메뉴 건너뛰기




Volumn 48, Issue 5, 2009, Pages 929-940

Complementation and reconstitution of fluorescence from circularly permuted and truncated green fluorescent protein

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL ANALYSIS; BIOSENSOR DESIGNS; CIRCULAR PERMUTATIONS; COMPLEMENTATION; DISSOCIATION CONSTANTS; FLUORESCENCE RECOVERIES; FOLDING PATHWAYS; GREEN FLUORESCENT PROTEINS; KINETIC PROPERTIES; LEAVE ONE OUTS; NATIVE STATE; PEPTIDE LIGANDS; PEPTIDE SEQUENCES; PROOF OF CONCEPTS; RATE-LIMITING STEPS; STATE PROCESS;

EID: 61449206131     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi802027g     Document Type: Article
Times cited : (30)

References (66)
  • 1
    • 0030738524 scopus 로고    scopus 로고
    • Monitoring protein-protein interactions in intact eukaryotic cells by βc-tosidase complementation
    • Rossi, F., Charlton, C. A., and Blau, H. M. (1997) Monitoring protein-protein interactions in intact eukaryotic cells by βc-tosidase complementation. Proc. Natl. Acad. Sci. U.S.A. 94, 8405-8410.
    • (1997) Proc. Natl. Acad. Sci. U.S.A , vol.94 , pp. 8405-8410
    • Rossi, F.1    Charlton, C.A.2    Blau, H.M.3
  • 2
    • 0033545844 scopus 로고    scopus 로고
    • Clonal selection and in vivo quantitation of protein interactions with protein-fragment complementation assays
    • Remy, I., and Michnick, S. W. (1999) Clonal selection and in vivo quantitation of protein interactions with protein-fragment complementation assays. Proc. Natl. Acad. Sci. U.S.A. 96, 5394-5399.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 5394-5399
    • Remy, I.1    Michnick, S.W.2
  • 3
    • 0032510783 scopus 로고    scopus 로고
    • A bacterial two-hybrid system based on a reconstituted signal transduction pathway
    • Karimova, G., Pidoux, J., Ullmann, A., and Ladant, D. (1998) A bacterial two-hybrid system based on a reconstituted signal transduction pathway. Proc. Natl. Acad. Sci. U.S.A. 95, 5752-5756.
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 5752-5756
    • Karimova, G.1    Pidoux, J.2    Ullmann, A.3    Ladant, D.4
  • 4
    • 0034647238 scopus 로고    scopus 로고
    • Antiparallel Leucine Zipper-Directed Protein Reassembly: Application to the Green Fluorescent Protein
    • Ghosh, I., Hamilton, A. D., and Regan, L. (2000) Antiparallel Leucine Zipper-Directed Protein Reassembly: Application to the Green Fluorescent Protein. J. Am. Chem. Soc. 122, 5658-5659.
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 5658-5659
    • Ghosh, I.1    Hamilton, A.D.2    Regan, L.3
  • 5
    • 0037995710 scopus 로고    scopus 로고
    • Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis
    • Hu, C. D., and Kerppola, T. K. (2003) Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis. Nat. Biotechnol. 21, 539-545.
    • (2003) Nat. Biotechnol , vol.21 , pp. 539-545
    • Hu, C.D.1    Kerppola, T.K.2
  • 6
    • 0034329620 scopus 로고    scopus 로고
    • A fluorescent indicator for detecting protein-protein interactions in vivo based on protein splicing
    • Ozawa, T., Nogami, S., Sato, M., Ohya, Y., and Umezawa, Y. (2000) A fluorescent indicator for detecting protein-protein interactions in vivo based on protein splicing. Anal. Chem. 72, 5151-5157.
    • (2000) Anal. Chem , vol.72 , pp. 5151-5157
    • Ozawa, T.1    Nogami, S.2    Sato, M.3    Ohya, Y.4    Umezawa, Y.5
  • 7
    • 0035894271 scopus 로고    scopus 로고
    • Protein splicing-based reconstitution of split green fluorescent protein for monitoring protein-protein interactions in bacteria: Improved sensitivity and reduced screening time
    • Ozawa, T., Takeuchi, T. M., Kaihara, A., Sato, M., and Umezawa, Y. (2001) Protein splicing-based reconstitution of split green fluorescent protein for monitoring protein-protein interactions in bacteria: Improved sensitivity and reduced screening time. Anal. Chem. 73, 5866-5874.
    • (2001) Anal. Chem , vol.73 , pp. 5866-5874
    • Ozawa, T.1    Takeuchi, T.M.2    Kaihara, A.3    Sato, M.4    Umezawa, Y.5
  • 8
    • 0035478478 scopus 로고    scopus 로고
    • Detection of protein-protein interactions in vivo based on protein splicing
    • Ozawa, T., and Umezawa, Y. (2001) Detection of protein-protein interactions in vivo based on protein splicing. Curr. Opin. Chem. Biol. 5, 578-583.
    • (2001) Curr. Opin. Chem. Biol , vol.5 , pp. 578-583
    • Ozawa, T.1    Umezawa, Y.2
  • 9
    • 33847337270 scopus 로고    scopus 로고
    • Inteins for split-protein reconstitutions and their applications
    • Belfort, M, Wood, D. W, Stoddard, B. L, and Derbyshire, V, Eds, pp, Springer, Berlin
    • Ozawa, T., and Umezawa, Y. (2005) Inteins for split-protein reconstitutions and their applications. In Homing Endonucleases and Inteins (Belfort, M., Wood, D. W., Stoddard, B. L., and Derbyshire, V., Eds.) pp307 - 323, Springer, Berlin.
    • (2005) Homing Endonucleases and Inteins , pp. 307-323
    • Ozawa, T.1    Umezawa, Y.2
  • 10
    • 34548576414 scopus 로고
    • Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan
    • Shimomura, O., Johnson, F. H., and Saiga, Y. (1962) Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea. J. Cell. Comp. Physiol. 59, 223-239.
    • (1962) Aequorea. J. Cell. Comp. Physiol , vol.59 , pp. 223-239
    • Shimomura, O.1    Johnson, F.H.2    Saiga, Y.3
  • 11
    • 0019892005 scopus 로고
    • Renaturation of Aequorea gree-fluorescent protein
    • Bokman, S. H., and Ward, W. W. (1981) Renaturation of Aequorea gree-fluorescent protein. Biochem. Biophys. Res. Commun. 101, 1372-1380.
    • (1981) Biochem. Biophys. Res. Commun , vol.101 , pp. 1372-1380
    • Bokman, S.H.1    Ward, W.W.2
  • 12
    • 0020482348 scopus 로고
    • Reversible denaturation of Aequorea green-fluorescent protein: Physical separation and characterization of the renatured protein
    • Ward, W. W., and Bokman, S. H. (1982) Reversible denaturation of Aequorea green-fluorescent protein: Physical separation and characterization of the renatured protein. Biochemistry 21, 4535-4540.
    • (1982) Biochemistry , vol.21 , pp. 4535-4540
    • Ward, W.W.1    Bokman, S.H.2
  • 13
    • 0029847806 scopus 로고    scopus 로고
    • Crystal structure of the Aequorea victoria green fluorescent protein
    • Ormo, M., Cubitt, A. B., Kallio, K., Gross, L. A., Tsien, R. Y., and Remington, S. J. (1996) Crystal structure of the Aequorea victoria green fluorescent protein. Science 273, 1392-1395.
    • (1996) Science , vol.273 , pp. 1392-1395
    • Ormo, M.1    Cubitt, A.B.2    Kallio, K.3    Gross, L.A.4    Tsien, R.Y.5    Remington, S.J.6
  • 14
    • 0029780351 scopus 로고    scopus 로고
    • The molecular structure of green fluorescent protein
    • Yang, F., Moss, L. G., and Phillips, G. N., Jr. (1996) The molecular structure of green fluorescent protein. Nat. Biotechnol. 14, 1246-1251.
    • (1996) Nat. Biotechnol , vol.14 , pp. 1246-1251
    • Yang, F.1    Moss, L.G.2    Phillips Jr., G.N.3
  • 15
    • 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., and Ward, W. W. (1993) Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein. Biochemistry 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
  • 17
    • 0030843865 scopus 로고    scopus 로고
    • Crystal structure and photodynamic behavior of the blue emission variant Y66H/Y145F of green fluorescent protein
    • Wachter, R. M., King, B. A., Heim, R., Kallio, K., Tsien, R. Y., Boxer, S. G., and Remington, S. J. (1997) Crystal structure and photodynamic behavior of the blue emission variant Y66H/Y145F of green fluorescent protein. Biochemistry 36, 9759-9765.
    • (1997) Biochemistry , vol.36 , pp. 9759-9765
    • Wachter, R.M.1    King, B.A.2    Heim, R.3    Kallio, K.4    Tsien, R.Y.5    Boxer, S.G.6    Remington, S.J.7
  • 18
    • 0034604399 scopus 로고    scopus 로고
    • Crystallographic and energetic analysis of binding of selected anions to the yellow variants of green fluorescent protein
    • Wachter, R. M., Yarbrough, D., Kallio, K., and Remington, S. J. (2000) Crystallographic and energetic analysis of binding of selected anions to the yellow variants of green fluorescent protein. J. Mol. Biol. 301, 157-171.
    • (2000) J. Mol. Biol , vol.301 , pp. 157-171
    • Wachter, R.M.1    Yarbrough, D.2    Kallio, K.3    Remington, S.J.4
  • 19
    • 0033674629 scopus 로고    scopus 로고
    • The structural basis for red fluorescence in the tetrameric GFP homolog DsRed
    • Wall, M. A., Socolich, M., and Ranganathan, R. (2000) The structural basis for red fluorescence in the tetrameric GFP homolog DsRed. Nat. Struct. Biol. 7, 1133-1138.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 1133-1138
    • Wall, M.A.1    Socolich, M.2    Ranganathan, R.3
  • 20
    • 0035895225 scopus 로고    scopus 로고
    • Refined crystal structure of DsRed, a red fluorescent protein from coral, at 2.0-Å resolution
    • Yarbrough, D., Wachter, R. M., Kallio, K, Matz, M. V., and Remington, S. J. (2001) Refined crystal structure of DsRed, a red fluorescent protein from coral, at 2.0-Å resolution. Proc. Natl. Acad. Sci. U.S.A. 98, 462-467.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 462-467
    • Yarbrough, D.1    Wachter, R.M.2    Kallio, K.3    Matz, M.V.4    Remington, S.J.5
  • 21
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • Chalfie, M., Tu, Y., Euskirchen, G., Ward, W. W., and Prasher, D. C. (1994) Green fluorescent protein as a marker for gene expression. Science 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
  • 23
    • 0034423297 scopus 로고    scopus 로고
    • Observing proteins in their natural habitat: The living cell
    • Bastiaens, P. I., and Pepperkok, R. (2000) Observing proteins in their natural habitat: The living cell. Trends Biochem. Sci. 25, 631-637.
    • (2000) Trends Biochem. Sci , vol.25 , pp. 631-637
    • Bastiaens, P.I.1    Pepperkok, R.2
  • 25
    • 0031885535 scopus 로고    scopus 로고
    • Green fluorescent protein as a noninvasive intracellular pH indicator
    • Kneen, M., Farinas, J., Li, Y., and Verkman, A. S. (1998) Green fluorescent protein as a noninvasive intracellular pH indicator. Biophys. J. 74, 1591-1599.
    • (1998) Biophys. J , vol.74 , pp. 1591-1599
    • Kneen, M.1    Farinas, J.2    Li, Y.3    Verkman, A.S.4
  • 27
    • 0033613235 scopus 로고    scopus 로고
    • Circular permutation and receptor insertion within green fluorescent proteins
    • Baird, G. S., Zacharias, D. A., and Tsien, R. Y. (1999) Circular permutation and receptor insertion within green fluorescent proteins. Proc. Natl. Acad. Sci. U.S.A. 96, 11241-11246.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 11241-11246
    • Baird, G.S.1    Zacharias, D.A.2    Tsien, R.Y.3
  • 29
    • 0036019354 scopus 로고    scopus 로고
    • Rational design of green fluorescent protein mutants as biosensor for bacterial endotoxin
    • Goh, Y. Y., Frecer, V., Ho, B., and Ding, J. L. (2002) Rational design of green fluorescent protein mutants as biosensor for bacterial endotoxin. Protein Eng. 15, 493-502.
    • (2002) Protein Eng , vol.15 , pp. 493-502
    • Goh, Y.Y.1    Frecer, V.2    Ho, B.3    Ding, J.L.4
  • 30
    • 0242585457 scopus 로고    scopus 로고
    • A novel fluorescent protein-based biosensor for Gram-negative bacteria
    • Goh, Y. Y., Ho, B., and Ding, J. L. (2002) A novel fluorescent protein-based biosensor for Gram-negative bacteria. Appl. Environ. Microbiol. 68, 6343-6352.
    • (2002) Appl. Environ. Microbiol , vol.68 , pp. 6343-6352
    • Goh, Y.Y.1    Ho, B.2    Ding, J.L.3
  • 32
    • 0034601826 scopus 로고    scopus 로고
    • Folding of green fluorescent protein and the cycle3 mutant
    • Fukuda, H., Arai, M., and Kuwajima, K. (2000) Folding of green fluorescent protein and the cycle3 mutant. Biochemistry 39, 12025-12032.
    • (2000) Biochemistry , vol.39 , pp. 12025-12032
    • Fukuda, H.1    Arai, M.2    Kuwajima, K.3
  • 33
    • 0031555862 scopus 로고    scopus 로고
    • A novel mutation which enhances the fluorescence of green fluorescent protein at high temperatures
    • Kimata, Y., Iwaki, M., Lim, C. R., and Kohno, K (1997) A novel mutation which enhances the fluorescence of green fluorescent protein at high temperatures. Biochem. Biophys. Res. Commun. 232, 69-73.
    • (1997) Biochem. Biophys. Res. Commun , vol.232 , pp. 69-73
    • Kimata, Y.1    Iwaki, M.2    Lim, C.R.3    Kohno, K.4
  • 34
    • 0030452512 scopus 로고    scopus 로고
    • Mutations that suppress the thermosensitivity of green fluorescent protein
    • Siemering, K. R., Golbik, R., Sever, R., and Haseloff, J. (1996) Mutations that suppress the thermosensitivity of green fluorescent protein. Curr. Biol. 6, 1653-1663.
    • (1996) Curr. Biol , vol.6 , pp. 1653-1663
    • Siemering, K.R.1    Golbik, R.2    Sever, R.3    Haseloff, J.4
  • 35
    • 0034562065 scopus 로고    scopus 로고
    • Crystal structure and refolding properties of the mutant F99S/M153T/V163A of the green fluorescent protein
    • Battistutta, R., Negro, A., and Zanotti, G. (2000) Crystal structure and refolding properties of the mutant F99S/M153T/V163A of the green fluorescent protein. Proteins 41, 429-437.
    • (2000) Proteins , vol.41 , pp. 429-437
    • Battistutta, R.1    Negro, A.2    Zanotti, G.3
  • 36
  • 37
    • 0028110130 scopus 로고
    • DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution
    • Stemmer, W. P. (1994) DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution. Proc. Natl. Acad. Sci. U.S.A. 91, 10747-10751.
    • (1994) Proc. Natl. Acad. Sci. U.S.A , vol.91 , pp. 10747-10751
    • Stemmer, W.P.1
  • 38
    • 13244296604 scopus 로고    scopus 로고
    • Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein
    • Cabantous, S., Terwilliger, T. C., and Waldo, G. S. (2005) Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein. Nat. Biotechnol. 23, 102-107.
    • (2005) Nat. Biotechnol , vol.23 , pp. 102-107
    • Cabantous, S.1    Terwilliger, T.C.2    Waldo, G.S.3
  • 39
    • 0029859408 scopus 로고    scopus 로고
    • Random circular permutation of genes and expressed polypeptide chains: Application of the method to the catalytic chains of aspartate transcarbamoylase
    • Graf, R., and Schachman, H. K. (1996) Random circular permutation of genes and expressed polypeptide chains: Application of the method to the catalytic chains of aspartate transcarbamoylase. Proc. Natl. Acad. Sci. U.S.A. 93, 11591-11596.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 11591-11596
    • Graf, R.1    Schachman, H.K.2
  • 40
    • 0032038349 scopus 로고    scopus 로고
    • In search of circular permuted variants of Escherichia coli dihydrofolate reductase
    • Iwakura, M. (1998) In search of circular permuted variants of Escherichia coli dihydrofolate reductase. Biosci., Biotechnol., Biochem. 62, 778-781.
    • (1998) Biosci., Biotechnol., Biochem , vol.62 , pp. 778-781
    • Iwakura, M.1
  • 41
    • 64349089456 scopus 로고    scopus 로고
    • Deleted at proof
    • Deleted at proof.
  • 42
    • 64349115240 scopus 로고    scopus 로고
    • Deleted at proof
    • Deleted at proof.
  • 43
    • 64349116007 scopus 로고    scopus 로고
    • Deleted at proof
    • Deleted at proof.
  • 44
    • 0028904072 scopus 로고
    • Protein fragments as models for events in protein folding pathways: Protein engineering analysis of the association of two complementary fragments of the barley chymotrypsin inhibitor 2 (CI-2)
    • Ruiz-Sanz, J., de Prat Gay, G., Otzen, D. E., and Fersht, A. R. (1995) Protein fragments as models for events in protein folding pathways: Protein engineering analysis of the association of two complementary fragments of the barley chymotrypsin inhibitor 2 (CI-2). Biochemistry 34, 1695-1701.
    • (1995) Biochemistry , vol.34 , pp. 1695-1701
    • Ruiz-Sanz, J.1    de Prat Gay, G.2    Otzen, D.E.3    Fersht, A.R.4
  • 45
    • 0037432318 scopus 로고    scopus 로고
    • Backbone dynamics of green fluorescent protein and the effect of histidine 148 substitution
    • Seifert, M. H., Georgescu, J., Ksiazek, D., Smialowski, P., Rehm, T., Steipe, B., and Holak, T. A. (2003) Backbone dynamics of green fluorescent protein and the effect of histidine 148 substitution. Biochemistry 42, 2500-2512.
    • (2003) Biochemistry , vol.42 , pp. 2500-2512
    • Seifert, M.H.1    Georgescu, J.2    Ksiazek, D.3    Smialowski, P.4    Rehm, T.5    Steipe, B.6    Holak, T.A.7
  • 46
    • 0000839619 scopus 로고    scopus 로고
    • Internal dynamics of green fluorescent protein
    • Helms, V., Straatsma, T. P., and McCammon, J. A. (1999) Internal dynamics of green fluorescent protein. J. Phys. Chem. B 103, 3263-3269.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 3263-3269
    • Helms, V.1    Straatsma, T.P.2    McCammon, J.A.3
  • 47
    • 0035437616 scopus 로고    scopus 로고
    • Functional characterization of permuted enhanced green fluorescent proteins comprising varying linker peptides
    • Akemann, W., Raj, C. D., and Knopfel, T. (2001) Functional characterization of permuted enhanced green fluorescent proteins comprising varying linker peptides. Photochem. Photobiol. 74, 356-363.
    • (2001) Photochem. Photobiol , vol.74 , pp. 356-363
    • Akemann, W.1    Raj, C.D.2    Knopfel, T.3
  • 48
    • 0037095730 scopus 로고    scopus 로고
    • DNAWorks: An automated method for designing oligonucleotides for PCR-based gene synthesis
    • Hoover, D. M., and Lubkowski, J. (2002) DNAWorks: An automated method for designing oligonucleotides for PCR-based gene synthesis. Nucleic Acids Res. 30, e43.
    • (2002) Nucleic Acids Res , vol.30
    • Hoover, D.M.1    Lubkowski, J.2
  • 49
    • 0028784138 scopus 로고
    • Single-step assembly of a gene and entire plasmid from large numbers of oligodeoxyribonucleotides
    • Stemmer, W. P., Crameri, A., Ha, K. D., Brennan, T. M., and Heyneker, H. L. (1995) Single-step assembly of a gene and entire plasmid from large numbers of oligodeoxyribonucleotides. Gene 164, 49-53.
    • (1995) Gene , vol.164 , pp. 49-53
    • Stemmer, W.P.1    Crameri, A.2    Ha, K.D.3    Brennan, T.M.4    Heyneker, H.L.5
  • 50
    • 31344474305 scopus 로고    scopus 로고
    • Strategies for protein coexpression in Escherichia coli
    • Tolia, N. H., and Joshua-Tor, L. (2006) Strategies for protein coexpression in Escherichia coli. Nat. Methods 3, 55-64.
    • (2006) Nat. Methods , vol.3 , pp. 55-64
    • Tolia, N.H.1    Joshua-Tor, L.2
  • 51
    • 26444467667 scopus 로고    scopus 로고
    • On-column protein refolding for crystallization
    • Oganesyan, N., Kim, S. H., and Kim, R. (2005) On-column protein refolding for crystallization. J. Struct. Funct. Genomics 6, 177-182.
    • (2005) J. Struct. Funct. Genomics , vol.6 , pp. 177-182
    • Oganesyan, N.1    Kim, S.H.2    Kim, R.3
  • 52
    • 84985493765 scopus 로고
    • Spectrophotometric identity of the energy transfer chromophores in Renilla and Aequorea green-fluorescent proteins
    • Ward, W. W., Cody, C. W., Hard, R. C., and Cormier, M. J. (1980) Spectrophotometric identity of the energy transfer chromophores in Renilla and Aequorea green-fluorescent proteins. Photochem. Photobiol. 31, 611-615.
    • (1980) Photochem. Photobiol , vol.31 , pp. 611-615
    • Ward, W.W.1    Cody, C.W.2    Hard, R.C.3    Cormier, M.J.4
  • 54
    • 0029757121 scopus 로고    scopus 로고
    • Ultra-fast excited state dynamics in green fluorescent protein: Multiple states and proton transfer
    • Chattoraj, M., King, B. A., Bublitz, G. U., and Boxer, S. G. (1996) Ultra-fast excited state dynamics in green fluorescent protein: Multiple states and proton transfer. Proc. Natl. Acad. Sci. U.S.A. 93, 8362-8367.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 8362-8367
    • Chattoraj, M.1    King, B.A.2    Bublitz, G.U.3    Boxer, S.G.4
  • 55
    • 33646030643 scopus 로고    scopus 로고
    • Understanding GFP posttranslational chemistry: Structures of designed variants that achieve backbone fragmentation, hydrolysis, and decarboxylation
    • Barondeau, D. P., Kassmann, C. J., Tainer, J. A., and Getzoff, E. D. (2006) Understanding GFP posttranslational chemistry: Structures of designed variants that achieve backbone fragmentation, hydrolysis, and decarboxylation. J. Am. Chem. Soc. 128, 4685-4693.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 4685-4693
    • Barondeau, D.P.1    Kassmann, C.J.2    Tainer, J.A.3    Getzoff, E.D.4
  • 56
    • 0028129906 scopus 로고
    • Stability and peptide binding affinity of an SH3 domain from the Caenorhabditis elegans signaling protein Sem-5
    • Lim, W. A., Fox, R. O., and Richards, F. M. (1994) Stability and peptide binding affinity of an SH3 domain from the Caenorhabditis elegans signaling protein Sem-5. Protein Sci. 3, 1261-1266.
    • (1994) Protein Sci , vol.3 , pp. 1261-1266
    • Lim, W.A.1    Fox, R.O.2    Richards, F.M.3
  • 57
    • 0025323546 scopus 로고
    • High-affinity binding of an influenza hemagglutinin-derived peptide to purified HLA-DR
    • Roche, P. A., and Cresswell, P. (1990) High-affinity binding of an influenza hemagglutinin-derived peptide to purified HLA-DR. J. Immunol. 144, 1849-1856.
    • (1990) J. Immunol , vol.144 , pp. 1849-1856
    • Roche, P.A.1    Cresswell, P.2
  • 58
    • 8344290520 scopus 로고    scopus 로고
    • Acid denaturation and refolding of green fluorescent protein
    • Enoki, S., Saeki, K., Maki, K., and Kuwajima, K. (2004) Acid denaturation and refolding of green fluorescent protein. Biochemistry 43, 14238-14248.
    • (2004) Biochemistry , vol.43 , pp. 14238-14248
    • Enoki, S.1    Saeki, K.2    Maki, K.3    Kuwajima, K.4
  • 59
    • 0028333737 scopus 로고
    • Chromophore-assisted laser inactivation of proteins is mediated by the photogeneration of free radicals
    • Liao, J. C., Roider, J., and Jay, D. G (1994) Chromophore-assisted laser inactivation of proteins is mediated by the photogeneration of free radicals. Proc. Natl. Acad. Sci. U.S.A. 91, 2659-2663.
    • (1994) Proc. Natl. Acad. Sci. U.S.A , vol.91 , pp. 2659-2663
    • Liao, J.C.1    Roider, J.2    Jay, D.G.3
  • 60
    • 0036203661 scopus 로고    scopus 로고
    • Fluorophore-assisted light inactivation: A high-throughput tool for direct target validation of proteins
    • Beck, S., Sakurai, T., Eustace, B. K., Beste, G., Schier, R., Rudert, F., and Jay, D. G. (2002) Fluorophore-assisted light inactivation: A high-throughput tool for direct target validation of proteins. Proteomics 2, 247-255.
    • (2002) Proteomics , vol.2 , pp. 247-255
    • Beck, S.1    Sakurai, T.2    Eustace, B.K.3    Beste, G.4    Schier, R.5    Rudert, F.6    Jay, D.G.7
  • 61
    • 0032879690 scopus 로고    scopus 로고
    • Chromophore-assisted laser inactivation (CALI) to elucidate cellular mechanisms of cancer
    • Jay, D. G., and Sakurai, T. (1999) Chromophore-assisted laser inactivation (CALI) to elucidate cellular mechanisms of cancer. Biochim. Biophys. Acta 1424, M39-M48.
    • (1999) Biochim. Biophys. Acta , vol.1424
    • Jay, D.G.1    Sakurai, T.2
  • 62
    • 0036228954 scopus 로고    scopus 로고
    • Dissecting the link between stress fibres and focal adhesions by CALI with EGFP fusion proteins
    • Rajfur, Z., Roy, P., Otey, C., Romer, L., and Jacobson, K. (2002) Dissecting the link between stress fibres and focal adhesions by CALI with EGFP fusion proteins. Nat. Cell Biol. 4, 286-293.
    • (2002) Nat. Cell Biol , vol.4 , pp. 286-293
    • Rajfur, Z.1    Roy, P.2    Otey, C.3    Romer, L.4    Jacobson, K.5
  • 64
    • 0031006611 scopus 로고    scopus 로고
    • Chromophore formation in green fluorescent protein
    • Reid, B. G., and Flynn, G. C. (1997) Chromophore formation in green fluorescent protein. Biochemistry 36, 6786-6791.
    • (1997) Biochemistry , vol.36 , pp. 6786-6791
    • Reid, B.G.1    Flynn, G.C.2
  • 65
    • 9244234443 scopus 로고    scopus 로고
    • Exploring the energy landscape of GFP by single-molecule mechanical experiments
    • Dietz, H., and Rief, M. (2004) Exploring the energy landscape of GFP by single-molecule mechanical experiments. Proc. Natl. Acad. Sci. U.S.A. 101, 16192-16197.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 16192-16197
    • Dietz, H.1    Rief, M.2
  • 66
    • 33750612930 scopus 로고    scopus 로고
    • Jackson, S. E., Craggs, T. D., and Huang, J. R. (2006) Understanding the folding of GFP using biophysical techniques. Expert Rev. Proteomics 3, 545-559.
    • Jackson, S. E., Craggs, T. D., and Huang, J. R. (2006) Understanding the folding of GFP using biophysical techniques. Expert Rev. Proteomics 3, 545-559.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.