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Functional expression and site-directed mutagenesis of photoactive yellow protein.
Mihara K, Hisatomi O, Imamoto Y, Kataoka M, Tokunaga F. Mihara K, et al. Among authors: kataoka m. J Biochem. 1997 May;121(5):876-80. doi: 10.1093/oxfordjournals.jbchem.a021668. J Biochem. 1997. PMID: 9192728
Alteration of conformation and dynamics of bacteriorhodopsin induced by protonation of Asp 85 and deprotonation of Schiff base as studied by 13C NMR.
Kawase Y, Tanio M, Kira A, Yamaguchi S, Tuzi S, Naito A, Kataoka M, Lanyi JK, Needleman R, Saitô H. Kawase Y, et al. Among authors: kataoka m. Biochemistry. 2000 Nov 28;39(47):14472-80. doi: 10.1021/bi0015820. Biochemistry. 2000. PMID: 11087400
According to previous X-ray diffraction studies, the D85N mutant of bacteriorhodopsin (bR) with unprotonated Schiff base assumes a protein conformation similar to that in the M photointermediate. ...Further, we found that in the M-like state the charged state of Asp …
According to previous X-ray diffraction studies, the D85N mutant of bacteriorhodopsin (bR) with unprotonated Schiff base assumes a protein c …
Direct observation of three conformations of MutS protein regulated by adenine nucleotides.
Kato R, Kataoka M, Kamikubo H, Kuramitsu S. Kato R, et al. Among authors: kataoka m. J Mol Biol. 2001 May 25;309(1):227-38. doi: 10.1006/jmbi.2001.4752. J Mol Biol. 2001. PMID: 11491292
Structure of the N intermediate of bacteriorhodopsin revealed by x-ray diffraction.
Kamikubo H, Kataoka M, Váró G, Oka T, Tokunaga F, Needleman R, Lanyi JK. Kamikubo H, et al. Among authors: kataoka m. Proc Natl Acad Sci U S A. 1996 Feb 20;93(4):1386-90. doi: 10.1073/pnas.93.4.1386. Proc Natl Acad Sci U S A. 1996. PMID: 8643641 Free PMC article.
The observed diffraction changes between N and the original state were essentially identical to the diffraction changes reported for the M intermediate of the D96N mutant of bacteriorhodopsin. Thus, we find that the protein conformations of the M and N intermediates …
The observed diffraction changes between N and the original state were essentially identical to the diffraction changes reported for the …
Intermediate conformational states of apocytochrome c.
Hamada D, Hoshino M, Kataoka M, Fink AL, Goto Y. Hamada D, et al. Among authors: kataoka m. Biochemistry. 1993 Oct 5;32(39):10351-8. doi: 10.1021/bi00090a010. Biochemistry. 1993. PMID: 8399178
Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding.
Nishii I, Kataoka M, Tokunaga F, Goto Y. Nishii I, et al. Among authors: kataoka m. Biochemistry. 1994 Apr 26;33(16):4903-9. doi: 10.1021/bi00182a019. Biochemistry. 1994. PMID: 8161550
Energy coupling in an ion pump. The reprotonation switch of bacteriorhodopsin.
Kataoka M, Kamikubo H, Tokunaga F, Brown LS, Yamazaki Y, Maeda A, Sheves M, Needleman R, Lanyi JK. Kataoka M, et al. J Mol Biol. 1994 Nov 4;243(4):621-38. doi: 10.1016/0022-2836(94)90037-x. J Mol Biol. 1994. PMID: 7966287
Reconstitution photoactive yellow protein from apoprotein and p-coumaric acid derivatives.
Imamoto Y, Ito T, Kataoka M, Tokunaga F. Imamoto Y, et al. Among authors: kataoka m. FEBS Lett. 1995 Oct 30;374(2):157-60. doi: 10.1016/0014-5793(95)01096-w. FEBS Lett. 1995. PMID: 7589524
Conformational change of helix G in the bacteriorhodopsin photocycle: investigation with heavy atom labeling and x-ray diffraction.
Oka T, Kamikubo H, Tokunaga F, Lanyi JK, Needleman R, Kataoka M. Oka T, et al. Among authors: kataoka m. Biophys J. 1999 Feb;76(2):1018-23. doi: 10.1016/S0006-3495(99)77266-8. Biophys J. 1999. PMID: 9916033 Free PMC article.
Photoreaction cycle of photoactive yellow protein from Ectothiorhodospira halophila studied by low-temperature spectroscopy.
Imamoto Y, Kataoka M, Tokunaga F. Imamoto Y, et al. Among authors: kataoka m. Biochemistry. 1996 Nov 12;35(45):14047-53. doi: 10.1021/bi961342d. Biochemistry. 1996. PMID: 8916889
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