% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Yanamala:5186,
      author       = {Yanamala, N. and Tirupula, K.C. and Balem, F. and
                      Klein-Seetharaman, J.},
      title        = {p{H}-dependent {I}nteraction of {R}hodopsin with
                      {C}yanidin-3-glucoside. 1. {S}tructural {A}spects},
      journal      = {Photochemistry and photobiology},
      volume       = {85},
      number       = {2},
      issn         = {0031-8655},
      address      = {Malden, Mass.},
      publisher    = {Wiley-Blackwell},
      reportid     = {PreJuSER-5186},
      pages        = {454 - 462},
      year         = {2009},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Anthocyanins are a class of phytochemicals that confer
                      color to flowers, fruits, vegetables and leaves. They are
                      part of our regular diet and serve as dietary supplements
                      because of numerous health benefits, including improved
                      vision. Recent studies have shown that the anthocyanin
                      cyanidin-3-O-glucoside (C3G) increased regeneration of the
                      dim-light photoreceptor rhodopsin (Matsumoto et al. [2003]
                      J. Agric. Food Chem., 51, 3560-3563). In an accompanying
                      study (Yanamala et al. [2009] Photochem. Photobiol.), we
                      show that C3G directly binds to rhodopsin in a pH-dependent
                      manner. In this study, we investigated the functional
                      consequences of C3G binding to rhodopsin. As observed
                      previously in rod outer segments, regeneration of purified
                      rhodopsin in detergent micelles is also accelerated in the
                      presence of C3G. Thermal denaturation and stability studies
                      using circular dichroism, fluorescence and UV/visible
                      absorbance spectroscopy show that C3G exerts a destabilizing
                      effect on rhodopsin structure while it only modestly alters
                      G-protein activation and the rates at which the
                      light-activated Metarhodopsin II state decays to opsin and
                      free retinal. These results indicate that the mechanism of
                      C3G-enhanced regeneration may be based on changes in opsin
                      structure promoting access to the retinal binding pocket.},
      keywords     = {Animals / Anthocyanins: chemistry / Anthocyanins:
                      metabolism / Cattle / Enzyme Activation / GTP-Binding
                      Proteins: metabolism / Glucosides: chemistry / Glucosides:
                      metabolism / Hydrogen-Ion Concentration / Protein Binding /
                      Protein Structure, Secondary / Rhodopsin: chemistry /
                      Rhodopsin: isolation $\&$ purification / Rhodopsin:
                      metabolism / Anthocyanins (NLM Chemicals) / Glucosides (NLM
                      Chemicals) / cyanidin 3-O-glucoside (NLM Chemicals) /
                      Rhodopsin (NLM Chemicals) / GTP-Binding Proteins (NLM
                      Chemicals) / J (WoSType)},
      cin          = {ISB-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ISB-2-20090406},
      pnm          = {Programm Biosoft},
      pid          = {G:(DE-Juel1)FUEK443},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19267871},
      UT           = {WOS:000266034900007},
      doi          = {10.1111/j.1751-1097.2008.00517.x},
      url          = {https://juser.fz-juelich.de/record/5186},
}