Ikura M - Search Results

1

Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible.

Barbato G, Ikura M, Kay LE, Pastor RW, Bax A. Barbato G, et al. Among authors: ikura m. Biochemistry. 1992 Jun 16;31(23):5269-78. doi: 10.1021/bi00138a005. Biochemistry. 1992. PMID: 1606151

2

Solution structure of calmodulin and its complex with a myosin light chain kinase fragment.

Ikura M, Barbato G, Klee CB, Bax A. Ikura M, et al. Cell Calcium. 1992 Jun-Jul;13(6-7):391-400. doi: 10.1016/0143-4160(92)90052-t. Cell Calcium. 1992. PMID: 1505004

3

Solution structure of a calmodulin-target peptide complex by multidimensional NMR.

Ikura M, Clore GM, Gronenborn AM, Zhu G, Klee CB, Bax A. Ikura M, et al. Science. 1992 May 1;256(5057):632-8. doi: 10.1126/science.1585175. Science. 1992. PMID: 1585175

4

An efficient 3D NMR technique for correlating the proton and 15N backbone amide resonances with the alpha-carbon of the preceding residue in uniformly 15N/13C enriched proteins.

Bax A, Ikura M. Bax A, et al. Among authors: ikura m. J Biomol NMR. 1991 May;1(1):99-104. doi: 10.1007/BF01874573. J Biomol NMR. 1991. PMID: 1668719

5

Multidimensional triple resonance NMR spectroscopy of isotopically uniformly enriched proteins: a powerful new strategy for structure determination.

Bax A, Ikura M, Kay LE, Barbato G, Spera S. Bax A, et al. Among authors: ikura m. Ciba Found Symp. 1991;161:108-19; discussion 119-35. doi: 10.1002/9780470514146.ch8. Ciba Found Symp. 1991. PMID: 1814691

6

Improved three-dimensional 1H-13C-1H correlation spectroscopy of a 13C-labeled protein using constant-time evolution.

Ikura M, Kay LE, Bax A. Ikura M, et al. J Biomol NMR. 1991 Sep;1(3):299-304. doi: 10.1007/BF01875522. J Biomol NMR. 1991. PMID: 1841700

7

Secondary structure and side-chain 1H and 13C resonance assignments of calmodulin in solution by heteronuclear multidimensional NMR spectroscopy.

Ikura M, Spera S, Barbato G, Kay LE, Krinks M, Bax A. Ikura M, et al. Biochemistry. 1991 Sep 24;30(38):9216-28. doi: 10.1021/bi00102a013. Biochemistry. 1991. PMID: 1909892

8

Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: indication of a conformational change in the central helix.

Ikura M, Kay LE, Krinks M, Bax A. Ikura M, et al. Biochemistry. 1991 Jun 4;30(22):5498-504. doi: 10.1021/bi00236a024. Biochemistry. 1991. PMID: 2036419

Comparison of the chemical shift values with those observed in peptide-free calmodulin [Ikura, M., Kay, L. E., & Bax, A. (1990) Biochemistry 29, 4659-4667] shows that binding of M13 peptide induces substantial chemical shift changes that are not localized in one …

Comparison of the chemical shift values with those observed in peptide-free calmodulin [Ikura, M., Kay, L. E., & Bax, A. ( …

9

Heteronuclear 3D NMR and isotopic labeling of calmodulin. Towards the complete assignment of the 1H NMR spectrum.

Ikura M, Marion D, Kay LE, Shih H, Krinks M, Klee CB, Bax A. Ikura M, et al. Biochem Pharmacol. 1990 Jul 1;40(1):153-60. doi: 10.1016/0006-2952(90)90190-v. Biochem Pharmacol. 1990. PMID: 2372304

10

A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin.

Ikura M, Kay LE, Bax A. Ikura M, et al. Biochemistry. 1990 May 15;29(19):4659-67. doi: 10.1021/bi00471a022. Biochemistry. 1990. PMID: 2372549

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