메뉴 건너뛰기




Volumn 422, Issue , 2007, Pages 338-351

Synthesis of a Stable Analog of the Phosphorylated Form of CheY: Phosphono-CheY

Author keywords

[No Author keywords available]

Indexed keywords

5,5' DITHIOBIS(2 NITROBENZOIC ACID); ASPARTIC ACID; BACTERIAL PROTEIN; CYSTEINE; DICHLOROMETHANE; METHYL GROUP; PHOSPHONIC ACID DERIVATIVE; PROTEIN DERIVATIVE; PROTEIN PHOSPHONO CHEY; TRIETHYLAMINE; TRIFLUOROMETHANESULFONIC ACID; UNCLASSIFIED DRUG;

EID: 34447105886     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(06)22016-0     Document Type: Chapter
Times cited : (4)

References (16)
  • 1
    • 0023656227 scopus 로고
    • Isolation of the glutamyl peptide labeled by the nucleotide analogue 2-(4-bromo-2,3-dioxobutylthio)-1,N(6)-ethenoadenosine 2′,5′-biphosphate in the active site of NADP+-specific isocitrate dehydrogenase
    • Bailey J.M., and Colman R.F. Isolation of the glutamyl peptide labeled by the nucleotide analogue 2-(4-bromo-2,3-dioxobutylthio)-1,N(6)-ethenoadenosine 2′,5′-biphosphate in the active site of NADP+-specific isocitrate dehydrogenase. J. Biol. Chem. 262 (1987) 12620-12626
    • (1987) J. Biol. Chem. , vol.262 , pp. 12620-12626
    • Bailey, J.M.1    Colman, R.F.2
  • 2
    • 0020643218 scopus 로고
    • Measurement of chemical phosphate in proteins
    • Buss J.E., and Stull J.T. Measurement of chemical phosphate in proteins. Methods Enzymol. 99 (1983) 7-14
    • (1983) Methods Enzymol. , vol.99 , pp. 7-14
    • Buss, J.E.1    Stull, J.T.2
  • 3
    • 0033567060 scopus 로고    scopus 로고
    • A comparison between the sulfhydryl reductants tris(2-carboxyethyl)phosphine and dithiothreitol for use in protein biochemistry
    • Getz E.B., Xiao M., Chakrabarty T., Cooke R., and Selvin P.R. A comparison between the sulfhydryl reductants tris(2-carboxyethyl)phosphine and dithiothreitol for use in protein biochemistry. Anal. Biochem. 273 (1999) 73-80
    • (1999) Anal. Biochem. , vol.273 , pp. 73-80
    • Getz, E.B.1    Xiao, M.2    Chakrabarty, T.3    Cooke, R.4    Selvin, P.R.5
  • 4
    • 0034624879 scopus 로고    scopus 로고
    • The 1.9 Å resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY
    • Halkides C.J., McEvoy M.M., Casper E., Matsumura P., Volz K., and Dahlquist F.W. The 1.9 Å resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY. Biochemistry 39 (2000) 5280-5286
    • (2000) Biochemistry , vol.39 , pp. 5280-5286
    • Halkides, C.J.1    McEvoy, M.M.2    Casper, E.3    Matsumura, P.4    Volz, K.5    Dahlquist, F.W.6
  • 5
    • 0032578435 scopus 로고    scopus 로고
    • Synthesis and biochemical characterization of an analog of CheY-phosphate, a signal transduction protein in bacterial chemotaxis
    • Halkides C.J., Zhu X., Phillion D.P., Matsumura P., and Dahlquist F.W. Synthesis and biochemical characterization of an analog of CheY-phosphate, a signal transduction protein in bacterial chemotaxis. Biochemistry 37 (1998) 13674-13680
    • (1998) Biochemistry , vol.37 , pp. 13674-13680
    • Halkides, C.J.1    Zhu, X.2    Phillion, D.P.3    Matsumura, P.4    Dahlquist, F.W.5
  • 6
    • 0032483501 scopus 로고    scopus 로고
    • Relative binding affinities of OmpR and OmpR-phosphate at the ompF and ompC regulatory sites
    • Head C.G., Tardy A., and Kenney L.J. Relative binding affinities of OmpR and OmpR-phosphate at the ompF and ompC regulatory sites. J. Mol. Biol. 281 (1998) 857-870
    • (1998) J. Mol. Biol. , vol.281 , pp. 857-870
    • Head, C.G.1    Tardy, A.2    Kenney, L.J.3
  • 7
    • 13344271882 scopus 로고
    • Inclusion bodies from proteins produced at high levels in Escherichia coli
    • Gierasch L., and King J. (Eds), American Association for the Advancement of Science, Washington, DC
    • Krueger J.M., Stock A.M., Schutt C.E., and Stock J.B. Inclusion bodies from proteins produced at high levels in Escherichia coli. In: Gierasch L., and King J. (Eds). "Protein Folding: Deciphering the Second Half of the Genetic Code" (1990), American Association for the Advancement of Science, Washington, DC 334
    • (1990) "Protein Folding: Deciphering the Second Half of the Genetic Code" , pp. 334
    • Krueger, J.M.1    Stock, A.M.2    Schutt, C.E.3    Stock, J.B.4
  • 10
    • 0030580330 scopus 로고    scopus 로고
    • Formation of sulfinate esters in the synthesis of triflates
    • Netscher T., and Bohrer P. Formation of sulfinate esters in the synthesis of triflates. Tetrahedron Lett. 37 (1996) 8359-8362
    • (1996) Tetrahedron Lett. , vol.37 , pp. 8359-8362
    • Netscher, T.1    Bohrer, P.2
  • 15
    • 0032401864 scopus 로고    scopus 로고
    • Evaluation of methods for the quantitation of cysteines in proteins
    • Wright S.K., and Viola R.E. Evaluation of methods for the quantitation of cysteines in proteins. Anal. Biochem. 265 (1998) 8-14
    • (1998) Anal. Biochem. , vol.265 , pp. 8-14
    • Wright, S.K.1    Viola, R.E.2
  • 16
    • 0029883898 scopus 로고    scopus 로고
    • A phosphotransferase activity of the Bacillus subtilis sporulation protein Sop0F that employs phosphoramidate substrates
    • Zapf J.W., Hoch J.A., and Whiteley J.M. A phosphotransferase activity of the Bacillus subtilis sporulation protein Sop0F that employs phosphoramidate substrates. Biochemistry 35 (1996) 2926-2933
    • (1996) Biochemistry , vol.35 , pp. 2926-2933
    • Zapf, J.W.1    Hoch, J.A.2    Whiteley, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.