Tugarinov V - Search Results

1

Backbone dynamics of escherichia coli adenylate kinase at the extreme stages of the catalytic cycle studied by (15)N NMR relaxation.

Shapiro YE, Sinev MA, Sineva EV, Tugarinov V, Meirovitch E. Shapiro YE, et al. Among authors: tugarinov v. Biochemistry. 2000 Jun 6;39(22):6634-44. doi: 10.1021/bi992076h. Biochemistry. 2000. PMID: 10828981

2

A "Steady-State" Relaxation Dispersion Nuclear Magnetic Resonance Experiment for Studies of Chemical Exchange in Degenerate ¹H Transitions of Methyl Groups.

Tugarinov V, Okuno Y, Torricella F, Karamanos TK, Clore GM. Tugarinov V, et al. J Phys Chem Lett. 2022 Dec 8;13(48):11271-11279. doi: 10.1021/acs.jpclett.2c02937. Epub 2022 Nov 30. J Phys Chem Lett. 2022. PMID: 36449372

3

A methyl-TROSY based ¹³C relaxation dispersion NMR experiment for studies of chemical exchange in proteins.

Tugarinov V, Baber JL, Clore GM. Tugarinov V, et al. J Biomol NMR. 2023 Jun;77(3):83-91. doi: 10.1007/s10858-023-00413-8. Epub 2023 Apr 25. J Biomol NMR. 2023. PMID: 37095392

4

Solution structures of a highly insecticidal recombinant scorpion alpha-toxin and a mutant with increased activity.

Tugarinov V, Kustanovich I, Zilberberg N, Gurevitz M, Anglister J. Tugarinov V, et al. Biochemistry. 1997 Mar 4;36(9):2414-24. doi: 10.1021/bi961497l. Biochemistry. 1997. PMID: 9054546

5

A model of a gp120 V3 peptide in complex with an HIV-neutralizing antibody based on NMR and mutant cycle-derived constraints.

Zvi A, Tugarinov V, Faiman GA, Horovitz A, Anglister J. Zvi A, et al. Among authors: tugarinov v. Eur J Biochem. 2000 Feb;267(3):767-79. doi: 10.1046/j.1432-1327.2000.01055.x. Eur J Biochem. 2000. PMID: 10651813 Free article.

The peptide converges to a unique position within the binding site, with the RGPG loop pointing into the center of the groove formed by the antibody complementary determining regions while retaining the beta-hairpin conformation and the type-VI RGPG turn [Tugarinov, V …

The peptide converges to a unique position within the binding site, with the RGPG loop pointing into the center of the groove formed by the …

6

A structural mode-coupling approach to 15N NMR relaxation in proteins.

Tugarinov V, Liang Z, Shapiro YE, Freed JH, Meirovitch E. Tugarinov V, et al. J Am Chem Soc. 2001 Apr 4;123(13):3055-63. doi: 10.1021/ja003803v. J Am Chem Soc. 2001. PMID: 11457016

7

A novel view of domain flexibility in E. coli adenylate kinase based on structural mode-coupling (15)N NMR relaxation.

Tugarinov V, Shapiro YE, Liang Z, Freed JH, Meirovitch E. Tugarinov V, et al. J Mol Biol. 2002 Jan 11;315(2):155-70. doi: 10.1006/jmbi.2001.5231. J Mol Biol. 2002. PMID: 11779236

8

Domain flexibility in ligand-free and inhibitor-bound Escherichia coli adenylate kinase based on a mode-coupling analysis of 15N spin relaxation.

Shapiro YE, Kahana E, Tugarinov V, Liang Z, Freed JH, Meirovitch E. Shapiro YE, et al. Among authors: tugarinov v. Biochemistry. 2002 May 21;41(20):6271-81. doi: 10.1021/bi012132q. Biochemistry. 2002. PMID: 12009888

9

A cis proline turn linking two beta-hairpin strands in the solution structure of an antibody-bound HIV-1IIIB V3 peptide.

Tugarinov V, Zvi A, Levy R, Anglister J. Tugarinov V, et al. Nat Struct Biol. 1999 Apr;6(4):331-5. doi: 10.1038/7567. Nat Struct Biol. 1999. PMID: 10201400

10

NMR structure of an anti-gp120 antibody complex with a V3 peptide reveals a surface important for co-receptor binding.

Tugarinov V, Zvi A, Levy R, Hayek Y, Matsushita S, Anglister J. Tugarinov V, et al. Structure. 2000 Apr 15;8(4):385-95. doi: 10.1016/s0969-2126(00)00119-2. Structure. 2000. PMID: 10801487 Free article.

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