Research Topics
| A S SpirinSummaryCountry: Russia Publications
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Detail Information
Publications
Omnipotent RNAAlexander S Spirin
Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia
FEBS Lett 530:4-8. 2002..It is proposed that the Woese universal precursor in the ancient RNA world could be a cell-free community of mixed RNA colonies growing and multiplying on solid surfaces...
The ribosome as an RNA-based molecular machineAlexander S Spirin
Institute of Protein Research, Russian Academy of Sciences, Moscow Region, Russia
RNA Biol 1:3-9. 2004....
High-throughput cell-free systems for synthesis of functionally active proteinsAlexander S Spirin
Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia
Trends Biotechnol 22:538-45. 2004....
[RNA polymerase as a molecular machine]A S Spirin
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia
Mol Biol (Mosk) 36:208-15. 2002....
Ribosome as a molecular machineAlexander S Spirin
Institute of Protein Research, Russian Academy of Sciences, 142290, Moscow Region, Pushchino, Russia
FEBS Lett 514:2-10. 2002..The GTP-dependent catalysis of conformational transitions by elongation factors during translation is also discussed...
Ab Ovo Usque Ad MalaA S Spirin
Biological Faculty, Lomonosov Moscow State University, Russia
Biochemistry (Mosc) 72:1281-3. 2007
How does a scanning ribosomal particle move along the 5'-untranslated region of eukaryotic mRNA? Brownian Ratchet modelAlexander S Spirin
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia 142290
Biochemistry 48:10688-92. 2009....
Ribosome-associated protein that inhibits translation at the aminoacyl-tRNA binding stageD E Agafonov
Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia
EMBO Rep 2:399-402. 2001..The function of the protein in adaptation of cells to environmental stress is discussed...
A novel stress-response protein that binds at the ribosomal subunit interface and arrests translationD E Agafonov
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia 142290
Cold Spring Harb Symp Quant Biol 66:509-14. 2001
Synergism in replication and translation of messenger RNA in a cell-free systemI Y Morozov
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region
Proc Natl Acad Sci U S A 90:9325-9. 1993..The coupled replication-translation of nonviral mRNA recombinants can serve as a useful model for studying the fundamental aspects of virus amplification and can be implemented for large-scale protein synthesis in vitro...
Viral Q beta RNA as a high expression vector for mRNA translation in a cell-free systemV L Katanaev
Institute of Protein Research, Russian Academy of Sciences, Moscow Region
FEBS Lett 359:89-92. 1995..Additionally, it resulted in a significantly enhanced synthesis of Q beta replicase as compared with its synthesis when the original Q beta RNA was used...
Cell-free production of biologically active polypeptides: application to the synthesis of antibacterial peptide cecropinK A Martemyanov
Institute of Protein Research, 142292 Pushchino, Moscow Region, Russia
Protein Expr Purif 21:456-61. 2001..The synthesis of functionally active antibacterial polypeptide cecropin P1 (31 amino acid residues) has been demonstrated...
Effective non-viral leader for cap-independent translation in a eukaryotic cell-free systemL A Shaloiko
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia 142290
Biotechnol Bioeng 88:730-9. 2004..We propose the obelin mRNA leader be used for effective cap-independent translation in eukaryotic cell-free systems, including combined transcription-translation systems with uncontrolled phage polymerase-catalyzed accumulation of mRNA...
The ribosome-associated inhibitor A reduces translation errorsDmitry E Agafonov
Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia
Biochem Biophys Res Commun 320:354-8. 2004..The role of the protein in adaptation of cells to environmental stress is discussed...
Intramolecular triple helix as a model for regular polyribonucleotide (CAA)(n)Alexander V Efimov
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia, Russian Federation
Biochem Biophys Res Commun 388:127-30. 2009..The difference from the known triple helices is that Watson-Crick hydrogen bond pairings do not take place in the interactions between the bases within the base triads...
Continuous-exchange protein-synthesizing systemsVladimir A Shirokov
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow, Russia
Methods Mol Biol 375:19-55. 2007..The ways to improve substrate supply in cell-free systems and mRNA design for eukaryotic system are discussed. Correct folding of the synthesized protein is demonstrated and discussed in detail...
Leader sequences of eukaryotic mRNA can be simultaneously bound to initiating 80S ribosome and 40S ribosomal subunitE A Sogorin
Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia
Biochemistry (Mosc) 77:342-5. 2012..It is supposed that the ability of mRNA leader sequences to bind simultaneously 80S ribosome and 40S subunit is independent of leader nature and may reflect previously unknown eukaryotic mechanisms of translation initiation...
Compact globular structure of Thermus thermophilus ribosomal protein S1 in solution: sedimentation and calorimetric studyOlga M Selivanova
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region 142290, Russia
J Biol Chem 278:36311-4. 2003..1 S) but does not lose its cooperativity and thermostability, this suggesting just the weakening of interdomain ionic interactions. The compact globular conformation of protein S1 seems to be most likely within the ribosome...
Step-wise formation of eukaryotic double-row polyribosomes and circular translation of polysomal mRNAGelina S Kopeina
Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia
Nucleic Acids Res 36:2476-88. 2008..Removal or replacements of 5' and 3' UTRs affected the initial phase of translation, but did not prevent the formation of the double-row polysomes during translation...
Chemical and enzymatic probing of spatial structure of the omega leader of tobacco mosaic virus RNAN E Shirokikh
Laboratory of Mechanisms of Protein Biosynthesis, Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia
Biochemistry (Mosc) 75:405-11. 2010....
Expression and stability of recombinant RQ-mRNAs in cell-free translation systemsV I Ugarov
Institute of Protein Research, Russian Academy of Sciences, Puschino, Moscow Region
FEBS Lett 341:131-4. 1994..The enhancement is due to protection of the recombinant mRNAs against endogenous ribonucleases and to an increased initial rate of translation in the case of the RQ-CAT mRNA...
A protein residing at the subunit interface of the bacterial ribosomeD E Agafonov
Institute of Protein Research, Russian Academy of Sciences, 142292 Pushchino, Moscow Region, Russia
Proc Natl Acad Sci U S A 96:12345-9. 1999..The protein was shown to stabilize ribosomes against dissociation. The possible role of the protein Y as ribosome association factor in translation is discussed...
Effective cotranslational folding of firefly luciferase without chaperones of the Hsp70 familyMaxim S Svetlov
Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia
Protein Sci 15:242-7. 2006..The results presented suggest that the chaperones of the Hsp70 family are not required for effective cotranslational folding of firefly luciferase...
The leader sequence of tobacco mosaic virus RNA devoid of Watson-Crick secondary structure possesses a cooperatively melted, compact conformationAlexey A Kovtun
Institute of Protein Research, Russian Academy of Sciences, Moscow Region, Pushchino 142290, Russia
Biochem Biophys Res Commun 358:368-72. 2007..Thus, the omega leader and its core (CAA)(n) repeat sequence devoid of secondary structure of the Watson-Crick type seem to be well structured elements of mRNA...
Synthesis of functionally active human proinsulin in a cell-free translation systemA A Kommer
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast 142290, Russia
Dokl Biochem Biophys 401:154-8. 2005
Quantitative analysis of ribosome-mRNA complexes at different translation stagesNikolay E Shirokikh
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia
Nucleic Acids Res 38:e15. 2010..We also point out the unique advantages of this new methodology, including the ability to assay sites of the ribosomal complex assembly on several mRNA species in the same reaction mixture...
Translation of non-capped mRNAs in a eukaryotic cell-free system: acceleration of initiation rate in the course of polysome formationOlga M Alekhina
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia
Nucleic Acids Res 35:6547-59. 2007..The eIF4F-mediated circularization of polysomes may be considered as a possible event that leads to the re-initiation switch and the resultant acceleration effect...
5'-poly(A) sequence as an effective leader for translation in eukaryotic cell-free systemsAnatoly T Gudkov
Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia
Biotechnol Bioeng 91:468-73. 2005..The possibility of the practical use of the constructs with the poly(A) leader for preparative protein production is demonstrated in the wheat germ continuous-exchange cell-free (CECF) translation system...
Ribosomal protein S1 from Thermus thermophilus: its detection, identification and overproductionVyacheslav M Shiryaev
Institute of Protein Research, Russian Academy of Sciences, 142290, Moscow Region, Pushchino, Russia
FEBS Lett 525:88. 2002..The gene of ribosomal protein S1 from Thermus thermophilus has been cloned and overexpressed in Escherichia coli. A procedure for purification of the protein has been developed...
Ribosomal protein S1 induces a conformational change of the 30S ribosomal subunitSultan Ch Agalarov
Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russian Federation
FEBS Lett 580:6797-9. 2006..It was concluded that protein S1 binds in the region of the neck of the 30S ribosomal subunit inducing a conformational change of its structure...
Eukaryotic elongation factor 1A interacts with the upstream pseudoknot domain in the 3' untranslated region of tobacco mosaic virus RNAVladimir V Zeenko
Friedrich Miescher Institute, CH-4002 Basel, Switzerland
J Virol 76:5678-91. 2002..Its possible role in the regulation of tobamovirus gene expression and replication is discussed...
