Zobrazeno 1 - 10
of 46
pro vyhledávání: '"K N, Bulygin"'
Autor:
Ludmila Frolova, Elena G. Bagryanskaya, Olesya A. Krumkacheva, K. N. Bulygin, Galina G. Karpova, Dmitri Graifer, Ivan O. Timofeev, Alexey A. Malygin, Maria I. Meschaninova, Matvey V. Fedin, Alya G. Venyaminova
Publikováno v:
Computational and Structural Biotechnology Journal
Computational and Structural Biotechnology Journal, Vol 19, Iss, Pp 4702-4710 (2021)
Computational and Structural Biotechnology Journal, Vol 19, Iss, Pp 4702-4710 (2021)
Graphical abstract
Highlights • DEER reveals the conformational variability of mRNA at the certain translation steps. • Elongation and termination complexes exist in 2 conformations in dynamic equilibrium. • The conformations of mRNA in 40
Highlights • DEER reveals the conformational variability of mRNA at the certain translation steps. • Elongation and termination complexes exist in 2 conformations in dynamic equilibrium. • The conformations of mRNA in 40
Autor:
Alexander V. Gopanenko, Galina G. Karpova, Elena S. Babaylova, Alexey E. Tupikin, Alexey A. Malygin, K. N. Bulygin, Marsel R. Kabilov
Publikováno v:
Nucleic Acids Research
In eukaryotic ribosomes, the conserved protein uS19, formerly known as S15, extends with its C-terminal tail to the decoding site. The cross-linking of uS19 to the A site codon has been detected using synthetic mRNAs bearing 4-thiouridine (s4U) resid
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms. 1863:194490
The eukaryotic ribosomal protein uS19 has a C-terminal tail that is absent in its bacterial homologue. This tail has been shown to be involved in the formation of the decoding site of human ribosomes. We studied here the previously unexplored functio
Autor:
Mieko Suzuki, Codjo Hountondji, Galina G. Karpova, K. N. Bulygin, Jean-Bernard Créchet, Blanche Aguida, Mayo Tanaka, Jean A. H. Cognet, Jun-ichi Nakayama, Soria Baouz
Publikováno v:
Biochimie. 158
The GGQ minidomain of the ribosomal protein eL42 was previously shown to contact the CCA-arm of P-site bound tRNA in human ribosome, indicating a possible involvement of the protein in the catalytic activity. Here, using Schizosaccharomyces pombe (S.
Publikováno v:
Biochimica et Biophysica Acta-Gene Regulatory Mechanisms
Biochimica et Biophysica Acta-Gene Regulatory Mechanisms, Elsevier, 2017, 1860 (7), pp.782-793. ⟨10.1016/j.bbagrm.2017.04.004⟩
Biochimica et Biophysica Acta-Gene Regulatory Mechanisms, Elsevier, 2017, 1860 (7), pp.782-793. ⟨10.1016/j.bbagrm.2017.04.004⟩
International audience; Here we employed site-directed cross-linking with the application of tRNA and mRNA analogues bearing an oxidized ribose at the 3′-terminus to investigate mutual arrangement of the main components of translation termination c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::756993a24068dfcb3161bbb999c95c98
https://hal.sorbonne-universite.fr/hal-01906422
https://hal.sorbonne-universite.fr/hal-01906422
Autor:
Dmitri Graifer, J. Stahl, L. Yu. Frolova, K. N. Bulygin, Yu. S. Khairulina, M. V. Molotkov, Aliya G. Venyaminova, Galina G. Karpova
Publikováno v:
Russian Journal of Bioorganic Chemistry. 34:691-697
Protein S3 fragments were determined that crosslink to modified mRNA analogues in positions +5 to +12 relative to the first nucleotide in the P-site bound codon in model complexes mimicking states of ribosomes at the elongation and translation termin
Autor:
Yu. S. Khairulina, M. V. Molotkov, K. N. Bulygin, Dmitri Graifer, Galina G. Karpova, Aliya G. Venyaminova
Publikováno v:
Molecular Biology. 42:270-276
Protein S15 is a characteristic component of the mammalian 80S ribosome that neighbors the mRNA codon at the decoding site and the downstream triplets. The S15 fragment juxtaposed in the human ribosome to mRNA nucleotides +4 to +12 relative to the fi
Autor:
Galina G. Karpova, Mariya I. Meschaninova, E. A. Popugaeva, Marina N. Repkova, Aliya G. Venyaminova, L. Yu. Frolova, Dmitri Graifer, K. N. Bulygin
Publikováno v:
Molecular Biology. 41:781-789
The arrangement of the stop codon and its 3′-flanking codon relative to the components of translation termination complexes of human 80S ribosomes was studied using mRNA analogs containing the stop signal UPuPuPu (Pu is A or G) and the photoreactiv
Autor:
E. A. Popugaeva, Dmitri Graifer, M. V. Molotkov, Aliya G. Venyaminova, Galina G. Karpova, Mariya I. Meschaninova, K. N. Bulygin
Publikováno v:
Russian Journal of Bioorganic Chemistry. 33:399-409
The protein environment of mRNA 3′ of the A-site codon (the decoding site) in the human 80S ribosome was studied using a set of oligoribonucleotide derivatives bearing a UUU triplet at the 5′-end and a perfluoroarylazide group at one of the nucle
Autor:
Ludmila Frolova, Galina G. Karpova, K. N. Bulygin, Yulia S. Bartuli, Alexey A. Malygin, Dmitri Graifer
Publikováno v:
RNA (New York, N.Y.). 22(2)
Translation termination in eukaryotes is mediated by release factors: eRF1, which is responsible for stop codon recognition and peptidyl-tRNA hydrolysis, and GTPase eRF3, which stimulates peptide release. Here, we have utilized ribose-specific probes