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Volumn 4, Issue , 2005, Pages

Monitoring protein stability in vivo

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN;

EID: 26844451326     PISSN: 14752859     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/1475-2859-4-23     Document Type: Review
Times cited : (17)

References (26)
  • 1
    • 0037140742 scopus 로고    scopus 로고
    • New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: Synthesis and biological applications
    • Adams SR, Campbell RE, Gross LA, Martin BR, Walkup GK, Yao Y, Llopis J, Tsien RY: New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications. J Am Chem Soc 2002, 124:6063-6076.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 6063-6076
    • Adams, S.R.1    Campbell, R.E.2    Gross, L.A.3    Martin, B.R.4    Walkup, G.K.5    Yao, Y.6    Llopis, J.7    Tsien, R.Y.8
  • 2
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson CM: Protein misfolding, evolution and disease. Trends Biochem Sci 1999, 24:329-32.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 5
    • 0034814860 scopus 로고    scopus 로고
    • Quantitative protein stability measurement in vivo
    • Ghaemmaghami S, Oas TG: Quantitative protein stability measurement in vivo. Nat Struct Biol 2001, 8:879-882.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 879-882
    • Ghaemmaghami, S.1    Oas, T.G.2
  • 6
    • 0028921834 scopus 로고
    • Improved green fluorescence
    • Heim R, Cubitt AB, Tsien RY: Improved green fluorescence. Nature 1995, 373:663-664.
    • (1995) Nature , vol.373 , pp. 663-664
    • Heim, R.1    Cubitt, A.B.2    Tsien, R.Y.3
  • 7
    • 0034581376 scopus 로고    scopus 로고
    • Fluorescent labeling of recombinant proteins in living cells with FlAsH
    • Griffin BA, Adams SR, Jones J, Tsien RY: Fluorescent labeling of recombinant proteins in living cells with FlAsH. Methods Enzymol 2000, 327:565-578.
    • (2000) Methods Enzymol. , vol.327 , pp. 565-578
    • Griffin, B.A.1    Adams, S.R.2    Jones, J.3    Tsien, R.Y.4
  • 8
    • 0347004717 scopus 로고    scopus 로고
    • Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling
    • Ignatova Z, Gierasch LM: Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling. Proc Natl Acad Sci U S A 2004, 101:523-528.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 523-528
    • Ignatova, Z.1    Gierasch, L.M.2
  • 9
    • 0028080090 scopus 로고
    • Split ubiquitin as a sensor of protein interactions in vivo
    • Johnsson N, Varshavsky A: Split ubiquitin as a sensor of protein interactions in vivo. Proc Natl Acad Sci U S A 1994, 91:10340-10344.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 10340-10344
    • Johnsson, N.1    Varshavsky, A.2
  • 10
    • 0035743872 scopus 로고    scopus 로고
    • In vivo detection of the cyclic osmoregulated periplasmic glucan of Ralstonia solanacearum by high-resolution magic angle spinning NMR
    • Wieruszeski JM, Bohin A, Bohin JP, Lippens G: In vivo detection of the cyclic osmoregulated periplasmic glucan of Ralstonia solanacearum by high-resolution magic angle spinning NMR. J Magn Reson 2001, 151:118-123.
    • (2001) J. Magn. Reson. , vol.151 , pp. 118-123
    • Wieruszeski, J.M.1    Bohin, A.2    Bohin, J.P.3    Lippens, G.4
  • 12
    • 1442264894 scopus 로고    scopus 로고
    • A new protein conformation indicator based on biarsenical fluorescein with an extended benzoic acid moiety
    • Nakanishi J, Maeda M, Umezawa Y: A new protein conformation indicator based on biarsenical fluorescein with an extended benzoic acid moiety. Anal Sci 2004, 20:273-278.
    • (2004) Anal. Sci. , vol.20 , pp. 273-278
    • Nakanishi, J.1    Maeda, M.2    Umezawa, Y.3
  • 13
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • Pervushin K, Riek R, Wider G, Wuthrich K: Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc Natl Acad Sci U S A 1997, 94:2366-12371.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 2366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wuthrich, K.4
  • 14
    • 0037436408 scopus 로고    scopus 로고
    • FRET-based in vivo screening for protein folding and increased protein stability
    • Philipps B, Hennecke J, Glockshuber R: FRET-based in vivo screening for protein folding and increased protein stability. J Mol Biol 2003, 327:239-49.
    • (2003) J. Mol. Biol. , vol.327 , pp. 239-249
    • Philipps, B.1    Hennecke, J.2    Glockshuber, R.3
  • 15
    • 0035951310 scopus 로고    scopus 로고
    • Detection of altered protein conformations in living cells
    • Raquet X, Eckert JH, Muller S, Johnsson N: Detection of altered protein conformations in living cells. J Mol Biol 2001, 305:927-938.
    • (2001) J. Mol. Biol. , vol.305 , pp. 927-938
    • Raquet, X.1    Eckert, J.H.2    Muller, S.3    Johnsson, N.4
  • 16
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross CA, Poirier MA: Protein aggregation and neurodegenerative disease. Nat Med 2004, 10:S10-S17.
    • (2004) Nat. Med. , vol.10
    • Ross, C.A.1    Poirier, M.A.2
  • 17
    • 0035807847 scopus 로고    scopus 로고
    • In-cell NMR spectroscopy
    • Serber Z, Dötsch V: In-cell NMR spectroscopy. Biochemistry 2001, 40:14317-14323.
    • (2001) Biochemistry , vol.40 , pp. 14317-14323
    • Serber, Z.1    Dötsch, V.2
  • 19
    • 0035913735 scopus 로고    scopus 로고
    • Evaluation of parameters critical to observing proteins inside living Escherichia coli cells by in-cell NMR spectroscopy
    • Serber Z, Ledwidge R, Miller SM, Dötsch V: Evaluation of parameters critical to observing proteins inside living Escherichia coli cells by in-cell NMR spectroscopy. J Am Chem Soc 2001, 123:8895-8901.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 8895-8901
    • Serber, Z.1    Ledwidge, R.2    Miller, S.M.3    Dötsch, V.4
  • 20
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien RY: The green fluorescent protein. Annu Rev Biochem 1998, 67:509-544.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 22
    • 0035743872 scopus 로고    scopus 로고
    • In vivo detection of the cyclic osmoregulated periplasmic glucan of Ralstonia solanacearum by high-resolution magic angle spinning NMR
    • Wieruszeski JM, Bohin A, Bohin JP, Lippens G: In vivo detection of the cyclic osmoregulated periplasmic glucan of Ralstonia solanacearum by high-resolution magic angle spinning NMR. J Magn Reson 2001, 151:118-23.
    • (2001) J. Magn. Reson. , vol.151 , pp. 118-123
    • Wieruszeski, J.M.1    Bohin, A.2    Bohin, J.P.3    Lippens, G.4
  • 23
    • 0035130371 scopus 로고    scopus 로고
    • Protein solubility and folding monitored in vivo by structural complementation of a genetic marker protein
    • Wigley WC, Stidham RD, Smith NM, Hunt JF, Thomas PJ: Protein solubility and folding monitored in vivo by structural complementation of a genetic marker protein. Nat Biotechnol 2001, 19:131-6.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 131-136
    • Wigley, W.C.1    Stidham, R.D.2    Smith, N.M.3    Hunt, J.F.4    Thomas, P.J.5
  • 24
    • 0036308719 scopus 로고    scopus 로고
    • Mutations that reduce aggregation of the Alzheimer's Aβ42 peptide: An unbiased search for the sequence determinants of Aβ amyloidogenesis
    • Wurth C, Guimard NK, Hecht MH: Mutations that reduce aggregation of the Alzheimer's Aβ42 peptide: an unbiased search for the sequence determinants of Aβ amyloidogenesis. J Mol Biol 2002, 319:1279-1290.
    • (2002) J. Mol. Biol. , vol.319 , pp. 1279-1290
    • Wurth, C.1    Guimard, N.K.2    Hecht, M.H.3
  • 26
    • 0027318513 scopus 로고
    • Macromolecular crowding: Biochemical, biophysical, and physiological consequences
    • Zimmerman SB, Minton AP: Macromolecular crowding: biochemical, biophysical, and physiological consequences. Annu Rev Biophys Biomol Struct 1993, 22:27-65.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.