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Items: 9

1.

Cotranslational Folding of Proteins on the Ribosome.

Liutkute M, Samatova E, Rodnina MV.

Biomolecules. 2020 Jan 7;10(1). pii: E97. doi: 10.3390/biom10010097. Review.

2.

Translational recoding: canonical translation mechanisms reinterpreted.

Rodnina MV, Korniy N, Klimova M, Karki P, Peng BZ, Senyushkina T, Belardinelli R, Maracci C, Wohlgemuth I, Samatova E, Peske F.

Nucleic Acids Res. 2020 Feb 20;48(3):1056-1067. doi: 10.1093/nar/gkz783.

PMID:
31511883
3.

Mechanisms and biomedical implications of -1 programmed ribosome frameshifting on viral and bacterial mRNAs.

Korniy N, Samatova E, Anokhina MM, Peske F, Rodnina MV.

FEBS Lett. 2019 Jul;593(13):1468-1482. doi: 10.1002/1873-3468.13478. Epub 2019 Jun 20.

4.

Modulation of HIV-1 Gag/Gag-Pol frameshifting by tRNA abundance.

Korniy N, Goyal A, Hoffmann M, Samatova E, Peske F, Pöhlmann S, Rodnina MV.

Nucleic Acids Res. 2019 Jun 4;47(10):5210-5222. doi: 10.1093/nar/gkz202.

5.

Ribosome rearrangements at the onset of translational bypassing.

Agirrezabala X, Samatova E, Klimova M, Zamora M, Gil-Carton D, Rodnina MV, Valle M.

Sci Adv. 2017 Jun 7;3(6):e1700147. doi: 10.1126/sciadv.1700147. eCollection 2017 Jun.

6.

High-efficiency translational bypassing of non-coding nucleotides specified by mRNA structure and nascent peptide.

Samatova E, Konevega AL, Wills NM, Atkins JF, Rodnina MV.

Nat Commun. 2014 Jul 21;5:4459. doi: 10.1038/ncomms5459.

PMID:
25041899
7.

Independent of their localization in protein the hydrophobic amino acid residues have no effect on the molten globule state of apomyoglobin and the disulfide bond on the surface of apomyoglobin stabilizes this intermediate state.

Melnik TN, Majorina MA, Larina DS, Kashparov IA, Samatova EN, Glukhov AS, Melnik BS.

PLoS One. 2014 Jun 3;9(6):e98645. doi: 10.1371/journal.pone.0098645. eCollection 2014.

8.

Folding intermediate and folding nucleus for I-->N and U-->I-->N transitions in apomyoglobin: contributions by conserved and nonconserved residues.

Samatova EN, Melnik BS, Balobanov VA, Katina NS, Dolgikh DA, Semisotnov GV, Finkelstein AV, Bychkova VE.

Biophys J. 2010 Apr 21;98(8):1694-702. doi: 10.1016/j.bpj.2009.12.4326.

9.

How strong are side chain interactions in the folding intermediate?

Samatova EN, Katina NS, Balobanov VA, Melnik BS, Dolgikh DA, Bychkova VE, Finkelstein AV.

Protein Sci. 2009 Oct;18(10):2152-9. doi: 10.1002/pro.229.

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