메뉴 건너뛰기




Volumn 236, Issue 1, 1996, Pages 149-154

Pbotoaffinity labeling of elongation factor-2 with 8-azido derivatives of GTP and ATP

Author keywords

ATP; Elongation factor 2; GTP; Photoaffinity labeling

Indexed keywords

ADENOSINE TRIPHOSPHATE DERIVATIVE; ELONGATION FACTOR 2; GUANOSINE TRIPHOSPHATE DERIVATIVE; 8 AZIDOADENOSINE TRIPHOSPHATE; 8 AZIDOGUANOSINE TRIPHOSPHATE; 8-AZIDOADENOSINE 5'-TRIPHOSPHATE; 8-AZIDOGUANOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AZIDE; DRUG DERIVATIVE; ELONGATION FACTOR; GUANOSINE TRIPHOSPHATE; PEPTIDE FRAGMENT;

EID: 0029670026     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.00149.x     Document Type: Article
Times cited : (5)

References (20)
  • 2
    • 0023657516 scopus 로고
    • Partial reassembly of active 60S ribosomal subunits from rat liver following treatment with dimethylmaleic anhydride
    • Conquet, F., Lavergne, J. P., Paleologue, A., Reboud, J. P. & Reboud, A. M. (1987) Partial reassembly of active 60S ribosomal subunits from rat liver following treatment with dimethylmaleic anhydride, Eur. J. Biochem. 163, 15–20.
    • (1987) Eur. J. Biochem. , vol.163 , pp. 15-20
    • Conquet, F.1    Lavergne, J.P.2    Paleologue, A.3    Reboud, J.P.4    Reboud, A.M.5
  • 3
    • 0027980558 scopus 로고
    • The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution
    • Czworkowski, J., Wang, J., Steitz, T. A. & Moore, P. B. (1994) The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution, EMBO J. 13, 3661–3668.
    • (1994) EMBO J. , vol.13 , pp. 3661-3668
    • Czworkowski, J.1    Wang, J.2    Steitz, T.A.3    Moore, P.B.4
  • 4
    • 0025824499 scopus 로고
    • Antheprot: an interactive graphic software for analysing protein structures from sequences
    • Geourjon, C., Deleage, G. & Roux, B. (1991) Antheprot: an interactive graphic software for analysing protein structures from sequences, J. Mol. Graphics 9, 188–190.
    • (1991) J. Mol. Graphics , vol.9 , pp. 188-190
    • Geourjon, C.1    Deleage, G.2    Roux, B.3
  • 5
    • 0027386028 scopus 로고
    • GTP‐binding to elongation factor eEF‐2 unmasks a tryptophan residue required for biological activity
    • Guillot, D., Penin, F., Di Pietro, A., Sontag, B., Lavergne, J. P. & Reboud, J. P. (1993a) GTP‐binding to elongation factor eEF‐2 unmasks a tryptophan residue required for biological activity, J. Biol. Chem. 268, 20911–20916.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20911-20916
    • Guillot, D.1    Penin, F.2    Di Pietro, A.3    Sontag, B.4    Lavergne, J.P.5    Reboud, J.P.6
  • 6
    • 0027332734 scopus 로고
    • Trp221 is involved in the protective effect of elongation factor eEF‐2 on the ricin/α‐sarcin site of the ribosome
    • Guillot, D., Lavergne, J. P. & Reboud, J. P. (1993b) Trp221 is involved in the protective effect of elongation factor eEF‐2 on the ricin/α‐sarcin site of the ribosome, J. Biol. Chem. 268, 26082–26084.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26082-26084
    • Guillot, D.1    Lavergne, J.P.2    Reboud, J.P.3
  • 7
    • 0024234855 scopus 로고
    • CLUSTAL: a package for performing multiple sequence alignements on a microcomputer
    • Higgins, D. G. & Sharp, P. M. (1988) CLUSTAL: a package for performing multiple sequence alignements on a microcomputer, Gene (Amst.) 73, 237–244.
    • (1988) Gene (Amst.) , vol.73 , pp. 237-244
    • Higgins, D.G.1    Sharp, P.M.2
  • 8
    • 50549168907 scopus 로고
    • Measurement of protein‐binding phenomena by gel filtration
    • Hummel, J. P. & Dreyer, W. J. (1962) Measurement of protein‐binding phenomena by gel filtration, Biochim. Biophys. Acta 63, 530–532.
    • (1962) Biochim. Biophys. Acta , vol.63 , pp. 530-532
    • Hummel, J.P.1    Dreyer, W.J.2
  • 9
    • 0025809566 scopus 로고
    • Strategies and reagents for photoaffinity labeling of mechanochemical proteins
    • King, S. M., Kim, H. & Haley, B. H. (1991) Strategies and reagents for photoaffinity labeling of mechanochemical proteins, Methods Enzymol. 196, 449–466.
    • (1991) Methods Enzymol. , vol.196 , pp. 449-466
    • King, S.M.1    Kim, H.2    Haley, B.H.3
  • 11
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage. Nature 227, 680–685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 12
    • 0024432767 scopus 로고
    • Heterogeneity of nature rat liver elongation factor 2
    • Marzouki, A., Lavergne, J. P., Reboud, J. P. & Reboud, A. M. (1989) Heterogeneity of nature rat liver elongation factor 2, FEBS Lett. 255, 72–76.
    • (1989) FEBS Lett. , vol.255 , pp. 72-76
    • Marzouki, A.1    Lavergne, J.P.2    Reboud, J.P.3    Reboud, A.M.4
  • 13
    • 0025203678 scopus 로고
    • The nucleotide‐binding site of HisP, a membrane protein of the histidine permease
    • Mimura, C. S., Admon, A., Hurt, K. A. & Ames, G. F. L. (1990) The nucleotide‐binding site of HisP, a membrane protein of the histidine permease, J. Biol. Chem. 265, 19535–19542.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19535-19542
    • Mimura, C.S.1    Admon, A.2    Hurt, K.A.3    Ames, G.F.L.4
  • 14
    • 0022425951 scopus 로고
    • Localization of the site of ADP‐ribosylation and GTP binding in the eukaryotic elongation factor EF‐2
    • Nilsson, L. & Nygård, O. (1985) Localization of the site of ADP‐ribosylation and GTP binding in the eukaryotic elongation factor EF‐2, Eur. J. Biochem. 148, 299–304.
    • (1985) Eur. J. Biochem. , vol.148 , pp. 299-304
    • Nilsson, L.1    Nygård, O.2
  • 15
    • 0023857051 scopus 로고
    • Translationnal dynamics. Interactions between the translational factors, tRNA and ribosomes during eukaryotic protein synthesis
    • Nilsson, L. & Nygård, O. (1988) Translationnal dynamics. Interactions between the translational factors, tRNA and ribosomes during eukaryotic protein synthesis, Eur. J. Biochem. 171, 293–299.
    • (1988) Eur. J. Biochem. , vol.171 , pp. 293-299
    • Nilsson, L.1    Nygård, O.2
  • 16
    • 0027988440 scopus 로고
    • Photoaffinity labeling of creatine kinase with 2‐azido and 8‐azidoadenosine triphosphate: identification of two peptides from the ATP‐binding domain
    • Olcott, M. C., Bradley, M. L. & Haley, B. H. (1994) Photoaffinity labeling of creatine kinase with 2‐azido and 8‐azidoadenosine triphosphate: identification of two peptides from the ATP‐binding domain, Biochemistry 33, 11935–11941.
    • (1994) Biochemistry , vol.33 , pp. 11935-11941
    • Olcott, M.C.1    Bradley, M.L.2    Haley, B.H.3
  • 17
    • 0019135764 scopus 로고
    • tRNA binding stabilizes rat liver 60S ribosomal subunits during treatment with LiCl
    • Reboud, A. M., Dubost, S., Buisson, M. & Reboud, J. P. (1980) tRNA binding stabilizes rat liver 60S ribosomal subunits during treatment with LiCl, J. Biol. Chem. 255, 6954–6961.
    • (1980) J. Biol. Chem. , vol.255 , pp. 6954-6961
    • Reboud, A.M.1    Dubost, S.2    Buisson, M.3    Reboud, J.P.4
  • 19
    • 0027406133 scopus 로고
    • Intrinsic tryptophan fluorescence of rat liver elongation factor eEF‐2 to monitor the interaction with guanylic and adenylic nucleotides and related conformational changes
    • Sontag, B., Reboud, A. M., Divita, G., Di Pietro, A., Guillot, D. & Reboud, J. P. (1993) Intrinsic tryptophan fluorescence of rat liver elongation factor eEF‐2 to monitor the interaction with guanylic and adenylic nucleotides and related conformational changes. Biochemistry 32, 1976–1980.
    • (1993) Biochemistry , vol.32 , pp. 1976-1980
    • Sontag, B.1    Reboud, A.M.2    Divita, G.3    Di Pietro, A.4    Guillot, D.5    Reboud, J.P.6
  • 20
    • 0027049566 scopus 로고
    • Identification of the guanine binding domain peptide of the GTP‐binding site of glucagon
    • Shoemaker, M., Lin, P. C. & Haley, B. (1992) Identification of the guanine binding domain peptide of the GTP‐binding site of glucagon, Protein Sci. 1, 884–891.
    • (1992) Protein Sci. , vol.1 , pp. 884-891
    • Shoemaker, M.1    Lin, P.C.2    Haley, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.