Arata Y - Search Results

1

Effector functions of a mouse IgG that lacks the entire CH1 domain. C1q binding and complement fixation in the absence of antigen.

Mizutani R, Igarashi T, Tanaka T, Shimada I, Arata Y. Mizutani R, et al. Among authors: arata y. J Immunol. 1993 Jan 1;150(1):131-8. J Immunol. 1993. PMID: 8417119

2

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

3

Post-translational modifications of immunoglobulin G: a mouse IgG variant that lacks the entire CH1 domain.

Masuda K, Yamaguchi Y, Kato K, Kim HH, Takahashi N, Shimada I, Arata Y. Masuda K, et al. Among authors: arata y. Mol Immunol. 1999 Oct-Nov;36(15-16):993-1003. doi: 10.1016/s0161-5890(99)00131-5. Mol Immunol. 1999. PMID: 10698303

4

Preparation of the Fv fragment from a short-chain mouse IgG2a anti-dansyl monoclonal antibody and use of selectively deuterated Fv analogues for two-dimensional 1H NMR analyses of the antigen-antibody interactions.

Takahashi H, Igarashi T, Shimada I, Arata Y. Takahashi H, et al. Among authors: arata y. Biochemistry. 1991 Mar 19;30(11):2840-7. doi: 10.1021/bi00225a016. Biochemistry. 1991. PMID: 1901020

The Fv fragment, a univalent antigen-binding unit with a molecular weight of 25,000, has successfully been prepared in high yield by limited proteolysis with clostripain of a short-chain mouse IgG2a anti-dansyl monoclonal antibody in which the entire CH1 domain is deleted [Igaras …

The Fv fragment, a univalent antigen-binding unit with a molecular weight of 25,000, has successfully been prepared in high yield by limited …

5

Structure of a mouse immunoglobulin G that lacks the entire CH1 domain: protein sequencing and small-angle X-ray scattering studies.

Igarashi T, Sato M, Katsube Y, Takio K, Tanaka T, Nakanishi M, Arata Y. Igarashi T, et al. Among authors: arata y. Biochemistry. 1990 Jun 19;29(24):5727-33. doi: 10.1021/bi00476a013. Biochemistry. 1990. PMID: 2116900

6

Proteolytic fragmentation with high specificity of mouse immunoglobulin G. Mapping of proteolytic cleavage sites in the hinge region.

Yamaguchi Y, Kim H, Kato K, Masuda K, Shimada I, Arata Y. Yamaguchi Y, et al. Among authors: arata y. J Immunol Methods. 1995 Apr 26;181(2):259-67. doi: 10.1016/0022-1759(95)00010-8. J Immunol Methods. 1995. PMID: 7745255

7

Comparative thermodynamic analyses of the Fv, Fab* and Fab fragments of anti-dansyl mouse monoclonal antibody.

Shimba N, Torigoe H, Takahashi H, Masuda K, Shimada I, Arata Y, Sarai A. Shimba N, et al. Among authors: arata y. FEBS Lett. 1995 Mar 6;360(3):247-50. doi: 10.1016/0014-5793(95)00113-n. FEBS Lett. 1995. PMID: 7883041 Free article.

8

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

9

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

10

Three-dimensional structures of the Fab fragment of murine N1G9 antibody from the primary immune response and of its complex with (4-hydroxy-3-nitrophenyl)acetate.

Mizutani R, Miura K, Nakayama T, Shimada I, Arata Y, Satow Y. Mizutani R, et al. Among authors: arata y. J Mol Biol. 1995 Nov 24;254(2):208-22. doi: 10.1006/jmbi.1995.0612. J Mol Biol. 1995. PMID: 7490744

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