메뉴 건너뛰기




Volumn 423, Issue 6936, 2003, Pages 185-190

Computational design of receptor and sensor proteins with novel functions

Author keywords

[No Author keywords available]

Indexed keywords

BIOSENSORS; BIOTECHNOLOGY; COMPUTATIONAL METHODS; ENZYMES;

EID: 0038752617     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01556     Document Type: Article
Times cited : (573)

References (30)
  • 1
    • 0033874150 scopus 로고    scopus 로고
    • Unnatural ligands for engineered proteins: New tools for chemical genetics
    • Bishop, A. et al. Unnatural ligands for engineered proteins: new tools for chemical genetics. Annu. Rev. Biophys. Biomol. Struct. 29, 577-606 (2000).
    • (2000) Annu. Rev. Biophys. Biomol. Struct. , vol.29 , pp. 577-606
    • Bishop, A.1
  • 3
    • 0035807809 scopus 로고    scopus 로고
    • Enzyme-like proteins by computational design
    • Bolon, D. N. & Mayo, S. L. Enzyme-like proteins by computational design. Proc. Natl Acad. Sci. USA 98, 14274-14279 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14274-14279
    • Bolon, D.N.1    Mayo, S.L.2
  • 4
    • 0037022813 scopus 로고    scopus 로고
    • Converting a maltose receptor into a nascent binuclear oxygenase by computational design
    • Benson, D. E., Haddy, A. E. & Hellinga, M. W. Converting a maltose receptor into a nascent binuclear oxygenase by computational design. Biochemistry 41, 3262-3267 (2002).
    • (2002) Biochemistry , vol.41 , pp. 3262-3267
    • Benson, D.E.1    Haddy, A.E.2    Hellinga, M.W.3
  • 5
    • 0032054156 scopus 로고    scopus 로고
    • Protein engineering and the development of generic biosensors
    • Hellinga, H. W. & Marvin, J. S. Protein engineering and the development of generic biosensors. Trends Biotechnol. 16, 183-189 (1998).
    • (1998) Trends Biotechnol. , vol.16 , pp. 183-189
    • Hellinga, H.W.1    Marvin, J.S.2
  • 6
    • 0036838307 scopus 로고    scopus 로고
    • Design, construction and analysis of a family of fluorescent biosensors
    • de Lorimier, R. M. et al. Design, construction and analysis of a family of fluorescent biosensors. Protein Sci. 11, 2655-2673 (2002).
    • (2002) Protein Sci. , vol.11 , pp. 2655-2673
    • De Lorimier, R.M.1
  • 7
    • 0037079012 scopus 로고    scopus 로고
    • Engineered gene circuits
    • Hasty, J., McMillen, D. & Collins, J. J. Engineered gene circuits. Nature 420, 224-230 (2002).
    • (2002) Nature , vol.420 , pp. 224-230
    • Hasty, J.1    McMillen, D.2    Collins, J.J.3
  • 8
    • 0036008086 scopus 로고    scopus 로고
    • Engineering selectivity and discrimination into ligand-receptor interfaces
    • Koh, J. T. Engineering selectivity and discrimination into ligand-receptor interfaces. Chain. Biol. 9, 17-23 (2002).
    • (2002) Chain. Biol. , vol.9 , pp. 17-23
    • Koh, J.T.1
  • 9
    • 0035847272 scopus 로고    scopus 로고
    • Separation of enantiomers: Needs, challenges, perspectives
    • Maier, N. M., Franco, P. & Lindner, W. Separation of enantiomers: needs, challenges, perspectives. J. Chromatogr. A 906, 3-33 (2001).
    • (2001) J. Chromatogr. A , vol.906 , pp. 3-33
    • Maier, N.M.1    Franco, P.2    Lindner, W.3
  • 10
    • 0035843136 scopus 로고    scopus 로고
    • Combinatorial and computational challenges for biocatalyst design
    • Arnold, F. H. Combinatorial and computational challenges for biocatalyst design. Nature 409, 253-257 (2001).
    • (2001) Nature , vol.409 , pp. 253-257
    • Arnold, F.H.1
  • 12
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: Fully automated sequence selection
    • Dahiyat, B. I. & Mayo, S. L. De novo protein design: Fully automated sequence selection. Science 278, 82-87 (1997).
    • (1997) Science , vol.278 , pp. 82-87
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 13
    • 0035896029 scopus 로고    scopus 로고
    • Generalized dead-end elimination algorithms make large-scale protein side-chain structure prediction tractable: Implications for protein design and structural genomics
    • Looger, L. L. & Hellinga, H. W. Generalized dead-end elimination algorithms make large-scale protein side-chain structure prediction tractable: implications for protein design and structural genomics. J. Mol. Biol. 307, 429-445 (2001).
    • (2001) J. Mol. Biol. , vol.307 , pp. 429-445
    • Looger, L.L.1    Hellinga, H.W.2
  • 14
    • 0036315558 scopus 로고    scopus 로고
    • Computer-aided design of a PDZ domain to recognize new target sequences
    • Reina, J. et al. Computer-aided design of a PDZ domain to recognize new target sequences. Nature Struct. Biol. 9, 621-627 (2002).
    • (2002) Nature Struct. Biol. , vol.9 , pp. 621-627
    • Reina, J.1
  • 15
    • 0027256676 scopus 로고
    • Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria
    • Tam, R. & Saier, M. H. Jr. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 57, 320-346 (1993).
    • (1993) Microbiol. Rev. , vol.57 , pp. 320-346
    • Tam, R.1    Saier M.H., Jr.2
  • 16
    • 0028244277 scopus 로고
    • Crystallographic analysis of the epimeric and anomeric specificity of the periplasmic transport/chemosensory protein receptor for D-glucose and D-galactose
    • Vyas, M. N., Vyas, N. K. & Quiocho, F. A. Crystallographic analysis of the epimeric and anomeric specificity of the periplasmic transport/chemosensory protein receptor for D-glucose and D-galactose. Biochemistry 33, 4762-4768 (1994).
    • (1994) Biochemistry , vol.33 , pp. 4762-4768
    • Vyas, M.N.1    Vyas, N.K.2    Quiocho, F.A.3
  • 17
    • 0027112289 scopus 로고
    • 1.7 Å x-ray structure of the periplasmic ribose receptor from Escherichia coli
    • Mowbray, S. L. & Cole, L. B. 1.7 Å X-ray structure of the periplasmic ribose receptor from Escherichia coli. J. Mol. Biol. 225, 155-175 (1992).
    • (1992) J. Mol. Biol. , vol.225 , pp. 155-175
    • Mowbray, S.L.1    Cole, L.B.2
  • 18
    • 0021205810 scopus 로고
    • Novel stereospecificity of the L-arabinose-binding protein
    • Quiocho, F. A. & Vyas, N. K. Novel stereospecificity of the L-arabinose-binding protein. Nature 310, 381-386 (1984).
    • (1984) Nature , vol.310 , pp. 381-386
    • Quiocho, F.A.1    Vyas, N.K.2
  • 19
    • 0032562651 scopus 로고    scopus 로고
    • The structure of glutamine-binding protein complexed with glutamine at 1.94 Å resolution: Comparisons with other amino acid binding proteins
    • Sun, Y. J., Rose, J., Wang, B. C. & Hsiao, C. D. The structure of glutamine-binding protein complexed with glutamine at 1.94 Å resolution: comparisons with other amino acid binding proteins. J. Mol. Biol. 278, 219-229 (1998).
    • (1998) J. Mol. Biol. , vol.278 , pp. 219-229
    • Sun, Y.J.1    Rose, J.2    Wang, B.C.3    Hsiao, C.D.4
  • 20
    • 0028174670 scopus 로고
    • Refined 1.89 Å structure of the histidine-binding protein complexed with histidine and its relationship with many other active transport/chemosensory proteins
    • Yao, N., Trakhanov, S. & Quiocho, F. A. Refined 1.89 Å structure of the histidine-binding protein complexed with histidine and its relationship with many other active transport/chemosensory proteins. Biochemistry 33, 4769-4779 (1994).
    • (1994) Biochemistry , vol.33 , pp. 4769-4779
    • Yao, N.1    Trakhanov, S.2    Quiocho, F.A.3
  • 22
    • 0029920337 scopus 로고    scopus 로고
    • Protein design automation
    • Dahiyat, B. I. & Mayo, S. L. Protein design automation. Protein Sci. 5, 895-903 (1996).
    • (1996) Protein Sci. , vol.5 , pp. 895-903
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 24
    • 0028115617 scopus 로고
    • Transmembrane signalling by a hybrid receptor: Communication from the domain of chemoreceptor Trg that recognizes sugar-binding proteins to the kinase/phosphatase domain of osmosensor
    • Baumgartner, J. W. et al. Transmembrane signalling by a hybrid receptor: communication from the domain of chemoreceptor Trg that recognizes sugar-binding proteins to the kinase/phosphatase domain of osmosensor. EnvZ. J. Bacteriol. 176, 1157-1163 (1994).
    • (1994) EnvZ. J. Bacteriol. , vol.176 , pp. 1157-1163
    • Baumgartner, J.W.1
  • 25
    • 0034226255 scopus 로고    scopus 로고
    • Genetically engineered whole-cell sensing systems: Coupling biological recognition with reporter genes
    • Daunert, S. et al. Genetically engineered whole-cell sensing systems: coupling biological recognition with reporter genes. Chem. Rev. 100, 2705-2738 (2000).
    • (2000) Chem. Rev. , vol.100 , pp. 2705-2738
    • Daunert, S.1
  • 26
    • 0036062587 scopus 로고    scopus 로고
    • Field detection and monitoring of explosives
    • Yinon, Y. Field detection and monitoring of explosives. Trends Anal. Chem. 21, 292-301 (2002).
    • (2002) Trends Anal. Chem. , vol.21 , pp. 292-301
    • Yinon, Y.1
  • 27
    • 0036629177 scopus 로고    scopus 로고
    • Using lobster noses to inspire robot sensor design
    • Mead, K. S. Using lobster noses to inspire robot sensor design. Trends Biotechnol. 20, 276-277 (2002).
    • (2002) Trends Biotechnol. , vol.20 , pp. 276-277
    • Mead, K.S.1
  • 28
    • 0035364193 scopus 로고    scopus 로고
    • Using novel fluorescent polymers as sensory materials for above-ground sensing of chemical signature compounds emanating from buried land mines
    • Cumming, C. L. et al. Using novel fluorescent polymers as sensory materials for above-ground sensing of chemical signature compounds emanating from buried land mines. IEEE Trans. Geosci. Remote Sens. 39, 1119-1128 (2001).
    • (2001) IEEE Trans. Geosci. Remote Sens. , vol.39 , pp. 1119-1128
    • Cumming, C.L.1
  • 29
    • 0038089365 scopus 로고    scopus 로고
    • Method for detection of buried explosives using a biosensor. US patent 5,972,638 (1999)
    • Burlage, R. S., Patek, D. R. & Everman, K. R. Method for detection of buried explosives using a biosensor. US patent 5,972,638 (1999).
    • Burlage, R.S.1    Patek, D.R.2    Everman, K.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.