Tolkatchev D - Search Results

1

Structure dissection of human progranulin identifies well-folded granulin/epithelin modules with unique functional activities.

Tolkatchev D, Malik S, Vinogradova A, Wang P, Chen Z, Xu P, Bennett HP, Bateman A, Ni F. Tolkatchev D, et al. Protein Sci. 2008 Apr;17(4):711-24. doi: 10.1110/ps.073295308. Protein Sci. 2008. PMID: 18359860 Free PMC article.

2

Three-dimensional structure and ligand interactions of the low molecular weight protein tyrosine phosphatase from Campylobacter jejuni.

Tolkatchev D, Shaykhutdinov R, Xu P, Plamondon J, Watson DC, Young NM, Ni F. Tolkatchev D, et al. Protein Sci. 2006 Oct;15(10):2381-94. doi: 10.1110/ps.062279806. Protein Sci. 2006. PMID: 17008719 Free PMC article.

3

Design and solution structure of a well-folded stack of two beta-hairpins based on the amino-terminal fragment of human granulin A.

Tolkatchev D, Ng A, Vranken W, Ni F. Tolkatchev D, et al. Biochemistry. 2000 Mar 21;39(11):2878-86. doi: 10.1021/bi992130u. Biochemistry. 2000. PMID: 10715107

4

A peptide derived from the C-terminal part of a plant cysteine protease folds into a stack of two beta-hairpins, a scaffold present in the emerging family of granulin-like growth factors.

Tolkatchev D, Xu P, Ni F. Tolkatchev D, et al. J Pept Res. 2001 Mar;57(3):227-33. doi: 10.1111/j.1399-3011.2001.00828.x. J Pept Res. 2001. PMID: 11298924

5

Solution structure of a llama single-domain antibody with hydrophobic residues typical of the VH/VL interface.

Vranken W, Tolkatchev D, Xu P, Tanha J, Chen Z, Narang S, Ni F. Vranken W, et al. Among authors: tolkatchev d. Biochemistry. 2002 Jul 9;41(27):8570-9. doi: 10.1021/bi012169a. Biochemistry. 2002. PMID: 12093273

6

Dissecting functional interactions in coagulation protein complexes by use of NMR spectroscopy.

Tolkatchev D, Koutychenko A, Ni F. Tolkatchev D, et al. Curr Protein Pept Sci. 2002 Jun;3(3):275-85. doi: 10.2174/1389203023380666. Curr Protein Pept Sci. 2002. PMID: 12188896 Review.

7

Probing the kinetic landscape of transient peptide-protein interactions by use of peptide (15)n NMR relaxation dispersion spectroscopy: binding of an antithrombin peptide to human prothrombin.

Tolkatchev D, Xu P, Ni F. Tolkatchev D, et al. J Am Chem Soc. 2003 Oct 15;125(41):12432-42. doi: 10.1021/ja021238l. J Am Chem Soc. 2003. PMID: 14531686

8

Rational design and selection of bivalent peptide ligands of thrombin incorporating P4-P1 tetrapeptide sequences: from good substrates to potent inhibitors.

Su Z, Vinogradova A, Koutychenko A, Tolkatchev D, Ni F. Su Z, et al. Among authors: tolkatchev d. Protein Eng Des Sel. 2004 Aug;17(8):647-57. doi: 10.1093/protein/gzh073. Epub 2004 Sep 9. Protein Eng Des Sel. 2004. PMID: 15358856

9

Transforming bivalent ligands into retractable enzyme inhibitors through polypeptide-protein interactions.

Tolkatchev D, Vinogradova A, Ni F. Tolkatchev D, et al. Bioorg Med Chem Lett. 2005 Dec 1;15(23):5120-3. doi: 10.1016/j.bmcl.2005.08.085. Epub 2005 Oct 3. Bioorg Med Chem Lett. 2005. PMID: 16202582

10

Design of hetero-bivalent polypeptides as kinetics-based sensors for high-sensitivity detection of weak molecular interactions.

Tonan K, Tolkatchev D, Xu P, Wang P, Plamondon J, Vinogradova A, Gingras R, Ni F. Tonan K, et al. Among authors: tolkatchev d. Adv Exp Med Biol. 2009;611:425-6. doi: 10.1007/978-0-387-73657-0_183. Adv Exp Med Biol. 2009. PMID: 19400250 No abstract available.

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