Arata Y - Search Results

1

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. Among authors: arata y. 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]. O …

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

2

Role of the domain-domain interaction in the construction of the antigen combining site. A comparative study by 1H-15N shift correlation NMR spectroscopy of the Fv and Fab fragments of anti-dansyl mouse monoclonal antibody.

Takahashi H, Tamura H, Shimba N, Shimada I, Arata Y. Takahashi H, et al. Among authors: arata y. J Mol Biol. 1994 Oct 28;243(3):494-503. doi: 10.1006/jmbi.1994.1675. J Mol Biol. 1994. PMID: 7966275

3

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: arata y. 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.

4

Dynamical structure of the hinge region of immunoglobulin G as studied by 13C nuclear magnetic resonance spectroscopy.

Kim H, Matsunaga C, Yoshino A, Kato K, Arata Y. Kim H, et al. Among authors: arata y. J Mol Biol. 1994 Feb 11;236(1):300-9. doi: 10.1006/jmbi.1994.1136. J Mol Biol. 1994. PMID: 8107111

5

Solution conformation of an antibacterial peptide, sarcotoxin IA, as determined by 1H-NMR.

Iwai H, Nakajima Y, Natori S, Arata Y, Shimada I. Iwai H, et al. Among authors: arata y. Eur J Biochem. 1993 Oct 15;217(2):639-44. doi: 10.1111/j.1432-1033.1993.tb18287.x. Eur J Biochem. 1993. PMID: 8223606 Free article.

6

A multinuclear NMR study of the affinity maturation of anti-NP mouse monoclonal antibodies: comparison of antibody combining sites of primary response antibody N1G9 and secondary response antibody 3B62.

Nakayama T, Arata Y, Shimada I. Nakayama T, et al. Among authors: arata y. Biochemistry. 1993 Dec 21;32(50):13961-8. doi: 10.1021/bi00213a028. Biochemistry. 1993. PMID: 8268173

7

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: arata y. Mol Immunol. 1993 Dec;30(18):1665-9. doi: 10.1016/0161-5890(93)90440-m. Mol Immunol. 1993. PMID: 8272079

8

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. Among authors: arata y. 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.

9

Folding topologies of human interleukin-6 and its mutants as studied by NMR spectroscopy.

Nishimura C, Watanabe A, Gouda H, Shimada I, Arata Y. Nishimura C, et al. Among authors: arata y. Biochemistry. 1996 Jan 9;35(1):273-81. doi: 10.1021/bi951949e. Biochemistry. 1996. PMID: 8555185

10

NMR study of the interaction between the B domain of staphylococcal protein A and the Fc portion of immunoglobulin G.

Gouda H, Shiraishi M, Takahashi H, Kato K, Torigoe H, Arata Y, Shimada I. Gouda H, et al. Among authors: arata y. Biochemistry. 1998 Jan 6;37(1):129-36. doi: 10.1021/bi970923f. Biochemistry. 1998. PMID: 9425032

A previous NMR analysis has shown that in solution FB is composed of a bundle of three alpha-helices, helix I, helix II, and helix III [Gouda, H., Torigoe, H., Saito, A., Sato, M., Arata, Y., and Shimada, I. (1992) Biochemistry 31, 9665-9672]. In contrast, the cryst …

A previous NMR analysis has shown that in solution FB is composed of a bundle of three alpha-helices, helix I, helix II, and helix III [Goud …

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