Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Natalia V. Kochneva-Pervukhova"'
Publikováno v:
PLoS ONE, Vol 7, Iss 1, p e29832 (2012)
BackgroundPolyglutamine expansion is responsible for several neurodegenerative disorders, among which Huntington disease is the most well-known. Studies in the yeast model demonstrated that both aggregation and toxicity of a huntingtin (htt) protein
Externí odkaz:
https://doaj.org/article/a126f683c7864c849bda5424748fc5ef
Autor:
Natalia V. Kochneva-Pervukhova, V. N. Urakov, Michael D. Ter-Avanesyan, Vladimir N. Smirnov, I. A. Valouev
Publikováno v:
Molecular Microbiology. 53:687-696
The translation termination factor eRF1 recognizes stop codons at the A site of the ribosome and induces peptidyl-tRNA hydrolysis at the peptidyl transferase centre. Recent data show that, besides translation, yeast eRF1 is also involved in cell cycl
Autor:
Michael D. Ter-Avanesyan, Igor A Valouev, Vladimir N. Smirnov, Natalia V. Kochneva-Pervukhova, Vitaly V. Kushnirov, Maria B. Chechenova
Publikováno v:
Yeast. 18:489-497
The yeast cytoplasmically-inherited nonsense suppressor [PSI(+)] determinant is presumed to be a manifestation of the aggregated prion-like state of the Sup35 protein. Overexpression of the Sup35 protein induces generation of [PSI(+)] determinants wi
Autor:
Vitaly V. Kushnirov, Michael D. Ter-Avanesyan, Natalia V. Kochneva-Pervukhova, Natalia S. Frolova, Maria B. Chechenova
Publikováno v:
The EMBO Journal. 19:324-331
The Sup35 protein (Sup35p) of Saccharomyces cerevisiae is a translation termination factor of the eRF3 family. The proteins of this family possess a conservative C-terminal domain responsible for translation termination and N-terminal extensions of d
Autor:
Michael D. Ter-Avanesyan, Olga V. Mitkevich, Vitaly V. Kushnirov, Elizaveta Rafaelevna Surina, Sergei V. Benevolensky, Natalia V. Kochneva-Pervukhova
Publikováno v:
Prion. 6(4)
Amyloids are fibrillar protein aggregates resulting from non-covalent autocatalytic polymerization of various structurally and functionally unrelated proteins. Previously we have selected DNA aptamers, which bind specifically to the in vitro assemble
Publikováno v:
PLoS ONE, Vol 7, Iss 1, p e29832 (2012)
PLoS ONE
PLoS ONE
BackgroundPolyglutamine expansion is responsible for several neurodegenerative disorders, among which Huntington disease is the most well-known. Studies in the yeast model demonstrated that both aggregation and toxicity of a huntingtin (htt) protein
Autor:
Valery N. Urakov, Natalia V. Kochneva-Pervukhova, Vladimir N. Smirnov, Anna N. Packeiser, Oleg O. Glebov, Igor A Valouev, Michael D. Ter-Avanesyan, Alexander Yu Vishnevsky
Publikováno v:
BMC Molecular Biology
BMC Molecular Biology, Vol 7, Iss 1, p 34 (2006)
BMC Molecular Biology, Vol 7, Iss 1, p 34 (2006)
Background Termination of translation in eukaryotes requires two release factors, eRF1, which recognizes all three nonsense codons and facilitates release of the nascent polypeptide chain, and eRF3 stimulating translation termination in a GTP-depende
Autor:
Vitaly V. Kushnirov, Michael D. Ter-Avanesyan, Barbara Szczesniak, Agnieszka Chacinska, Natalia V. Kochneva-Pervukhova, Magdalena Boguta
Publikováno v:
Current genetics. 39(2)
Yeast SUP7 or SUP11 nonsense suppressors have no phenotypic expression in strains deficient in the isopentenylation of A37 in tRNA. Here we show that such strains spontaneously produce cells with a nonsense suppressor phenotype which is related to th
Autor:
Sergey Paushkin, Michael D. Ter-Avanesyan, Mick F. Tuite, Vitaly V. Kushnirov, Brian S. Cox, Natalia V. Kochneva-Pervukhova
Publikováno v:
The EMBO journal. 17(19)
The SUP35 gene of Saccharomyces cerevisiae encodes the polypeptide chain release factor eRF3. This protein (also called Sup35p) is thought to be able to undergo a heritable conformational switch, similarly to mammalian prions, giving rise to the cyto