Shichida Y - Search Results

1

Structures of aspartic acid-96 in the L and N intermediates of bacteriorhodopsin: analysis by Fourier transform infrared spectroscopy.

Maeda A, Sasaki J, Shichida Y, Yoshizawa T, Chang M, Ni B, Needleman R, Lanyi JK. Maeda A, et al. Among authors: shichida y. Biochemistry. 1992 May 19;31(19):4684-90. doi: 10.1021/bi00134a022. Biochemistry. 1992. PMID: 1316157

2

Protein changes associated with reprotonation of the Schiff base in the photocycle of Asp96-->Asn bacteriorhodopsin. The MN intermediate with unprotonated Schiff base but N-like protein structure.

Sasaki J, Shichida Y, Lanyi JK, Maeda A. Sasaki J, et al. Among authors: shichida y. J Biol Chem. 1992 Oct 15;267(29):20782-6. J Biol Chem. 1992. PMID: 1400394 Free article.

3

Water structural changes in the bacteriorhodopsin photocycle: analysis by Fourier transform infrared spectroscopy.

Maeda A, Sasaki J, Shichida Y, Yoshizawa T. Maeda A, et al. Among authors: shichida y. Biochemistry. 1992 Jan 21;31(2):462-7. doi: 10.1021/bi00117a023. Biochemistry. 1992. PMID: 1731905

4

Difference in molecular properties between chicken green and rhodopsin as related to the functional difference between cone and rod photoreceptor cells.

Imai H, Imamoto Y, Yoshizawa T, Shichida Y. Imai H, et al. Among authors: shichida y. Biochemistry. 1995 Aug 22;34(33):10525-31. doi: 10.1021/bi00033a026. Biochemistry. 1995. PMID: 7654707

5

Water structural changes in lumirhodopsin, metarhodopsin I, and metarhodopsin II upon photolysis of bovine rhodopsin: analysis by Fourier transform infrared spectroscopy.

Maeda A, Ohkita YJ, Sasaki J, Shichida Y, Yoshizawa T. Maeda A, et al. Among authors: shichida y. Biochemistry. 1993 Nov 16;32(45):12033-8. doi: 10.1021/bi00096a013. Biochemistry. 1993. PMID: 8218280

This is similar to the case of photoreaction of bacteriorhodopsin, in which stronger hydrogen bonding of water is formed in the L intermediate than the M intermediate [Maeda, A., Sasaki, J., Shichida, Y., & Yoshizawa, T. (1992) Biochemistry 31, 462-467]....

This is similar to the case of photoreaction of bacteriorhodopsin, in which stronger hydrogen bonding of water is formed in the L intermedia …

6

Water and peptide backbone structure in the active center of bovine rhodopsin.

Nagata T, Terakita A, Kandori H, Kojima D, Shichida Y, Maeda A. Nagata T, et al. Among authors: shichida y. Biochemistry. 1997 May 20;36(20):6164-70. doi: 10.1021/bi962920t. Biochemistry. 1997. PMID: 9166788

7

The hydrogen-bonding network of water molecules and the peptide backbone in the region connecting Asp83, Gly120, and Glu113 in bovine rhodopsin.

Nagata T, Terakita A, Kandori H, Shichida Y, Maeda A. Nagata T, et al. Among authors: shichida y. Biochemistry. 1998 Dec 8;37(49):17216-22. doi: 10.1021/bi9810149. Biochemistry. 1998. PMID: 9860835

Previous studies [Nagata, T., Terakita, A., Kandori, H., Kojima, D., Shichida, Y., and Maeda, A. (1997) Biochemistry 36, 6164-6170] showed that one of the water molecules which undergoes structural changes in this process forms hydrogen bonds with Glu113 and the Sch …

Previous studies [Nagata, T., Terakita, A., Kandori, H., Kojima, D., Shichida, Y., and Maeda, A. (1997) Biochemistry 36, 6164- …

8

Structural change of threonine 89 upon photoisomerization in bacteriorhodopsin as revealed by polarized FTIR spectroscopy.

Kandori H, Kinoshita N, Yamazaki Y, Maeda A, Shichida Y, Needleman R, Lanyi JK, Bizounok M, Herzfeld J, Raap J, Lugtenburg J. Kandori H, et al. Among authors: shichida y. Biochemistry. 1999 Jul 27;38(30):9676-83. doi: 10.1021/bi990713y. Biochemistry. 1999. PMID: 10423246

9

Effect of anion binding on iodopsin studied by low-temperature fourier transform infrared spectroscopy.

Imamoto Y, Hirano T, Imai H, Kandori H, Maeda A, Yoshizawa T, Groesbeek M, Lugtenburg J, Shichida Y. Imamoto Y, et al. Among authors: shichida y. Biochemistry. 1999 Sep 7;38(36):11749-54. doi: 10.1021/bi990587y. Biochemistry. 1999. PMID: 10512631

10

Photocycle of phoborhodopsin from haloalkaliphilic bacterium (Natronobacterium pharaonis) studied by low-temperature spectrophotometry.

Hirayama J, Imamoto Y, Shichida Y, Kamo N, Tomioka H, Yoshizawa T. Hirayama J, et al. Among authors: shichida y. Biochemistry. 1992 Feb 25;31(7):2093-8. doi: 10.1021/bi00122a029. Biochemistry. 1992. PMID: 1536851

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