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Volumn , Issue , 2005, Pages 421-474

Self-assembly of peptides and its potential application

Author keywords

[No Author keywords available]

Indexed keywords

BIOPHYSICS;

EID: 58149397927     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1533/9781845690830.3.421     Document Type: Chapter
Times cited : (3)

References (232)
  • 2
    • 0032703862 scopus 로고    scopus 로고
    • Self-assembly of peptides in medicine: two sides of the coin
    • Aggeli A., Boden N., Zhang S. Self-assembly of peptides in medicine: two sides of the coin. Mol. Med. Today 1999, 5:512-513.
    • (1999) Mol. Med. Today , vol.5 , pp. 512-513
    • Aggeli, A.1    Boden, N.2    Zhang, S.3
  • 6
    • 0033535551 scopus 로고    scopus 로고
    • Control of cyrstal nucleation by patterned self-assembled monolayers
    • Aizenberg J., Black A.J., Whitesides G.M. Control of cyrstal nucleation by patterned self-assembled monolayers. Nature 1999, 398:495-498.
    • (1999) Nature , vol.398 , pp. 495-498
    • Aizenberg, J.1    Black, A.J.2    Whitesides, G.M.3
  • 7
    • 0030111359 scopus 로고    scopus 로고
    • Hypersensitization of multidrug resistent human ovarian carcinoma cells by pluronic P85 block copolymer
    • Alakhov V.Y., Moskaleva E.Y., Batrakova E.V. Hypersensitization of multidrug resistent human ovarian carcinoma cells by pluronic P85 block copolymer. Bioconjugate Chem 1996, 7:209-216.
    • (1996) Bioconjugate Chem , vol.7 , pp. 209-216
    • Alakhov, V.Y.1    Moskaleva, E.Y.2    Batrakova, E.V.3
  • 8
    • 0032170975 scopus 로고    scopus 로고
    • Polycarprolactone-b-poly(ethylene oxide) block copolymer micelles as a novel drug delivery vehicle for neurotrophic agents FK506 and L-685,818
    • Allen C., Yu Y., Maysinger D., Eisenberg A. Polycarprolactone-b-poly(ethylene oxide) block copolymer micelles as a novel drug delivery vehicle for neurotrophic agents FK506 and L-685,818. Bioconjugate Chem 1998, 9:564-572.
    • (1998) Bioconjugate Chem , vol.9 , pp. 564-572
    • Allen, C.1    Yu, Y.2    Maysinger, D.3    Eisenberg, A.4
  • 9
    • 0037192526 scopus 로고    scopus 로고
    • Chemists look to follow biology lead
    • Alper J. Chemists look to follow biology lead. Science 2002, 295:2396-2397.
    • (2002) Science , vol.295 , pp. 2396-2397
    • Alper, J.1
  • 10
    • 0033937682 scopus 로고    scopus 로고
    • Conformational behavior of ionic self-complementary peptides
    • Altman M., Lee P., Rich A., Zhang S. Conformational behavior of ionic self-complementary peptides. Protein Sci 2000, 9:1095-1105.
    • (2000) Protein Sci , vol.9 , pp. 1095-1105
    • Altman, M.1    Lee, P.2    Rich, A.3    Zhang, S.4
  • 11
    • 0035839615 scopus 로고    scopus 로고
    • Tat fusion proteins containing tyrosine 42-deleted IkBa Arrest Osteoclastogenesis
    • Amer Y.-A., Dowdy S.F., Ross F.P., Clohisy J.C., Teitelbaum S.L. Tat fusion proteins containing tyrosine 42-deleted IkBa Arrest Osteoclastogenesis. J. Biol. Chem 2001, 276:30499-30503.
    • (2001) J. Biol. Chem , vol.276 , pp. 30499-30503
    • Amer, Y.-A.1    Dowdy, S.F.2    Ross, F.P.3    Clohisy, J.C.4    Teitelbaum, S.L.5
  • 12
    • 0037433498 scopus 로고    scopus 로고
    • New cyclic peptide assemblies with hydrophobic cavities: the structural and thermodynamic basis of a new class of peptide nanotubes
    • Amorin M., Castedo L., Granja J.R. New cyclic peptide assemblies with hydrophobic cavities: the structural and thermodynamic basis of a new class of peptide nanotubes. J. Am. Chem. Soc 2003, 125:2844-2845.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 2844-2845
    • Amorin, M.1    Castedo, L.2    Granja, J.R.3
  • 13
    • 0021755248 scopus 로고
    • Mechanism of protein salting in and salting out by divalent cation salts: balance between hydration and salt binding
    • Arakawa T., Timasheff S.N. Mechanism of protein salting in and salting out by divalent cation salts: balance between hydration and salt binding. Biochemistry 1984, 23:5912-5923.
    • (1984) Biochemistry , vol.23 , pp. 5912-5923
    • Arakawa, T.1    Timasheff, S.N.2
  • 14
    • 0345166881 scopus 로고    scopus 로고
    • Cu nanocrystal growth on peptide nanotubes by biomineralization: size control of Cu nanocrystals by tuning peptide conformation
    • Banerjee I.A., Yu L., Matsui H. Cu nanocrystal growth on peptide nanotubes by biomineralization: size control of Cu nanocrystals by tuning peptide conformation. Proc. Natl. Acad. Sci. USA 2003, 100:14678-14682.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14678-14682
    • Banerjee, I.A.1    Yu, L.2    Matsui, H.3
  • 16
    • 0000019441 scopus 로고    scopus 로고
    • Cooperativity and stability in a Langevin model of proteinlike folding
    • Berriz G.F., Gutin A.M., Shakhnovich E.I. Cooperativity and stability in a Langevin model of proteinlike folding. J. Chem. Phys 1997, 106:9276-9285.
    • (1997) J. Chem. Phys , vol.106 , pp. 9276-9285
    • Berriz, G.F.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 19
    • 0036968308 scopus 로고    scopus 로고
    • Taking the cell by stealth or storm? Protein transduction domains (PTD) as versatile vectors for delivery
    • Bogoyevitch M.A., Kendrick T.S., Ng D.C.H., Barr R.K. Taking the cell by stealth or storm? Protein transduction domains (PTD) as versatile vectors for delivery. DNA and Cell Biology 2002, 2:879-894.
    • (2002) DNA and Cell Biology , vol.2 , pp. 879-894
    • Bogoyevitch, M.A.1    Kendrick, T.S.2    Ng, D.C.H.3    Barr, R.K.4
  • 21
    • 0016715114 scopus 로고
    • Structures of alternating polypeptides and their possible prebiotic significance
    • Brack A., Orgel L.E. Structures of alternating polypeptides and their possible prebiotic significance. Nature 1975, 256:383.
    • (1975) Nature , vol.256 , pp. 383
    • Brack, A.1    Orgel, L.E.2
  • 24
    • 0037134812 scopus 로고    scopus 로고
    • Templated-directed assembly of a de novo designed protein
    • Brown C.L., Aksay I.A., Saville D.A., Hecht M.H. Templated-directed assembly of a de novo designed protein. J. Am. Chem. Soc 2002, 124:6846-6848.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 6846-6848
    • Brown, C.L.1    Aksay, I.A.2    Saville, D.A.3    Hecht, M.H.4
  • 25
    • 0005609336 scopus 로고    scopus 로고
    • Self-assembly of peptide based nanotubes
    • Buriak J.M., Ghadiri M.R. Self-assembly of peptide based nanotubes. Mater. Sci. Eng. C 1997, 4:207-212.
    • (1997) Mater. Sci. Eng. C , vol.4 , pp. 207-212
    • Buriak, J.M.1    Ghadiri, M.R.2
  • 27
    • 0026256792 scopus 로고
    • Fluorescence studies of amphiphilic poly(methacrylic acid)-block-polystyrene-block-poly(methacrylic acid) micelles
    • Cao T., Munk P., Ramireddy C., Tuzar Z., Webber S.E. Fluorescence studies of amphiphilic poly(methacrylic acid)-block-polystyrene-block-poly(methacrylic acid) micelles. Macromolecules 1991, 24:6300-6305.
    • (1991) Macromolecules , vol.24 , pp. 6300-6305
    • Cao, T.1    Munk, P.2    Ramireddy, C.3    Tuzar, Z.4    Webber, S.E.5
  • 28
    • 0034571041 scopus 로고    scopus 로고
    • Self-assembly of a Β-sheet protein governed by relief of electrostatic repulsion relative to van der Waals attraction
    • Caplan M.R., Moore P.N., Zhang S., Kamm R.D., Lauffenburger D.A. Self-assembly of a Β-sheet protein governed by relief of electrostatic repulsion 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
  • 29
    • 0036027555 scopus 로고    scopus 로고
    • Control of self-assembling oligopeptide matrix formation through systematic variation of amino acid sequence
    • Caplan M.R., Schwartzfarb E.M., Zhang S., Kamm R.D., Lauffenburger D.A. Control of self-assembling oligopeptide matrix formation through systematic variation of amino acid sequence. Biomaterials 2002, 23:219-227.
    • (2002) Biomaterials , vol.23 , pp. 219-227
    • Caplan, M.R.1    Schwartzfarb, E.M.2    Zhang, S.3    Kamm, R.D.4    Lauffenburger, D.A.5
  • 30
    • 0034603151 scopus 로고    scopus 로고
    • Hollow capsule processing through colloidal templating and self-assembly
    • Caruso F. Hollow capsule processing through colloidal templating and self-assembly. Chem. Eur. J 2000, 6:413-419.
    • (2000) Chem. Eur. J , vol.6 , pp. 413-419
    • Caruso, F.1
  • 31
    • 0030342681 scopus 로고    scopus 로고
    • Conformational switching in designed peptides: the helix/sheet transition
    • Cerpa R., Cohen F.E., Kuntz I.D. Conformational switching in designed peptides: the helix/sheet transition. Fold. Des 1996, 1:91-101.
    • (1996) Fold. Des , vol.1 , pp. 91-101
    • Cerpa, R.1    Cohen, F.E.2    Kuntz, I.D.3
  • 34
    • 0000650678 scopus 로고    scopus 로고
    • Nucleated antiparallel Β-sheet that folds and undergoes self-assembly: a template promoted folding strategy toward controlled molecular architecures
    • Choo D.W., Schneider J.P., Graciani N.R., Kelly J.W. Nucleated antiparallel Β-sheet that folds and undergoes self-assembly: a template promoted folding strategy toward controlled molecular architecures. Macromolecules 1996, 29:355-366.
    • (1996) Macromolecules , vol.29 , pp. 355-366
    • Choo, D.W.1    Schneider, J.P.2    Graciani, N.R.3    Kelly, J.W.4
  • 35
    • 0037452628 scopus 로고    scopus 로고
    • Factors governing the self-assembly of a Β-hairpin peptide at the air-water interface
    • Colfer S., Kelly J.W., Powers E.T. Factors governing the self-assembly of a Β-hairpin peptide at the air-water interface. Langmuir 2003, 19:1312-1318.
    • (2003) Langmuir , vol.19 , pp. 1312-1318
    • Colfer, S.1    Kelly, J.W.2    Powers, E.T.3
  • 37
    • 0035902938 scopus 로고    scopus 로고
    • Nanowire nanosensors for highly sensitive and selective detection of biological and chemical species
    • Cui Y., Wei Q., Park H., Lieber C.M. Nanowire nanosensors for highly sensitive and selective detection of biological and chemical species. Science 2001, 293:1289-1292.
    • (2001) Science , vol.293 , pp. 1289-1292
    • Cui, Y.1    Wei, Q.2    Park, H.3    Lieber, C.M.4
  • 38
    • 0031984072 scopus 로고    scopus 로고
    • Trojan peptides: the penetratin system for intracellular delivery
    • Daniele D., Alain P., Gerard C. Trojan peptides: the penetratin system for intracellular delivery. Trends Cell Biol 1998, 84-87.
    • (1998) Trends Cell Biol , pp. 84-87
    • Daniele, D.1    Alain, P.2    Gerard, C.3
  • 39
    • 0028239908 scopus 로고
    • The third helix of the antennapedia homeodomain translocates through biological barriers
    • Derossi D., Joliot A.H., Chassaing G., Prochiantz A. The third helix of the antennapedia homeodomain translocates through biological barriers. J. Biol. Chem 1994, 269:10444-10450.
    • (1994) J. Biol. Chem , vol.269 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 40
    • 0029982569 scopus 로고    scopus 로고
    • Cell internalization of the third helix of the antennapedia homeodomain is receptor-independent
    • Derossi D., Calvet S., Trembleau A., Brunissen A., Chassaing G., Prochiantz A. Cell internalization of the third helix of the antennapedia homeodomain is receptor-independent. J. Biol. Chem 1996, 271:18188-18193.
    • (1996) J. Biol. Chem , vol.271 , pp. 18188-18193
    • Derossi, D.1    Calvet, S.2    Trembleau, A.3    Brunissen, A.4    Chassaing, G.5    Prochiantz, A.6
  • 41
    • 0031984072 scopus 로고    scopus 로고
    • Trojan peptdies: the penetratin system for intracellular delivery
    • Derossi D., Chassaing G., Prochiantz A. Trojan peptdies: the penetratin system for intracellular delivery. Trends Cell Biol 1998, 8:84-87.
    • (1998) Trends Cell Biol , vol.8 , pp. 84-87
    • Derossi, D.1    Chassaing, G.2    Prochiantz, A.3
  • 42
    • 0037146030 scopus 로고    scopus 로고
    • Au nanowire fabrication from sequenced histidine-rich peptide
    • Djalali R., Chen Y., Matsui H. Au nanowire fabrication from sequenced histidine-rich peptide. J. Am. Chem. Soc 2002, 124:13660-13661.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 13660-13661
    • Djalali, R.1    Chen, Y.2    Matsui, H.3
  • 43
    • 0037620437 scopus 로고    scopus 로고
    • Au nanocrystal growth on nanotubes controlled by conformations and charges of sequenced peptide templates
    • Djalali R., Chen Y., Matsui H. Au nanocrystal growth on nanotubes controlled by conformations and charges of sequenced peptide templates. J. Am. Chem. Soc 2003, 125:5873-5879.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 5873-5879
    • Djalali, R.1    Chen, Y.2    Matsui, H.3
  • 44
    • 33749620498 scopus 로고    scopus 로고
    • Fabrication of Au nanowires on peptide nanotubes by tuning sequenced peptide conformations
    • Djalali R., Chen Y., Matsui H. Fabrication of Au nanowires on peptide nanotubes by tuning sequenced peptide conformations. Polymeric Materials: Sci. &Eng 2003, 88:29-30.
    • (2003) Polymeric Materials: Sci. &Eng , vol.88 , pp. 29-30
    • Djalali, R.1    Chen, Y.2    Matsui, H.3
  • 45
    • 0035961329 scopus 로고    scopus 로고
    • The structural basis of protein folding and its links with human disease
    • Dobson C.M. The structural basis of protein folding and its links with human disease. Phil. Trans. R. Soc. Lond. B 2001, 356:133-145.
    • (2001) Phil. Trans. R. Soc. Lond. B , vol.356 , pp. 133-145
    • Dobson, C.M.1
  • 46
    • 0037024373 scopus 로고    scopus 로고
    • Bio-inspired materials chemistry
    • Dujardin E., Mann S. Bio-inspired materials chemistry. Adv. Mater 2002, 14:775-788.
    • (2002) Adv. Mater , vol.14 , pp. 775-788
    • Dujardin, E.1    Mann, S.2
  • 47
    • 0031471203 scopus 로고    scopus 로고
    • Intercellular trafficking and protein delivery by a herpes virus structural protein
    • Elliott G., O'hare P. Intercellular trafficking and protein delivery by a herpes virus structural protein. Cell 1997, 88:223-233.
    • (1997) Cell , vol.88 , pp. 223-233
    • Elliott, G.1    O'hare, P.2
  • 48
    • 0035478616 scopus 로고    scopus 로고
    • VE-cadherin-derived cell-penetrating peptide, pVEC, with carrier functions
    • Elmquist A., Lindgren M., Bartfai T., Langel U. VE-cadherin-derived cell-penetrating peptide, pVEC, with carrier functions. Exp. Cell Res 2001, 269:237-244.
    • (2001) Exp. Cell Res , vol.269 , pp. 237-244
    • Elmquist, A.1    Lindgren, M.2    Bartfai, T.3    Langel, U.4
  • 50
    • 0036568327 scopus 로고    scopus 로고
    • Folding of a small helical protein using hydrogen bonds and hydrophobicity forces
    • Favrin G., Irback A., Wallin S. Folding of a small helical protein using hydrogen bonds and hydrophobicity forces. Proteins 2002, 47:99-105.
    • (2002) Proteins , vol.47 , pp. 99-105
    • Favrin, G.1    Irback, A.2    Wallin, S.3
  • 53
    • 0345550440 scopus 로고    scopus 로고
    • Structures of helical Β-tapes and twisted ribbons: the role of side-chain interactions on twist and bend behavior
    • Fishwick C.W.G., Beevers A.J., Carrick L.M., Whitehouse C.D., Aggeli A., Boden N. Structures of helical Β-tapes and twisted ribbons: the role of side-chain interactions on twist and bend behavior. Nano Lett 2003, 3:1475-1479.
    • (2003) Nano Lett , vol.3 , pp. 1475-1479
    • Fishwick, C.W.G.1    Beevers, A.J.2    Carrick, L.M.3    Whitehouse, C.D.4    Aggeli, A.5    Boden, N.6
  • 54
    • 0142042549 scopus 로고    scopus 로고
    • Synthesis and organization of nanoscale II-IV semiconductor materials using evolved peptide specificity and viral capsid assembly
    • Flynn C.E., Mao C., Hayhurst A., Williams J.L., Georgiou G., Iverson B., Belcher A.M. Synthesis and organization of nanoscale II-IV semiconductor materials using evolved peptide specificity and viral capsid assembly. J. Mater. Chem 2003, 13:2414-2421.
    • (2003) J. Mater. Chem , vol.13 , pp. 2414-2421
    • Flynn, C.E.1    Mao, C.2    Hayhurst, A.3    Williams, J.L.4    Georgiou, G.5    Iverson, B.6    Belcher, A.M.7
  • 56
    • 0038072777 scopus 로고    scopus 로고
    • Assemblies of metal nanoparticles and self-assembled peptide fibrils-formation of double helical and single-chain arrays of metal nanoparticles
    • Fu X., Wang Y., Huang L., Sha Y., Gui L., Lai L., Tang Youqi Assemblies of metal nanoparticles and self-assembled peptide fibrils-formation of double helical and single-chain arrays of metal nanoparticles. Adv. Mater 2003, 15:902-906.
    • (2003) Adv. Mater , vol.15 , pp. 902-906
    • Fu, X.1    Wang, Y.2    Huang, L.3    Sha, Y.4    Gui, L.5    Lai, L.6    Tang, Y.7
  • 57
    • 2742587089 scopus 로고    scopus 로고
    • Sequence effects on helix-sheet conformational transitions of designed amphiphilic peptides
    • Fukushima Y. Sequence effects on helix-sheet conformational transitions of designed amphiphilic peptides. Bull. Chem. Soc. Jpn 1996, 69:701-708.
    • (1996) Bull. Chem. Soc. Jpn , vol.69 , pp. 701-708
    • Fukushima, Y.1
  • 58
    • 0037699014 scopus 로고    scopus 로고
    • Concentration effect on the aggregation of a self-assembling oligopeptide
    • Fung S.Y., Keyes C., Duhamel J., Chen P. Concentration effect on the aggregation of a self-assembling oligopeptide. Biophys. J 2003, 85:537-548.
    • (2003) Biophys. J , vol.85 , pp. 537-548
    • Fung, S.Y.1    Keyes, C.2    Duhamel, J.3    Chen, P.4
  • 61
    • 0037461411 scopus 로고    scopus 로고
    • Self-assembly of a designed protein polymer into Β-sheet fibrils and responsive gels
    • Goeden-Wood N.L., Keasling J.D., Muller S.J. Self-assembly of a designed protein polymer into Β-sheet fibrils and responsive gels. Macromolecules 2003, 36:2932-2938.
    • (2003) Macromolecules , vol.36 , pp. 2932-2938
    • Goeden-Wood, N.L.1    Keasling, J.D.2    Muller, S.J.3
  • 62
    • 0032005174 scopus 로고    scopus 로고
    • An oligopeptide transporter is expressed at high levels in the pancreatic carcinoma cell lines AsPc-1 and Capan-2
    • Gonzalez D.E., Covitz K.M., Sadee W., Mrsny R.J. An oligopeptide transporter is expressed at high levels in the pancreatic carcinoma cell lines AsPc-1 and Capan-2. Cancer Res 1998, 58:519-525.
    • (1998) Cancer Res , vol.58 , pp. 519-525
    • Gonzalez, D.E.1    Covitz, K.M.2    Sadee, W.3    Mrsny, R.J.4
  • 63
    • 0031696773 scopus 로고    scopus 로고
    • Effect of denaturant and protein concentrations upon protein refolding and aggregation: a simple lattice model
    • Gupta P., Hall C.K., Voegler A.C. Effect of denaturant and protein concentrations upon protein refolding and aggregation: a simple lattice model. Protein Sci 1998, 7:2642-2652.
    • (1998) Protein Sci , vol.7 , pp. 2642-2652
    • Gupta, P.1    Hall, C.K.2    Voegler, A.C.3
  • 64
    • 0025275241 scopus 로고
    • Molecular determinants of amyloid deposition in Alzheimer's disease: conformational studies of synthetic Β-protein fragments
    • Halverson K., Fraser P.E., Kirschner D.A., Lansbury P.T. Molecular determinants of amyloid deposition in Alzheimer's disease: conformational studies of synthetic Β-protein fragments. Biochemistry 1990, 29:2639-2644.
    • (1990) Biochemistry , vol.29 , pp. 2639-2644
    • Halverson, K.1    Fraser, P.E.2    Kirschner, D.A.3    Lansbury, P.T.4
  • 66
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scarpie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper J.D., Lansbury P.T. Models of amyloid seeding in Alzheimer's disease and scarpie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem 1997, 66:385-407.
    • (1997) Annu. Rev. Biochem , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury, P.T.2
  • 67
    • 0035079856 scopus 로고    scopus 로고
    • Conformational propagation with prion-like characteristics in a simple lattice model of protein folding
    • Harrison P.M., Chan H.S., Prusiner S.B., Cohen F.E. Conformational propagation with prion-like characteristics in a simple lattice model of protein folding. Protein Sci 2001, 10:819-835.
    • (2001) Protein Sci , vol.10 , pp. 819-835
    • Harrison, P.M.1    Chan, H.S.2    Prusiner, S.B.3    Cohen, F.E.4
  • 68
    • 0030737872 scopus 로고    scopus 로고
    • Lattice and off-lattice side chain models of protein folding: linear time structure prediction better than 86% of optimal
    • Hart W.E., Istrail S. Lattice and off-lattice side chain models of protein folding: linear time structure prediction better than 86% of optimal. J. Comp. Biol 1997, 4:241-259.
    • (1997) J. Comp. Biol , vol.4 , pp. 241-259
    • Hart, W.E.1    Istrail, S.2
  • 69
    • 0035941074 scopus 로고    scopus 로고
    • Self-assembly and mineralization of peptide-amphiphile nanofibers
    • Hartgerink J.D., Beniash E., Stupp S.I. Self-assembly and mineralization of peptide-amphiphile nanofibers. Science 2001, 294:1684-1688.
    • (2001) Science , vol.294 , pp. 1684-1688
    • Hartgerink, J.D.1    Beniash, E.2    Stupp, S.I.3
  • 70
    • 0033023173 scopus 로고    scopus 로고
    • Noninvasive intracellular delivery of functional peptides and proteins
    • Hawiger J. Noninvasive intracellular delivery of functional peptides and proteins. Curr. Opin. Chem. Biol 1999, 3:89-94.
    • (1999) Curr. Opin. Chem. Biol , vol.3 , pp. 89-94
    • Hawiger, J.1
  • 71
    • 1642441997 scopus 로고    scopus 로고
    • Dentin matrix protein 1 immobilized on type I collagen fibrils facilitates apatite deposition in vitro
    • He G., George A. Dentin matrix protein 1 immobilized on type I collagen fibrils facilitates apatite deposition in vitro. J. Biol. Chem 2004, 279:11646-11656.
    • (2004) J. Biol. Chem , vol.279 , pp. 11646-11656
    • He, G.1    George, A.2
  • 72
    • 0043287306 scopus 로고    scopus 로고
    • Nucleation of apatite crystals in vitro by self-assembled dentin matrix protein 1
    • He G., Dahl T., Veis A., George A. Nucleation of apatite crystals in vitro by self-assembled dentin matrix protein 1. Nature Mater 2003, 2:552-558.
    • (2003) Nature Mater , vol.2 , pp. 552-558
    • He, G.1    Dahl, T.2    Veis, A.3    George, A.4
  • 73
    • 0037039862 scopus 로고    scopus 로고
    • Third-generation biomedical materials
    • Hench L.L., Polak J.M. Third-generation biomedical materials. Science 2002, 295:1014-1017.
    • (2002) Science , vol.295 , pp. 1014-1017
    • Hench, L.L.1    Polak, J.M.2
  • 74
    • 0034612266 scopus 로고    scopus 로고
    • Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds
    • Holmes T.C., 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
  • 75
    • 0141483558 scopus 로고    scopus 로고
    • Effect of amino acid sequence and pH on nanofiber formation with self-assembling peptides EAK16-II and EAK16-IV
    • Hong Y., Legge R.L., Zhang S., Chen P. Effect of amino acid sequence and pH on nanofiber formation with self-assembling peptides EAK16-II and EAK16-IV. Biomacromolecules 2003, 4:1433-1442.
    • (2003) Biomacromolecules , vol.4 , pp. 1433-1442
    • Hong, Y.1    Legge, R.L.2    Zhang, S.3    Chen, P.4
  • 76
    • 8644285594 scopus 로고    scopus 로고
    • Critical self-assembly concentration of an ionic-complementary peptide EAK16-I
    • Hong Y., Lau L.S., Legge R.L., Chen P. Critical self-assembly concentration of an ionic-complementary peptide EAK16-I. J. Adhesion 2004, 80:913-931.
    • (2004) J. Adhesion , vol.80 , pp. 913-931
    • Hong, Y.1    Lau, L.S.2    Legge, R.L.3    Chen, P.4
  • 78
    • 0036629182 scopus 로고    scopus 로고
    • Towards quantitative assays with peptide chips: a surface engineering approach
    • Houseman B.T., Mrksich M. Towards quantitative assays with peptide chips: a surface engineering approach. Trends Biotechnol 2002, 20:279-281.
    • (2002) Trends Biotechnol , vol.20 , pp. 279-281
    • Houseman, B.T.1    Mrksich, M.2
  • 79
    • 0037259922 scopus 로고    scopus 로고
    • Supramolecular structure of helical ribbons self-assembled from a Β-sheet peptide
    • Hwang W., Marini D.M., Kamm R.D., Zhang S. Supramolecular structure of helical ribbons self-assembled from a Β-sheet peptide. J. Chem. Phys 2003, 118:389-397.
    • (2003) J. Chem. Phys , vol.118 , pp. 389-397
    • Hwang, W.1    Marini, D.M.2    Kamm, R.D.3    Zhang, S.4
  • 80
    • 0026770377 scopus 로고
    • Integrins: versatility, modulation, and signaling in cell adhesion
    • Hynes R.O. Integrins: versatility, modulation, and signaling in cell adhesion. Cell 1992, 69:11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 81
    • 0037192460 scopus 로고    scopus 로고
    • Functional materials based on self-assembly of polymeric supramolecules
    • Ikkala O., Ten Brinke G. Functional materials based on self-assembly of polymeric supramolecules. Science 2002, 295:2407-2409.
    • (2002) Science , vol.295 , pp. 2407-2409
    • Ikkala, O.1    Ten Brinke, G.2
  • 82
    • 0032994142 scopus 로고    scopus 로고
    • Lattice simulation of aggregation funnels for protein folding
    • Istrail S., Schwartz R., King J. Lattice simulation of aggregation funnels for protein folding. J. Comp. Biol 1999, 6:143-162.
    • (1999) J. Comp. Biol , vol.6 , pp. 143-162
    • Istrail, S.1    Schwartz, R.2    King, J.3
  • 83
    • 0034679845 scopus 로고    scopus 로고
    • Formation of multilamella vesicles ('Onions') in peptide based surfactant
    • Jayakumar R., Murugesan M., Ahmed M.R. Formation of multilamella vesicles ('Onions') in peptide based surfactant. Bioorg. Med. Chem. Lett 2000, 10:1547-1550.
    • (2000) Bioorg. Med. Chem. Lett , vol.10 , pp. 1547-1550
    • Jayakumar, R.1    Murugesan, M.2    Ahmed, M.R.3
  • 84
    • 0021348342 scopus 로고
    • Characteristics of shear-induced aggregation in whole blood
    • Jen C.J., Mcintire L.V. Characteristics of shear-induced aggregation in whole blood. J. Lab. Clin. Med 1984, 103:115-124.
    • (1984) J. Lab. Clin. Med , vol.103 , pp. 115-124
    • Jen, C.J.1    Mcintire, L.V.2
  • 85
    • 0034821249 scopus 로고    scopus 로고
    • High activity enzyme microcrystal multilayer films
    • Jin W., Shi X., Caruso F. High activity enzyme microcrystal multilayer films. J. Am. Chem. Soc 2001, 123:8121-8122.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 8121-8122
    • Jin, W.1    Shi, X.2    Caruso, F.3
  • 86
    • 4143071284 scopus 로고    scopus 로고
    • Self-assembly of the ionic peptide EAK16: the effect of charge distributions on self-assembly
    • Jun S., Hong Y., Imamura H., Ha B.-Y., Bechhoefer J., Chen P. Self-assembly of the ionic peptide EAK16: the effect of charge distributions on self-assembly. Biophys. J 2004, 87:1249-1259.
    • (2004) Biophys. J , vol.87 , pp. 1249-1259
    • Jun, S.1    Hong, Y.2    Imamura, H.3    Ha, B.-Y.4    Bechhoefer, J.5    Chen, P.6
  • 88
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • Kelly J.W. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol 1998, 8:101-106.
    • (1998) Curr. Opin. Struct. Biol , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 89
    • 2942632812 scopus 로고    scopus 로고
    • Self-assembling peptide as a potential carrier for hydrophobic compounds
    • Keyes-Baig C., Duhamel J., Fung S.Y., Bezaire J., Chen P. Self-assembling peptide as a potential carrier for hydrophobic compounds. J. Am. Chem. Soc 2004, 126:7522-7532.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 7522-7532
    • Keyes-Baig, C.1    Duhamel, J.2    Fung, S.Y.3    Bezaire, J.4    Chen, P.5
  • 90
    • 12944315062 scopus 로고    scopus 로고
    • Anomalous salt effects on DNA conformation: experiment and theory
    • Khan M.O., Mel'nikov S.M., Jonsson B. Anomalous salt effects on DNA conformation: experiment and theory. Macromolecules 1999, 32:8836-8840.
    • (1999) Macromolecules , vol.32 , pp. 8836-8840
    • Khan, M.O.1    Mel'nikov, S.M.2    Jonsson, B.3
  • 91
    • 0035208275 scopus 로고    scopus 로고
    • Cellular internalization of a cargo complex with a novel peptide derived from the third helix of the islet-1 homeodomain. Comparison with the penetratin peptide
    • Kilk K., Magzoub M., Pooga M., Eriksson L.E., Langel U., Graslund A. Cellular internalization of a cargo complex with a novel peptide derived from the third helix of the islet-1 homeodomain. Comparison with the penetratin peptide. Bioconjugate Chem 2001, 12:911-916.
    • (2001) Bioconjugate Chem , vol.12 , pp. 911-916
    • Kilk, K.1    Magzoub, M.2    Pooga, M.3    Eriksson, L.E.4    Langel, U.5    Graslund, A.6
  • 92
    • 0037162463 scopus 로고    scopus 로고
    • Self-assembling peptide hydrogel fosters chondrocyte extracellular matrix production and cell division: implications for cartilage tissue repair
    • Kisiday J., Jin M., Kurz B., Hung H., Semino C., Zhang S., Grodzinsky A.J. Self-assembling peptide hydrogel fosters chondrocyte extracellular matrix production and cell division: implications for cartilage tissue repair. Proc. Natl. Acad. Sci. USA 2002, 99:9996-10001.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9996-10001
    • Kisiday, J.1    Jin, M.2    Kurz, B.3    Hung, H.4    Semino, C.5    Zhang, S.6    Grodzinsky, A.J.7
  • 93
    • 0032167025 scopus 로고    scopus 로고
    • Dicarboxylic oligopeptide bolaamphiphiles: proton-triggered self-assembly of microtubes with loose solid surfaces
    • Kogiso M., Ohnishi S., Yase K., Masuda M., Shimizu T. Dicarboxylic oligopeptide bolaamphiphiles: proton-triggered self-assembly of microtubes with loose solid surfaces. Langmuir 1998, 14:4978-4986.
    • (1998) Langmuir , vol.14 , pp. 4978-4986
    • Kogiso, M.1    Ohnishi, S.2    Yase, K.3    Masuda, M.4    Shimizu, T.5
  • 94
    • 1842634772 scopus 로고    scopus 로고
    • Metal-comlexed nanofiber formation in water from dicarboxylic valylvaline bolaamphiphiles
    • Kogiso M., Okada Y., Yase K., Shimizu T. Metal-comlexed nanofiber formation in water from dicarboxylic valylvaline bolaamphiphiles. J. Colloid Interface Sci 2004, 273:394-399.
    • (2004) J. Colloid Interface Sci , vol.273 , pp. 394-399
    • Kogiso, M.1    Okada, Y.2    Yase, K.3    Shimizu, T.4
  • 96
    • 0030004644 scopus 로고    scopus 로고
    • The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyolid
    • Lai Z., Colon W., Kelly J.W. The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyolid. Biochemistry 1996, 35:6470-6482.
    • (1996) Biochemistry , vol.35 , pp. 6470-6482
    • Lai, Z.1    Colon, W.2    Kelly, J.W.3
  • 97
    • 0025047522 scopus 로고
    • New method of drug delivery
    • Langer R. New method of drug delivery. Science 1990, 249:1527-1533.
    • (1990) Science , vol.249 , pp. 1527-1533
    • Langer, R.1
  • 98
    • 0032580354 scopus 로고    scopus 로고
    • Drug delivery and targeting
    • Langer R. Drug delivery and targeting. Nature 1998, 392:5-10.
    • (1998) Nature , vol.392 , pp. 5-10
    • Langer, R.1
  • 99
    • 0034233888 scopus 로고    scopus 로고
    • Biomaterials: status, challenges, and perspectives
    • Langer R. Biomaterials: status, challenges, and perspectives. AIChE J 2000, 46:1286-1289.
    • (2000) AIChE J , vol.46 , pp. 1286-1289
    • Langer, R.1
  • 100
    • 0035816535 scopus 로고    scopus 로고
    • Drugs on targets
    • Langer R. Drugs on targets. Science 2001, 293:58-59.
    • (2001) Science , vol.293 , pp. 58-59
    • Langer, R.1
  • 101
    • 0034616839 scopus 로고    scopus 로고
    • Protofilaments, filaments, ribbons, and fibrils from peptidomimetic self-assembly: implications for amyloid fibril formation and materials science
    • Lashuel H.A., Labrenz S.R., Woo L., Serpell L.C., Kelly J.W. Protofilaments, filaments, ribbons, and fibrils from peptidomimetic self-assembly: implications for amyloid fibril formation and materials science. J. Am. Chem. Soc 2000, 122:5262-5277.
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 5262-5277
    • Lashuel, H.A.1    Labrenz, S.R.2    Woo, L.3    Serpell, L.C.4    Kelly, J.W.5
  • 102
    • 0036206184 scopus 로고    scopus 로고
    • Identifying peptide ligands for the cell surface receptors using cell-growth-on-bead assay and one-bead one compound combinatorial library
    • Lau D.H., Guo L., Liu R., Song A., Shao C., Lam K.S. Identifying peptide ligands for the cell surface receptors using cell-growth-on-bead assay and one-bead one compound combinatorial library. Biotechnol. Lett 2002, 24:497-500.
    • (2002) Biotechnol. Lett , vol.24 , pp. 497-500
    • Lau, D.H.1    Guo, L.2    Liu, R.3    Song, A.4    Shao, C.5    Lam, K.S.6
  • 103
    • 0036146551 scopus 로고    scopus 로고
    • James Gimzewski discusses the potential of nanobiotechnology
    • Lawrence R.N. James Gimzewski discusses the potential of nanobiotechnology. Drug Discov. Today 2002, 7:18-21.
    • (2002) Drug Discov. Today , vol.7 , pp. 18-21
    • Lawrence, R.N.1
  • 105
    • 0037192455 scopus 로고    scopus 로고
    • Toward self-organization and complex matter
    • Lehn J.-M. Toward self-organization and complex matter. Science 2002, 295:2400-2403.
    • (2002) Science , vol.295 , pp. 2400-2403
    • Lehn, J.-M.1
  • 107
    • 0031759126 scopus 로고    scopus 로고
    • Visualization of PEOPBLA-pyrene polymeric micelles by atomic force microscopy
    • Liaw J., Aoyagi T., Kataoka K., Sakurai Y., Okano T. Visualization of PEOPBLA-pyrene polymeric micelles by atomic force microscopy. Pharmaceutical Res 1998, 15:1721-1726.
    • (1998) Pharmaceutical Res , vol.15 , pp. 1721-1726
    • Liaw, J.1    Aoyagi, T.2    Kataoka, K.3    Sakurai, Y.4    Okano, T.5
  • 108
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid Β-protein fibrils: detection of nuclei and quantitation of rate constants
    • Lomakin A., Chung D.S., Benedek G.B., Kirschner D.A., Teplow D.B. On the nucleation and growth of amyloid Β-protein fibrils: detection of nuclei and quantitation of rate constants. Proc. Natl. Acad. Sci. USA 1996, 93:1125-1129.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1125-1129
    • Lomakin, A.1    Chung, D.S.2    Benedek, G.B.3    Kirschner, D.A.4    Teplow, D.B.5
  • 112
    • 0033915849 scopus 로고    scopus 로고
    • Nanobiotechnology: the fabrication and applications of chemical and biological nanostructures
    • Lowe C.R. Nanobiotechnology: the fabrication and applications of chemical and biological nanostructures. Curr. Opin. Struct. Biol 2000, 10:428-434.
    • (2000) Curr. Opin. Struct. Biol , vol.10 , pp. 428-434
    • Lowe, C.R.1
  • 113
    • 0003008343 scopus 로고    scopus 로고
    • Synthetic DNA delivery systems
    • Luo D., Saltzman W.M. Synthetic DNA delivery systems. Nature Biotech 2000, 18:33-37.
    • (2000) Nature Biotech , vol.18 , pp. 33-37
    • Luo, D.1    Saltzman, W.M.2
  • 114
    • 3042854377 scopus 로고    scopus 로고
    • Polyaniline nanowires on Si surfaces fabricated with DNA templates
    • Ma Y., Zhang J., Zhang G., He H. Polyaniline nanowires on Si surfaces fabricated with DNA templates. J. Am. Chem. Soc 2004, 126:7097-7101.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 7097-7101
    • Ma, Y.1    Zhang, J.2    Zhang, G.3    He, H.4
  • 115
    • 0032605317 scopus 로고    scopus 로고
    • Pharmaceutical perspectives of non-viral gene therapy
    • Mahato R.I., Smith L.C., Rolland A. Pharmaceutical perspectives of non-viral gene therapy. Adv. Genet 1999, 41:95-156.
    • (1999) Adv. Genet , vol.41 , pp. 95-156
    • Mahato, R.I.1    Smith, L.C.2    Rolland, A.3
  • 119
    • 0000590549 scopus 로고    scopus 로고
    • Left-handed helical ribbon intermediates in the self-assembly of a Β-sheet peptide
    • Marini D.M., Hwang W., Lauffenburger D.A., Zhang S., Kamm R.D. 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
  • 120
    • 0023461350 scopus 로고
    • Helix stabilization by Glu-Lys+ salt bridges in short peptides of de novo design
    • Marqusee S., Baldwin R.L. Helix stabilization by Glu-Lys+ salt bridges in short peptides of de novo design. Proc. Natl. Acad. Sci. USA 1987, 84:8898-8902.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 8898-8902
    • Marqusee, S.1    Baldwin, R.L.2
  • 121
    • 85031235543 scopus 로고    scopus 로고
    • Self-assembled peptide nanotube: assembling mechanism and fabrications
    • Matsui H. Self-assembled peptide nanotube: assembling mechanism and fabrications. Recent Res. Develop. Phys. Chem 2002, 6:351-370.
    • (2002) Recent Res. Develop. Phys. Chem , vol.6 , pp. 351-370
    • Matsui, H.1
  • 122
    • 0033741820 scopus 로고    scopus 로고
    • Crystalline glysylglycine bolaamphiphile tubules and their pH-sensitive structural transformation
    • Matsui H., Gologan B. Crystalline glysylglycine bolaamphiphile tubules and their pH-sensitive structural transformation. J. Phys. Chem. B 2000, 104:1183-3386.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 1183-3386
    • Matsui, H.1    Gologan, B.2
  • 123
    • 0034258246 scopus 로고    scopus 로고
    • Controlled immobilization of peptide nanotube-templated metallic wires on Au surfaces
    • Matsui H., Gologan B., Douberly G.E. Controlled immobilization of peptide nanotube-templated metallic wires on Au surfaces. Eur. Phys. J. D 2001, 16:403-406.
    • (2001) Eur. Phys. J. D , vol.16 , pp. 403-406
    • Matsui, H.1    Gologan, B.2    Douberly, G.E.3
  • 124
    • 0028839438 scopus 로고
    • Comparison of lethal and nonlethal Transthyretin variants and their relationship to amyloid disease
    • Mccutchen S.L., Lai Z., Miroy G.J., Kelly J.W., Colon W. Comparison of lethal and nonlethal Transthyretin variants and their relationship to amyloid disease. Biochemistry 1995, 34:13527-13536.
    • (1995) Biochemistry , vol.34 , pp. 13527-13536
    • Mccutchen, S.L.1    Lai, Z.2    Miroy, G.J.3    Kelly, J.W.4    Colon, W.5
  • 126
    • 0037072576 scopus 로고    scopus 로고
    • Prospects for cationic polymers in gene and oligonucleotide therapy against cancer
    • Merdan T., Kopecek J., Kissel T. Prospects for cationic polymers in gene and oligonucleotide therapy against cancer. Adv. Drug Del. Rev 2002, 54:715-758.
    • (2002) Adv. Drug Del. Rev , vol.54 , pp. 715-758
    • Merdan, T.1    Kopecek, J.2    Kissel, T.3
  • 127
    • 0033169046 scopus 로고    scopus 로고
    • Biotechnology as a route to nanotechnology
    • Merkle R.C. Biotechnology as a route to nanotechnology. Trends Biotechnol 1999, 17:271-274.
    • (1999) Trends Biotechnol , vol.17 , pp. 271-274
    • Merkle, R.C.1
  • 128
    • 0030864812 scopus 로고    scopus 로고
    • Engineering peptides and proteins that undergo Α-toΒ transitions
    • Mihara H., Takahashi Y. Engineering peptides and proteins that undergo Α-toΒ transitions. Curr. Opin. Struct. Biol 1997, 7:501-508.
    • (1997) Curr. Opin. Struct. Biol , vol.7 , pp. 501-508
    • Mihara, H.1    Takahashi, Y.2
  • 129
    • 0032204284 scopus 로고    scopus 로고
    • Formation of oriented helical peptide layers on a gold surface due to the self-assembling properties of peptides
    • Miura Y., Kimura S. Formation of oriented helical peptide layers on a gold surface due to the self-assembling properties of peptides. Langmuir 1998, 14:6935-6940.
    • (1998) Langmuir , vol.14 , pp. 6935-6940
    • Miura, Y.1    Kimura, S.2
  • 130
    • 0030804766 scopus 로고    scopus 로고
    • A new peptide vector for efficient delivery of oligonucleotides into mammalian cells
    • Morris M.C., Vidal P., Chaloin F., Heitz F., Divita G. A new peptide vector for efficient delivery of oligonucleotides into mammalian cells. Nucleic Acids Res 1997, 25:2730-2736.
    • (1997) Nucleic Acids Res , vol.25 , pp. 2730-2736
    • Morris, M.C.1    Vidal, P.2    Chaloin, F.3    Heitz, F.4    Divita, G.5
  • 131
    • 0035204427 scopus 로고    scopus 로고
    • A peptide carrier for the delivery of biologically active proteins into mammalian cells
    • Morris M.C., Depollier J., Mery J., Heitz F., Divita G. A peptide carrier for the delivery of biologically active proteins into mammalian cells. Nat. Biotechnol 2001, 19:1173-1176.
    • (2001) Nat. Biotechnol , vol.19 , pp. 1173-1176
    • Morris, M.C.1    Depollier, J.2    Mery, J.3    Heitz, F.4    Divita, G.5
  • 132
    • 0001338169 scopus 로고    scopus 로고
    • A surface chemistry approach to sutdying cell adhesion
    • Mrksich M. A surface chemistry approach to sutdying cell adhesion. Chem. Soc. Rev 2000, 29:267-273.
    • (2000) Chem. Soc. Rev , vol.29 , pp. 267-273
    • Mrksich, M.1
  • 133
    • 0030000062 scopus 로고    scopus 로고
    • Using self-assembled monolayers to understand the interactions of manmade surfaces with proteins and cells
    • Mrksich M., Whitesides G.M. Using self-assembled monolayers to understand the interactions of manmade surfaces with proteins and cells. Annu. Rev. Biophys. Biomol. Struct 1996, 25:55-78.
    • (1996) Annu. Rev. Biophys. Biomol. Struct , vol.25 , pp. 55-78
    • Mrksich, M.1    Whitesides, G.M.2
  • 134
    • 0025276149 scopus 로고
    • Peptides as conformational switch: medium-induced conformational transitions of designed peptides
    • Mutter M., Hersperger R. Peptides as conformational switch: medium-induced conformational transitions of designed peptides. Angew. Chem. Int. Ed. Engl 1990, 29:185-187.
    • (1990) Angew. Chem. Int. Ed. Engl , vol.29 , pp. 185-187
    • Mutter, M.1    Hersperger, R.2
  • 135
    • 33748242285 scopus 로고
    • Switch peptides: pH-induced Α-helix to Β-sheet transtions of bis-amphiphilic oligopeptides
    • Mutter M., Gassmann R., Buttkus U., Altmann K.-H. Switch peptides: pH-induced Α-helix to Β-sheet transtions of bis-amphiphilic oligopeptides. Angew. Chem. Int. Ed. Engl 1991, 30:1514-1516.
    • (1991) Angew. Chem. Int. Ed. Engl , vol.30 , pp. 1514-1516
    • Mutter, M.1    Gassmann, R.2    Buttkus, U.3    Altmann, K.-H.4
  • 137
    • 0033813664 scopus 로고    scopus 로고
    • Cancer cell targeted drug delivery utilizing oligopeptide transporter activity
    • Nakanishi T., Tamai I., Takaki A., Tsuji A. Cancer cell targeted drug delivery utilizing oligopeptide transporter activity. Int. J. Cancer 2000, 88:274-280.
    • (2000) Int. J. Cancer , vol.88 , pp. 274-280
    • Nakanishi, T.1    Tamai, I.2    Takaki, A.3    Tsuji, A.4
  • 138
    • 0015520388 scopus 로고
    • The effects of salts on the free energy of the peptide group
    • Nandi P.K., Robinson D.R. The effects of salts on the free energy of the peptide group. J. Am. Chem. Soc 1972, 94:1299-1308.
    • (1972) J. Am. Chem. Soc , vol.94 , pp. 1299-1308
    • Nandi, P.K.1    Robinson, D.R.2
  • 139
    • 0038789021 scopus 로고    scopus 로고
    • Self-assembly combining two bioactive peptide-amphiphile molecules into nanofibers by electrostatic attraction
    • Niece K.L., Hartgerink J.D., Donners J.J.J.M., Stupp S.I. Self-assembly combining two bioactive peptide-amphiphile molecules into nanofibers by electrostatic attraction. J. Am. Chem. Soc 2003, 125:7146-7147.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 7146-7147
    • Niece, K.L.1    Hartgerink, J.D.2    Donners, J.J.J.M.3    Stupp, S.I.4
  • 140
    • 0037161668 scopus 로고    scopus 로고
    • Rapidly recovering hydrogel scaffolds from self-assembling diblock copolypeptide amphiphiles
    • Nowak A.P., Breedveld V., Pakstis L., Ozbas B., Pine D.J., Pochan D., Deming T.J. Rapidly recovering hydrogel scaffolds from self-assembling diblock copolypeptide amphiphiles. Nature 2002, 417:424-428.
    • (2002) Nature , vol.417 , pp. 424-428
    • Nowak, A.P.1    Breedveld, V.2    Pakstis, L.3    Ozbas, B.4    Pine, D.J.5    Pochan, D.6    Deming, T.J.7
  • 141
    • 0031590315 scopus 로고    scopus 로고
    • Extensive cellular uptake into endothelial cells of an amphipathic beta-sheet forming peptide
    • Oehlke J., Krause E., Wiesner B., Beyermann M., Bienert M. Extensive cellular uptake into endothelial cells of an amphipathic beta-sheet forming peptide. FEBS Lett 1997, 415:196-199.
    • (1997) FEBS Lett , vol.415 , pp. 196-199
    • Oehlke, J.1    Krause, E.2    Wiesner, B.3    Beyermann, M.4    Bienert, M.5
  • 142
    • 0032508926 scopus 로고    scopus 로고
    • Cellular uptake of an alpha-helical amphipathic model peptide with the potential to deliver polar compounds into the cell interior non-endocytically
    • Oehlke J., Scheller A., Wiesner B., Krause E., Beyermann M., Klauschenz E., Melzig M., Bienert M. Cellular uptake of an alpha-helical amphipathic model peptide with the potential to deliver polar compounds into the cell interior non-endocytically. Biochim. Biophys. Acta 1998, 1414:127-139.
    • (1998) Biochim. Biophys. Acta , vol.1414 , pp. 127-139
    • Oehlke, J.1    Scheller, A.2    Wiesner, B.3    Krause, E.4    Beyermann, M.5    Klauschenz, E.6    Melzig, M.7    Bienert, M.8
  • 145
    • 0344440985 scopus 로고    scopus 로고
    • Isolation of lung tumor specific peptides from a random peptide library: generation of diagnostic and cell-targeting reagents
    • Oyama T., Sykes K.F., Samli K.N., Minna J.D., Johnston S.A., Brown K.C. Isolation of lung tumor specific peptides from a random peptide library: generation of diagnostic and cell-targeting reagents. Cancer Lett 2003, 202:219-230.
    • (2003) Cancer Lett , vol.202 , pp. 219-230
    • Oyama, T.1    Sykes, K.F.2    Samli, K.N.3    Minna, J.D.4    Johnston, S.A.5    Brown, K.C.6
  • 146
    • 0002754017 scopus 로고
    • Formation of self-assembled monolayers by chemisorption of derivatives of oligo(ethylene glycol) of structure HS(CH2)11(OCH2CH2)mOH on gold
    • Pale-Grosdemange C., Simon E.S., Prime K.L., Whitesides G.M. Formation of self-assembled monolayers by chemisorption of derivatives of oligo(ethylene glycol) of structure HS(CH2)11(OCH2CH2)mOH on gold. J. Am. Chem. Soc 1991, 113:12-20.
    • (1991) J. Am. Chem. Soc , vol.113 , pp. 12-20
    • Pale-Grosdemange, C.1    Simon, E.S.2    Prime, K.L.3    Whitesides, G.M.4
  • 147
    • 0023186714 scopus 로고
    • Chimeric peptides as a vehicle for peptide pharmaceutical delivery through the blood-brain barrier
    • Pardridge W.M., Kumagai A.K., Eisenberg J.B. Chimeric peptides as a vehicle for peptide pharmaceutical delivery through the blood-brain barrier. Biochem. Biophys. Res. Comm 1987, 146:307-313.
    • (1987) Biochem. Biophys. Res. Comm , vol.146 , pp. 307-313
    • Pardridge, W.M.1    Kumagai, A.K.2    Eisenberg, J.B.3
  • 148
    • 0037117499 scopus 로고    scopus 로고
    • Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid Β-peptide of amyloid plaques
    • Perutz M.F., Pope B.J., Owen D., Wanker E.E., Scherzinger E. Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid Β-peptide of amyloid plaques. Proc. Natl. Acad. Sci. USA 2002, 99:5596-5600.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5596-5600
    • Perutz, M.F.1    Pope, B.J.2    Owen, D.3    Wanker, E.E.4    Scherzinger, E.5
  • 149
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • Pierschbacher M.D., Ruoslahti E. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 1984, 309:30-33.
    • (1984) Nature , vol.309 , pp. 30-33
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 151
    • 0036797347 scopus 로고    scopus 로고
    • Size-controlled self-assembly of peptide nanotubes using polycarbonate membranes as templates
    • Porrata P., Goun E., Matsui H. Size-controlled self-assembly of peptide nanotubes using polycarbonate membranes as templates. Chem. Mater 2002, 14:4378-4381.
    • (2002) Chem. Mater , vol.14 , pp. 4378-4381
    • Porrata, P.1    Goun, E.2    Matsui, H.3
  • 152
    • 0035977635 scopus 로고    scopus 로고
    • Medium-dependent self-assembly of an amphiphilic peptide: direct observation of peptide phase domains at the air-water interface
    • Powers E.T., Kelly J.W. Medium-dependent self-assembly of an amphiphilic peptide: direct observation of peptide phase domains at the air-water interface. J. Am. Chem. Soc 2001, 123:775-776.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 775-776
    • Powers, E.T.1    Kelly, J.W.2
  • 153
    • 0037016788 scopus 로고    scopus 로고
    • Ordered Langmuir-Blodgett films of amphiphilic Β-hairpin peptides imaged by atomic force microscopy
    • Powers E.T., Yang S.I., Lieber C.M., Kelly J.W. Ordered Langmuir-Blodgett films of amphiphilic Β-hairpin peptides imaged by atomic force microscopy. Angew. Chem. Int. Ed 2002, 41:127-130.
    • (2002) Angew. Chem. Int. Ed , vol.41 , pp. 127-130
    • Powers, E.T.1    Yang, S.I.2    Lieber, C.M.3    Kelly, J.W.4
  • 154
    • 0027364324 scopus 로고
    • Multiple integrins mediate cell attachment to cytotactin/tenascin
    • Prieto A.L., Edelman G.M., Crossin K.L. Multiple integrins mediate cell attachment to cytotactin/tenascin. Proc. Natl. Acad. Sci. USA 1993, 90:10154-10158.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10154-10158
    • Prieto, A.L.1    Edelman, G.M.2    Crossin, K.L.3
  • 155
    • 0035950480 scopus 로고    scopus 로고
    • Permeability of ibuprofen in various polyelectrolyte multilayers
    • Qiu X., Donath E., Mohwald H. Permeability of ibuprofen in various polyelectrolyte multilayers. Macromol. Mater. Eng 2001, 286:591-597.
    • (2001) Macromol. Mater. Eng , vol.286 , pp. 591-597
    • Qiu, X.1    Donath, E.2    Mohwald, H.3
  • 156
    • 0035928938 scopus 로고    scopus 로고
    • Studies on the drug release properties of polysaccharide multilayers encapsulated ibuprofen microparticles
    • Qiu X., Laporatti S., Donath E., Mohwald H. Studies on the drug release properties of polysaccharide multilayers encapsulated ibuprofen microparticles. Langmuir 2001, 17:5375-5380.
    • (2001) Langmuir , vol.17 , pp. 5375-5380
    • Qiu, X.1    Laporatti, S.2    Donath, E.3    Mohwald, H.4
  • 157
    • 0037466613 scopus 로고    scopus 로고
    • Casting metal nanowires within discrete self-assembled peptide
    • Reches M., Gazit E. Casting metal nanowires within discrete self-assembled peptide. Science 2003, 300:625-627.
    • (2003) Science , vol.300 , pp. 625-627
    • Reches, M.1    Gazit, E.2
  • 158
    • 0037192459 scopus 로고    scopus 로고
    • Synthesis beyond the molecule
    • Reinhoudt D.N., Crego-Calama M. Synthesis beyond the molecule. Science 2002, 295:2403-2407.
    • (2002) Science , vol.295 , pp. 2403-2407
    • Reinhoudt, D.N.1    Crego-Calama, M.2
  • 160
    • 0033960784 scopus 로고    scopus 로고
    • Aggregation of an amyloidogenic fragment of human islet amyloid polypeptide
    • Rhoades E., Agarwal J., Gafni A. Aggregation of an amyloidogenic fragment of human islet amyloid polypeptide. Biochim. Biophys. Acta 2000, 1476:230-238.
    • (2000) Biochim. Biophys. Acta , vol.1476 , pp. 230-238
    • Rhoades, E.1    Agarwal, J.2    Gafni, A.3
  • 161
  • 162
    • 0029775681 scopus 로고    scopus 로고
    • RGD and other recognition sequences for integrins
    • Ruoslahti E. RGD and other recognition sequences for integrins. Annu. Rev. Cell Dev. Biol 1996, 12:697-715.
    • (1996) Annu. Rev. Cell Dev. Biol , vol.12 , pp. 697-715
    • Ruoslahti, E.1
  • 163
    • 0037844737 scopus 로고    scopus 로고
    • Engineering the morphology of a self-assembling protein fibre
    • Ryadnov M.G., Woolfson D.N. Engineering the morphology of a self-assembling protein fibre. Nature Mater 2003, 2:329-332.
    • (2003) Nature Mater , vol.2 , pp. 329-332
    • Ryadnov, M.G.1    Woolfson, D.N.2
  • 164
    • 0346848865 scopus 로고    scopus 로고
    • Nanotech approaches to drug delivery and imaging
    • Sahoo S.K., Labhasetwar V. Nanotech approaches to drug delivery and imaging. Drug Discov. Today 2003, 8:1112-1120.
    • (2003) Drug Discov. Today , vol.8 , pp. 1112-1120
    • Sahoo, S.K.1    Labhasetwar, V.2
  • 165
    • 84903492522 scopus 로고    scopus 로고
    • Self-assembled nanobiomaterials
    • American Scientific Publishers, Stevenson Ranch, CA, H.S. Nalwa (Ed.)
    • Santoso S., Zhang S. Self-assembled nanobiomaterials. Encyclopedia of Nanoscience and Nanotechnology 2003, American Scientific Publishers, Stevenson Ranch, CA. H.S. Nalwa (Ed.).
    • (2003) Encyclopedia of Nanoscience and Nanotechnology
    • Santoso, S.1    Zhang, S.2
  • 166
    • 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
  • 167
    • 0036866835 scopus 로고    scopus 로고
    • Structures, function and applications of amphiphilic peptides
    • Santoso S.S., Vauthey S., Zhang S. Structures, function and applications of amphiphilic peptides. Curr. Opin. Coll. Inter. Sci 2002, 7:262-266.
    • (2002) Curr. Opin. Coll. Inter. Sci , vol.7 , pp. 262-266
    • Santoso, S.S.1    Vauthey, S.2    Zhang, S.3
  • 168
    • 0038797831 scopus 로고    scopus 로고
    • Ligand-targeted liposomal anticancer drugs
    • Sapra P., Allen T.M. Ligand-targeted liposomal anticancer drugs. Progress in Lipid Research 2003, 42:439-462.
    • (2003) Progress in Lipid Research , vol.42 , pp. 439-462
    • Sapra, P.1    Allen, T.M.2
  • 172
    • 0035826219 scopus 로고    scopus 로고
    • Thin solid films roll up into nanotubes
    • Schmidt O.G., Eberl K. Thin solid films roll up into nanotubes. Nature 2001, 410:168.
    • (2001) Nature , vol.410 , pp. 168
    • Schmidt, O.G.1    Eberl, K.2
  • 174
    • 0037197883 scopus 로고    scopus 로고
    • Emulating biology: building nanostructures from the bottom up
    • Seeman N.C., Belch A.M. Emulating biology: building nanostructures from the bottom up. Proc. Natl. Acad. Sci. USA 2002, 99:6451-6455.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6451-6455
    • Seeman, N.C.1    Belch, A.M.2
  • 175
    • 0037672212 scopus 로고    scopus 로고
    • Functional differentiation of hepatocyte-like spheroid structures from putative liver progenitor cells in three-dimensional peptide scaffolds
    • Semino C., Merok J.R., Crane G.G., Panagiotakos G., Zhang S. Functional differentiation of hepatocyte-like spheroid structures from putative liver progenitor cells in three-dimensional peptide scaffolds. Differentiation 2003, 71:262-270.
    • (2003) Differentiation , vol.71 , pp. 262-270
    • Semino, C.1    Merok, J.R.2    Crane, G.G.3    Panagiotakos, G.4    Zhang, S.5
  • 176
    • 2342648102 scopus 로고    scopus 로고
    • Entrapment of migrating hippocampal neural cells in three-dimensional peptide nanofiber scaffold
    • Semino C.E., Kasahara J., Hayashi Y., Zhang S. Entrapment of migrating hippocampal neural cells in three-dimensional peptide nanofiber scaffold. Tissue Eng 2004, 10:643-655.
    • (2004) Tissue Eng , vol.10 , pp. 643-655
    • Semino, C.E.1    Kasahara, J.2    Hayashi, Y.3    Zhang, S.4
  • 179
    • 0035930578 scopus 로고    scopus 로고
    • Molecules get wired
    • Service R.F. Molecules get wired. Science 2001, 294:2442-2443.
    • (2001) Science , vol.294 , pp. 2442-2443
    • Service, R.F.1
  • 180
    • 0037192527 scopus 로고    scopus 로고
    • Can chemists assemble a future for molecular electronics?
    • Service R.F. Can chemists assemble a future for molecular electronics?. Science 2002, 295:2398-2399.
    • (2002) Science , vol.295 , pp. 2398-2399
    • Service, R.F.1
  • 181
    • 0000870658 scopus 로고    scopus 로고
    • Exploring the space of protein folding Hamiltonians: the balance of forces in a minimalist Β-barrel model
    • Shea J.-E., Nochomovitz Y.D., Guo Z., Brooks C.L.I. Exploring the space of protein folding Hamiltonians: the balance of forces in a minimalist Β-barrel model. J. Chem. Phys 1998, 109:2895-2903.
    • (1998) J. Chem. Phys , vol.109 , pp. 2895-2903
    • Shea, J.-E.1    Nochomovitz, Y.D.2    Guo, Z.3    Brooks, C.L.I.4
  • 182
    • 0035917248 scopus 로고    scopus 로고
    • Release behavior of thin-walled microcapsules composed of polyelectrolyte multilayers
    • Shi X., Caruso F. Release behavior of thin-walled microcapsules composed of polyelectrolyte multilayers. Langmuir 2001, 17:2036-2042.
    • (2001) Langmuir , vol.17 , pp. 2036-2042
    • Shi, X.1    Caruso, F.2
  • 183
    • 0036159271 scopus 로고    scopus 로고
    • Different mechanisms for cellular internalization of the HIV-1 Tat-derived cell penetrating peptide and recombinant proteins fused to Tat
    • Silhol M., Tyagi M., Giacca M., Lebleu B.V. Different mechanisms for cellular internalization of the HIV-1 Tat-derived cell penetrating peptide and recombinant proteins fused to Tat. Eur. J. Biochem 2002, 269:494-501.
    • (2002) Eur. J. Biochem , vol.269 , pp. 494-501
    • Silhol, M.1    Tyagi, M.2    Giacca, M.3    Lebleu, B.V.4
  • 184
    • 0037592877 scopus 로고    scopus 로고
    • Insight into the mechanism of the peptide-based gene delivery system MPG: implications for delivery of siRNA into mammalian cells
    • Simeoni F., Morris M.C., Heitz F., Divita G. Insight into the mechanism of the peptide-based gene delivery system MPG: implications for delivery of siRNA into mammalian cells. Nucleic Acids Res 2003, 31:2717-2724.
    • (2003) Nucleic Acids Res , vol.31 , pp. 2717-2724
    • Simeoni, F.1    Morris, M.C.2    Heitz, F.3    Divita, G.4
  • 185
    • 0033849738 scopus 로고    scopus 로고
    • Review: history of the amyloid fibril
    • Sipe J.D., Cohen A.S. Review: history of the amyloid fibril. J. Struct. Biol 2000, 130:88-98.
    • (2000) J. Struct. Biol , vol.130 , pp. 88-98
    • Sipe, J.D.1    Cohen, A.S.2
  • 186
    • 0034315782 scopus 로고    scopus 로고
    • Bridging the gap between homopolymer and protein models: a discontinuous molecular dynamics study
    • Smith A.V., Hall C.K. 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
  • 189
    • 0027988116 scopus 로고
    • Surfactant properties of Alzheimer's AΒ peptides and the mechanism of amyloid aggregation
    • Soreghan B., Kosmoski J., Glabe C. Surfactant properties of Alzheimer's AΒ peptides and the mechanism of amyloid aggregation. J. Biol. Chem 1994, 269:28551-28554.
    • (1994) J. Biol. Chem , vol.269 , pp. 28551-28554
    • Soreghan, B.1    Kosmoski, J.2    Glabe, C.3
  • 191
    • 0001402956 scopus 로고    scopus 로고
    • Self-assembling chiral monolayers of helical peptides bound to gold via side-chain thioethers
    • Strong A.E., Moore B.D. Self-assembling chiral monolayers of helical peptides bound to gold via side-chain thioethers. Chem. Commun 1998, 473-474.
    • (1998) Chem. Commun , pp. 473-474
    • Strong, A.E.1    Moore, B.D.2
  • 192
    • 0032979901 scopus 로고    scopus 로고
    • Self-assembling monolayers of helical oligopeptides on gold with applications in molecular electronics
    • Strong A.E., Moore B.D. Self-assembling monolayers of helical oligopeptides on gold with applications in molecular electronics. J. Mater. Chem 1999, 9:1097-1105.
    • (1999) J. Mater. Chem , vol.9 , pp. 1097-1105
    • Strong, A.E.1    Moore, B.D.2
  • 193
    • 1842373831 scopus 로고    scopus 로고
    • Molecular manipulation of microstructures: biomaterials, ceramics, and semiconductors
    • Stupp S.I., Braun P.V. Molecular manipulation of microstructures: biomaterials, ceramics, and semiconductors. Science 1997, 277:1242-1248.
    • (1997) Science , vol.277 , pp. 1242-1248
    • Stupp, S.I.1    Braun, P.V.2
  • 194
    • 0031798017 scopus 로고    scopus 로고
    • Design of a peptide undergoing ΑΒ structural transition and amyloid fibrillogenesis by the introduction of a hydrophobic defect
    • Takahashi Y., Ueno A., Mihara H. Design of a peptide undergoing ΑΒ structural transition and amyloid fibrillogenesis by the introduction of a hydrophobic defect. Chem. Eur. J 1998, 4:2475-2484.
    • (1998) Chem. Eur. J , vol.4 , pp. 2475-2484
    • Takahashi, Y.1    Ueno, A.2    Mihara, H.3
  • 195
    • 0033015586 scopus 로고    scopus 로고
    • Optimization of hydrophobic domains in peptides that undergo transformation from Α-helix to Β-fibril
    • Takahashi Y., Ueno A., Mihara H. Optimization of hydrophobic domains in peptides that undergo transformation from Α-helix to Β-fibril. Bioorg. Med. Chem 1999, 7:177-185.
    • (1999) Bioorg. Med. Chem , vol.7 , pp. 177-185
    • Takahashi, Y.1    Ueno, A.2    Mihara, H.3
  • 196
    • 0033117927 scopus 로고    scopus 로고
    • Deciphering the timescale and mechanism of protein folding using minimal off-lattice models
    • Thirumalai D., Klimov D.K. Deciphering the timescale and mechanism of protein folding using minimal off-lattice models. Curr. Opin. Struct. Biol 1999, 9:197-207.
    • (1999) Curr. Opin. Struct. Biol , vol.9 , pp. 197-207
    • Thirumalai, D.1    Klimov, D.K.2
  • 197
    • 0034613057 scopus 로고    scopus 로고
    • The antennapedia peptide penatratin translocates across lipid bilayers - the first direct observation
    • Thoren P.E.G., Persson D., Karlsson B., Norden B. The antennapedia peptide penatratin translocates across lipid bilayers - the first direct observation. FEBS Lett 2000, 482:265-268.
    • (2000) FEBS Lett , vol.482 , pp. 265-268
    • Thoren, P.E.G.1    Persson, D.2    Karlsson, B.3    Norden, B.4
  • 198
    • 0037051027 scopus 로고    scopus 로고
    • The role of surface science in bioengineered materials
    • Tirrell M., Kokkoli E., Biesalski M. The role of surface science in bioengineered materials. Surf. Sci 2002, 500:61-83.
    • (2002) Surf. Sci , vol.500 , pp. 61-83
    • Tirrell, M.1    Kokkoli, E.2    Biesalski, M.3
  • 199
    • 0036836978 scopus 로고    scopus 로고
    • Novel branching membrane translocational peptide as gene delivery vector
    • Tung C.H., Mueller S., Weissleder R. Novel branching membrane translocational peptide as gene delivery vector. Bioorg. Med. Chem 2002, 10:3609-3614.
    • (2002) Bioorg. Med. Chem , vol.10 , pp. 3609-3614
    • Tung, C.H.1    Mueller, S.2    Weissleder, R.3
  • 200
    • 0344936650 scopus 로고    scopus 로고
    • The helix-coil transition of DNA duplexes and hairpins observed by multiple fluorescence parameters
    • Vamosi G., Clegg R.M. The helix-coil transition of DNA duplexes and hairpins observed by multiple fluorescence parameters. Biochemistry 1998, 37:14300-14316.
    • (1998) Biochemistry , vol.37 , pp. 14300-14316
    • Vamosi, G.1    Clegg, R.M.2
  • 201
    • 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
  • 202
    • 0043236283 scopus 로고    scopus 로고
    • Protein folding and misfolding: a paradigm of self-assembly and regulation in complex biological systems
    • Vendruscolo M., Zurdo J., Macphee C.E., Dobson C.M. Protein folding and misfolding: a paradigm of self-assembly and regulation in complex biological systems. Phil. Trans. R. Soc. Lond 2003, 361:1205-1222.
    • (2003) Phil. Trans. R. Soc. Lond , vol.361 , pp. 1205-1222
    • Vendruscolo, M.1    Zurdo, J.2    Macphee, C.E.3    Dobson, C.M.4
  • 203
    • 0032764932 scopus 로고    scopus 로고
    • Application of membrane-active peptides for nonviral gene delivery
    • Wagner E. Application of membrane-active peptides for nonviral gene delivery. Adv. Drug Del. Rev 1999, 38:279-289.
    • (1999) Adv. Drug Del. Rev , vol.38 , pp. 279-289
    • Wagner, E.1
  • 205
    • 0028279006 scopus 로고
    • Importance of environment in determining secondary structure in proteins
    • Waterhous D.V., Johnson W.C. Importance of environment in determining secondary structure in proteins. Biochemistry 1994, 33:2121-2128.
    • (1994) Biochemistry , vol.33 , pp. 2121-2128
    • Waterhous, D.V.1    Johnson, W.C.2
  • 207
    • 0037192505 scopus 로고    scopus 로고
    • Self-assembly at all scales
    • Whitesides G.M., Grzybowski B. Self-assembly at all scales. Science 2002, 295:2418-2421.
    • (2002) Science , vol.295 , pp. 2418-2421
    • Whitesides, G.M.1    Grzybowski, B.2
  • 208
    • 0026433721 scopus 로고
    • Molecular self-assembly and nanochemistry: a chemical strategy for the synthesis of nanostructures
    • Whitesides G.M., Mathias J.P., Seto C.T. Molecular self-assembly and nanochemistry: a chemical strategy for the synthesis of nanostructures. Science 1991, 254:1312-1319.
    • (1991) Science , vol.254 , pp. 1312-1319
    • Whitesides, G.M.1    Mathias, J.P.2    Seto, C.T.3
  • 209
    • 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 B.L., Shieh H.-M., Hecht M.H. 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
  • 210
    • 0035957336 scopus 로고    scopus 로고
    • Self-assembled monolayers from a designed combinatorial library of de novo Β-sheet proteins
    • Xu G., Wang W., Groves J.T., Hecht M.H. Self-assembled monolayers from a designed combinatorial library of de novo Β-sheet proteins. Proc. Natl. Acad. Sci. USA 2001, 98:3652-3657.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3652-3657
    • Xu, G.1    Wang, W.2    Groves, J.T.3    Hecht, M.H.4
  • 211
    • 0036909872 scopus 로고    scopus 로고
    • Three-dimensional assembly of Au nano particles using dipeptides
    • Xu L., Guo Y., Xie R., Zhuang J., Yang W., Li T. Three-dimensional assembly of Au nano particles using dipeptides. Nanotechnology 2002, 13:725-728.
    • (2002) Nanotechnology , vol.13 , pp. 725-728
    • Xu, L.1    Guo, Y.2    Xie, R.3    Zhuang, J.4    Yang, W.5    Li, T.6
  • 212
    • 0025734184 scopus 로고
    • Adhesive recognition sequences
    • Yamada K.M. Adhesive recognition sequences. J. Biol. Chem 1991, 266:12809-12812.
    • (1991) J. Biol. Chem , vol.266 , pp. 12809-12812
    • Yamada, K.M.1
  • 213
    • 0037063510 scopus 로고    scopus 로고
    • Substrate-facilitated assembly of elastin-like peptides: studies by variable-temperature in situ atomic force microscopy
    • Yang G., Woodhouse K.A., Yip C.M. Substrate-facilitated assembly of elastin-like peptides: studies by variable-temperature in situ atomic force microscopy. J. Am. Chem. Soc 2002, 124:10648-10649.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 10648-10649
    • Yang, G.1    Woodhouse, K.A.2    Yip, C.M.3
  • 214
    • 4544227313 scopus 로고    scopus 로고
    • Self-assembled aggregates of IgGs as templates for the growth of clusters of gold nanoparticles
    • Yang J., Mayer M., Kriebel J.K., Garstecki P., Whitesides G.M. Self-assembled aggregates of IgGs as templates for the growth of clusters of gold nanoparticles. Angew. Chem. Int. Ed 2004, 43:1555-1558.
    • (2004) Angew. Chem. Int. Ed , vol.43 , pp. 1555-1558
    • Yang, J.1    Mayer, M.2    Kriebel, J.K.3    Garstecki, P.4    Whitesides, G.M.5
  • 215
    • 0029247467 scopus 로고
    • Fluorescence studies of associating polymers in water: determination of the chain aggregation number and a model for the association process
    • Yekta A., Xu B., Duhamel J., Adiwidjaja H., Winnik M.A. Fluorescence studies of associating polymers in water: determination of the chain aggregation number and a model for the association process. Macromolecules 1995, 28:956-966.
    • (1995) Macromolecules , vol.28 , pp. 956-966
    • Yekta, A.1    Xu, B.2    Duhamel, J.3    Adiwidjaja, H.4    Winnik, M.A.5
  • 216
    • 0345724791 scopus 로고    scopus 로고
    • Direct growth of shape-controlled nanocrystals on nanotubes via biological recognition
    • Yu L., Banerjee I.A., Matsui H. Direct growth of shape-controlled nanocrystals on nanotubes via biological recognition. J. Am. Chem. Soc 2003, 125:14837-14840.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 14837-14840
    • Yu, L.1    Banerjee, I.A.2    Matsui, H.3
  • 217
    • 1542402288 scopus 로고    scopus 로고
    • Incorporation of sequenced peptides on nanotubes for Pt coating: smart control of nucleation and morphology via activation of metal binding sites on amino acids
    • Yu L., Banerjee I.A., Matsui H. Incorporation of sequenced peptides on nanotubes for Pt coating: smart control of nucleation and morphology via activation of metal binding sites on amino acids. J. Mater. Chem 2004, 14:739-743.
    • (2004) J. Mater. Chem , vol.14 , pp. 739-743
    • Yu, L.1    Banerjee, I.A.2    Matsui, H.3
  • 218
    • 2442512235 scopus 로고    scopus 로고
    • Size-controlled Ni nanocrystal growth on peptide nanotubes and their magnetic properties
    • Yu L., Banerjee I.A., Shima M., Rajan K., Matsui H. Size-controlled Ni nanocrystal growth on peptide nanotubes and their magnetic properties. Adv. Mater 2004, 16:709-712.
    • (2004) Adv. Mater , vol.16 , pp. 709-712
    • Yu, L.1    Banerjee, I.A.2    Shima, M.3    Rajan, K.4    Matsui, H.5
  • 219
    • 0033524453 scopus 로고    scopus 로고
    • Gene delivery: a single nuclear localization signal peptide is sufficient to carry DNA to the cell nucleus
    • Zanta M.A., Pascale B.V., Behr J.P. Gene delivery: a single nuclear localization signal peptide is sufficient to carry DNA to the cell nucleus. Proc. Natl. Acad. Sci. USA 1999, 96:91-96.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 91-96
    • Zanta, M.A.1    Pascale, B.V.2    Behr, J.P.3
  • 220
    • 0011980705 scopus 로고    scopus 로고
    • Molecular self-assembly
    • Elsevier, Oxford, K.H.J. Buschow, R.W. Cahn, M.C. Hemings, B. Ilschner, E.J. Kramer, S. Mahajan (Eds.)
    • Zhang S. Molecular self-assembly. Encyclopedia of materials: science and technology 2001, 5822-5829. Elsevier, Oxford. K.H.J. Buschow, R.W. Cahn, M.C. Hemings, B. Ilschner, E.J. Kramer, S. Mahajan (Eds.).
    • (2001) Encyclopedia of materials: science and technology , pp. 5822-5829
    • Zhang, S.1
  • 221
    • 0036890278 scopus 로고    scopus 로고
    • Emerging biological materials through molecular self-assembly
    • Zhang S. Emerging biological materials through molecular self-assembly. Biotechnol. Adv 2002, 20:321-339.
    • (2002) Biotechnol. Adv , vol.20 , pp. 321-339
    • Zhang, S.1
  • 222
    • 0141765883 scopus 로고    scopus 로고
    • Fabrication of novel biomaterials through molecular self-assembly
    • Zhang S. Fabrication of novel biomaterials through molecular self-assembly. Nature Biotech 2003, 21:1171-1178.
    • (2003) Nature Biotech , vol.21 , pp. 1171-1178
    • Zhang, S.1
  • 223
    • 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. Reactive and Functional Polymers 1999, 41:91-102.
    • (1999) Reactive and Functional Polymers , vol.41 , pp. 91-102
    • Zhang, S.1    Altman, M.2
  • 224
    • 0031034117 scopus 로고    scopus 로고
    • Direct conversion of an oligopeptide from a Β-sheet to an Α-helix: a model for amyloid formation
    • Zhang S., Rich A. Direct conversion of an oligopeptide from a Β-sheet to an Α-helix: a model for amyloid formation. Proc. Natl. Acad. Sci. USA 1997, 94:23-28.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 23-28
    • Zhang, S.1    Rich, A.2
  • 225
    • 0026758377 scopus 로고
    • Zoutin, a putative Z-DNA binding protein in Saccharomyces cerevisiae
    • Zhang S., Lockshin C., Herbert A., Winter E., Rich A. Zoutin, a putative Z-DNA binding protein in Saccharomyces cerevisiae. EMBO. J 1992, 11:3787-3796.
    • (1992) EMBO. J , vol.11 , pp. 3787-3796
    • Zhang, S.1    Lockshin, C.2    Herbert, A.3    Winter, E.4    Rich, A.5
  • 226
    • 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
  • 227
    • 0028184678 scopus 로고
    • Unusually stable Β-sheet formation in an ionic self-complementary oligopeptide
    • Zhang S., Lockshin C., Cook R., Rich A. Unusually stable Β-sheet formation in an ionic self-complementary oligopeptide. Biopolymers 1994, 34:663-672.
    • (1994) Biopolymers , vol.34 , pp. 663-672
    • Zhang, S.1    Lockshin, C.2    Cook, R.3    Rich, A.4
  • 228
    • 0029411957 scopus 로고
    • Self-complementary oligopeptide matrices support mammalian cell attachment
    • Zhang S., Holmes T., Dipersio C.M., Hynes R.O., Su X., Rich A. Self-complementary oligopeptide matrices support mammalian cell attachment. Biomaterials 1995, 16:1385-1393.
    • (1995) Biomaterials , vol.16 , pp. 1385-1393
    • Zhang, S.1    Holmes, T.2    Dipersio, C.M.3    Hynes, R.O.4    Su, X.5    Rich, A.6
  • 230
    • 0036897817 scopus 로고    scopus 로고
    • Design of nanostructured biological materials through self-assembly of peptides and proteins
    • Zhang S., Marini D.M., Hwang W., Santoso S. Design of nanostructured 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


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