메뉴 건너뛰기




Volumn 18, Issue 4, 2008, Pages 491-498

Synthetic biology through biomolecular design and engineering

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID;

EID: 49549115943     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2008.06.006     Document Type: Review
Times cited : (75)

References (75)
  • 1
    • 12044251859 scopus 로고
    • Use of hydrogen-bonds to control molecular aggregation-self-assembly of 3-dimensional networks with large chambers
    • Simard M., Su D., and Wuest J.D. Use of hydrogen-bonds to control molecular aggregation-self-assembly of 3-dimensional networks with large chambers. J Am Chem Soc 113 (1991) 4696-4698
    • (1991) J Am Chem Soc , vol.113 , pp. 4696-4698
    • Simard, M.1    Su, D.2    Wuest, J.D.3
  • 2
    • 38749117220 scopus 로고    scopus 로고
    • Peptide and protein building blocks for synthetic biology: from programming biomolecules to self-organized biomolecular systems
    • Bromley E.H.C., Channon K., Moutevelis E., and Woolfson D.N. Peptide and protein building blocks for synthetic biology: from programming biomolecules to self-organized biomolecular systems. ACS Chem Biol 3 (2008) 38-50
    • (2008) ACS Chem Biol , vol.3 , pp. 38-50
    • Bromley, E.H.C.1    Channon, K.2    Moutevelis, E.3    Woolfson, D.N.4
  • 3
    • 33845965687 scopus 로고    scopus 로고
    • Synthetic biology projects in vitro
    • Forster A.C., and Church G.M. Synthetic biology projects in vitro. Genome Res 17 (2007) 1-6
    • (2007) Genome Res , vol.17 , pp. 1-6
    • Forster, A.C.1    Church, G.M.2
  • 4
    • 11144287342 scopus 로고    scopus 로고
    • The many faces of PNA
    • Nielsen P.E. The many faces of PNA. Lett Pep Sci 10 (2003) 135-147
    • (2003) Lett Pep Sci , vol.10 , pp. 135-147
    • Nielsen, P.E.1
  • 5
    • 27744485401 scopus 로고    scopus 로고
    • Adding amino acids to the genetic repertoire
    • Xie J., and Schultz P.G. Adding amino acids to the genetic repertoire. Curr Opin Chem Biol 9 (2005) 548-554
    • (2005) Curr Opin Chem Biol , vol.9 , pp. 548-554
    • Xie, J.1    Schultz, P.G.2
  • 6
    • 0542421525 scopus 로고    scopus 로고
    • Foldamers: a manifesto
    • Gellman S. Foldamers: a manifesto. Acc Chem Res 31 (1998) 173-180
    • (1998) Acc Chem Res , vol.31 , pp. 173-180
    • Gellman, S.1
  • 7
    • 33748358358 scopus 로고    scopus 로고
    • Toward beta-amino acid proteins: a cooperatively folded beta-peptide quaternary structure
    • •] this study presents the first example of a quaternary peptide structure designed using beta amino acid basic units.
    • •] this study presents the first example of a quaternary peptide structure designed using beta amino acid basic units.
    • (2006) J Am Chem Soc , vol.128 , pp. 11338-11339
    • Qiu, J.X.1    Petersson, E.J.2    Matthews, E.E.3    Schepartz, A.4
  • 8
    • 34249003323 scopus 로고    scopus 로고
    • Discrete heterogeneous quaternary structure formed by alpha/beta-peptide foldamers and alpha-peptides
    • •] this study presents the first example of a quaternary peptide structure designed using beta amino acid basic units. In this case both alpha and beta amino acids were combined in the design.
    • •] this study presents the first example of a quaternary peptide structure designed using beta amino acid basic units. In this case both alpha and beta amino acids were combined in the design.
    • (2007) J Am Chem Soc , vol.129 , pp. 6376-6377
    • Price, J.L.1    Horne, W.S.2    Gellman, S.H.3
  • 10
    • 0034641910 scopus 로고    scopus 로고
    • Interconversion of single and double helices formed from synthetic molecular strands
    • Berl V., Huc I., Khoury R.G., Krische M.J., and Lehn J.M. Interconversion of single and double helices formed from synthetic molecular strands. Nature 407 (2000) 720-723
    • (2000) Nature , vol.407 , pp. 720-723
    • Berl, V.1    Huc, I.2    Khoury, R.G.3    Krische, M.J.4    Lehn, J.M.5
  • 12
    • 0034837153 scopus 로고    scopus 로고
    • Functionalized oligoanthranilamides: modular and conformationally controlled scaffolds
    • Hamuro Y., and Hamilton A.D. Functionalized oligoanthranilamides: modular and conformationally controlled scaffolds. Bioorg Med Chem 9 (2001) 2355-2363
    • (2001) Bioorg Med Chem , vol.9 , pp. 2355-2363
    • Hamuro, Y.1    Hamilton, A.D.2
  • 13
    • 35048842920 scopus 로고    scopus 로고
    • The herringbone helix: a noncanonical folding in aromatic-aliphatic peptides
    • Delsuc N., Godde F., Kauffmann B., Leger J.M., and Huc I. The herringbone helix: a noncanonical folding in aromatic-aliphatic peptides. J Am Chem Soc 129 (2007) 11348-11349
    • (2007) J Am Chem Soc , vol.129 , pp. 11348-11349
    • Delsuc, N.1    Godde, F.2    Kauffmann, B.3    Leger, J.M.4    Huc, I.5
  • 14
    • 36549056638 scopus 로고    scopus 로고
    • Benzoylurea oligomers: synthetic foldamers that mimic extended alpha helices
    • Rodriguez J.M., and Hamilton A.D. Benzoylurea oligomers: synthetic foldamers that mimic extended alpha helices. Angew Chem Int Ed Engl 46 (2007) 8614-8617
    • (2007) Angew Chem Int Ed Engl , vol.46 , pp. 8614-8617
    • Rodriguez, J.M.1    Hamilton, A.D.2
  • 15
    • 41649094864 scopus 로고    scopus 로고
    • Naphthyridine-based helical foldamers and macrocycles: synthesis, cation binding, and supramolecular assemblies
    • Petitjean A., Cuccia L.A., Schmutz M., and Lehn J.M. Naphthyridine-based helical foldamers and macrocycles: synthesis, cation binding, and supramolecular assemblies. J Org Chem 73 (2008) 2481-2495
    • (2008) J Org Chem , vol.73 , pp. 2481-2495
    • Petitjean, A.1    Cuccia, L.A.2    Schmutz, M.3    Lehn, J.M.4
  • 17
    • 38449100431 scopus 로고    scopus 로고
    • Reprogramming the amino-acid substrate specificity of orthogonal aminoacyl-tRNA synthetases to expand the genetic code of eukaryotic cells
    • Cropp T.A., Anderson J.C., and Chin J.W. Reprogramming the amino-acid substrate specificity of orthogonal aminoacyl-tRNA synthetases to expand the genetic code of eukaryotic cells. Nat Protoc 2 (2007) 2590-2600
    • (2007) Nat Protoc , vol.2 , pp. 2590-2600
    • Cropp, T.A.1    Anderson, J.C.2    Chin, J.W.3
  • 18
    • 33748953866 scopus 로고    scopus 로고
    • Genetic parts to program bacteria
    • An excellent and comprehensive review of genetic engineering (what we term biomolecular enegineering) approaches to synthetic biology.
    • Voigt C.A. Genetic parts to program bacteria. Curr Opin Biotechnol 17 (2006) 548-557. An excellent and comprehensive review of genetic engineering (what we term biomolecular enegineering) approaches to synthetic biology.
    • (2006) Curr Opin Biotechnol , vol.17 , pp. 548-557
    • Voigt, C.A.1
  • 19
    • 33746655784 scopus 로고    scopus 로고
    • The architectonics of programmable RNA and DNA nanostructures
    • This review introduces and summarizes a great deal of current work in the field of DNA-based nanostructure design and self-assembly. Two-dimensional and three-dimensional structures of both DNA and RNA are discussed.
    • Jaeger L., and Chworos A. The architectonics of programmable RNA and DNA nanostructures. Curr Opin Struct Biol 16 (2006) 531-543. This review introduces and summarizes a great deal of current work in the field of DNA-based nanostructure design and self-assembly. Two-dimensional and three-dimensional structures of both DNA and RNA are discussed.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 531-543
    • Jaeger, L.1    Chworos, A.2
  • 21
    • 33645028600 scopus 로고    scopus 로고
    • Folding DNA to create nanoscale shapes and patterns
    • This landmark paper demonstrates how virtually any two-dimensional shape can be designed and self-assembled from oligo-DNA strands. Additionally, surface features can be included in the design.
    • Rothemund P.W.K. Folding DNA to create nanoscale shapes and patterns. Nature 440 (2006) 297-302. This landmark paper demonstrates how virtually any two-dimensional shape can be designed and self-assembled from oligo-DNA strands. Additionally, surface features can be included in the design.
    • (2006) Nature , vol.440 , pp. 297-302
    • Rothemund, P.W.K.1
  • 23
    • 40749140401 scopus 로고    scopus 로고
    • Hierarchical self-assembly of DNA into symmetric supramolecular polyhedra
    • He Y., Ye T., Su M., Zhang C., Ribbe A.E., Jiang W., and Mao C. Hierarchical self-assembly of DNA into symmetric supramolecular polyhedra. Nature 452 (2008) 198-201
    • (2008) Nature , vol.452 , pp. 198-201
    • He, Y.1    Ye, T.2    Su, M.3    Zhang, C.4    Ribbe, A.E.5    Jiang, W.6    Mao, C.7
  • 24
    • 34547659777 scopus 로고    scopus 로고
    • An autonomous polymerization motor powered by DNA hybridization
    • In this article the authors present the first instance of a DNA-based man-made molecular motor, driven by the intrinsic kinetic instability of the system. This is a step forward from previous designs, which have relied on cycling reactants to drive the system.
    • Venkataraman S., Dirks R., Rothemund P., Winfree E., and Pierce N. An autonomous polymerization motor powered by DNA hybridization. Nat Nanotechnol 2 (2007) 490-494. In this article the authors present the first instance of a DNA-based man-made molecular motor, driven by the intrinsic kinetic instability of the system. This is a step forward from previous designs, which have relied on cycling reactants to drive the system.
    • (2007) Nat Nanotechnol , vol.2 , pp. 490-494
    • Venkataraman, S.1    Dirks, R.2    Rothemund, P.3    Winfree, E.4    Pierce, N.5
  • 25
    • 17444433002 scopus 로고    scopus 로고
    • The design of coiled-coil structures and assemblies
    • Woolfson D.N. The design of coiled-coil structures and assemblies. Adv Protein Chem 70 (2005) 79-112
    • (2005) Adv Protein Chem , vol.70 , pp. 79-112
    • Woolfson, D.N.1
  • 26
    • 0037595546 scopus 로고    scopus 로고
    • Comprehensive identification of human bZIP interactions with coiled-coil arrays
    • Newman J.R., and Keating A.E. Comprehensive identification of human bZIP interactions with coiled-coil arrays. Science 300 (2003) 2097-2101
    • (2003) Science , vol.300 , pp. 2097-2101
    • Newman, J.R.1    Keating, A.E.2
  • 27
    • 33749025290 scopus 로고    scopus 로고
    • Stability of 100 homo and heterotypic coiled-coil a-a' pairs for ten amino acids (A, L, I, V, N, K, S, T, E, and R)
    • The authors have exhaustively characterized effects on coiled coil stability of the substitution of 10 different amino acids into a & a' positions of the coiled coil heptad repeat.
    • Acharya A., Rishi V., and Vinson C. Stability of 100 homo and heterotypic coiled-coil a-a' pairs for ten amino acids (A, L, I, V, N, K, S, T, E, and R). Biochemistry 45 (2006) 11324-11332. The authors have exhaustively characterized effects on coiled coil stability of the substitution of 10 different amino acids into a & a' positions of the coiled coil heptad repeat.
    • (2006) Biochemistry , vol.45 , pp. 11324-11332
    • Acharya, A.1    Rishi, V.2    Vinson, C.3
  • 28
    • 33745164260 scopus 로고    scopus 로고
    • Semirational design of Jun-Fos coiled coils with increased affinity: universal implications for leucine zipper prediction and design
    • Mason J.M., Schmitz M.A., Müller K.M., and Arndt K.M. Semirational design of Jun-Fos coiled coils with increased affinity: universal implications for leucine zipper prediction and design. Proc Natl Acad Sci U S A 103 (2006) 8989-8994
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 8989-8994
    • Mason, J.M.1    Schmitz, M.A.2    Müller, K.M.3    Arndt, K.M.4
  • 29
    • 9444231571 scopus 로고    scopus 로고
    • Engineered and designed peptide-based fibrous biomaterials
    • MacPhee C.E., and Woolfson D.N. Engineered and designed peptide-based fibrous biomaterials. Curr Opin Solid State Mater Sci 8 (2004) 141-149
    • (2004) Curr Opin Solid State Mater Sci , vol.8 , pp. 141-149
    • MacPhee, C.E.1    Woolfson, D.N.2
  • 30
    • 33751421457 scopus 로고    scopus 로고
    • Peptide-based fibrous biomaterials: some things old, new and borrowed
    • Woolfson D.N., and Ryadnov M.G. Peptide-based fibrous biomaterials: some things old, new and borrowed. Curr Opin Chem Biol 10 (2006) 559-567
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 559-567
    • Woolfson, D.N.1    Ryadnov, M.G.2
  • 31
    • 34547421668 scopus 로고    scopus 로고
    • Engineering nanoscale order into a designed protein fiber
    • Possibly the best structural description to date for a designed self-assembled peptide-based fiber system, in this case a coiled coil assembly.
    • Papapostolou D., Smith A.M., Atkins E.D., Oliver S.J., Ryadnov M.G., Serpell L.C., and Woolfson D.N. Engineering nanoscale order into a designed protein fiber. Proc Natl Acad Sci U S A 104 (2007) 10853-10858. Possibly the best structural description to date for a designed self-assembled peptide-based fiber system, in this case a coiled coil assembly.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 10853-10858
    • Papapostolou, D.1    Smith, A.M.2    Atkins, E.D.3    Oliver, S.J.4    Ryadnov, M.G.5    Serpell, L.C.6    Woolfson, D.N.7
  • 32
    • 36749098972 scopus 로고    scopus 로고
    • d-Periodic collagen-mimetic microfibers
    • •], this paper presents the design of a peptide-based fibrous system with exquisite nanoscale ultrastructure. In this case, the design is based on the tripeptide-motif for fibrillar collagens.
    • •], this paper presents the design of a peptide-based fibrous system with exquisite nanoscale ultrastructure. In this case, the design is based on the tripeptide-motif for fibrillar collagens.
    • (2007) J Am Chem Soc , vol.129 , pp. 14780-14787
    • Rele, S.1    Song, Y.2    Apkarian, R.P.3    Qu, Z.4    Conticello, V.P.5    Chaikof, E.L.6
  • 33
    • 34250660127 scopus 로고    scopus 로고
    • Effect of ionic strength on the self-assembly, morphology and gelation of pH responsive beta-sheet tape-forming peptides
    • Carrick L.M., Aggeli A., Boden N., Fisher J., Ingham E., and Waigh T.A. Effect of ionic strength on the self-assembly, morphology and gelation of pH responsive beta-sheet tape-forming peptides. Tetrahedron 63 (2007) 7457-7467
    • (2007) Tetrahedron , vol.63 , pp. 7457-7467
    • Carrick, L.M.1    Aggeli, A.2    Boden, N.3    Fisher, J.4    Ingham, E.5    Waigh, T.A.6
  • 34
    • 38349039334 scopus 로고    scopus 로고
    • Design of a selective metal ion switch for self-assembly of peptide-based fibrils
    • Dublin S.N., and Conticello V.P. Design of a selective metal ion switch for self-assembly of peptide-based fibrils. J Am Chem Soc 130 (2008) 49-51
    • (2008) J Am Chem Soc , vol.130 , pp. 49-51
    • Dublin, S.N.1    Conticello, V.P.2
  • 35
    • 42149100461 scopus 로고    scopus 로고
    • Electrostatic control of thickness and stiffness in a designed protein fiber
    • Papapostolou D., Bromley E.H.C., Bano C., and Woolfson D.N. Electrostatic control of thickness and stiffness in a designed protein fiber. J Am Chem Soc 130 (2008) 5124-5130
    • (2008) J Am Chem Soc , vol.130 , pp. 5124-5130
    • Papapostolou, D.1    Bromley, E.H.C.2    Bano, C.3    Woolfson, D.N.4
  • 37
    • 41149104937 scopus 로고    scopus 로고
    • Designing peptide based nanomaterials
    • Ulijn R.V., and Smith A.M. Designing peptide based nanomaterials. Chem Soc Rev 37 (2008) 664-675
    • (2008) Chem Soc Rev , vol.37 , pp. 664-675
    • Ulijn, R.V.1    Smith, A.M.2
  • 38
    • 0000933784 scopus 로고
    • A consensus zinc finger peptide - design, high-affinity metal-binding, a ph-dependent structure, and a His to Cys sequence variant
    • Krizek B.A., Amann B.T., Kilfoil V.J., Merkle D.L., and Berg J.M. A consensus zinc finger peptide - design, high-affinity metal-binding, a ph-dependent structure, and a His to Cys sequence variant. J Am Chem Soc 113 (1991) 4518-4523
    • (1991) J Am Chem Soc , vol.113 , pp. 4518-4523
    • Krizek, B.A.1    Amann, B.T.2    Kilfoil, V.J.3    Merkle, D.L.4    Berg, J.M.5
  • 39
    • 33746592898 scopus 로고    scopus 로고
    • Knowledge-based potentials in protein design
    • Poole A., and Ranganathan R. Knowledge-based potentials in protein design. Curr Opin Struc Biol 16 (2006) 508-513
    • (2006) Curr Opin Struc Biol , vol.16 , pp. 508-513
    • Poole, A.1    Ranganathan, R.2
  • 40
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • Lockless S., and Ranganathan R. Evolutionarily conserved pathways of energetic connectivity in protein families. Science 286 (1999) 295-299
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.1    Ranganathan, R.2
  • 41
    • 0034721944 scopus 로고    scopus 로고
    • Analysis of covariation in an SH3 domain sequence alignment: applications in tertiary contact prediction and the design of compensating hydrophobic core substitutions
    • Larson S.M., Di Nardo A.A., and Davidson A.R. Analysis of covariation in an SH3 domain sequence alignment: applications in tertiary contact prediction and the design of compensating hydrophobic core substitutions. J Mol Biol 303 (2000) 433-446
    • (2000) J Mol Biol , vol.303 , pp. 433-446
    • Larson, S.M.1    Di Nardo, A.A.2    Davidson, A.R.3
  • 44
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: fully automated sequence selection
    • Dahiyat B.I., and Mayo S.L. De novo protein design: fully automated sequence selection. Science 278 (1997) 82-87
    • (1997) Science , vol.278 , pp. 82-87
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 46
    • 33746635140 scopus 로고    scopus 로고
    • Design of protein conformational switches
    • Ambroggio X.I., and Kuhlman B. Design of protein conformational switches. Curr Opin Struct Biol 16 (2006) 525-530
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 525-530
    • Ambroggio, X.I.1    Kuhlman, B.2
  • 47
    • 27544509859 scopus 로고    scopus 로고
    • ZiCo: a peptide designed to switch folded state upon binding zinc
    • Cerasoli E., Sharpe B.K., and Woolfson D.N. ZiCo: a peptide designed to switch folded state upon binding zinc. J Am Chem Soc 127 (2005) 15008-15009
    • (2005) J Am Chem Soc , vol.127 , pp. 15008-15009
    • Cerasoli, E.1    Sharpe, B.K.2    Woolfson, D.N.3
  • 48
    • 31944435091 scopus 로고    scopus 로고
    • Computational design of a single amino acid sequence that can switch between two distinct protein folds
    • Ambroggio X.I., and Kuhlman B. Computational design of a single amino acid sequence that can switch between two distinct protein folds. J Am Chem Soc 128 (2006) 1154-1161
    • (2006) J Am Chem Soc , vol.128 , pp. 1154-1161
    • Ambroggio, X.I.1    Kuhlman, B.2
  • 49
    • 11244335621 scopus 로고    scopus 로고
    • Sequence and structural duality: designing peptides to adopt two stable conformations
    • Pandya M.J., Cerasoli E., Joseph A., Stoneman R.G., Waite E., and Woolfson D.N. Sequence and structural duality: designing peptides to adopt two stable conformations. J Am Chem Soc 126 (2004) 17016-17024
    • (2004) J Am Chem Soc , vol.126 , pp. 17016-17024
    • Pandya, M.J.1    Cerasoli, E.2    Joseph, A.3    Stoneman, R.G.4    Waite, E.5    Woolfson, D.N.6
  • 50
    • 0037155826 scopus 로고    scopus 로고
    • A designed system for assessing how sequence affects alpha to beta conformational transitions in proteins
    • Ciani B., Hutchinson E.G., Sessions R.B., and Woolfson D.N. A designed system for assessing how sequence affects alpha to beta conformational transitions in proteins. J Biol Chem 277 (2002) 10150-10155
    • (2002) J Biol Chem , vol.277 , pp. 10150-10155
    • Ciani, B.1    Hutchinson, E.G.2    Sessions, R.B.3    Woolfson, D.N.4
  • 51
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien R.Y. The green fluorescent protein. Annu Rev Biochem 67 (1998) 509-544
    • (1998) Annu Rev Biochem , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 52
    • 33746673730 scopus 로고    scopus 로고
    • Yeast two-hybrid contributions to interactome mapping
    • Parrish J., Gulyas K., and Finley Jr. Yeast two-hybrid contributions to interactome mapping. Curr Opin Biotechnol 17 (2006) 387-393
    • (2006) Curr Opin Biotechnol , vol.17 , pp. 387-393
    • Parrish, J.1    Gulyas, K.2    Finley, Jr.3
  • 53
    • 0035956861 scopus 로고    scopus 로고
    • Nanohedra: using symmetry to design self-assembling protein cages, layers, crystals, and filaments
    • Padilla J.E., Colovos C., and Yeates T.O. Nanohedra: using symmetry to design self-assembling protein cages, layers, crystals, and filaments. Proc Natl Acad Sci U S A 98 (2001) 2217-2221
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 2217-2221
    • Padilla, J.E.1    Colovos, C.2    Yeates, T.O.3
  • 55
    • 0033549738 scopus 로고    scopus 로고
    • Self-assembly of a tetrahedral lectin into predesigned diamondlike protein crystals
    • Dotan N., Arad D., Frolow F., and Freeman A. Self-assembly of a tetrahedral lectin into predesigned diamondlike protein crystals. Angew Chem Int Ed Engl 38 (1999) 2363-2366
    • (1999) Angew Chem Int Ed Engl , vol.38 , pp. 2363-2366
    • Dotan, N.1    Arad, D.2    Frolow, F.3    Freeman, A.4
  • 56
    • 0141865703 scopus 로고    scopus 로고
    • Self-assembly of proteins into designed networks
    • Ringler P., and Schulz G. Self-assembly of proteins into designed networks. Science 302 (2003) 106-109
    • (2003) Science , vol.302 , pp. 106-109
    • Ringler, P.1    Schulz, G.2
  • 58
    • 28544451327 scopus 로고    scopus 로고
    • Foundations for engineering biology
    • Endy D. Foundations for engineering biology. Nature 438 (2005) 449-453
    • (2005) Nature , vol.438 , pp. 449-453
    • Endy, D.1
  • 60
    • 0031809503 scopus 로고    scopus 로고
    • Thermodynamic and theoretical aspects of cubic mesophases in nature and biological amphiphiles
    • Templer R.H. Thermodynamic and theoretical aspects of cubic mesophases in nature and biological amphiphiles. Curr Opin Colloid Interface Sci 3 (1998) 255-263
    • (1998) Curr Opin Colloid Interface Sci , vol.3 , pp. 255-263
    • Templer, R.H.1
  • 61
    • 23044490778 scopus 로고    scopus 로고
    • Same in the membrane: designing systems to modulate membrane proteins
    • Booth P.J. Same in the membrane: designing systems to modulate membrane proteins. Curr Opin Struct Biol 15 (2005) 435-440
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 435-440
    • Booth, P.J.1
  • 62
    • 34247531351 scopus 로고    scopus 로고
    • Diffusion of liquid domains in lipid bilayer membranes
    • Cicuta P., Keller S.L., and Veatch S.L. Diffusion of liquid domains in lipid bilayer membranes. J Phys Chem B 111 (2007) 3328-3331
    • (2007) J Phys Chem B , vol.111 , pp. 3328-3331
    • Cicuta, P.1    Keller, S.L.2    Veatch, S.L.3
  • 63
    • 28444488355 scopus 로고    scopus 로고
    • Solving the membrane protein folding problem
    • Bowie J.U. Solving the membrane protein folding problem. Nature 438 (2005) 581-589
    • (2005) Nature , vol.438 , pp. 581-589
    • Bowie, J.U.1
  • 64
    • 34447509267 scopus 로고    scopus 로고
    • Nano-enabled synthetic biology
    • Doktycz M., and Simpson M. Nano-enabled synthetic biology. Mol Sys Biol (2007) 3
    • (2007) Mol Sys Biol , pp. 3
    • Doktycz, M.1    Simpson, M.2
  • 66
    • 33747130345 scopus 로고    scopus 로고
    • Miniaturising the laboratory in emulsion droplets
    • This review is an excellent introduction into using water-in-oil emulsions for femtolitre-scale chemistry, and high-throughput techniques. Emphasis is on using these techniques for the study of in vitro directed evolution.
    • Griffiths A.D., and Tawfik D.S. Miniaturising the laboratory in emulsion droplets. Trends Biotechnol 24 (2006) 395-402. This review is an excellent introduction into using water-in-oil emulsions for femtolitre-scale chemistry, and high-throughput techniques. Emphasis is on using these techniques for the study of in vitro directed evolution.
    • (2006) Trends Biotechnol , vol.24 , pp. 395-402
    • Griffiths, A.D.1    Tawfik, D.S.2
  • 67
    • 0031854986 scopus 로고    scopus 로고
    • Man-made cell-like compartments for molecular evolution
    • Tawfik D.S., and Griffiths A.D. Man-made cell-like compartments for molecular evolution. Nat Biotechnol 16 (1998) 652-656
    • (1998) Nat Biotechnol , vol.16 , pp. 652-656
    • Tawfik, D.S.1    Griffiths, A.D.2
  • 68
    • 2942654776 scopus 로고    scopus 로고
    • A novel emulsion mixture for in vitro compartmentalization of transcription and translation in the rabbit reticulocyte system
    • Ghadessy F.J., and Holliger P. A novel emulsion mixture for in vitro compartmentalization of transcription and translation in the rabbit reticulocyte system. Protein Eng Des Sel 17 (2004) 201-204
    • (2004) Protein Eng Des Sel , vol.17 , pp. 201-204
    • Ghadessy, F.J.1    Holliger, P.2
  • 70
    • 34447512987 scopus 로고    scopus 로고
    • Functional bionetworks from nanoliter water droplets
    • A novel idea for encapsulation and study of both water-soluble and membrane-soluble components is presented. Water droplets coated in lipid monolayers are generated by adding water-to-oil-lipid mixtures. The droplets can then be fused to generate networks of droplets connected by lipid bilayers, which can house integral membrane proteins.
    • Holden M.A., Needham D., and Bayley H. Functional bionetworks from nanoliter water droplets. J Am Chem Soc 129 (2007) 8650-8655. A novel idea for encapsulation and study of both water-soluble and membrane-soluble components is presented. Water droplets coated in lipid monolayers are generated by adding water-to-oil-lipid mixtures. The droplets can then be fused to generate networks of droplets connected by lipid bilayers, which can house integral membrane proteins.
    • (2007) J Am Chem Soc , vol.129 , pp. 8650-8655
    • Holden, M.A.1    Needham, D.2    Bayley, H.3
  • 72
    • 37549070328 scopus 로고    scopus 로고
    • On the way towards 'basic autonomous agents': stochastic simulations of minimal lipid-peptide cells
    • Ruiz-Mirazo K., and Mavelli F. On the way towards 'basic autonomous agents': stochastic simulations of minimal lipid-peptide cells. Biosystems 91 (2008) 374-387
    • (2008) Biosystems , vol.91 , pp. 374-387
    • Ruiz-Mirazo, K.1    Mavelli, F.2
  • 73
    • 31044439550 scopus 로고    scopus 로고
    • Essential genes of a minimal bacterium
    • In this article the authors probe the entire genome of Mycoplasma genitalium and identify 382 genes essential for the viability of the organism.
    • Glass J., Garcia N., Alperovich N., Yooseph S., Lewis M., Maruf M., Hutchison C., Smith H., and Venter C. Essential genes of a minimal bacterium. Proc Natl Acad Sci U S A 103 (2006) 425-430. In this article the authors probe the entire genome of Mycoplasma genitalium and identify 382 genes essential for the viability of the organism.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 425-430
    • Glass, J.1    Garcia, N.2    Alperovich, N.3    Yooseph, S.4    Lewis, M.5    Maruf, M.6    Hutchison, C.7    Smith, H.8    Venter, C.9
  • 74
    • 39449112551 scopus 로고    scopus 로고
    • Complete chemical synthesis, assembly, and cloning of a Mycoplasma genitalium genome
    • •], the authors are able to demonstrate the complete chemical synthesis of the genome of an entire organism, Mycoplasma genitalium. To date, this is the largest and most complex example of the complete chemical synthesis of genomic DNA.
    • •], the authors are able to demonstrate the complete chemical synthesis of the genome of an entire organism, Mycoplasma genitalium. To date, this is the largest and most complex example of the complete chemical synthesis of genomic DNA.
    • (2008) Science , pp. 1151721
    • Gibson, D.1    Benders, G.2    Pfannkoch, C.3    Denisova, E.4    Tillson, H.5    Zaveri, J.6    Stockwell, T.7    Brownley, A.8    Thomas, D.9    Algire, M.10
  • 75
    • 35148900129 scopus 로고    scopus 로고
    • Synthetic protocell biology: from reproduction to computation
    • Here the authors present a detailed review of protocell design in synthetic biology, with a large number of references and discussions of the rational behind this approach as well as many practical and theoretical considerations.
    • Solé R.V., Munteanu A., Caso R., and Macía J. Synthetic protocell biology: from reproduction to computation. Philos Trans R Soc Lond B Biol Sci 362 (2007) 1727-1739. Here the authors present a detailed review of protocell design in synthetic biology, with a large number of references and discussions of the rational behind this approach as well as many practical and theoretical considerations.
    • (2007) Philos Trans R Soc Lond B Biol Sci , vol.362 , pp. 1727-1739
    • Solé, R.V.1    Munteanu, A.2    Caso, R.3    Macía, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.