메뉴 건너뛰기




Volumn 38, Issue 2, 2004, Pages 253-260

Molecular morphology of eukaryotic class-1 translation termination factor eRF1 in solution

Author keywords

Conformational changes in ribosome; Eukaryotes; Molecule shape in solution; Release factor eRF1; Small angle X ray scattering; UV fluorescence

Indexed keywords

AMINOACYL TRANSFER RNA; TRANSLATION TERMINATION FACTOR; TRANSLATION TERMINATION FACTOR RF1; UNCLASSIFIED DRUG;

EID: 3543044390     PISSN: 00268933     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:MBIL.0000023742.62903.ef     Document Type: Article
Times cited : (1)

References (25)
  • 1
    • 2142816828 scopus 로고    scopus 로고
    • Class-1 translation termination factors are functional analogs of aminoacyl-tRNAs
    • Kisselev L.L. 2003. Class-1 translation termination factors are functional analogs of aminoacyl-tRNAs. Mol. Biol. 37, 931-943.
    • (2003) Mol. Biol. , vol.37 , pp. 931-943
    • Kisselev, L.L.1
  • 2
    • 0037439231 scopus 로고    scopus 로고
    • Termination of translation: Interplay of mRNA, rRNAs and release factors?
    • Kisselev L.L., Ehrenberg M., Frolova L.Yu. 2003 Termination of translation: interplay of mRNA, rRNAs and release factors? EMBO J. 22, 175-182.
    • (2003) EMBO J. , vol.22 , pp. 175-182
    • Kisselev, L.L.1    Ehrenberg, M.2    Frolova, L.Yu.3
  • 3
    • 0034603210 scopus 로고    scopus 로고
    • The crystal structure of human eukaryotic release factor eRF1 - Mechanism of stop codon recognition and peptidyl-tRNA hydrolysis
    • Song H., Mugnier P., Das A.K., Webb H.M., Evans D.R., Tuite M.F., Hemmings B.A., Barford D. 2000. The crystal structure of human eukaryotic release factor eRF1 - mechanism of stop codon recognition and peptidyl-tRNA hydrolysis. Cell. 100, 311-321.
    • (2000) Cell , vol.100 , pp. 311-321
    • Song, H.1    Mugnier, P.2    Das, A.K.3    Webb, H.M.4    Evans, D.R.5    Tuite, M.F.6    Hemmings, B.A.7    Barford, D.8
  • 6
    • 0034185463 scopus 로고    scopus 로고
    • Class-1 polypeptide chain release factors are structurally and functionally similar to suppressor tRNAs and comprise different structural-functional families of prokaryotic/mitochondrial and eukaryotic/archaebacterial factors
    • Kisselev L.L., Oparina N.Yu., Frolova L.Yu. 2000. Class-1 polypeptide chain release factors are structurally and functionally similar to suppressor tRNAs and comprise different structural-functional families of prokaryotic/mitochondrial and eukaryotic/archaebacterial factors. Mol. Biol. 34, 427-442.
    • (2000) Mol. Biol. , vol.34 , pp. 427-442
    • Kisselev, L.L.1    Oparina, N.Yu.2    Frolova, L.Yu.3
  • 10
    • 84990419571 scopus 로고
    • Improved techniq for calculating X-ray scattering intensity of biopolymers in solution: Evaluation of the form, volume and surface of the particle
    • Pavlov M.Y., Fedorov B.A. 1983. Improved techniq for calculating X-ray scattering intensity of biopolymers in solution: evaluation of the form, volume and surface of the particle. Biopolymers. 22, 1507-1511.
    • (1983) Biopolymers , vol.22 , pp. 1507-1511
    • Pavlov, M.Y.1    Fedorov, B.A.2
  • 11
    • 0034496657 scopus 로고    scopus 로고
    • Solution scattering data analysis methods and their application
    • Svergun D.I. 2000. Solution scattering data analysis methods and their application. J. Appl. Crystallogr. 33, 530-534.
    • (2000) J. Appl. Crystallogr. , vol.33 , pp. 530-534
    • Svergun, D.I.1
  • 12
    • 0036816606 scopus 로고    scopus 로고
    • Advances in structure analysis using small angle scattering in solution
    • Svergun D. I., Koch M. H. 2002. Advances in structure analysis using small angle scattering in solution. J. Cur. Opin. Struct, Biol. 12, 654-660.
    • (2002) J. Cur. Opin. Struct, Biol. , vol.12 , pp. 654-660
    • Svergun, D.I.1    Koch, M.H.2
  • 13
    • 0012340669 scopus 로고    scopus 로고
    • Small-angle X-ray scattering by solutions of biological macromolecules
    • Eds. Fanchon E., Geissler G., Hodeau J.-L., Regnard J.-R., Timmins P.A. N.Y: Oxford University Press
    • Vachette P., Svergun D.I. 2000. Small-angle X-ray scattering by solutions of biological macromolecules. In "Structure and Dynamics of Biomolecules". Eds. Fanchon E., Geissler G., Hodeau J.-L., Regnard J.-R., Timmins P.A. N.Y: Oxford University Press, pp. 199-237.
    • (2000) Structure and Dynamics of Biomolecules , pp. 199-237
    • Vachette, P.1    Svergun, D.I.2
  • 14
    • 0035853671 scopus 로고    scopus 로고
    • Novel quaternary structure of the dimeric α-crystallin domen with chaperone like aktivity
    • Feil I.K., Malfois M., Hendle J., van der Zandt H., Svergun D.I. 2001. Novel quaternary structure of the dimeric α-crystallin domen with chaperone like aktivity. J. Biol. Chem. 276, 12024-12029.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12024-12029
    • Feil, I.K.1    Malfois, M.2    Hendle, J.3    Van Der Zandt, H.4    Svergun, D.I.5
  • 16
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small angle scattering
    • Volkov V.V., Svergun D. I. 2003. Uniqueness of ab initio shape determination in small angle scattering. J. Appl. Cryst. 36, 862-866.
    • (2003) J. Appl. Cryst. , vol.36 , pp. 862-866
    • Volkov, V.V.1    Svergun, D.I.2
  • 18
    • 84944815124 scopus 로고
    • Small-angle scattering data treatment by the regularization method
    • Svergun D.I., Semenyuk A.V., Feigin L.A. 1988. Small-angle scattering data treatment by the regularization method. Acta Cryst. A. 24, 244-251.
    • (1988) Acta Cryst. A , vol.24 , pp. 244-251
    • Svergun, D.I.1    Semenyuk, A.V.2    Feigin, L.A.3
  • 19
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect - Transform methods using perceptual criteria
    • Svergun D.I. 1992. Determination of the regularization parameter in indirect - transform methods using perceptual criteria. J. Appl. Cryst. 25, 495-502.
    • (1992) J. Appl. Cryst. , vol.25 , pp. 495-502
    • Svergun, D.I.1
  • 20
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering atomic coordinate
    • Svergun D.I., Barberato C., Koch M.H.J. 1995. CRYSOL - a program to evaluate X-ray solution scattering atomic coordinate. J. Appl. Crystallogr. 28, 768-774.
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-774
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 21
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun D.I. 1999. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76, 2879-2885.
    • (1999) Biophys. J. , vol.76 , pp. 2879-2885
    • Svergun, D.I.1
  • 22
    • 0036216442 scopus 로고    scopus 로고
    • Highly conserved NIKS tetrapeptide is functionally essential in eukaryotic translation termination factor eRF1
    • Frolova L.Yu., Alim Seit-Nebi, Kisselev L.L. 2002. Highly conserved NIKS tetrapeptide is functionally essential in eukaryotic translation termination factor eRF1. RNA. 8, 129-136.
    • (2002) RNA , vol.8 , pp. 129-136
    • Frolova, L.Yu.1    Alim Seit-Nebi2    Kisselev, L.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.