메뉴 건너뛰기




Volumn 419, Issue 4, 2012, Pages 676-681

Screening of a highly soluble and oxygen-independent blue fluorescent protein from metagenome

Author keywords

Blue fluorescent protein; Cell imaging; NADPH; Reporter

Indexed keywords

BLUE FLUORESCENT PROTEIN; GENOMIC DNA; METAGENOMIC DNA; OXYGEN; PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

EID: 84858751576     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.02.075     Document Type: Article
Times cited : (17)

References (17)
  • 1
    • 33749005086 scopus 로고    scopus 로고
    • In vivo and in vitro protein solubility assays using split GFP
    • Cabantous S., Waldo G.S. In vivo and in vitro protein solubility assays using split GFP. Nat. Methods 2006, 3:845-854.
    • (2006) Nat. Methods , vol.3 , pp. 845-854
    • Cabantous, S.1    Waldo, G.S.2
  • 2
    • 0141706507 scopus 로고    scopus 로고
    • Biotechnological applications of green fluorescent protein
    • March J.C., Rao G., Bentley W.E. Biotechnological applications of green fluorescent protein. Appl. Microbiol. Biotechnol. 2003, 62:303-315.
    • (2003) Appl. Microbiol. Biotechnol. , vol.62 , pp. 303-315
    • March, J.C.1    Rao, G.2    Bentley, W.E.3
  • 3
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • Chalfie M., Tu Y., Euskirchen G., Ward W.W., Prasher D.C. Green fluorescent protein as a marker for gene expression. Science 1994, 263:802-805.
    • (1994) Science , vol.263 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 4
    • 0027465627 scopus 로고
    • Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein
    • Cody C.W., Prasher D.C., Westler W.M., Prendergast F.G., Ward W.W. Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein. Biochemistry 1993, 32:1212-1218.
    • (1993) Biochemistry , vol.32 , pp. 1212-1218
    • Cody, C.W.1    Prasher, D.C.2    Westler, W.M.3    Prendergast, F.G.4    Ward, W.W.5
  • 6
    • 57849124147 scopus 로고    scopus 로고
    • Screening of promoters from metagenomic DNA and their use for the construction of expression vectors
    • Han S.S., Lee J.Y., Kim W.H., Shin H.J., Kim G.J. Screening of promoters from metagenomic DNA and their use for the construction of expression vectors. J. Microbiol. Biotechnol. 2008, 18:1634-1640.
    • (2008) J. Microbiol. Biotechnol. , vol.18 , pp. 1634-1640
    • Han, S.S.1    Lee, J.Y.2    Kim, W.H.3    Shin, H.J.4    Kim, G.J.5
  • 7
    • 19144369096 scopus 로고    scopus 로고
    • Substrate-induced gene-expression screening of environmental metagenome libraries for isolation of catabolic genes
    • Uchiyama T., Abe T., Ikemura T., Watanabe K. Substrate-induced gene-expression screening of environmental metagenome libraries for isolation of catabolic genes. Nat. Biotechnol. 2005, 23:88-93.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 88-93
    • Uchiyama, T.1    Abe, T.2    Ikemura, T.3    Watanabe, K.4
  • 9
    • 1442359485 scopus 로고    scopus 로고
    • Functional tuning of a salvaged green fluorescent protein variant with a new sequence space by directed evolution
    • Nam S.H., Oh K.H., Kim G.J., Kim H.S. Functional tuning of a salvaged green fluorescent protein variant with a new sequence space by directed evolution. Protein Eng. 2003, 16:1099-1105.
    • (2003) Protein Eng. , vol.16 , pp. 1099-1105
    • Nam, S.H.1    Oh, K.H.2    Kim, G.J.3    Kim, H.S.4
  • 10
    • 70449575862 scopus 로고    scopus 로고
    • Metabolic engineering of Clostridium acetobutylicum M5 for highly selective butanol production
    • Lee J.Y., Jang Y.S., Lee J., Papoutsakis E.T., Lee S.Y. Metabolic engineering of Clostridium acetobutylicum M5 for highly selective butanol production. Biotechnol. J. 2009, 4:1432-1440.
    • (2009) Biotechnol. J. , vol.4 , pp. 1432-1440
    • Lee, J.Y.1    Jang, Y.S.2    Lee, J.3    Papoutsakis, E.T.4    Lee, S.Y.5
  • 11
    • 58149133711 scopus 로고    scopus 로고
    • The SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes
    • Kavanagh K., Jornvall H., Persson B., Oppermann U. The SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes. Cell. Mol. Life Sci. 2008, 65:3895-3906.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 3895-3906
    • Kavanagh, K.1    Jornvall, H.2    Persson, B.3    Oppermann, U.4
  • 12
    • 0039699818 scopus 로고    scopus 로고
    • SDR and MDR: completed genome sequences show these protein families to be large, of old origin, and of complex nature
    • Jornvall H., Hoog J.O., Persson B. SDR and MDR: completed genome sequences show these protein families to be large, of old origin, and of complex nature. FEBS Lett. 1999, 445:261-264.
    • (1999) FEBS Lett. , vol.445 , pp. 261-264
    • Jornvall, H.1    Hoog, J.O.2    Persson, B.3
  • 13
    • 4143080269 scopus 로고    scopus 로고
    • Fluorescent intensity of a novel NADPH-binding protein of Vibrio vulnificus can be improved by directed evolution
    • Chang C.C., Chuang Y.C., Chang M.C. Fluorescent intensity of a novel NADPH-binding protein of Vibrio vulnificus can be improved by directed evolution. Biochem. Biophys. Res. Commun. 2004, 322:303-309.
    • (2004) Biochem. Biophys. Res. Commun. , vol.322 , pp. 303-309
    • Chang, C.C.1    Chuang, Y.C.2    Chang, M.C.3
  • 15
    • 79955648856 scopus 로고    scopus 로고
    • Structure of a NADPH-dependent blue fluorescent protein revealed the unique role of Gly176 on the fluorescence enhancement
    • Kao T.H., Chen Y., Pai C.H., Chang M.C., Wang A.H. Structure of a NADPH-dependent blue fluorescent protein revealed the unique role of Gly176 on the fluorescence enhancement. J. Struct. Biol. 2011, 174:485-493.
    • (2011) J. Struct. Biol. , vol.174 , pp. 485-493
    • Kao, T.H.1    Chen, Y.2    Pai, C.H.3    Chang, M.C.4    Wang, A.H.5
  • 16
    • 72949124850 scopus 로고    scopus 로고
    • Generation of a fast maturating red fluorescent protein by a combined approach of elongation mutagenesis and functional salvage screening
    • Choi E.S., Han S.S., Cheong D.E., Park M.Y., Kim J.S., Kim G.J. Generation of a fast maturating red fluorescent protein by a combined approach of elongation mutagenesis and functional salvage screening. Biochem. Biophys. Res. Commun. 2010, 391:598-603.
    • (2010) Biochem. Biophys. Res. Commun. , vol.391 , pp. 598-603
    • Choi, E.S.1    Han, S.S.2    Cheong, D.E.3    Park, M.Y.4    Kim, J.S.5    Kim, G.J.6
  • 17
    • 34247892395 scopus 로고    scopus 로고
    • A short-chain dehydrogenase/reductase from Vibrio vulnificus with both blue fluorescence and oxidoreductase activity
    • Polizzi K.M., Moore D.A., Bommarius A.S. A short-chain dehydrogenase/reductase from Vibrio vulnificus with both blue fluorescence and oxidoreductase activity. Chem. Commun. 2007, 1843-1845.
    • (2007) Chem. Commun. , pp. 1843-1845
    • Polizzi, K.M.1    Moore, D.A.2    Bommarius, A.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.