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Volumn 17, Issue 6, 2013, Pages 946-951

Constructing arrays of proteins

Author keywords

[No Author keywords available]

Indexed keywords

DNA; METAL; PEPTIDE; PROTEIN;

EID: 84890207552     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2013.10.004     Document Type: Review
Times cited : (19)

References (46)
  • 2
    • 84878219940 scopus 로고    scopus 로고
    • Complex archimedean tiling self-assembled from DNA nanostructures
    • Zhang F., Liu Y., Yan H. Complex archimedean tiling self-assembled from DNA nanostructures. J Am Chem Soc 2013, 135:7458-7461.
    • (2013) J Am Chem Soc , vol.135 , pp. 7458-7461
    • Zhang, F.1    Liu, Y.2    Yan, H.3
  • 6
    • 84860588472 scopus 로고    scopus 로고
    • Porous protein crystals as reaction vessels for controlling magnetic properties of nanoparticles
    • Abe S., Tsujimoto M., Yoneda K., Ohba M., Hikage T., Takano M., Kitagawa S., Ueno T. Porous protein crystals as reaction vessels for controlling magnetic properties of nanoparticles. Small 2012, 8:1314-1319.
    • (2012) Small , vol.8 , pp. 1314-1319
    • Abe, S.1    Tsujimoto, M.2    Yoneda, K.3    Ohba, M.4    Hikage, T.5    Takano, M.6    Kitagawa, S.7    Ueno, T.8
  • 8
    • 78649423017 scopus 로고    scopus 로고
    • Re-structuring protein crystals porosity for biotemplating by chemical modification of lysine residues
    • Cohen-Hadar N., Lagziel-Simis S., Wine Y., Frolow F., Freeman A. Re-structuring protein crystals porosity for biotemplating by chemical modification of lysine residues. Biotechnol Bioeng 2011, 108:1-11.
    • (2011) Biotechnol Bioeng , vol.108 , pp. 1-11
    • Cohen-Hadar, N.1    Lagziel-Simis, S.2    Wine, Y.3    Frolow, F.4    Freeman, A.5
  • 9
    • 80052577978 scopus 로고    scopus 로고
    • Generation of protein lattices by fusing proteins with matching rotational symmetry
    • Sinclair J.C., Davies K.M., Venien-Bryan C., Noble M.E. Generation of protein lattices by fusing proteins with matching rotational symmetry. Nat Nanotechnol 2011, 6:558-562.
    • (2011) Nat Nanotechnol , vol.6 , pp. 558-562
    • Sinclair, J.C.1    Davies, K.M.2    Venien-Bryan, C.3    Noble, M.E.4
  • 10
    • 0033549738 scopus 로고    scopus 로고
    • Self-assembly of a tetrahedral lectin into predesigned diamondlike protein crystals
    • Dotan N., Arad D., Frolow F., Freeman A. Self-assembly of a tetrahedral lectin into predesigned diamondlike protein crystals. Angew Chem 1999, 38:2363-2366.
    • (1999) Angew Chem , vol.38 , pp. 2363-2366
    • Dotan, N.1    Arad, D.2    Frolow, F.3    Freeman, A.4
  • 11
    • 0141865703 scopus 로고    scopus 로고
    • Self-assembly of proteins into designed networks
    • Ringler P., Schulz G.E. Self-assembly of proteins into designed networks. Science 2003, 302:106-109.
    • (2003) Science , vol.302 , pp. 106-109
    • Ringler, P.1    Schulz, G.E.2
  • 12
    • 0035956861 scopus 로고    scopus 로고
    • Nanohedra: using symmetry to design self assembling protein cages, layers, crystals, and filaments
    • Padilla J.E., Colovos C., Yeates T.O. Nanohedra: using symmetry to design self assembling protein cages, layers, crystals, and filaments. Proc Natl Acad Sci U S A 2001, 98:2217-2221.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 2217-2221
    • Padilla, J.E.1    Colovos, C.2    Yeates, T.O.3
  • 13
    • 84861652462 scopus 로고    scopus 로고
    • Structure of a 16-nm cage designed by using protein oligomers
    • Lai Y.T., Cascio D., Yeates T.O. Structure of a 16-nm cage designed by using protein oligomers. Science 2012, 336:1129.
    • (2012) Science , vol.336 , pp. 1129
    • Lai, Y.T.1    Cascio, D.2    Yeates, T.O.3
  • 14
    • 84878245260 scopus 로고    scopus 로고
    • Structure and flexibility of nanoscale protein cages designed by symmetric self-assembly
    • Lai Y.T., Tsai K.L., Sawaya M.R., Asturias F.J., Yeates T.O. Structure and flexibility of nanoscale protein cages designed by symmetric self-assembly. J Am Chem Soc 2013, 135:7738-7743.
    • (2013) J Am Chem Soc , vol.135 , pp. 7738-7743
    • Lai, Y.T.1    Tsai, K.L.2    Sawaya, M.R.3    Asturias, F.J.4    Yeates, T.O.5
  • 15
    • 84860262383 scopus 로고    scopus 로고
    • Metal-directed, chemically tunable assembly of one-, two- and three-dimensional crystalline protein arrays
    • Brodin J.D., Ambroggio X.I., Tang C., Parent K.N., Baker T.S., Tezcan F.A. Metal-directed, chemically tunable assembly of one-, two- and three-dimensional crystalline protein arrays. Nat Chem 2012, 4:375-382.
    • (2012) Nat Chem , vol.4 , pp. 375-382
    • Brodin, J.D.1    Ambroggio, X.I.2    Tang, C.3    Parent, K.N.4    Baker, T.S.5    Tezcan, F.A.6
  • 17
    • 84894942090 scopus 로고    scopus 로고
    • An accurate binding interaction model in de novo computational protein design of interactions: if you build it, they will bind
    • pii: S1047-8477(13)00083-X (Epub ahead of print)
    • London N., Ambroggio X. An accurate binding interaction model in de novo computational protein design of interactions: if you build it, they will bind. J Struct Biol 2013, pii: S1047-8477(13)00083-X (Epub ahead of print). 10.1016/j.jsb.2013.03.012.
    • (2013) J Struct Biol
    • London, N.1    Ambroggio, X.2
  • 18
    • 84879412394 scopus 로고    scopus 로고
    • Combined computational design of a zinc-binding site and a protein-protein interaction: one open zinc coordination site was not a robust hotspot for de novo ubiquitin binding
    • Der B.S., Jha R.K., Lewis S.M., Thompson P.M., Guntas G., Kuhlman B. Combined computational design of a zinc-binding site and a protein-protein interaction: one open zinc coordination site was not a robust hotspot for de novo ubiquitin binding. Proteins 2013, 81:1245-1255. 10.1002/prot.24280.
    • (2013) Proteins , vol.81 , pp. 1245-1255
    • Der, B.S.1    Jha, R.K.2    Lewis, S.M.3    Thompson, P.M.4    Guntas, G.5    Kuhlman, B.6
  • 24
    • 0032490948 scopus 로고    scopus 로고
    • Design and self-assembly of two-dimensional DNA crystals
    • Winfree E., Liu F., Wenzler L.A., Seeman N.C. Design and self-assembly of two-dimensional DNA crystals. Nature 1998, 394:539-544.
    • (1998) Nature , vol.394 , pp. 539-544
    • Winfree, E.1    Liu, F.2    Wenzler, L.A.3    Seeman, N.C.4
  • 25
    • 33645028600 scopus 로고    scopus 로고
    • Folding DNA to create nanoscale shapes and patterns
    • Rothemund P.W. Folding DNA to create nanoscale shapes and patterns. Nature 2006, 440:297-302.
    • (2006) Nature , vol.440 , pp. 297-302
    • Rothemund, P.W.1
  • 28
    • 84872225092 scopus 로고    scopus 로고
    • On the binding affinity of macromolecular interactions: daring to ask why proteins interact
    • Kastritis P.L., Bonvin A.M. On the binding affinity of macromolecular interactions: daring to ask why proteins interact. J R Soc Interface 2012, 10:0835.
    • (2012) J R Soc Interface , vol.10 , pp. 0835
    • Kastritis, P.L.1    Bonvin, A.M.2
  • 29
    • 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
  • 30
    • 0037117591 scopus 로고    scopus 로고
    • Beyond molecules: self-assembly of mesoscopic and macroscopic components
    • Whitesides G.M., Boncheva M. Beyond molecules: self-assembly of mesoscopic and macroscopic components. Proc Natl Acad Sci U S A 2002, 99:4769-4774.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 4769-4774
    • Whitesides, G.M.1    Boncheva, M.2
  • 31
    • 84881099558 scopus 로고    scopus 로고
    • Strategies to control the binding mode of de novo designed protein interactions
    • Der B.S., Kuhlman B. Strategies to control the binding mode of de novo designed protein interactions. Curr Opin Struct Biol 2013, 23:639-646.
    • (2013) Curr Opin Struct Biol , vol.23 , pp. 639-646
    • Der, B.S.1    Kuhlman, B.2
  • 34
  • 35
    • 79959764418 scopus 로고    scopus 로고
    • Templated construction of a Zn-selective protein dimerization motif
    • Salgado E.N., Brodin J.D., To M.M., Tezcan F.A. Templated construction of a Zn-selective protein dimerization motif. Inorg Chem 2011, 50:6323-6329.
    • (2011) Inorg Chem , vol.50 , pp. 6323-6329
    • Salgado, E.N.1    Brodin, J.D.2    To, M.M.3    Tezcan, F.A.4
  • 37
    • 77951146397 scopus 로고    scopus 로고
    • Self-assembly of coiled coils in synthetic biology: inspiration and progress
    • Robson Marsden H., Kros A. Self-assembly of coiled coils in synthetic biology: inspiration and progress. Angew Chem 2010, 49:2988-3005.
    • (2010) Angew Chem , vol.49 , pp. 2988-3005
    • Robson Marsden, H.1    Kros, A.2
  • 38
    • 77955836670 scopus 로고    scopus 로고
    • Coiled coils: attractive protein folding motifs for the fabrication of self-assembled, responsive and bioactive materials
    • Apostolovic B., Danial M., Klok H.A. Coiled coils: attractive protein folding motifs for the fabrication of self-assembled, responsive and bioactive materials. Chem Soc Rev 2010, 39:3541-3575.
    • (2010) Chem Soc Rev , vol.39 , pp. 3541-3575
    • Apostolovic, B.1    Danial, M.2    Klok, H.A.3
  • 39
    • 84875765522 scopus 로고    scopus 로고
    • A set of de novo designed parallel heterodimeric coiled coils with quantified dissociation constants in the micromolar to sub-nanomolar regime
    • Thomas F., Boyle A.L., Burton A.J., Woolfson D.N. A set of de novo designed parallel heterodimeric coiled coils with quantified dissociation constants in the micromolar to sub-nanomolar regime. J Am Chem Soc 2013, 135:5161-5166.
    • (2013) J Am Chem Soc , vol.135 , pp. 5161-5166
    • Thomas, F.1    Boyle, A.L.2    Burton, A.J.3    Woolfson, D.N.4
  • 40
    • 65249090233 scopus 로고    scopus 로고
    • Beneficial effect of solubility enhancers on protein crystal nucleation and growth
    • Gosavi R.A., Bhamidi V., Varanasi S., Schall C.A. Beneficial effect of solubility enhancers on protein crystal nucleation and growth. Langmuir 2009, 25:4579-4587.
    • (2009) Langmuir , vol.25 , pp. 4579-4587
    • Gosavi, R.A.1    Bhamidi, V.2    Varanasi, S.3    Schall, C.A.4
  • 41
    • 0030806177 scopus 로고    scopus 로고
    • Enhancement of protein crystal nucleation by critical density fluctuations
    • ten Wolde P.R., Frenkel D. Enhancement of protein crystal nucleation by critical density fluctuations. Science 1997, 277:1975-1978.
    • (1997) Science , vol.277 , pp. 1975-1978
    • ten Wolde, P.R.1    Frenkel, D.2
  • 42
    • 58749108308 scopus 로고    scopus 로고
    • Kinetic analysis of protein crystal nucleation in gel matrix
    • Wang L., Liu X.Y. Kinetic analysis of protein crystal nucleation in gel matrix. Biophys J 2008, 95:5931-5940.
    • (2008) Biophys J , vol.95 , pp. 5931-5940
    • Wang, L.1    Liu, X.Y.2
  • 43
    • 38749149916 scopus 로고    scopus 로고
    • Protein crystallization: from purified protein to diffraction-quality crystal
    • Chayen N.E., Saridakis E. Protein crystallization: from purified protein to diffraction-quality crystal. Nat Methods 2008, 5:147-153.
    • (2008) Nat Methods , vol.5 , pp. 147-153
    • Chayen, N.E.1    Saridakis, E.2
  • 45
    • 33747035087 scopus 로고    scopus 로고
    • Metal ion-mediated reduction in surface entropy improves diffraction quality of crystals of the IRAK-4 death domain
    • Lasker M.V., Kuruvilla S.M., Gajjar M.M., Kapoor A., Nair S.K. Metal ion-mediated reduction in surface entropy improves diffraction quality of crystals of the IRAK-4 death domain. J Biomol Tech 2006, 17:114-121.
    • (2006) J Biomol Tech , vol.17 , pp. 114-121
    • Lasker, M.V.1    Kuruvilla, S.M.2    Gajjar, M.M.3    Kapoor, A.4    Nair, S.K.5
  • 46
    • 77953984062 scopus 로고    scopus 로고
    • New surface contacts formed upon reductive lysine methylation: improving the probability of protein crystallization
    • Sledz P., Zheng H., Murzyn K., Chruszcz M., Zimmerman M.D., Chordia M.D., Joachimiak A., Minor W. New surface contacts formed upon reductive lysine methylation: improving the probability of protein crystallization. Protein Sci 2010, 19:1395-1404.
    • (2010) Protein Sci , vol.19 , pp. 1395-1404
    • Sledz, P.1    Zheng, H.2    Murzyn, K.3    Chruszcz, M.4    Zimmerman, M.D.5    Chordia, M.D.6    Joachimiak, A.7    Minor, W.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.