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Volumn 66, Issue 1, 2007, Pages 96-109

Effects of chain length on the aggregation of model polyglutamine peptides: Molecular dynamics simulations

Author keywords

Amyloid; Intermediate resolution model; Molecular dynamics; Polyglutamine; Protein aggregation

Indexed keywords

GLUTAMINE; PEPTIDE DERIVATIVE; POLYGLUTAMINE;

EID: 33845652619     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21132     Document Type: Article
Times cited : (61)

References (87)
  • 1
    • 0033791230 scopus 로고    scopus 로고
    • Protein aggregation and pathogenesis of Huntington's disease: Mechanisms and correlations
    • Wanker EE. Protein aggregation and pathogenesis of Huntington's disease: mechanisms and correlations. Biol Chem 2000;381:937-942.
    • (2000) Biol Chem , vol.381 , pp. 937-942
    • Wanker, E.E.1
  • 5
    • 0029298231 scopus 로고
    • Gain of glutamines, gain of function?
    • Housman D. Gain of glutamines, gain of function? Nat Genet 1995;10:3-4.
    • (1995) Nat Genet , vol.10 , pp. 3-4
    • Housman, D.1
  • 13
    • 0035084096 scopus 로고    scopus 로고
    • Solubilization and disaggregation of polyglutamine peptides
    • Chen S, Wetzl R. Solubilization and disaggregation of polyglutamine peptides. Protein Sci 2001;10:887-891.
    • (2001) Protein Sci , vol.10 , pp. 887-891
    • Chen, S.1    Wetzl, R.2
  • 15
    • 0033613212 scopus 로고    scopus 로고
    • Insoluble detergent-resistant aggregates form between pathological and nonpathological lengths of polyglutamine in mammilian cells
    • Kazantsev A, Preisinger E, Dranovsky A, Goldgaber D, Housman D. Insoluble detergent-resistant aggregates form between pathological and nonpathological lengths of polyglutamine in mammilian cells. Proc Natl Acad Sci USA 1999;96:11404-11409.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11404-11409
    • Kazantsev, A.1    Preisinger, E.2    Dranovsky, A.3    Goldgaber, D.4    Housman, D.5
  • 16
    • 0033600124 scopus 로고    scopus 로고
    • The length of polyglutamine tract, its level of expression, the rate of degradation, and the transglutaminase activity influence the formation of intracellular aggregates
    • de Cristofaro T, Affaitati A, Cariello L, Avvedimento EV, Varrone S. The length of polyglutamine tract, its level of expression, the rate of degradation, and the transglutaminase activity influence the formation of intracellular aggregates. Biochem Biophys Res Commun 1999;260:150-158.
    • (1999) Biochem Biophys Res Commun , vol.260 , pp. 150-158
    • De Cristofaro, T.1    Affaitati, A.2    Cariello, L.3    Avvedimento, E.V.4    Varrone, S.5
  • 18
    • 0031945025 scopus 로고    scopus 로고
    • Aggregation of N-terminal huntingtin is dependent of the length of its glutamine repeats
    • Li S-H, Li X-J. Aggregation of N-terminal huntingtin is dependent of the length of its glutamine repeats. Hum Mol Genet 1998;7: 777-782.
    • (1998) Hum Mol Genet , vol.7 , pp. 777-782
    • Li, S.-H.1    Li, X.-J.2
  • 21
    • 0037062561 scopus 로고    scopus 로고
    • Amyloid-like features of polyglutamine aggregates and their assembly kinetics
    • Chen S, Berthelier V, Hamilton JB, O'Nuallain B, Wetzel R. Amyloid-like features of polyglutamine aggregates and their assembly kinetics. Biochemistry 2002;41:7391-7399.
    • (2002) Biochemistry , vol.41 , pp. 7391-7399
    • Chen, S.1    Berthelier, V.2    Hamilton, J.B.3    O'Nuallain, B.4    Wetzel, R.5
  • 23
    • 0031948607 scopus 로고    scopus 로고
    • Cleavage, aggregation and toxicity of the expanded androgen receptor in spinal and bulbar muscular atrophy
    • Merry, DE, Kobayashi Y, Bailey CK, Taye AA, Fischbeck KH. Cleavage, aggregation and toxicity of the expanded androgen receptor in spinal and bulbar muscular atrophy. Hum Mol Genet 1998;7:693-701.
    • (1998) Hum Mol Genet , vol.7 , pp. 693-701
    • Merry, D.E.1    Kobayashi, Y.2    Bailey, C.K.3    Taye, A.A.4    Fischbeck, K.H.5
  • 24
    • 55449095000 scopus 로고    scopus 로고
    • Molecular origin of polyglutamine aggreagation in neurodegenerative diseases
    • Khare SD, Ding F, Gwanmesia KN, Dokholyan NV. Molecular origin of polyglutamine aggreagation in neurodegenerative diseases. PLoS Comput Biol 2005;1:230-235.
    • (2005) PLoS Comput Biol , vol.1 , pp. 230-235
    • Khare, S.D.1    Ding, F.2    Gwanmesia, K.N.3    Dokholyan, N.V.4
  • 25
    • 4444295047 scopus 로고    scopus 로고
    • A structural model of polyglutamine determined from a host-guest method combining experiments and landscape theory
    • Finke JM, Cheung MS, Onuchic JN. A structural model of polyglutamine determined from a host-guest method combining experiments and landscape theory. Biophys J 2004;87:1900-1918.
    • (2004) Biophys J , vol.87 , pp. 1900-1918
    • Finke, J.M.1    Cheung, M.S.2    Onuchic, J.N.3
  • 26
    • 0033450855 scopus 로고    scopus 로고
    • Folding of oligoglutamines: A theoretical approach based upon thermodynamics and molecular mechanics
    • Starikov EB, Lerach H, Wanker EE. Folding of oligoglutamines: a theoretical approach based upon thermodynamics and molecular mechanics. J Biomol Struct Dynamics 1999;17:409-427.
    • (1999) J Biomol Struct Dynamics , vol.17 , pp. 409-427
    • Starikov, E.B.1    Lerach, H.2    Wanker, E.E.3
  • 27
    • 0344270858 scopus 로고    scopus 로고
    • Differential hydrophobicity drives self-assembly in Huntington's disease
    • Burke MG, Woscholski R, Yaliraki SN. Differential hydrophobicity drives self-assembly in Huntington's disease. Proc Natl Acad Sci USA 2003;100:13928-13933.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13928-13933
    • Burke, M.G.1    Woscholski, R.2    Yaliraki, S.N.3
  • 28
    • 0035882559 scopus 로고    scopus 로고
    • Alpha-helix formation: Discontinuous molecular dynamics on an intermediate resolution model
    • Smith AV, Hall CK. Alpha-helix formation: discontinuous molecular dynamics on an intermediate resolution model. Proteins: Struct Funct Genet 2001;44:344-360.
    • (2001) Proteins: Struct Funct Genet , vol.44 , pp. 344-360
    • Smith, A.V.1    Hall, C.K.2
  • 29
    • 0034315782 scopus 로고    scopus 로고
    • Bridging the gap between homopolymer and protein models: A discontinuous molecular dynamics study
    • Smith AV, Hall CK. Bridging the gap between homopolymer and protein models: a discontinuous molecular dynamics study. J Chem Phys 2000;113:9331-9342.
    • (2000) J Chem Phys , vol.113 , pp. 9331-9342
    • Smith, A.V.1    Hall, C.K.2
  • 30
    • 0035882537 scopus 로고    scopus 로고
    • Assembly of a tetrameric α-helical bundle: Computer simulations on an intermediate resolution protein model
    • Smith AV, Hall CK. Assembly of a tetrameric α-helical bundle: computer simulations on an intermediate resolution protein model. Proteins: Struct Funct Genet 2001;44:376-391.
    • (2001) Proteins: Struct Funct Genet , vol.44 , pp. 376-391
    • Smith, A.V.1    Hall, C.K.2
  • 31
    • 7244253280 scopus 로고    scopus 로고
    • Solvent effects on the conformational transition of a model polyalanine peptide
    • Nguyen HD, Marchut AJ, Hall CK. Solvent effects on the conformational transition of a model polyalanine peptide. Protein Sci 2004;13:2909-2904.
    • (2004) Protein Sci , vol.13 , pp. 2909-12904
    • Nguyen, H.D.1    Marchut, A.J.2    Hall, C.K.3
  • 32
    • 0035823222 scopus 로고    scopus 로고
    • Protein folding versus aggregation: Computer simulations on an intermediate resolution protein model
    • Smith AV, Hall CK. Protein folding versus aggregation: computer simulations on an intermediate resolution protein model. J Mol Biol 2001;312:187-202.
    • (2001) J Mol Biol , vol.312 , pp. 187-202
    • Smith, A.V.1    Hall, C.K.2
  • 33
    • 9244260521 scopus 로고    scopus 로고
    • Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides
    • Nguyen HD, Hall CK. Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides. Proc Natl Acad Sci USA 2004;101:16180-16185.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 16180-16185
    • Nguyen, H.D.1    Hall, C.K.2
  • 34
    • 10044280719 scopus 로고    scopus 로고
    • Phase diagrams describing fibrillization by polyalanine peptides
    • Nguyen HD, Hall CK. Phase diagrams describing fibrillization by polyalanine peptides. Biophys J 2004;87:4122-4134.
    • (2004) Biophys J , vol.87 , pp. 4122-4134
    • Nguyen, H.D.1    Hall, C.K.2
  • 35
    • 15744382287 scopus 로고    scopus 로고
    • Kinetics of fibril formation by polyalanine peptides
    • Nguyen HD, Hall CK. Kinetics of fibril formation by polyalanine peptides. J Biol Chem 2005;280:9074-9082.
    • (2005) J Biol Chem , vol.280 , pp. 9074-9082
    • Nguyen, H.D.1    Hall, C.K.2
  • 36
    • 33744827373 scopus 로고    scopus 로고
    • Sidechain interactions determine amyloid formation by model polyglutamine peptides in molecular dynamics simulations
    • Marchut AJ, Hall CK. Sidechain interactions determine amyloid formation by model polyglutamine peptides in molecular dynamics simulations. Biophys J 2006;90:4574-4584.
    • (2006) Biophys J , vol.90 , pp. 4574-4584
    • Marchut, A.J.1    Hall, C.K.2
  • 37
    • 33747032067 scopus 로고    scopus 로고
    • Spontaneous formation of annular structures observed in molecular dynamics simulations of polyglutamine peptides
    • Marchut AJ, Hall CK. Spontaneous formation of annular structures observed in molecular dynamics simulations of polyglutamine peptides. Comput Chem Biol 2006;30:215-218.
    • (2006) Comput Chem Biol , vol.30 , pp. 215-218
    • Marchut, A.J.1    Hall, C.K.2
  • 41
    • 27644528932 scopus 로고    scopus 로고
    • A single disulfide bond differentiates aggregation pathways of β2-microglobulin
    • Chen Y, Dokholyan NV. A single disulfide bond differentiates aggregation pathways of β2-microglobulin. J Mol Biol 2005;354: 473-482.
    • (2005) J Mol Biol , vol.354 , pp. 473-482
    • Chen, Y.1    Dokholyan, N.V.2
  • 42
    • 0033080367 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegenerative diseases: Molecular aspects
    • Perutz MF. Glutamine repeats and neurodegenerative diseases: molecular aspects. Trends Biochem Sci 1999;24:58-63.
    • (1999) Trends Biochem Sci , vol.24 , pp. 58-63
    • Perutz, M.F.1
  • 44
    • 0027988041 scopus 로고
    • Polar zippers: Their role in human disease
    • Perutz M. Polar zippers: their role in human disease. Protein Sci 1994;3:1629-1637.
    • (1994) Protein Sci , vol.3 , pp. 1629-1637
    • Perutz, M.1
  • 45
    • 0028283985 scopus 로고
    • Glutamine repeats as polar zippers: Their possible role in inherited neurodegenerative diseases
    • Perutz MF, Johnson T, Suzuki M, Finch JT. Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc Natl Acad Sci USA 1994;91:5355-5358.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5355-5358
    • Perutz, M.F.1    Johnson, T.2    Suzuki, M.3    Finch, J.T.4
  • 46
    • 0035833997 scopus 로고    scopus 로고
    • An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel β-fibrils
    • Bevivino AE, Loll PJ. An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel β-fibrils. Proc Natl Acad Sci USA 2001;98:11955-11960.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11955-11960
    • Bevivino, A.E.1    Loll, P.J.2
  • 47
    • 0035976971 scopus 로고    scopus 로고
    • Intra- and intermolecular β-pleated sheet formation in glutamine-repeat inserted myoglobin as a model for polyglutamine diseases
    • Tanaka M, Morishima I, Akagi T, Hashikawa T, Nukina N. Intra- and intermolecular β-pleated sheet formation in glutamine-repeat inserted myoglobin as a model for polyglutamine diseases. J Biol Chem 2001;276:45470-45475.
    • (2001) J Biol Chem , vol.276 , pp. 45470-45475
    • Tanaka, M.1    Morishima, I.2    Akagi, T.3    Hashikawa, T.4    Nukina, N.5
  • 50
    • 16544383250 scopus 로고    scopus 로고
    • Hsp70 and hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer
    • Wacker JL, Zareie MH, Fong H, Sarikaya M, Muchowski PJ. Hsp70 and hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer. Nat Struct Mol Biol 2004;11:1215-1222.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1215-1222
    • Wacker, J.L.1    Zareie, M.H.2    Fong, H.3    Sarikaya, M.4    Muchowski, P.J.5
  • 51
    • 0036415838 scopus 로고    scopus 로고
    • α-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils
    • Lashuel HA, Petre BM, Wall J, Simon M, Nowak RJ, Walz T, Lansbury, PT Jr., α-Synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils. J Mol Biol 2002;322:1089-1102.
    • (2002) J Mol Biol , vol.322 , pp. 1089-1102
    • Lashuel, H.A.1    Petre, B.M.2    Wall, J.3    Simon, M.4    Nowak, R.J.5    Walz, T.6    Lansbury Jr., P.T.7
  • 52
    • 0037072284 scopus 로고    scopus 로고
    • Annular α-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes
    • Ding TT, Lee S-J, Rochet J-C, Lansbury PT Jr. Annular α-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes. Biochemistry 2002;41:10209-10217.
    • (2002) Biochemistry , vol.41 , pp. 10209-10217
    • Ding, T.T.1    Lee, S.-J.2    Rochet, J.-C.3    Lansbury Jr., P.T.4
  • 54
    • 31944449691 scopus 로고    scopus 로고
    • Evidence that perutz's double-β-stranded subunity structure for β-amyloids also applies to their channel-forming structures in membrances
    • Singer SJ, Dewji NN. Evidence that perutz's double-β-stranded subunity structure for β-amyloids also applies to their channel-forming structures in membrances. Proc Natl Acad Sci USA 2006;103:1546-1550.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 1546-1550
    • Singer, S.J.1    Dewji, N.N.2
  • 56
    • 14044278010 scopus 로고    scopus 로고
    • New model for crystalline polyglutamine assemblies and their connection with amyloid fibrils
    • Sikorski P, Atkins E. New model for crystalline polyglutamine assemblies and their connection with amyloid fibrils. Biomacromolecules 2005;6:425-432.
    • (2005) Biomacromolecules , vol.6 , pp. 425-432
    • Sikorski, P.1    Atkins, E.2
  • 60
    • 3142699791 scopus 로고    scopus 로고
    • Template-assisted filament growth by parallel stacking of tau
    • Margittai M, Langen R. Template-assisted filament growth by parallel stacking of tau. Proc Natl Acad Sci USA 2004;101: 10278-10283.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 10278-10283
    • Margittai, M.1    Langen, R.2
  • 62
    • 0036052739 scopus 로고    scopus 로고
    • Ideas of order for amyloid fibril structure
    • Wetzel R. Ideas of order for amyloid fibril structure. Structure 2002;10:1031-1036.
    • (2002) Structure , vol.10 , pp. 1031-1036
    • Wetzel, R.1
  • 64
    • 2942616602 scopus 로고    scopus 로고
    • Evidence for assembly of prions with left-handed β helices into trimers
    • Govaerts C, Wille H, Prusiner SB, Cohen FE. Evidence for assembly of prions with left-handed β helices into trimers. Proc Natl Acad Sci USA 2004;101:8342-8347.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8342-8347
    • Govaerts, C.1    Wille, H.2    Prusiner, S.B.3    Cohen, F.E.4
  • 65
    • 22144432561 scopus 로고    scopus 로고
    • Md simulations indicate a possible role of parallel β-helices in seeded aggregation of poly-gln
    • Stork M, Giese A, Kretschmar HA, Tavan P. Md simulations indicate a possible role of parallel β-helices in seeded aggregation of poly-gln. Biophys J 2005;88:2442-2451.
    • (2005) Biophys J , vol.88 , pp. 2442-2451
    • Stork, M.1    Giese, A.2    Kretschmar, H.A.3    Tavan, P.4
  • 66
    • 26444534036 scopus 로고    scopus 로고
    • Characterization of a possible amyloidogenic precursor in glutamine-repeat neurodegenerative diseases
    • Armen RS, Bernard BM, Day R, Alonso DOV, Daggett V. Characterization of a possible amyloidogenic precursor in glutamine-repeat neurodegenerative diseases. Proc Natl Acad Sci USA 2005;102:13433-13438.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 13433-13438
    • Armen, R.S.1    Bernard, B.M.2    Day, R.3    Alonso, D.O.V.4    Daggett, V.5
  • 67
    • 0034761941 scopus 로고    scopus 로고
    • Initial process of polyglutamine aggregate formation in vivo
    • Kimura Y, Koitabashi S, Kakizuka A, Fujita T. Initial process of polyglutamine aggregate formation in vivo. Gene Cell 2001;6: 887-897.
    • (2001) Gene Cell , vol.6 , pp. 887-897
    • Kimura, Y.1    Koitabashi, S.2    Kakizuka, A.3    Fujita, T.4
  • 68
    • 84946639640 scopus 로고
    • Molecular dynamics of rigid and non-rigid necklaces of hard disks
    • Bellemans A, Orban J, Belle DV. Molecular dynamics of rigid and non-rigid necklaces of hard disks. Mol Phys 1980;39:781-792.
    • (1980) Mol Phys , vol.39 , pp. 781-792
    • Bellemans, A.1    Orban, J.2    Belle, D.V.3
  • 69
    • 0000439253 scopus 로고
    • Molecular dynamics study of a polymer chain in solution
    • Rapaport DC. Molecular dynamics study of a polymer chain in solution. J Chem Phys 1979;71:3299-3303.
    • (1979) J Chem Phys , vol.71 , pp. 3299-3303
    • Rapaport, D.C.1
  • 70
    • 36849126204 scopus 로고
    • Studies in molecular dynamics. I. General method
    • Alder BJ, Wainwright TE. Studies in molecular dynamics. I. General method. J Chem Phys 1959;31:459-466.
    • (1959) J Chem Phys , vol.31 , pp. 459-466
    • Alder, B.J.1    Wainwright, T.E.2
  • 72
    • 0031161658 scopus 로고    scopus 로고
    • Molecular dynamics for polymeric fluids using discontinuous potentials
    • Smith SW, Freeman BD, Hall CK. Molecular dynamics for polymeric fluids using discontinuous potentials. J Comput Phys 1997;134:16-30.
    • (1997) J Comput Phys , vol.134 , pp. 16-30
    • Smith, S.W.1    Freeman, B.D.2    Hall, C.K.3
  • 73
    • 36749107785 scopus 로고
    • Molecular dynamics simulations at constant pressure and/or temperature
    • Andersen HC. Molecular dynamics simulations at constant pressure and/or temperature. J Chem Phys 1980;72:2384-2393.
    • (1980) J Chem Phys , vol.72 , pp. 2384-2393
    • Andersen, H.C.1
  • 76
    • 0034571041 scopus 로고    scopus 로고
    • Self-assembly of a β-sheet protein governed by relief of electrostatic replulsion relative to van der waals attraction
    • Caplan MR, Moore PN, Zhang S, Kamm RD, Lauffenburger DA. Self-assembly of a β-sheet protein governed by relief of electrostatic replulsion relative to van der waals attraction. Biomacromolecules 2000;1:627-631.
    • (2000) Biomacromolecules , vol.1 , pp. 627-631
    • Caplan, M.R.1    Moore, P.N.2    Zhang, S.3    Kamm, R.D.4    Lauffenburger, D.A.5
  • 78
    • 0344490335 scopus 로고    scopus 로고
    • Conducting nanowires built by controlled self-assembly of amyloid fibers and selective metal deposition
    • Scheibel T, Parthasarathy R, Sawicki G, Lin XM, Jaeger H. Conducting nanowires built by controlled self-assembly of amyloid fibers and selective metal deposition. Proc Natl Acad Sci USA 2003;100:4527-4532.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4527-4532
    • Scheibel, T.1    Parthasarathy, R.2    Sawicki, G.3    Lin, X.M.4    Jaeger, H.5
  • 79
    • 0000590549 scopus 로고    scopus 로고
    • Left-handed helical ribbon intermediates in the self-assembly of a β-sheet peptide
    • Marini DM, Hwang W, Lauffenburger DA, Zhang S, Kamm RD. Left-handed helical ribbon intermediates in the self-assembly of a β-sheet peptide. Nano Lett 2002;2:295-299.
    • (2002) Nano Lett , vol.2 , pp. 295-299
    • Marini, D.M.1    Hwang, W.2    Lauffenburger, D.A.3    Zhang, S.4    Kamm, R.D.5
  • 80
    • 0001608018 scopus 로고    scopus 로고
    • Self-assembly of surfactant-like peptides with variable glycine tails to form nanotubes and nanovesicles
    • Santoso S, Hwang W, Hartman H, Zhang S. Self-assembly of surfactant-like peptides with variable glycine tails to form nanotubes and nanovesicles. Nano Lett 2002;2:687-691.
    • (2002) Nano Lett , vol.2 , pp. 687-691
    • Santoso, S.1    Hwang, W.2    Hartman, H.3    Zhang, S.4
  • 81
    • 0037117535 scopus 로고    scopus 로고
    • Molecular self-assembly of surfactant-like peptides to form nanotubes and nanovesicles
    • Vauthey S, Santoso S, Gong H, Watson N, Zhang S. Molecular self-assembly of surfactant-like peptides to form nanotubes and nanovesicles. Proc Natl Acad Sci USA 2002;99:5355-5360.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5355-5360
    • Vauthey, S.1    Santoso, S.2    Gong, H.3    Watson, N.4    Zhang, S.5
  • 82
    • 0036897817 scopus 로고    scopus 로고
    • Design of nano-structured biological materials through self-assembly of peptides and proteins
    • Zhang S, Marini DM, Hwang W, Santoso S. Design of nano-structured biological materials through self-assembly of peptides and proteins. Curr Opin Chem Biol 2002;6:865-871.
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 865-871
    • Zhang, S.1    Marini, D.M.2    Hwang, W.3    Santoso, S.4
  • 83
    • 0034612266 scopus 로고    scopus 로고
    • Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds
    • Holmes TC, de Lacalle S, Su X, Liu G, Rich A, Zhang S. Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds. Proc Natl Acad Sci USA 2000;97:6728-6733.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6728-6733
    • Holmes, T.C.1    De Lacalle, S.2    Su, X.3    Liu, G.4    Rich, A.5    Zhang, S.6
  • 84
    • 0032682396 scopus 로고    scopus 로고
    • Peptide self-assembly in functional polymer science and engineering
    • Zhang S, Altman M. Peptide self-assembly in functional polymer science and engineering. React Funct Polym 1999;41:91-102.
    • (1999) React Funct Polym , vol.41 , pp. 91-102
    • Zhang, S.1    Altman, M.2
  • 85
    • 0029064713 scopus 로고
    • Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides
    • Xiong H, Buckwalter BL, Shieh HM, Hecht MH. Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides. Proc Natl Acad Sci USA 1995;92:6349-6353.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6349-6353
    • Xiong, H.1    Buckwalter, B.L.2    Shieh, H.M.3    Hecht, M.H.4
  • 86
    • 0027416047 scopus 로고
    • Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane
    • Zhang S, Holmes T, Lockshin C, Rich A. Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane. Proc Natl Acad Sci USA 1993;90:3334-3338.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3334-3338
    • Zhang, S.1    Holmes, T.2    Lockshin, C.3    Rich, A.4


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