Kato K - Search Results

1

[Molecular structural analyses of large proteins by NMR].

Kato K, Arata Y. Kato K, et al. Tanpakushitsu Kakusan Koso. 1992 Feb;37(3 Suppl):508-28. Tanpakushitsu Kakusan Koso. 1992. PMID: 1549726 Review. Japanese. No abstract available.

2

Multinuclear NMR study of the structure of the Fv fragment of anti-dansyl mouse IgG2a antibody.

Takahashi H, Odaka A, Kawaminami S, Matsunaga C, Kato K, Shimada I, Arata Y. Takahashi H, et al. Among authors: kato k. Biochemistry. 1991 Jul 2;30(26):6611-9. doi: 10.1021/bi00240a034. Biochemistry. 1991. PMID: 2054359

3

Application of 13C nuclear magnetic resonance spectroscopy to molecular structural analyses of antibody molecules.

Kato K, Matsunaga C, Nishimura Y, Waelchli M, Kainosho M, Arata Y. Kato K, et al. J Biochem. 1989 Jun;105(6):867-9. doi: 10.1093/oxfordjournals.jbchem.a122769. J Biochem. 1989. PMID: 2768215 Free article.

4

Application of 13C NMR spectroscopy to paratope mapping for larger antigen-Fab complexes.

Kim H, Kato K, Yamato S, Igarashi T, Matsunaga C, Ohtsuka H, Higuchi A, Nomura N, Noguchi H, Arata Y. Kim H, et al. Among authors: kato k. FEBS Lett. 1994 Jun 13;346(2-3):246-50. doi: 10.1016/0014-5793(94)00486-2. FEBS Lett. 1994. PMID: 8013642 Free article.

5

Molecular structural studies of effector functions of a mouse immunoglobulin G that lacks the entire CH1 domain: small-angle X-ray scattering, nanosecond fluorescence depolarization and stable isotope-aided NMR analyses.

Mizutani R, Matsunaga C, Kouyama T, Sato M, Katsube Y, Kato K, Shimada I, Arata Y. Mizutani R, et al. Among authors: kato k. Mol Immunol. 1993 Dec;30(18):1665-9. doi: 10.1016/0161-5890(93)90440-m. Mol Immunol. 1993. PMID: 8272079

6

13C NMR study of the mode of interaction in solution of the B fragment of staphylococcal protein A and the Fc fragments of mouse immunoglobulin G.

Kato K, Gouda H, Takaha W, Yoshino A, Matsunaga C, Arata Y. Kato K, et al. FEBS Lett. 1993 Aug 9;328(1-2):49-54. doi: 10.1016/0014-5793(93)80963-u. FEBS Lett. 1993. PMID: 8344434 Free article.

7

13C-NMR spectral analysis of the structures of mouse immunoglobulin G1 carrying allotypes a and j.

Kim H, Kato K, Higuchi A, Nomura N, Noguchi H, Arata Y. Kim H, et al. Among authors: kato k. J Immunol Methods. 1992 Aug 30;153(1-2):223-7. doi: 10.1016/0022-1759(92)90325-n. J Immunol Methods. 1992. PMID: 1517593

8

A 13C NMR study of the hinge region of a mouse monoclonal antibody.

Matsunaga C, Kato K, Arata Y. Matsunaga C, et al. Among authors: kato k. J Biomol NMR. 1991 Nov;1(4):379-90. doi: 10.1007/BF02192861. J Biomol NMR. 1991. PMID: 1841706

A 13C NMR study is reported of the hinge region of an intact mouse monoclonal antibody with a molecular weight of 150 K. Cys, Ile, and Pro analogs of the antibody labeled with 13C at the carbonyl carbon were prepared by growing hybridoma cells in the serum-free media. Reso …

A 13C NMR study is reported of the hinge region of an intact mouse monoclonal antibody with a molecular weight of 150 K. Cys, Ile, an …

9

Carbon-13 NMR study of switch variant anti-dansyl antibodies: antigen binding and domain-domain interactions.

Kato K, Matsunaga C, Odaka A, Yamato S, Takaha W, Shimada I, Arata Y. Kato K, et al. Biochemistry. 1991 Jul 2;30(26):6604-10. doi: 10.1021/bi00240a033. Biochemistry. 1991. PMID: 2054358

Spectral assignments have been made by following the procedure described previously for the switch variant antibodies labeled with [1-13C]Met [Kato, K., Matsunaga, C., Igarashi, T., Kim, H., Odaka, A., Shimada, I., & Arata, Y. (1991) Biochemistry 30, 270-278]. . …

Spectral assignments have been made by following the procedure described previously for the switch variant antibodies labeled with [1-13C]Me …

10

A 1H-NMR study of the solution conformation of Icaria chemotactic peptide and its [Lys7] analog: effects on the physiological activity of a substitution of proline to lysine at position 7.

Shimada I, Kato K, Saito K, Kitada C, Fujino M, Nakajima T, Arata Y. Shimada I, et al. Among authors: kato k. Biochem Biophys Res Commun. 1990 Apr 30;168(2):596-603. doi: 10.1016/0006-291x(90)92362-4. Biochem Biophys Res Commun. 1990. PMID: 2110453

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