M D Ter-Avanesyan
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Explore the profile of M D Ter-Avanesyan including associated specialties, affiliations and a list of published articles.
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44
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1901
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Recent Articles
1.
Alexandrov A, Serpionov G, Kushnirov V, Ter-Avanesyan M
Prion
. 2016 May;
10(3):221-7.
PMID: 27220690
Proteins with expanded polyglutamine (polyQ) regions are prone to form amyloids, which can cause diseases in humans and toxicity in yeast. Recently, we showed that in yeast non-toxic amyloids of...
2.
Mironova L, Provorov N, Ter-Avanesyan M, Inge-Vechtomov S, Smirnov V, Surguchov A
Curr Genet
. 2013 Nov;
5(2):149-52.
PMID: 24186231
Mutants of the yeast Saccharomyces cerevisiae carrying ribosomal suppressor mutations in either sup1 or sup2 genes express a higher sensitivity to paromomycin - aminoglycoside antibiotic known to induce translational errors...
3.
Ter-Avanesyan M, Mironova L, Inge-Vechtomov S, Zlatkin I, Smirnov V, Surguchov A
Curr Genet
. 2013 Nov;
7(5):357-62.
PMID: 24173416
Mutations in sup1 and sup2 genes may cause cycloheximide-dependent growth in yeast Saccharomyces cerevisiae. Two classes of such mutants are described in the paper: 1) high temperature sensitive mutants, which...
4.
Afanasieva E, Kushnirov V, Ter-Avanesyan M
Biochemistry (Mosc)
. 2012 Feb;
76(13):1375-84.
PMID: 22339593
Mammalian prions are infectious agents of proteinaceous nature that cause several incurable neurodegenerative diseases. Interspecies transmission of prions is usually impeded or impossible. Barriers in prion transmission are caused by...
5.
Shkundina I, Ter-Avanesyan M
Biochemistry (Mosc)
. 2008 Feb;
72(13):1519-36.
PMID: 18282140
Prions were originally defined as infectious agents of protein nature, which caused neurodegenerative diseases in animals and humans. The prion concept implies that the infectious agent is a protein in...
6.
Agaphonov M, Plotnikova T, Fokina A, Romanova N, Packeiser A, Kang H, et al.
FEMS Yeast Res
. 2007 May;
7(7):1145-52.
PMID: 17498212
In yeast, functions of the endoplasmic reticulum (ER) depend on the Golgi apparatus Ca2+ pool, which is replenished by the medial-Golgi ion pump Pmr1p. Here, to dissect the role of...
7.
Valouev I, Urakov V, Kochneva-Pervukhova N, Smirnov V, Ter-Avanesyan M
Mol Microbiol
. 2004 Jul;
53(2):687-96.
PMID: 15228544
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,...
8.
Urakov V, Valouev I, Lewitin E, Paushkin S, Kosorukov V, Kushnirov V, et al.
BMC Mol Biol
. 2001 Sep;
2:9.
PMID: 11570975
Background: Termination of translation in eukaryotes is controlled by two interacting polypeptide chain release factors, eRFl and eRF3. eRFl recognizes nonsense codons UAA, UAG and UGA, while eRF3 stimulates polypeptide...
9.
Chacinska A, Szczesniak B, Kochneva-Pervukhova N, Kushnirov V, Ter-Avanesyan M, Boguta M
Curr Genet
. 2001 Jun;
39(2):62-7.
PMID: 11405097
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...
10.
Kochneva-Pervukhova N, Chechenova M, Valouev I, Kushnirov V, Smirnov V, Ter-Avanesyan M
Yeast
. 2001 Apr;
18(6):489-97.
PMID: 11284005
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...