Gudkov AT - Search Results

1

Mutations in the G-domain of elongation factor G from Thermus thermophilus affect both its interaction with GTP and fusidic acid.

Martemyanov KA, Liljas A, Yarunin AS, Gudkov AT. Martemyanov KA, et al. Among authors: gudkov at. J Biol Chem. 2001 Aug 3;276(31):28774-8. doi: 10.1074/jbc.M102023200. Epub 2001 May 22. J Biol Chem. 2001. PMID: 11371559 Free article.

2

An intact conformation at the tip of elongation factor G domain IV is functionally important.

Martemyanov KA, Yarunin AS, Liljas A, Gudkov AT. Martemyanov KA, et al. Among authors: gudkov at. FEBS Lett. 1998 Aug 28;434(1-2):205-8. doi: 10.1016/s0014-5793(98)00982-x. FEBS Lett. 1998. PMID: 9738479 Free article.

3

Increased functional activity of elongation factor G with G16V mutation in the GTP-binding domain.

Martemyanov KA, Liljas A, Gudkov AT. Martemyanov KA, et al. Among authors: gudkov at. Biochemistry (Mosc). 1998 Oct;63(10):1216-9. Biochemistry (Mosc). 1998. PMID: 9864458

4

Domain IV of elongation factor G from Thermus thermophilus is strictly required for translocation.

Martemyanov KA, Gudkov AT. Martemyanov KA, et al. Among authors: gudkov at. FEBS Lett. 1999 Jun 11;452(3):155-9. doi: 10.1016/s0014-5793(99)00635-3. FEBS Lett. 1999. PMID: 10386581 Free article.

5

Extremely thermostable elongation factor G from Aquifex aeolicus: cloning, expression, purification, and characterization in a heterologous translation system.

Martemyanov KA, Liljas A, Gudkov AT. Martemyanov KA, et al. Among authors: gudkov at. Protein Expr Purif. 2000 Apr;18(3):257-61. doi: 10.1006/prep.1999.1178. Protein Expr Purif. 2000. PMID: 10733877

6

Domain III of elongation factor G from Thermus thermophilus is essential for induction of GTP hydrolysis on the ribosome.

Martemyanov KA, Gudkov AT. Martemyanov KA, et al. Among authors: gudkov at. J Biol Chem. 2000 Nov 17;275(46):35820-4. doi: 10.1074/jbc.M002656200. J Biol Chem. 2000. PMID: 10940297 Free article.

7

Structural insights into fusidic acid resistance and sensitivity in EF-G.

Hansson S, Singh R, Gudkov AT, Liljas A, Logan DT. Hansson S, et al. Among authors: gudkov at. J Mol Biol. 2005 May 13;348(4):939-49. doi: 10.1016/j.jmb.2005.02.066. J Mol Biol. 2005. PMID: 15843024

8

Direct expression of PCR products in a cell-free transcription/translation system: synthesis of antibacterial peptide cecropin.

Martemyanov KA, Spirin AS, Gudkov AT. Martemyanov KA, et al. Among authors: gudkov at. FEBS Lett. 1997 Sep 8;414(2):268-70. doi: 10.1016/s0014-5793(97)01011-9. FEBS Lett. 1997. PMID: 9315699 Free article.

9

Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site.

Laurberg M, Kristensen O, Martemyanov K, Gudkov AT, Nagaev I, Hughes D, Liljas A. Laurberg M, et al. Among authors: gudkov at. J Mol Biol. 2000 Nov 3;303(4):593-603. doi: 10.1006/jmbi.2000.4168. J Mol Biol. 2000. PMID: 11054294

10

Cell-free production of biologically active polypeptides: application to the synthesis of antibacterial peptide cecropin.

Martemyanov KA, Shirokov VA, Kurnasov OV, Gudkov AT, Spirin AS. Martemyanov KA, et al. Among authors: gudkov at. Protein Expr Purif. 2001 Apr;21(3):456-61. doi: 10.1006/prep.2001.1400. Protein Expr Purif. 2001. PMID: 11281721

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