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Volumn 15, Issue 10, 2008, Pages 1104-1115

Cross-Strand Split Tetra-Cys Motifs as Structure Sensors in a β-Sheet Protein

Author keywords

CHEMBIO; PROTEINS

Indexed keywords

CYSTEINE; PROTEIN;

EID: 53849114687     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2008.09.006     Document Type: Article
Times cited : (39)

References (25)
  • 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 S.R., Campbell R.E., Gross L.A., Martin B.R., Walkup G.K., Yao Y., Llopis J., and Tsien R.Y. New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications. J. Am. Chem. Soc. 124 (2002) 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
    • 33745213371 scopus 로고    scopus 로고
    • CrAsH: a biarsenical multi-use affinity probe with low non-specific fluorescence
    • Cao H., Chen B., Squier T.C., and Mayer M.U. CrAsH: a biarsenical multi-use affinity probe with low non-specific fluorescence. Chem. Commun. (Camb.) 28 (2006) 2601-2603
    • (2006) Chem. Commun. (Camb.) , vol.28 , pp. 2601-2603
    • Cao, H.1    Chen, B.2    Squier, T.C.3    Mayer, M.U.4
  • 3
    • 0031784567 scopus 로고    scopus 로고
    • Probing the folding pathway of a β-clam protein with single-tryptophan constructs
    • Clark P.L., Weston B.F., and Gierasch L.M. Probing the folding pathway of a β-clam protein with single-tryptophan constructs. Fold. Des. 3 (1998) 401-412
    • (1998) Fold. Des. , vol.3 , pp. 401-412
    • Clark, P.L.1    Weston, B.F.2    Gierasch, L.M.3
  • 4
    • 0037433511 scopus 로고    scopus 로고
    • Effects of As(III) binding on α-helical structure
    • Cline D.J., Thorpe C., and Schneider J.P. Effects of As(III) binding on α-helical structure. J. Am. Chem. Soc. 125 (2003) 2923-2929
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 2923-2929
    • Cline, D.J.1    Thorpe, C.2    Schneider, J.P.3
  • 5
    • 0000007711 scopus 로고
    • The crystal structure of the arsenite complex of dithiothreitol
    • Cruse W.B.T., and James M.N.G. The crystal structure of the arsenite complex of dithiothreitol. Acta Crystallogr. B 28 (1972) 1325-1331
    • (1972) Acta Crystallogr. B , vol.28 , pp. 1325-1331
    • Cruse, W.B.T.1    James, M.N.G.2
  • 6
    • 0027445111 scopus 로고
    • Transfer of arsenite from glutathione to dithiols: a model of interaction
    • Delnomdedieu M., Basti M.M., Otvos J.D., and Thomas D.J. Transfer of arsenite from glutathione to dithiols: a model of interaction. Chem. Res. Toxicol. 6 (1993) 598-602
    • (1993) Chem. Res. Toxicol. , vol.6 , pp. 598-602
    • Delnomdedieu, M.1    Basti, M.M.2    Otvos, J.D.3    Thomas, D.J.4
  • 8
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin B.A., Adams S.R., and Tsien R.Y. Specific covalent labeling of recombinant protein molecules inside live cells. Science 281 (1998) 269-272
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 9
    • 0034581376 scopus 로고    scopus 로고
    • Fluorescent labeling of recombinant proteins in living cells with FlAsH
    • Griffin B.A., Adams S.R., Jones J., and Tsien R.Y. Fluorescent labeling of recombinant proteins in living cells with FlAsH. Methods Enzymol. 327 (2000) 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
  • 10
    • 0347004717 scopus 로고    scopus 로고
    • Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling
    • Ignatova Z., and Gierasch L.M. Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling. Proc. Natl. Acad. Sci. USA 101 (2004) 523-528
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 523-528
    • Ignatova, Z.1    Gierasch, L.M.2
  • 12
    • 0032779633 scopus 로고    scopus 로고
    • Glutathione (GSH) reduces the open probability of mechanosensitive channels in Escherichia coli protoplasts
    • Koprowski P., and Kubalski A. Glutathione (GSH) reduces the open probability of mechanosensitive channels in Escherichia coli protoplasts. Pflugers Arch. 438 (1999) 361-364
    • (1999) Pflugers Arch. , vol.438 , pp. 361-364
    • Koprowski, P.1    Kubalski, A.2
  • 13
    • 0041819708 scopus 로고    scopus 로고
    • Crystallographic analysis of an "anticalin" with tailored specificity for fluorescein reveals high structural plasticity of the lipocalin loop region
    • Korndorfer I.P., Beste G., and Skerra A. Crystallographic analysis of an "anticalin" with tailored specificity for fluorescein reveals high structural plasticity of the lipocalin loop region. Proteins 53 (2003) 121-129
    • (2003) Proteins , vol.53 , pp. 121-129
    • Korndorfer, I.P.1    Beste, G.2    Skerra, A.3
  • 14
    • 36248979206 scopus 로고    scopus 로고
    • Surveying polypeptide and protein domain conformation and association with FlAsH and ReAsH
    • Luedtke N.W., Dexter R.J., Fried D.B., and Schepartz A. Surveying polypeptide and protein domain conformation and association with FlAsH and ReAsH. Nat. Chem. Biol. 3 (2007) 779-784
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 779-784
    • Luedtke, N.W.1    Dexter, R.J.2    Fried, D.B.3    Schepartz, A.4
  • 15
    • 33645881071 scopus 로고    scopus 로고
    • Pathways of disulfide bond formation in Escherichia coli
    • Messens J., and Collet J.F. Pathways of disulfide bond formation in Escherichia coli. Int. J. Biochem. Cell Biol. 38 (2006) 1050-1062
    • (2006) Int. J. Biochem. Cell Biol. , vol.38 , pp. 1050-1062
    • Messens, J.1    Collet, J.F.2
  • 17
    • 2442514066 scopus 로고    scopus 로고
    • Equilibrium characterization of the As(III)-cysteine and the As(III)-glutathione systems in aqueous solution
    • Rey N.A., Howarth O.W., and Pereira-Maia E.C. Equilibrium characterization of the As(III)-cysteine and the As(III)-glutathione systems in aqueous solution. J. Inorg. Biochem. 98 (2004) 1151-1159
    • (2004) J. Inorg. Biochem. , vol.98 , pp. 1151-1159
    • Rey, N.A.1    Howarth, O.W.2    Pereira-Maia, E.C.3
  • 18
    • 33846247876 scopus 로고    scopus 로고
    • Mass spectrometric evidence for different complexes of peptides and proteins with arsenic(III), arsenic(V), copper(II), and zinc(II) species
    • Schmidt A.C., Koppelt J., Neustadt M., and Otto M. Mass spectrometric evidence for different complexes of peptides and proteins with arsenic(III), arsenic(V), copper(II), and zinc(II) species. Rapid Commun. Mass Spectrom. 21 (2007) 153-163
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 153-163
    • Schmidt, A.C.1    Koppelt, J.2    Neustadt, M.3    Otto, M.4
  • 19
    • 33747889595 scopus 로고    scopus 로고
    • Synthesis and characterization of a rare arsenic trithiolate with an organic disulfide linkage and 2-chloro-benzo-1,3,2-dithiastibole
    • Shaikh T.A., Parkin S., and Atwood D.A. Synthesis and characterization of a rare arsenic trithiolate with an organic disulfide linkage and 2-chloro-benzo-1,3,2-dithiastibole. J. Organomet. Chem. 691 (2006) 4167-4171
    • (2006) J. Organomet. Chem. , vol.691 , pp. 4167-4171
    • Shaikh, T.A.1    Parkin, S.2    Atwood, D.A.3
  • 20
    • 33645383800 scopus 로고    scopus 로고
    • Structural characteristics of 2-halo-1,3,2-dithiarsenic compounds and tris-(pentafluorophenylthio)-arsen
    • Shaikh T.A., Ronald C., Bakus I.I., Parkin S., and Atwood D.A. Structural characteristics of 2-halo-1,3,2-dithiarsenic compounds and tris-(pentafluorophenylthio)-arsen. J. Organomet. Chem. 691 (2006) 1825-1833
    • (2006) J. Organomet. Chem. , vol.691 , pp. 1825-1833
    • Shaikh, T.A.1    Ronald, C.2    Bakus, I.I.3    Parkin, S.4    Atwood, D.A.5
  • 21
    • 17444432962 scopus 로고    scopus 로고
    • Thermodynamics of the As(III)-thiol interaction: arsenite and monomethylarsenite complexes with glutathione, dihydrolipoic acid, and other thiol ligands
    • Spuches A.M., Kruszyna H.G., Rich A.M., and Wilcox D.E. Thermodynamics of the As(III)-thiol interaction: arsenite and monomethylarsenite complexes with glutathione, dihydrolipoic acid, and other thiol ligands. Inorg. Chem. 44 (2005) 2964-2972
    • (2005) Inorg. Chem. , vol.44 , pp. 2964-2972
    • Spuches, A.M.1    Kruszyna, H.G.2    Rich, A.M.3    Wilcox, D.E.4
  • 22
    • 0034802605 scopus 로고    scopus 로고
    • 2 binds not only to CCXXCC motifs but also non-specifically to endogenous cysteine-rich proteins
    • 2 binds not only to CCXXCC motifs but also non-specifically to endogenous cysteine-rich proteins. Pflugers Arch. 442 (2001) 859-866
    • (2001) Pflugers Arch. , vol.442 , pp. 859-866
    • Stroffekova, K.1    Proenza, C.2    Beam, K.G.3
  • 23
    • 0030631229 scopus 로고    scopus 로고
    • Local interactions in a Schellman motif dictate interhelical arrangement in a protein fragment
    • Sukumar M., and Gierasch L.M. Local interactions in a Schellman motif dictate interhelical arrangement in a protein fragment. Fold. Des. 2 (1997) 211-222
    • (1997) Fold. Des. , vol.2 , pp. 211-222
    • Sukumar, M.1    Gierasch, L.M.2
  • 24
    • 37549048693 scopus 로고    scopus 로고
    • Prospecting the proteome: identification of naturally occurring binding motifs for biarsenical probes
    • Wang T., Yan P., Squier T.C., and Mayer M.U. Prospecting the proteome: identification of naturally occurring binding motifs for biarsenical probes. ChemBioChem 8 (2007) 1937-1940
    • (2007) ChemBioChem , vol.8 , pp. 1937-1940
    • Wang, T.1    Yan, P.2    Squier, T.C.3    Mayer, M.U.4
  • 25
    • 0026724165 scopus 로고
    • Mutating the charged residues in the binding pocket of cellular retinoic acid-binding protein simultaneously reduces its binding affinity to retinoic acid and increases its thermostability
    • Zhang J., Liu Z.P., Jones T.A., Gierasch L.M., and Sambrook J.F. Mutating the charged residues in the binding pocket of cellular retinoic acid-binding protein simultaneously reduces its binding affinity to retinoic acid and increases its thermostability. Proteins 13 (1992) 87-99
    • (1992) Proteins , vol.13 , pp. 87-99
    • Zhang, J.1    Liu, Z.P.2    Jones, T.A.3    Gierasch, L.M.4    Sambrook, J.F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.