 1156
    • (2003) J. Mol. Biol. , vol.326 , pp. 1147-1156
    • Green, J.1    Goldsbury, C.2    Aebi, U.3
  • 16
    • 0025366838 scopus 로고
    • Islet amyloid polypeptide: Pinpointing amino acid residues linked to amyloid fibril formation
    • P. Westermark, and U. Engström C. Betsholtz Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation Proc. Natl. Acad. Sci. USA 87 1990 5036 5040
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5036-5040
    • Westermark, P.1    Engström, U.2    Betsholtz, C.3
  • 17
    • 0032972592 scopus 로고    scopus 로고
    • Effects of sequential proline substitutions on amyloid formation by human amylin20-29
    • D.F. Moriarty, and D.P. Raleigh Effects of sequential proline substitutions on amyloid formation by human amylin20-29 Biochemistry 38 1999 1811 1818
    • (1999) Biochemistry , vol.38 , pp. 1811-1818
    • Moriarty, D.F.1    Raleigh, D.P.2
  • 18
    • 84860232628 scopus 로고    scopus 로고
    • Two-dimensional infrared spectroscopy reveals the complex behaviour of an amyloid fibril inhibitor
    • C.T. Middleton, and P. Marek M.T. Zanni Two-dimensional infrared spectroscopy reveals the complex behaviour of an amyloid fibril inhibitor Nat. Chem. 4 2012 355 360
    • (2012) Nat. Chem. , vol.4 , pp. 355-360
    • Middleton, C.T.1    Marek, P.2    Zanni, M.T.3
  • 19
    • 84873685394 scopus 로고    scopus 로고
    • Comparative molecular dynamics study of human islet amyloid polypeptide (IAPP) and rat IAPP oligomers
    • G. Liang, and J. Zhao J. Zheng Comparative molecular dynamics study of human islet amyloid polypeptide (IAPP) and rat IAPP oligomers Biochemistry 52 2013 1089 1100
    • (2013) Biochemistry , vol.52 , pp. 1089-1100
    • Liang, G.1    Zhao, J.2    Zheng, J.3
  • 21
    • 8144228619 scopus 로고    scopus 로고
    • Amylin replacement with pramlintide as an adjunct to insulin therapy improves long-term glycaemic and weight control in Type 1 diabetes mellitus: A 1-year, randomized controlled trial
    • R.E. Ratner, and R. Dickey O.G. Kolterman Amylin replacement with pramlintide as an adjunct to insulin therapy improves long-term glycaemic and weight control in Type 1 diabetes mellitus: a 1-year, randomized controlled trial Diabet. Med. 21 2004 1204 1212
    • (2004) Diabet. Med. , vol.21 , pp. 1204-1212
    • Ratner, R.E.1    Dickey, R.2    Kolterman, O.G.3
  • 22
    • 28444467706 scopus 로고    scopus 로고
    • Pramlintide in the treatment of type 1 and type 2 diabetes mellitus
    • G.J. Ryan, L.J. Jobe, and R. Martin Pramlintide in the treatment of type 1 and type 2 diabetes mellitus Clin. Ther. 27 2005 1500 1512
    • (2005) Clin. Ther. , vol.27 , pp. 1500-1512
    • Ryan, G.J.1    Jobe, L.J.2    Martin, R.3
  • 23
    • 0035969513 scopus 로고    scopus 로고
    • Islet amyloid and type 2 diabetes: From molecular misfolding to islet pathophysiology
    • E.T. Jaikaran, and A. Clark Islet amyloid and type 2 diabetes: from molecular misfolding to islet pathophysiology Biochim. Biophys. Acta 1537 2001 179 203
    • (2001) Biochim. Biophys. Acta , vol.1537 , pp. 179-203
    • Jaikaran, E.T.1    Clark, A.2
  • 24
    • 0033538015 scopus 로고    scopus 로고
    • Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in vitro
    • R. Kayed, and J. Bernhagen A. Kapurniotu Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in vitro J. Mol. Biol. 287 1999 781 796
    • (1999) J. Mol. Biol. , vol.287 , pp. 781-796
    • Kayed, R.1    Bernhagen, J.2    Kapurniotu, A.3
  • 25
    • 0025820540 scopus 로고
    • Molecular model-building of amylin and α-calcitonin gene-related polypeptide hormones using a combination of knowledge sources
    • J. Saldanha, and D. Mahadevan Molecular model-building of amylin and α-calcitonin gene-related polypeptide hormones using a combination of knowledge sources Protein Eng. 4 1991 539 544
    • (1991) Protein Eng. , vol.4 , pp. 539-544
    • Saldanha, J.1    Mahadevan, D.2
  • 26
    • 33747119677 scopus 로고    scopus 로고
    • Conserved and cooperative assembly of membrane-bound α-helical states of islet amyloid polypeptide
    • J.D. Knight, J.A. Hebda, and A.D. Miranker Conserved and cooperative assembly of membrane-bound α-helical states of islet amyloid polypeptide Biochemistry 45 2006 9496 9508
    • (2006) Biochemistry , vol.45 , pp. 9496-9508
    • Knight, J.D.1    Hebda, J.A.2    Miranker, A.D.3
  • 27
    • 67650533782 scopus 로고    scopus 로고
    • Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy
    • R.P.R. Nanga, and J.R. Brender A. Ramamoorthy Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy J. Am. Chem. Soc. 131 2009 8252 8261
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 8252-8261
    • Nanga, R.P.R.1    Brender, J.R.2    Ramamoorthy, A.3
  • 28
    • 66449087200 scopus 로고    scopus 로고
    • Dynamic α-helix structure of micelle-bound human amylin
    • S.M. Patil, and S. Xu A.T. Alexandrescu Dynamic α-helix structure of micelle-bound human amylin J. Biol. Chem. 284 2009 11982 11991
    • (2009) J. Biol. Chem. , vol.284 , pp. 11982-11991
    • Patil, S.M.1    Xu, S.2    Alexandrescu, A.T.3
  • 29
    • 33845960266 scopus 로고    scopus 로고
    • Direct detection of transient α-helical states in islet amyloid polypeptide
    • J.A. Williamson, and A.D. Miranker Direct detection of transient α-helical states in islet amyloid polypeptide Protein Sci. 16 2007 110 117
    • (2007) Protein Sci. , vol.16 , pp. 110-117
    • Williamson, J.A.1    Miranker, A.D.2
  • 30
    • 70349207190 scopus 로고    scopus 로고
    • Solution state structures of human pancreatic amylin and pramlintide
    • J.R. Cort, and Z. Liu N.H. Andersen Solution state structures of human pancreatic amylin and pramlintide Protein Eng. Des. Sel. 22 2009 497 513
    • (2009) Protein Eng. Des. Sel. , vol.22 , pp. 497-513
    • Cort, J.R.1    Liu, Z.2    Andersen, N.H.3
  • 31
    • 16244376187 scopus 로고    scopus 로고
    • The parallel superpleated β-structure as a model for amyloid fibrils of human amylin
    • A.V. Kajava, U. Aebi, and A.C. Steven The parallel superpleated β-structure as a model for amyloid fibrils of human amylin J. Mol. Biol. 348 2005 247 252
    • (2005) J. Mol. Biol. , vol.348 , pp. 247-252
    • Kajava, A.V.1    Aebi, U.2    Steven, A.C.3
  • 32
    • 36749033116 scopus 로고    scopus 로고
    • Peptide conformation and supramolecular organization in amylin fibrils: Constraints from solid-state NMR
    • S. Luca, and W.-M. Yau R. Tycko Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR Biochemistry 46 2007 13505 13522
    • (2007) Biochemistry , vol.46 , pp. 13505-13522
    • Luca, S.1    Yau, W.-M.2    Tycko, R.3
  • 33
    • 80053492187 scopus 로고    scopus 로고
    • 2DIR spectroscopy of human amylin fibrils reflects stable β-sheet structure
    • L. Wang, and C.T. Middleton J.L. Skinner 2DIR spectroscopy of human amylin fibrils reflects stable β-sheet structure J. Am. Chem. Soc. 133 2011 16062 16071
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 16062-16071
    • Wang, L.1    Middleton, C.T.2    Skinner, J.L.3
  • 34
    • 84863116618 scopus 로고    scopus 로고
    • Fibril structure of human islet amyloid polypeptide
    • S. Bedrood, and Y. Li R. Langen Fibril structure of human islet amyloid polypeptide J. Biol. Chem. 287 2012 5235 5241
    • (2012) J. Biol. Chem. , vol.287 , pp. 5235-5241
    • Bedrood, S.1    Li, Y.2    Langen, R.3
  • 35
    • 50049095633 scopus 로고    scopus 로고
    • Atomic structure of the cross-β spine of islet amyloid polypeptide (amylin)
    • J.J.W. Wiltzius, and S.A. Sievers D. Eisenberg Atomic structure of the cross-β spine of islet amyloid polypeptide (amylin) Protein Sci. 17 2008 1467 1474
    • (2008) Protein Sci. , vol.17 , pp. 1467-1474
    • Wiltzius, J.J.W.1    Sievers, S.A.2    Eisenberg, D.3
  • 36
    • 0023787576 scopus 로고
    • Amyloid fibrils formed from a segment of the pancreatic islet amyloid protein
    • G.G. Glenner, E.D. Eanes, and C.A. Wiley Amyloid fibrils formed from a segment of the pancreatic islet amyloid protein Biochem. Biophys. Res. Commun. 155 1988 608 614
    • (1988) Biochem. Biophys. Res. Commun. , vol.155 , pp. 608-614
    • Glenner, G.G.1    Eanes, E.D.2    Wiley, C.A.3
  • 37
    • 0024451138 scopus 로고
    • Isolation and sequence determination of rat islet amyloid polypeptide
    • J. Asai, and M. Nakazato H. Matsuo Isolation and sequence determination of rat islet amyloid polypeptide Biochem. Biophys. Res. Commun. 164 1989 400 405
    • (1989) Biochem. Biophys. Res. Commun. , vol.164 , pp. 400-405
    • Asai, J.1    Nakazato, M.2    Matsuo, H.3
  • 38
    • 0035804936 scopus 로고    scopus 로고
    • Identification of a novel human islet amyloid polypeptide β-sheet domain and factors influencing fibrillogenesis
    • E.T. Jaikaran, and C.E. Higham P.E. Fraser Identification of a novel human islet amyloid polypeptide β-sheet domain and factors influencing fibrillogenesis J. Mol. Biol. 308 2001 515 525
    • (2001) J. Mol. Biol. , vol.308 , pp. 515-525
    • Jaikaran, E.T.1    Higham, C.E.2    Fraser, P.E.3
  • 39
    • 10844254749 scopus 로고    scopus 로고
    • Role of aromatic interactions in amyloid formation by peptides derived from human Amylin
    • S.M. Tracz, and A. Abedini D.P. Raleigh Role of aromatic interactions in amyloid formation by peptides derived from human Amylin Biochemistry 43 2004 15901 15908
    • (2004) Biochemistry , vol.43 , pp. 15901-15908
    • Tracz, S.M.1    Abedini, A.2    Raleigh, D.P.3
  • 40
    • 0033579545 scopus 로고    scopus 로고
    • Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin
    • M.R. Nilsson, and D.P. Raleigh Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin J. Mol. Biol. 294 1999 1375 1385
    • (1999) J. Mol. Biol. , vol.294 , pp. 1375-1385
    • Nilsson, M.R.1    Raleigh, D.P.2
  • 41
    • 28944455381 scopus 로고    scopus 로고
    • Destabilization of human IAPP amyloid fibrils by proline mutations outside of the putative amyloidogenic domain: Is there a critical amyloidogenic domain in human IAPP?
    • A. Abedini, and D.P. Raleigh Destabilization of human IAPP amyloid fibrils by proline mutations outside of the putative amyloidogenic domain: is there a critical amyloidogenic domain in human IAPP? J. Mol. Biol. 355 2006 274 281
    • (2006) J. Mol. Biol. , vol.355 , pp. 274-281
    • Abedini, A.1    Raleigh, D.P.2
  • 42
    • 76149118090 scopus 로고    scopus 로고
    • Solution structures of rat amylin peptide: Simulation, theory, and experiment
    • A.S. Reddy, and L. Wang J.J. De Pablo Solution structures of rat amylin peptide: simulation, theory, and experiment Biophys. J. 98 2010 443 451
    • (2010) Biophys. J. , vol.98 , pp. 443-451
    • Reddy, A.S.1    Wang, L.2    De Pablo, J.J.3
  • 43
    • 77958454277 scopus 로고    scopus 로고
    • Stable and metastable states of human amylin in solution
    • A.S. Reddy, and L. Wang J.J. de Pablo Stable and metastable states of human amylin in solution Biophys. J. 99 2010 2208 2216
    • (2010) Biophys. J. , vol.99 , pp. 2208-2216
    • Reddy, A.S.1    Wang, L.2    De Pablo, J.J.3
  • 44
    • 73249115986 scopus 로고    scopus 로고
    • Human islet amyloid polypeptide monomers form ordered β-hairpins: A possible direct amyloidogenic precursor
    • N.F. Dupuis, and C. Wu M.T. Bowers Human islet amyloid polypeptide monomers form ordered β-hairpins: a possible direct amyloidogenic precursor J. Am. Chem. Soc. 131 2009 18283 18292
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 18283-18292
    • Dupuis, N.F.1    Wu, C.2    Bowers, M.T.3
  • 45
    • 79955896407 scopus 로고    scopus 로고
    • The amyloid formation mechanism in human IAPP: Dimers have β-strand monomer-monomer interfaces
    • N.F. Dupuis, and C. Wu M.T. Bowers The amyloid formation mechanism in human IAPP: dimers have β-strand monomer-monomer interfaces J. Am. Chem. Soc. 133 2011 7240 7243
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 7240-7243
    • Dupuis, N.F.1    Wu, C.2    Bowers, M.T.3
  • 46
    • 34249071886 scopus 로고    scopus 로고
    • A bias-exchange approach to protein folding
    • S. Piana, and A. Laio A bias-exchange approach to protein folding J. Phys. Chem. B 111 2007 4553 4559
    • (2007) J. Phys. Chem. B , vol.111 , pp. 4553-4559
    • Piana, S.1    Laio, A.2
  • 47
    • 69049099679 scopus 로고    scopus 로고
    • A kinetic model of trp-cage folding from multiple biased molecular dynamics simulations
    • F. Marinelli, and F. Pietrucci S. Piana A kinetic model of trp-cage folding from multiple biased molecular dynamics simulations PLOS Comput. Biol. 5 2009 e1000452
    • (2009) PLOS Comput. Biol. , vol.5 , pp. 1000452
    • Marinelli, F.1    Pietrucci, F.2    Piana, S.3
  • 48
    • 84857770472 scopus 로고    scopus 로고
    • Multidimensional view of amyloid fibril nucleation in atomistic detail
    • F. Baftizadeh, and X. Biarnes A. Laio Multidimensional view of amyloid fibril nucleation in atomistic detail J. Am. Chem. Soc. 134 2012 3886 3894
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 3886-3894
    • Baftizadeh, F.1    Biarnes, X.2    Laio, A.3
  • 49
    • 4444282928 scopus 로고    scopus 로고
    • A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6
    • C. Oostenbrink, and A. Villa W.F. van Gunsteren A biomolecular force field based on the free enthalpy of hydration and solvation: the GROMOS force-field parameter sets 53A5 and 53A6 J. Comput. Chem. 25 2004 1656 1676
    • (2004) J. Comput. Chem. , vol.25 , pp. 1656-1676
    • Oostenbrink, C.1    Villa, A.2    Van Gunsteren, W.F.3
  • 50
    • 0002775934 scopus 로고
    • Intercation models for water in relation to protein hydration
    • B. Pullman, Reidel Dordrecht
    • H. Berendsen, J. Postma, and W.F. Van Gunsteren Intercation models for water in relation to protein hydration B. Pullman, Intermolecular Forces 1981 Reidel Dordrecht 331 332
    • (1981) Intermolecular Forces , pp. 331-332
    • Berendsen, H.1    Postma, J.2    Van Gunsteren, W.F.3
  • 51
    • 0035526029 scopus 로고    scopus 로고
    • Structure and dynamics of the TIP3P, SPC, and SPC/E water models at 298 K
    • P. Mark, and L. Nilsson Structure and dynamics of the TIP3P, SPC, and SPC/E water models at 298 K J. Phys. Chem. A 105 2001 9954 9960
    • (2001) J. Phys. Chem. A , vol.105 , pp. 9954-9960
    • Mark, P.1    Nilsson, L.2
  • 52
    • 33846823909 scopus 로고
    • Particle mesh Ewald - An N.Log(N) method for Ewald sums in large systems
    • T. Darden, D. York, and L. Pedersen Particle mesh Ewald - an N.Log(N) method for Ewald sums in large systems J. Chem. Phys. 98 1993 10089 10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 54
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • B. Hess, and H. Bekker J. Fraaije LINCS: a linear constraint solver for molecular simulations J. Comput. Chem. 18 1997 1463 1472
    • (1997) J. Comput. Chem. , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Fraaije, J.3
  • 55
    • 84943502952 scopus 로고
    • A molecular-dynamics method for simulations in the canonical ensemble
    • S. Nose A molecular-dynamics method for simulations in the canonical ensemble Mol. Phys. 52 1984 255 268
    • (1984) Mol. Phys. , vol.52 , pp. 255-268
    • Nose, S.1
  • 56
    • 34547809547 scopus 로고
    • A unified formulation of the constant temperature molecular-dynamics methods
    • S. Nose A unified formulation of the constant temperature molecular-dynamics methods J. Chem. Phys. 81 1984 511 519
    • (1984) J. Chem. Phys. , vol.81 , pp. 511-519
    • Nose, S.1
  • 57
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • W.G. Hoover Canonical dynamics: equilibrium phase-space distributions Phys. Rev. A 31 1985 1695 1697
    • (1985) Phys. Rev. A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 58
    • 0019707626 scopus 로고
    • Polymorphic transitions in single-crystals - A new molecular-dynamics method
    • M. Parrinello, and A. Rahman Polymorphic transitions in single-crystals - a new molecular-dynamics method J. Appl. Phys. 52 1981 7182 7190
    • (1981) J. Appl. Phys. , vol.52 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 59
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • B. Hess, and C. Kutzner E. Lindahl GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation J. Chem. Theory Comput. 4 2008 435 447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Lindahl, E.3
  • 60
    • 73349098763 scopus 로고    scopus 로고
    • A collective variable for the efficient exploration of protein β-sheet structures: Application to SH3 and GB1
    • F. Pietrucci, and A. Laio A collective variable for the efficient exploration of protein β-sheet structures: application to SH3 and GB1 J. Chem. Theory Comput. 5 2009 2197 2201
    • (2009) J. Chem. Theory Comput. , vol.5 , pp. 2197-2201
    • Pietrucci, F.1    Laio, A.2
  • 61
    • 0029619259 scopus 로고
    • Knowledge-based protein secondary structure assignment
    • D. Frishman, and P. Argos Knowledge-based protein secondary structure assignment Proteins 23 1995 566 579
    • (1995) Proteins , vol.23 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 62
    • 69349100797 scopus 로고    scopus 로고
    • PLUMED: A portable plugin for free-energy calculations with molecular dynamics
    • M. Bonomi, and D. Branduardi M. Parrinello PLUMED: a portable plugin for free-energy calculations with molecular dynamics Comput. Phys. Commun. 180 2009 1961 1972
    • (2009) Comput. Phys. Commun. , vol.180 , pp. 1961-1972
    • Bonomi, M.1    Branduardi, D.2    Parrinello, M.3
  • 63
    • 80055015114 scopus 로고    scopus 로고
    • METAGUI. A VMD interface for analyzing metadynamics and molecular dynamics simulations
    • X. Biarnes, and F. Pietrucci A. Laio METAGUI. A VMD interface for analyzing metadynamics and molecular dynamics simulations Comput. Phys. Commun. 183 2012 203 211
    • (2012) Comput. Phys. Commun. , vol.183 , pp. 203-211
    • Biarnes, X.1    Pietrucci, F.2    Laio, A.3
  • 66
    • 4243613377 scopus 로고
    • Multicanonical ensemble: A new approach to simulate first-order phase transitions
    • B.A. Berg, and T. Neuhaus Multicanonical ensemble: a new approach to simulate first-order phase transitions Phys. Rev. Lett. 68 1992 9 12
    • (1992) Phys. Rev. Lett. , vol.68 , pp. 9-12
    • Berg, B.A.1    Neuhaus, T.2
  • 67
    • 0034229302 scopus 로고    scopus 로고
    • Hyperparallel tempering Monte Carlo simulation of polymeric systems
    • Q. Yan, and J.J. de Pablo Hyperparallel tempering Monte Carlo simulation of polymeric systems J. Chem. Phys. 113 2000 1276
    • (2000) J. Chem. Phys. , vol.113 , pp. 1276
    • Yan, Q.1    De Pablo, J.J.2
  • 69
    • 58149299971 scopus 로고    scopus 로고
    • Metadynamics: A method to simulate rare events and reconstruct the free energy in biophysics, chemistry and material science
    • A. Laio, and F.L. Gervasio Metadynamics: a method to simulate rare events and reconstruct the free energy in biophysics, chemistry and material science Rep. Prog. Phys. 71 2008 126601
    • (2008) Rep. Prog. Phys. , vol.71 , pp. 126601
    • Laio, A.1    Gervasio, F.L.2
  • 70
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for freeenergy calculations on biomolecules. I. The method
    • S. Kumar, and J.M. Rosenberg P.A. Kollman The weighted histogram analysis method for freeenergy calculations on biomolecules. I. The method J. Comput. Chem. 13 1992 1011 1021
    • (1992) J. Comput. Chem. , vol.13 , pp. 1011-1021
    • Kumar, S.1    Rosenberg, J.M.2    Kollman, P.A.3
  • 71
    • 0000577041 scopus 로고
    • Large-amplitude nonlinear motions in proteins
    • A.E. García Large-amplitude nonlinear motions in proteins Phys. Rev. Lett. 68 1992 2696 2699
    • (1992) Phys. Rev. Lett. , vol.68 , pp. 2696-2699
    • García, A.E.1
  • 72
    • 0021449809 scopus 로고
    • Quasi-harmonic method for studying very low frequency modes in proteins
    • R.M. Levy, and A.R. Srinivasan J.A. McCammon Quasi-harmonic method for studying very low frequency modes in proteins Biopolymers 23 1984 1099 1112
    • (1984) Biopolymers , vol.23 , pp. 1099-1112
    • Levy, R.M.1    Srinivasan, A.R.2    McCammon, J.A.3
  • 74
    • 67650022868 scopus 로고    scopus 로고
    • Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process
    • J.J.W. Wiltzius, and S.A. Sievers D. Eisenberg Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process Protein Sci. 18 2009 1521 1530
    • (2009) Protein Sci. , vol.18 , pp. 1521-1530
    • Wiltzius, J.J.W.1    Sievers, S.A.2    Eisenberg, D.3


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