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PUBMED FOR HANDHELDS

Journal Abstract Search


1096 related items for PubMed ID: 16939215

  • 1. Hydrogen-bonding interaction of the protonated schiff base with halides in a chloride-pumping bacteriorhodopsin mutant.
    Shibata M, Ihara K, Kandori H.
    Biochemistry; 2006 Sep 05; 45(35):10633-40. PubMed ID: 16939215
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  • 6. Strongly hydrogen-bonded water molecule present near the retinal chromophore of Leptosphaeria rhodopsin, the bacteriorhodopsin-like proton pump from a eukaryote.
    Sumii M, Furutani Y, Waschuk SA, Brown LS, Kandori H.
    Biochemistry; 2005 Nov 22; 44(46):15159-66. PubMed ID: 16285719
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  • 8. FTIR spectroscopy of the K photointermediate of Neurospora rhodopsin: structural changes of the retinal, protein, and water molecules after photoisomerization.
    Furutani Y, Bezerra AG, Waschuk S, Sumii M, Brown LS, Kandori H.
    Biochemistry; 2004 Aug 03; 43(30):9636-46. PubMed ID: 15274618
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  • 9. Structural changes in bacteriorhodopsin following retinal photoisomerization from the 13-cis form.
    Mizuide N, Shibata M, Friedman N, Sheves M, Belenky M, Herzfeld J, Kandori H.
    Biochemistry; 2006 Sep 05; 45(35):10674-81. PubMed ID: 16939219
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  • 11. Relocation of water molecules between the Schiff base and the Thr46-Asp96 region during light-driven unidirectional proton transport by bacteriorhodopsin: an FTIR study of the N intermediate.
    Maeda A, Gennis RB, Balashov SP, Ebrey TG.
    Biochemistry; 2005 Apr 26; 44(16):5960-8. PubMed ID: 15835885
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  • 12. Low-temperature FTIR study of Gloeobacter rhodopsin: presence of strongly hydrogen-bonded water and long-range structural protein perturbation upon retinal photoisomerization.
    Hashimoto K, Choi AR, Furutani Y, Jung KH, Kandori H.
    Biochemistry; 2010 Apr 20; 49(15):3343-50. PubMed ID: 20230053
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  • 13. Strongly hydrogen-bonded water molecules in the Schiff base region of rhodopsins.
    Furutani Y, Shibata M, Kandori H.
    Photochem Photobiol Sci; 2005 Sep 20; 4(9):661-6. PubMed ID: 16121274
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  • 18. Structural changes of water molecules during the photoactivation processes in bovine rhodopsin.
    Furutani Y, Shichida Y, Kandori H.
    Biochemistry; 2003 Aug 19; 42(32):9619-25. PubMed ID: 12911303
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  • 20. Structural changes in the Schiff base region of squid rhodopsin upon photoisomerization studied by low-temperature FTIR spectroscopy.
    Ota T, Furutani Y, Terakita A, Shichida Y, Kandori H.
    Biochemistry; 2006 Mar 07; 45(9):2845-51. PubMed ID: 16503639
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