메뉴 건너뛰기




Volumn 10, Issue 7, 2014, Pages

De Novo Design and Experimental Characterization of Ultrashort Self-Associating Peptides

Author keywords

[No Author keywords available]

Indexed keywords

ASSOCIATION REACTIONS; HYDROGELS; POTENTIAL ENERGY; SINGLE CRYSTALS; X RAY CRYSTALLOGRAPHY;

EID: 84905474731     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1003718     Document Type: Article
Times cited : (38)

References (108)
  • 1
    • 41149104937 scopus 로고    scopus 로고
    • Designing peptide based nanomaterials
    • Ulijn RV, Smith AM, (2008) Designing peptide based nanomaterials. Chem Soc Rev 37: 664-675.
    • (2008) Chem Soc Rev , vol.37 , pp. 664-675
    • Ulijn, R.V.1    Smith, A.M.2
  • 2
    • 0037192505 scopus 로고    scopus 로고
    • Self-Assembly at All Scales
    • Whitesides GM, Grzybowski B, (2002) Self-Assembly at All Scales. Science 295: 2418-2421.
    • (2002) Science , vol.295 , pp. 2418-2421
    • Whitesides, G.M.1    Grzybowski, B.2
  • 3
    • 33746377894 scopus 로고    scopus 로고
    • Protein Misfolding, Functional Amyloid, and Human Disease
    • Chiti F, Dobson CM, (2006) Protein Misfolding, Functional Amyloid, and Human Disease. Annu Rev Biochem 75: 333-366.
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 4
    • 28244484729 scopus 로고    scopus 로고
    • Structures for amyloid fibrils
    • Makin OS, Serpell LC, (2005) Structures for amyloid fibrils. FEBS J 272: 5950-5961.
    • (2005) FEBS J , vol.272 , pp. 5950-5961
    • Makin, O.S.1    Serpell, L.C.2
  • 5
    • 33750361540 scopus 로고    scopus 로고
    • A century-old debate on protein aggregation and neurodegeneration enters the clinic
    • Lansbury PT, Lashuel HA, (2006) A century-old debate on protein aggregation and neurodegeneration enters the clinic. Nature 443: 774-779.
    • (2006) Nature , vol.443 , pp. 774-779
    • Lansbury, P.T.1    Lashuel, H.A.2
  • 6
    • 45449091418 scopus 로고    scopus 로고
    • Amyloidogenesis of natively unfolded proteins
    • Uversky VN, (2008) Amyloidogenesis of natively unfolded proteins. Current Alzheimer Research 5: 260.
    • (2008) Current Alzheimer Research , vol.5 , pp. 260
    • Uversky, V.N.1
  • 7
    • 84860013075 scopus 로고    scopus 로고
    • Structure of an intermediate state in protein folding and aggregation
    • Neudecker P, Robustelli P, Cavalli A, Walsh P, Lundström P, et al. (2012) Structure of an intermediate state in protein folding and aggregation. Science 336: 362-366.
    • (2012) Science , vol.336 , pp. 362-366
    • Neudecker, P.1    Robustelli, P.2    Cavalli, A.3    Walsh, P.4    Lundström, P.5
  • 8
    • 0037144424 scopus 로고    scopus 로고
    • Amyloid Fibril Formation by Pentapeptide and Tetrapeptide Fragments of Human Calcitonin
    • Reches M, Porat Y, Gazit E, (2002) Amyloid Fibril Formation by Pentapeptide and Tetrapeptide Fragments of Human Calcitonin. J Biol Chem 277: 35475-35480.
    • (2002) J Biol Chem , vol.277 , pp. 35475-35480
    • Reches, M.1    Porat, Y.2    Gazit, E.3
  • 10
    • 34249290108 scopus 로고    scopus 로고
    • Atomic structures of amyloid cross-β spines reveal varied steric zippers
    • Sawaya MR, Sambashivan S, Nelson R, Ivanova MI, Sievers SA, et al. (2007) Atomic structures of amyloid cross-β spines reveal varied steric zippers. Nature 447: 453-457.
    • (2007) Nature , vol.447 , pp. 453-457
    • Sawaya, M.R.1    Sambashivan, S.2    Nelson, R.3    Ivanova, M.I.4    Sievers, S.A.5
  • 11
    • 79952158815 scopus 로고    scopus 로고
    • Natural tri- to hexapeptides self-assemble in water to amyloid β-type fiber aggregates by unexpected α-helical intermediate structures
    • Hauser CAE, Deng R, Mishra A, Loo Y, Khoe U, et al. (2011) Natural tri- to hexapeptides self-assemble in water to amyloid β-type fiber aggregates by unexpected α-helical intermediate structures. Proc Natl Acad Sci USA 108: 1361-1366.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 1361-1366
    • Hauser, C.A.E.1    Deng, R.2    Mishra, A.3    Loo, Y.4    Khoe, U.5
  • 12
    • 84872201218 scopus 로고    scopus 로고
    • Aliphatic peptides show similar self-assembly to amyloid core sequences, challenging the importance of aromatic interactions in amyloidosis
    • Lakshmanan A, Cheong DW, Accardo A, Di Fabrizio E, Riekel C, et al. (2013) Aliphatic peptides show similar self-assembly to amyloid core sequences, challenging the importance of aromatic interactions in amyloidosis. Proc Natl Acad Sci USA 110: 519-524.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 519-524
    • Lakshmanan, A.1    Cheong, D.W.2    Accardo, A.3    Di Fabrizio, E.4    Riekel, C.5
  • 13
    • 34247245185 scopus 로고    scopus 로고
    • Peptide self-assembly at the nanoscale: a challenging target for computational and experimental biotechnology
    • Colombo G, Soto P, Gazit E, (2007) Peptide self-assembly at the nanoscale: a challenging target for computational and experimental biotechnology. Trends Biotechnol 25: 211-218.
    • (2007) Trends Biotechnol , vol.25 , pp. 211-218
    • Colombo, G.1    Soto, P.2    Gazit, E.3
  • 14
    • 77955825528 scopus 로고    scopus 로고
    • Molecular self-assembly and applications of designer peptide amphiphiles
    • Zhao X, Pan F, Xu H, Yaseen M, Shan H, et al. (2010) Molecular self-assembly and applications of designer peptide amphiphiles. Chem Soc Rev 39: 3480-3498.
    • (2010) Chem Soc Rev , vol.39 , pp. 3480-3498
    • Zhao, X.1    Pan, F.2    Xu, H.3    Yaseen, M.4    Shan, H.5
  • 15
    • 0036890278 scopus 로고    scopus 로고
    • Emerging biological materials through molecular self-assembly
    • Zhang S, (2002) Emerging biological materials through molecular self-assembly. Biotechnol Adv 20: 321-339.
    • (2002) Biotechnol Adv , vol.20 , pp. 321-339
    • Zhang, S.1
  • 16
    • 0036897817 scopus 로고    scopus 로고
    • Design of nanostructured biological materials through self-assembly of peptides and proteins
    • Zhang S, Marini DM, Hwang W, Santoso S, (2002) Design of nanostructured biological materials through self-assembly of peptides and proteins. Curr Opin Chem Biol 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
  • 17
    • 33846678796 scopus 로고    scopus 로고
    • Designer Self-Assembling Peptide Materials
    • Zhao X, Zhang S, (2007) Designer Self-Assembling Peptide Materials. Macromol Biosci 7: 13-22.
    • (2007) Macromol Biosci , vol.7 , pp. 13-22
    • Zhao, X.1    Zhang, S.2
  • 19
    • 0141765883 scopus 로고    scopus 로고
    • Fabrication of novel biomaterials through molecular self-assembly
    • Zhang S, (2003) Fabrication of novel biomaterials through molecular self-assembly. Nat Biotech 21: 1171-1178.
    • (2003) Nat Biotech , vol.21 , pp. 1171-1178
    • Zhang, S.1
  • 21
    • 33750269500 scopus 로고    scopus 로고
    • Molecular designer self-assembling peptides
    • Zhao X, Zhang S, (2006) Molecular designer self-assembling peptides. Chem Soc Rev 35: 1105-1110.
    • (2006) Chem Soc Rev , vol.35 , pp. 1105-1110
    • Zhao, X.1    Zhang, S.2
  • 24
    • 68749100661 scopus 로고    scopus 로고
    • Self-assembly of polypeptide-based block copolymer amphiphiles
    • Carlsen A, Lecommandoux S, (2009) Self-assembly of polypeptide-based block copolymer amphiphiles. Curr Opin Colloid Interface Sci 14: 329-339.
    • (2009) Curr Opin Colloid Interface Sci , vol.14 , pp. 329-339
    • Carlsen, A.1    Lecommandoux, S.2
  • 25
    • 84858074134 scopus 로고    scopus 로고
    • Short self-assembling peptides as building blocks for modern nanodevices
    • Lakshmanan A, Zhang S, Hauser CAE, (2012) Short self-assembling peptides as building blocks for modern nanodevices. Trends Biotechnol 30: 155-165.
    • (2012) Trends Biotechnol , vol.30 , pp. 155-165
    • Lakshmanan, A.1    Zhang, S.2    Hauser, C.A.E.3
  • 26
    • 34547316314 scopus 로고    scopus 로고
    • Self-assembled peptide nanostructures: the design of molecular building blocks and their technological utilization
    • Gazit E, (2007) Self-assembled peptide nanostructures: the design of molecular building blocks and their technological utilization. Chem Soc Rev 36: 1263-1269.
    • (2007) Chem Soc Rev , vol.36 , pp. 1263-1269
    • Gazit, E.1
  • 27
    • 77949343018 scopus 로고    scopus 로고
    • Peptide-Based Methods for the Preparation of Nanostructured Inorganic Materials
    • Chen C-L, Rosi NL, (2010) Peptide-Based Methods for the Preparation of Nanostructured Inorganic Materials. Angew Chem Int Ed 49: 1924-1942.
    • (2010) Angew Chem Int Ed , vol.49 , pp. 1924-1942
    • Chen, C.-L.1    Rosi, N.L.2
  • 28
    • 78650088238 scopus 로고    scopus 로고
    • Designer Self-Assembling Peptide Materials for Diverse Applications
    • Hauser CAE, Zhang S, (2010) Designer Self-Assembling Peptide Materials for Diverse Applications. Macromol Symp 295: 30-48.
    • (2010) Macromol Symp , vol.295 , pp. 30-48
    • Hauser, C.A.E.1    Zhang, S.2
  • 29
    • 84858074803 scopus 로고    scopus 로고
    • Self-Assembly of Short Peptides for Nanotechnological Applications
    • Humana Press
    • Gazit E (2008) Self-Assembly of Short Peptides for Nanotechnological Applications. NanoBioTechnology: Humana Press. pp. 385-395.
    • (2008) NanoBioTechnology , pp. 385-395
    • Gazit, E.1
  • 30
    • 0037466613 scopus 로고    scopus 로고
    • Casting Metal Nanowires Within Discrete Self-Assembled Peptide Nanotubes
    • Reches M, Gazit E, (2003) Casting Metal Nanowires Within Discrete Self-Assembled Peptide Nanotubes. Science 300: 625-627.
    • (2003) Science , vol.300 , pp. 625-627
    • Reches, M.1    Gazit, E.2
  • 31
    • 68949088198 scopus 로고    scopus 로고
    • Self-Assembly of Phenylalanine Oligopeptides: Insights from Experiments and Simulations
    • Tamamis P, Adler-Abramovich L, Reches M, Marshall K, Sikorski P, et al. (2009) Self-Assembly of Phenylalanine Oligopeptides: Insights from Experiments and Simulations. Biophys J 96: 5020-5029.
    • (2009) Biophys J , vol.96 , pp. 5020-5029
    • Tamamis, P.1    Adler-Abramovich, L.2    Reches, M.3    Marshall, K.4    Sikorski, P.5
  • 32
    • 77952850295 scopus 로고    scopus 로고
    • Self-assembly and application of diphenylalanine-based nanostructures
    • Yan X, Zhu P, Li J, (2010) Self-assembly and application of diphenylalanine-based nanostructures. Chem Soc Rev 39: 1877-1890.
    • (2010) Chem Soc Rev , vol.39 , pp. 1877-1890
    • Yan, X.1    Zhu, P.2    Li, J.3
  • 33
    • 0037460608 scopus 로고    scopus 로고
    • Using Self-consistent Fields to Bias Monte Carlo Methods with Applications to Designing and Sampling Protein Sequences
    • Zou J, Saven JG, (2003) Using Self-consistent Fields to Bias Monte Carlo Methods with Applications to Designing and Sampling Protein Sequences. J Chem Phys 118: 3843-3854.
    • (2003) J Chem Phys , vol.118 , pp. 3843-3854
    • Zou, J.1    Saven, J.G.2
  • 34
    • 0034246020 scopus 로고    scopus 로고
    • Biased Monte Carlo optimization of protein sequences
    • Cootes AP, Curmi PMG, Torda AE, (2000) Biased Monte Carlo optimization of protein sequences. J Chem Phys 113: 2489-2496.
    • (2000) J Chem Phys , vol.113 , pp. 2489-2496
    • Cootes, A.P.1    Curmi, P.M.G.2    Torda, A.E.3
  • 35
    • 0345306764 scopus 로고    scopus 로고
    • Design of a Novel Globular Protein Fold with Atomic-Level Accuracy
    • Kuhlman B, Dantae G, Ireton GC, Verani G, Stoddard BL, et al. (2003) Design of a Novel Globular Protein Fold with Atomic-Level Accuracy. Science 302: 1364-1368.
    • (2003) Science , vol.302 , pp. 1364-1368
    • Kuhlman, B.1    Dantae, G.2    Ireton, G.C.3    Verani, G.4    Stoddard, B.L.5
  • 36
    • 0036300662 scopus 로고    scopus 로고
    • Accurate Computer-Based Design of a New Backbone Conformation in the Second Turn of Protein 1
    • Kuhlman B, O'Neill JW, Kim DE, Zhang KYJ, Baker D, (2002) Accurate Computer-Based Design of a New Backbone Conformation in the Second Turn of Protein 1. J Mol Biol 315: 471-477.
    • (2002) J Mol Biol , vol.315 , pp. 471-477
    • Kuhlman, B.1    O'Neill, J.W.2    Kim, D.E.3    Zhang, K.Y.J.4    Baker, D.5
  • 37
    • 0026179489 scopus 로고
    • A New Approach to the Rapid Determination of Protein Side Chain Conformations
    • Tuffery P, Etchebest C, Hazout S, Lavery R, (1991) A New Approach to the Rapid Determination of Protein Side Chain Conformations. J Biomol Struct Dyn 8: 1267-1289.
    • (1991) J Biomol Struct Dyn , vol.8 , pp. 1267-1289
    • Tuffery, P.1    Etchebest, C.2    Hazout, S.3    Lavery, R.4
  • 38
    • 0026589733 scopus 로고
    • The dead-end elimination theorem and its use in side-chain positioning
    • Desmet J, Maeyer MD, Hazes B, Lasters I, (1992) The dead-end elimination theorem and its use in side-chain positioning. Nature 356: 539-542.
    • (1992) Nature , vol.356 , pp. 539-542
    • Desmet, J.1    Maeyer, M.D.2    Hazes, B.3    Lasters, I.4
  • 39
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: Fully automated sequence selection
    • Dahiyat BI, Mayo SL, (1997) De novo protein design: Fully automated sequence selection. Science 278: 82-87.
    • (1997) Science , vol.278 , pp. 82-87
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 40
    • 0034682869 scopus 로고    scopus 로고
    • Automatic protein design with all atom force-fields by exact and heuristic optimization
    • Wernisch L, Hery S, Wodak SJ, (2000) Automatic protein design with all atom force-fields by exact and heuristic optimization. J Mol Biol 301: 713-736.
    • (2000) J Mol Biol , vol.301 , pp. 713-736
    • Wernisch, L.1    Hery, S.2    Wodak, S.J.3
  • 42
    • 33747882591 scopus 로고    scopus 로고
    • Improved pruning algorithms and divide-and-conquer strategies for dead-end elimination, with application to protein design
    • Georgiev I, Lilien RH, Donald BR, (2006) Improved pruning algorithms and divide-and-conquer strategies for dead-end elimination, with application to protein design. Bioinformatics 22: e174.
    • (2006) Bioinformatics , vol.22
    • Georgiev, I.1    Lilien, R.H.2    Donald, B.R.3
  • 43
    • 0028343413 scopus 로고
    • Application of a Self-Consisten Mean Field Theory to Predict Protein Side-Chains conformation and Estimate their Conformational Entropy
    • Koehl P, Delarue M, (1994) Application of a Self-Consisten Mean Field Theory to Predict Protein Side-Chains conformation and Estimate their Conformational Entropy. J Mol Biol 239: 249.
    • (1994) J Mol Biol , vol.239 , pp. 249
    • Koehl, P.1    Delarue, M.2
  • 44
    • 0028223845 scopus 로고
    • Predicting Protein Mutant Energetics by Self-Consistent Ensemble Optimization
    • Lee C, (1994) Predicting Protein Mutant Energetics by Self-Consistent Ensemble Optimization. J Mol Biol 236: 918-939.
    • (1994) J Mol Biol , vol.236 , pp. 918-939
    • Lee, C.1
  • 45
    • 0031561289 scopus 로고    scopus 로고
    • Statistical Mechanics of the Combinatorial Synthesis and Analysis of Folding Macromolecules
    • Saven JG, Wolynes PG, (1997) Statistical Mechanics of the Combinatorial Synthesis and Analysis of Folding Macromolecules. J Phys Chem B 101: 8375-8389.
    • (1997) J Phys Chem B , vol.101 , pp. 8375-8389
    • Saven, J.G.1    Wolynes, P.G.2
  • 46
    • 0034635349 scopus 로고    scopus 로고
    • Statistical Theory of Combinatorial Libraries of Folding Proteins: Energetic Discrimination of a Target Structure
    • Zou JM, Saven JG, (2000) Statistical Theory of Combinatorial Libraries of Folding Proteins: Energetic Discrimination of a Target Structure. J Mol Biol 296: 281-294.
    • (2000) J Mol Biol , vol.296 , pp. 281-294
    • Zou, J.M.1    Saven, J.G.2
  • 47
    • 0035936702 scopus 로고    scopus 로고
    • Statistical Theory of Protein Combinatorial Libraries: Packing Interactions, Backbone Flexibility, and the Sequence Variability of a Main-chain Structure
    • Kono H, Saven JG, (2001) Statistical Theory of Protein Combinatorial Libraries: Packing Interactions, Backbone Flexibility, and the Sequence Variability of a Main-chain Structure. J Mol Biol 306: 607-628.
    • (2001) J Mol Biol , vol.306 , pp. 607-628
    • Kono, H.1    Saven, J.G.2
  • 48
    • 0033042104 scopus 로고    scopus 로고
    • Improvement of side-chain modeling in proteins with the self-consistent mean field theory method based on an analysis of the factors influencing prediction
    • Mendes J, Soares CM, Carrondo MA, (1999) Improvement of side-chain modeling in proteins with the self-consistent mean field theory method based on an analysis of the factors influencing prediction. Biopolymers 50: 111-131.
    • (1999) Biopolymers , vol.50 , pp. 111-131
    • Mendes, J.1    Soares, C.M.2    Carrondo, M.A.3
  • 49
    • 0037699589 scopus 로고    scopus 로고
    • Integrated Structural, Computational and Experimental Approach for Lead Optimization: Design of Compstatin Variants with Improved Activity
    • Klepeis JL, Floudas CA, Morikis D, Tsokos CG, Argyropoulos E, et al. (2003) Integrated Structural, Computational and Experimental Approach for Lead Optimization: Design of Compstatin Variants with Improved Activity. J Am Chem Soc 125: 8422-8423.
    • (2003) J Am Chem Soc , vol.125 , pp. 8422-8423
    • Klepeis, J.L.1    Floudas, C.A.2    Morikis, D.3    Tsokos, C.G.4    Argyropoulos, E.5
  • 50
    • 3042785531 scopus 로고    scopus 로고
    • Design of Peptide Analogs with Improved Activity using a Novel de novo Protein Design Approach
    • Klepeis JL, Floudas CA, Morikis D, Tsokos CG, Lambris JD, (2004) Design of Peptide Analogs with Improved Activity using a Novel de novo Protein Design Approach. Ind Eng Chem Res 43: 3817-3826.
    • (2004) Ind Eng Chem Res , vol.43 , pp. 3817-3826
    • Klepeis, J.L.1    Floudas, C.A.2    Morikis, D.3    Tsokos, C.G.4    Lambris, J.D.5
  • 51
    • 40449101942 scopus 로고    scopus 로고
    • Computational De Novo Peptide and Protein Design: Rigid Templates versus Flexible Templates
    • Fung HK, Welsh WJ, Floudas CA, (2008) Computational De Novo Peptide and Protein Design: Rigid Templates versus Flexible Templates. Ind Eng Chem Res 47: 993-1001.
    • (2008) Ind Eng Chem Res , vol.47 , pp. 993-1001
    • Fung, H.K.1    Welsh, W.J.2    Floudas, C.A.3
  • 54
    • 84861052232 scopus 로고    scopus 로고
    • De Novo Peptide Design with C3a Receptor Agonist and Antagonist Activities: Theoretical Predictions and Experimental Validation
    • Bellows-Peterson ML, Fung HK, Floudas CA, Kieslich CA, Zhang L, et al. (2012) De Novo Peptide Design with C3a Receptor Agonist and Antagonist Activities: Theoretical Predictions and Experimental Validation. J Med Chem 55: 4159-4168.
    • (2012) J Med Chem , vol.55 , pp. 4159-4168
    • Bellows-Peterson, M.L.1    Fung, H.K.2    Floudas, C.A.3    Kieslich, C.A.4    Zhang, L.5
  • 55
    • 84896497750 scopus 로고    scopus 로고
    • De Novo Peptide Design and Experimental Validation of Histone Methyltransferase Inhibitors
    • Smadbeck J, Peterson MB, Zee BM, Garapaty S, Mago A, et al. (2014) De Novo Peptide Design and Experimental Validation of Histone Methyltransferase Inhibitors. PLoS ONE 9: e90095.
    • (2014) PLoS ONE , vol.9
    • Smadbeck, J.1    Peterson, M.B.2    Zee, B.M.3    Garapaty, S.4    Mago, A.5
  • 56
    • 84862025262 scopus 로고    scopus 로고
    • Optimization of affinity, specificity and function of designed influenza inhibitors using deep sequencing
    • Whitehead TA, Chevalier A, Song Y, Dreyfus C, Fleishman SJ, et al. (2012) Optimization of affinity, specificity and function of designed influenza inhibitors using deep sequencing. Nat Biotechnol 3: 543-548.
    • (2012) Nat Biotechnol , vol.3 , pp. 543-548
    • Whitehead, T.A.1    Chevalier, A.2    Song, Y.3    Dreyfus, C.4    Fleishman, S.J.5
  • 57
    • 70349463121 scopus 로고    scopus 로고
    • Computational design of Candida boidinii xylose reductase for altered cofactor specificity
    • Khoury GA, Fazelinia H, Chin JW, Pantazes RJ, Cirino PC, et al. (2009) Computational design of Candida boidinii xylose reductase for altered cofactor specificity. Protein Sci 18: 2125-2138.
    • (2009) Protein Sci , vol.18 , pp. 2125-2138
    • Khoury, G.A.1    Fazelinia, H.2    Chin, J.W.3    Pantazes, R.J.4    Cirino, P.C.5
  • 58
    • 77958157337 scopus 로고    scopus 로고
    • OptCDR: a general computational method for the design of antibody complementarity determining regions for targeted epitope binding
    • Pantazes RJ, Maranas CD, (2010) OptCDR: a general computational method for the design of antibody complementarity determining regions for targeted epitope binding. Protein Eng Des Sel 23: 849-858.
    • (2010) Protein Eng Des Sel , vol.23 , pp. 849-858
    • Pantazes, R.J.1    Maranas, C.D.2
  • 59
    • 78649244595 scopus 로고    scopus 로고
    • Discovery of entry inhibitors for HIV-1 via a new de novo protein design framework
    • Bellows ML, Taylor MS, Cole PA, Shen L, Siliciano RF, et al. (2010) Discovery of entry inhibitors for HIV-1 via a new de novo protein design framework. Biophys J 99: 3445-3453.
    • (2010) Biophys J , vol.99 , pp. 3445-3453
    • Bellows, M.L.1    Taylor, M.S.2    Cole, P.A.3    Shen, L.4    Siliciano, R.F.5
  • 62
    • 84892898809 scopus 로고    scopus 로고
    • Protein folding and de novo protein design for biotechnological applications
    • Khoury GA, Smadbeck J, Kieslich CA, Floudas CA, (2014) Protein folding and de novo protein design for biotechnological applications. Trends Biotechnol 32: 99-109.
    • (2014) Trends Biotechnol , vol.32 , pp. 99-109
    • Khoury, G.A.1    Smadbeck, J.2    Kieslich, C.A.3    Floudas, C.A.4
  • 63
    • 75849152422 scopus 로고    scopus 로고
    • Computational protein design: Advances in the design and redesign of biomolecular nanostructures
    • Saven JG, (2010) Computational protein design: Advances in the design and redesign of biomolecular nanostructures. Curr Opin Colloid Interface Sci 15: 13-17.
    • (2010) Curr Opin Colloid Interface Sci , vol.15 , pp. 13-17
    • Saven, J.G.1
  • 64
    • 70350334391 scopus 로고    scopus 로고
    • Computer-aided design of functional protein interactions
    • Mandell DJ, Kortemme T, (2009) Computer-aided design of functional protein interactions. Nat Chem Biol 5: 797-807.
    • (2009) Nat Chem Biol , vol.5 , pp. 797-807
    • Mandell, D.J.1    Kortemme, T.2
  • 66
    • 36448933773 scopus 로고    scopus 로고
    • A de novo designed protein-protein interface
    • Huang P-S, Love JJ, Mayo SL, (2007) A de novo designed protein-protein interface. Protein Sci 16: 2770-2774.
    • (2007) Protein Sci , vol.16 , pp. 2770-2774
    • Huang, P.-S.1    Love, J.J.2    Mayo, S.L.3
  • 67
    • 1442335007 scopus 로고    scopus 로고
    • Probabilistic approach to the design of symmetric protein quaternary structures
    • Fu X, Kono H, Saven JG, (2003) Probabilistic approach to the design of symmetric protein quaternary structures. Protein Eng 16: 971-977.
    • (2003) Protein Eng , vol.16 , pp. 971-977
    • Fu, X.1    Kono, H.2    Saven, J.G.3
  • 68
    • 84861676223 scopus 로고    scopus 로고
    • Computational Design of Self-Assembling Protein Nanomaterials with Atomic Level Accuracy
    • King NP, Sheffler W, Sawaya MR, Vollmar BS, Sumida JP, et al. (2012) Computational Design of Self-Assembling Protein Nanomaterials with Atomic Level Accuracy. Science 336: 1171-1174.
    • (2012) Science , vol.336 , pp. 1171-1174
    • King, N.P.1    Sheffler, W.2    Sawaya, M.R.3    Vollmar, B.S.4    Sumida, J.P.5
  • 69
    • 79960065022 scopus 로고    scopus 로고
    • Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation
    • Sievers SA, Karanicolas J, Chang HW, Zhao A, Jiang L, et al. (2011) Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation. Nature 475: 96-100.
    • (2011) Nature , vol.475 , pp. 96-100
    • Sievers, S.A.1    Karanicolas, J.2    Chang, H.W.3    Zhao, A.4    Jiang, L.5
  • 70
    • 38349008761 scopus 로고    scopus 로고
    • Toward Full-Sequence De Novo Protein Design with Flexible Templates for Human Beta-Defensin-2
    • Fung HK, Floudas CA, Taylor MS, Zhang L, Morikis D, (2008) Toward Full-Sequence De Novo Protein Design with Flexible Templates for Human Beta-Defensin-2. Biophys J 94: 584-599.
    • (2008) Biophys J , vol.94 , pp. 584-599
    • Fung, H.K.1    Floudas, C.A.2    Taylor, M.S.3    Zhang, L.4    Morikis, D.5
  • 71
    • 23944486752 scopus 로고    scopus 로고
    • Computational Comparison Studies of Quadratic Assignment Like Formulations for the In Silico Sequence Selection Problem in De Novo Protein Design
    • Fung HK, Rao S, Floudas CA, Prokopyev O, Pardalos PM, et al. (2005) Computational Comparison Studies of Quadratic Assignment Like Formulations for the In Silico Sequence Selection Problem in De Novo Protein Design. J Comb Optim 10: 41-60.
    • (2005) J Comb Optim , vol.10 , pp. 41-60
    • Fung, H.K.1    Rao, S.2    Floudas, C.A.3    Prokopyev, O.4    Pardalos, P.M.5
  • 72
    • 33845292929 scopus 로고    scopus 로고
    • Novel Formulations for the Sequence Selection Problem in De Novo Protein Design with Flexible Templates
    • Fung HK, Taylor MS, Floudas CA, (2007) Novel Formulations for the Sequence Selection Problem in De Novo Protein Design with Flexible Templates. Optim Method Softw 22: 51-71.
    • (2007) Optim Method Softw , vol.22 , pp. 51-71
    • Fung, H.K.1    Taylor, M.S.2    Floudas, C.A.3
  • 73
    • 23844557146 scopus 로고    scopus 로고
    • A Novel Ensemble-Based Scoring and Search Algorithm for Protein Redesign and Its Application to Modify the Substrate Specificity of the Gramicidin Synthetase A Phenylalanine Adenylation Enzyme
    • Lilien RH, Stevens BW, Anderson AC, Donald BR, (2005) A Novel Ensemble-Based Scoring and Search Algorithm for Protein Redesign and Its Application to Modify the Substrate Specificity of the Gramicidin Synthetase A Phenylalanine Adenylation Enzyme. J Comput Biol 12: 740-761.
    • (2005) J Comput Biol , vol.12 , pp. 740-761
    • Lilien, R.H.1    Stevens, B.W.2    Anderson, A.C.3    Donald, B.R.4
  • 74
    • 79958780734 scopus 로고    scopus 로고
    • Ultrasmall natural peptides self-assemble to strong temperature-resistant helical fibers in scaffolds suitable for tissue engineering
    • Mishra A, Loo Y, Deng R, Chuah YJ, Hee HT, et al. (2011) Ultrasmall natural peptides self-assemble to strong temperature-resistant helical fibers in scaffolds suitable for tissue engineering. Nano Today 6: 232-239.
    • (2011) Nano Today , vol.6 , pp. 232-239
    • Mishra, A.1    Loo, Y.2    Deng, R.3    Chuah, Y.J.4    Hee, H.T.5
  • 75
    • 80053200885 scopus 로고    scopus 로고
    • Ultrasmall Peptides Self-Assemble into Diverse Nanostructures: Morphological Evaluation and Potential Implications
    • Lakshmanan A, Hauser CAE, (2011) Ultrasmall Peptides Self-Assemble into Diverse Nanostructures: Morphological Evaluation and Potential Implications. Int J Mol Sci 12: 5736-5746.
    • (2011) Int J Mol Sci , vol.12 , pp. 5736-5746
    • Lakshmanan, A.1    Hauser, C.A.E.2
  • 76
    • 0035823520 scopus 로고    scopus 로고
    • Analysis of the Minimal Amyloid-forming Fragment of the Islet Amyloid Polypeptide: An Experimental Support for the Key Role of the Phenylalanine Residue in Amyloid Formation
    • Azriel R, Gazit E, (2001) Analysis of the Minimal Amyloid-forming Fragment of the Islet Amyloid Polypeptide: An Experimental Support for the Key Role of the Phenylalanine Residue in Amyloid Formation. J Biol Chem 276: 34156-34161.
    • (2001) J Biol Chem , vol.276 , pp. 34156-34161
    • Azriel, R.1    Gazit, E.2
  • 77
    • 84881400310 scopus 로고    scopus 로고
    • Influence of metal salts on the hydrogelation properties of ultrashort aliphatic peptides
    • Mishra A, Chan K-H, Reithofer MR, Hauser CAE, (2013) Influence of metal salts on the hydrogelation properties of ultrashort aliphatic peptides. R Soc Chem Adv 3: 9985-9993.
    • (2013) R Soc Chem Adv , vol.3 , pp. 9985-9993
    • Mishra, A.1    Chan, K.-H.2    Reithofer, M.R.3    Hauser, C.A.E.4
  • 78
    • 29944436353 scopus 로고    scopus 로고
    • Probing the importance of lateral hydrophobic association in self-assembling peptide hydrogelators
    • Rajagopal K, Ozbas B, Pochan D, Schneider J, (2006) Probing the importance of lateral hydrophobic association in self-assembling peptide hydrogelators. Eur Biophys J 35: 162-169.
    • (2006) Eur Biophys J , vol.35 , pp. 162-169
    • Rajagopal, K.1    Ozbas, B.2    Pochan, D.3    Schneider, J.4
  • 79
    • 33744932979 scopus 로고    scopus 로고
    • The structure of nanotubes formed by diphenylalanine, the core recognition motif of Alzheimer's β-amyloid polypeptide
    • Gorbitz CH, (2006) The structure of nanotubes formed by diphenylalanine, the core recognition motif of Alzheimer's β-amyloid polypeptide. Chem Commun 22: 2332-2334.
    • (2006) Chem Commun , vol.22 , pp. 2332-2334
    • Gorbitz, C.H.1
  • 80
    • 77049089028 scopus 로고    scopus 로고
    • Role of Water in Directing Diphenylalanine Assembly into Nanotubes and Nanowires
    • Kim J, Han TH, Kim Y-I, Park JS, Choi J, et al. (2010) Role of Water in Directing Diphenylalanine Assembly into Nanotubes and Nanowires. Adv Mater 22: 583-587.
    • (2010) Adv Mater , vol.22 , pp. 583-587
    • Kim, J.1    Han, T.H.2    Kim, Y.-I.3    Park, J.S.4    Choi, J.5
  • 82
    • 0001227655 scopus 로고
    • The nature of π-π interactions
    • Hunter CA, Sanders JKM, (1990) The nature of π-π interactions. J Am Chem Soc 112: 5525-5534.
    • (1990) J Am Chem Soc , vol.112 , pp. 5525-5534
    • Hunter, C.A.1    Sanders, J.K.M.2
  • 83
    • 84862202391 scopus 로고    scopus 로고
    • Rethinking the term "pi-stacking"
    • Martinez CR, Iverson BL, (2012) Rethinking the term "pi-stacking". Chem Sci 3: 2191-2201.
    • (2012) Chem Sci , vol.3 , pp. 2191-2201
    • Martinez, C.R.1    Iverson, B.L.2
  • 87
    • 77956941468 scopus 로고    scopus 로고
    • Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease
    • Apostol MI, Sawaya MR, Cascio D, Eisenberg D, (2010) Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease. J Biol Chem 285: 29671-29675.
    • (2010) J Biol Chem , vol.285 , pp. 29671-29675
    • Apostol, M.I.1    Sawaya, M.R.2    Cascio, D.3    Eisenberg, D.4
  • 88
    • 78650982368 scopus 로고    scopus 로고
    • β2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages
    • Liu C, Sawaya MR, Eisenberg D, (2011) β2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages. Nat Struct Mol Biol 18: 49-55.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 49-55
    • Liu, C.1    Sawaya, M.R.2    Eisenberg, D.3
  • 90
    • 50049095633 scopus 로고    scopus 로고
    • Atomic structure of the cross-β spine of islet amyloid polypeptide (amylin)
    • Wiltzius JJ, Sievers SA, Sawaya MR, Cascio D, Popov D, et al. (2008) Atomic structure of the cross-β spine of islet amyloid polypeptide (amylin). Protein Sci 17: 1467-1474.
    • (2008) Protein Sci , vol.17 , pp. 1467-1474
    • Wiltzius, J.J.1    Sievers, S.A.2    Sawaya, M.R.3    Cascio, D.4    Popov, D.5
  • 92
    • 0001616080 scopus 로고    scopus 로고
    • Replica-exchange molecular dynamics method for protein folding
    • Sugita Y, Okamoto Y, (1999) Replica-exchange molecular dynamics method for protein folding. Chem Phys Lett 314: 141-151.
    • (1999) Chem Phys Lett , vol.314 , pp. 141-151
    • Sugita, Y.1    Okamoto, Y.2
  • 93
    • 33750050261 scopus 로고    scopus 로고
    • A Novel High Resolution Cα-Cα Distance Dependent Force Field Based on a High Quality Decoy Set
    • Rajgaria R, McAllister SR, Floudas CA, (2006) A Novel High Resolution Cα-Cα Distance Dependent Force Field Based on a High Quality Decoy Set. Proteins 65: 726-741.
    • (2006) Proteins , vol.65 , pp. 726-741
    • Rajgaria, R.1    McAllister, S.R.2    Floudas, C.A.3
  • 94
    • 38549146473 scopus 로고    scopus 로고
    • Distance Dependent Centroid to Centroid Force Fields Using High Resolution Decoys
    • Rajgaria R, McAllister SR, Floudas CA, (2008) Distance Dependent Centroid to Centroid Force Fields Using High Resolution Decoys. Proteins 70: 950-970.
    • (2008) Proteins , vol.70 , pp. 950-970
    • Rajgaria, R.1    McAllister, S.R.2    Floudas, C.A.3
  • 95
    • 77949617607 scopus 로고    scopus 로고
    • PyRosetta: a script-based interface for implementing molecular modeling algorithms using Rosetta
    • Chaudhury S, Lyskov S, Gray JJ, (2010) PyRosetta: a script-based interface for implementing molecular modeling algorithms using Rosetta. Bioinformatics 26: 689-691.
    • (2010) Bioinformatics , vol.26 , pp. 689-691
    • Chaudhury, S.1    Lyskov, S.2    Gray, J.J.3
  • 97
    • 0141956090 scopus 로고    scopus 로고
    • Generalized born model with a simple smoothing function
    • Im W, Lee MS, Brooks CL III, (2003) Generalized born model with a simple smoothing function. J Comput Chem 24: 1691-1702.
    • (2003) J Comput Chem , vol.24 , pp. 1691-1702
    • Im, W.1    Lee, M.S.2    Brooks III, C.L.3
  • 98
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • Springer
    • Güntert P (2004) Automated NMR structure calculation with CYANA. Protein NMR Techniques: Springer. pp. 353-378.
    • (2004) Protein NMR Techniques , pp. 353-378
    • Güntert, P.1
  • 99
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert P, Mumenthaler C, Wüthrich K, (1997) Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol 273: 283-298.
    • (1997) J Mol Biol , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 101
    • 0029011701 scopus 로고
    • A 2nd Generation Force-Field For The Simulation Of Proteins, Nucleic-Acids, And Organic-Molecules
    • Cornell WD, Cieplak P, Bayly CI, Gould IR, Merz KM, et al. (1995) A 2nd Generation Force-Field For The Simulation Of Proteins, Nucleic-Acids, And Organic-Molecules. J Am Chem Soc 117: 5179-5197.
    • (1995) J Am Chem Soc , vol.117 , pp. 5179-5197
    • Cornell, W.D.1    Cieplak, P.2    Bayly, C.I.3    Gould, I.R.4    Merz, K.M.5
  • 102
    • 0004127220 scopus 로고    scopus 로고
    • Cambridge University Pres
    • Lidl R (1997) Finite fields: Cambridge University Press.
    • (1997) Finite fields
    • Lidl, R.1
  • 103
    • 33846108775 scopus 로고    scopus 로고
    • Manual Solid-Phase Peptide Synthesis of Metallocene-Peptide Bioconjugates
    • Kirin SI, Noor F, Metzler-Nolte N, Mier W, (2007) Manual Solid-Phase Peptide Synthesis of Metallocene-Peptide Bioconjugates. J Chem Educ 84: 108.
    • (2007) J Chem Educ , vol.84 , pp. 108
    • Kirin, S.I.1    Noor, F.2    Metzler-Nolte, N.3    Mier, W.4
  • 104
    • 84883711188 scopus 로고    scopus 로고
    • Tunable Mechanical Properties of Ultrasmall Peptide Hydrogels by Crosslinking and Functionalization to Achieve the 3D Distribution of Cells
    • Seow WY, Hauser CA, (2013) Tunable Mechanical Properties of Ultrasmall Peptide Hydrogels by Crosslinking and Functionalization to Achieve the 3D Distribution of Cells. Adv Healthc Mater 2: 1219-1223.
    • (2013) Adv Healthc Mater , vol.2 , pp. 1219-1223
    • Seow, W.Y.1    Hauser, C.A.2
  • 106
    • 77950793231 scopus 로고    scopus 로고
    • Experimental phasing with SHELXC/D/E: combining chain tracing with density modification
    • Sheldrick GM, (2010) Experimental phasing with SHELXC/D/E: combining chain tracing with density modification. Acta Crystallogr Sect D Biol Crystallogr 66: 479-485.
    • (2010) Acta Crystallogr Sect D Biol Crystallogr , vol.66 , pp. 479-485
    • Sheldrick, G.M.1
  • 107
    • 0030880598 scopus 로고    scopus 로고
    • SHELXL: High-resolution refinement
    • In: Charles W. Carter Jr RMS, editor. Academic Press
    • Sheldrick GM, Schneider TR (1997) SHELXL: High-resolution refinement. In: Charles W. Carter Jr RMS, editor. Methods Enzymol: Academic Press. pp. 319-343.
    • (1997) Methods Enzymol , pp. 319-343
    • Sheldrick, G.M.1    Schneider, T.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.