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1. Bubis, J; Ortiz, JO; Moller, C
   Chemical modification of transducin with iodoacetic acid: Transducin-alphacarboxymethylated at Cys(347) allows transducin binding to light-activatedrhodopsin but prevents its release in the presence of GTP
   ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
   
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2. Meng, EC; Bourne, HR
   Receptor activation: what does the rhodopsin structure tell us?
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   Molecular biology of light transduction by the mammalian photoreceptor, rhodopsin
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   Structural aspects of the G-protein receptor, rhodopsin
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5. Abdulaev, NG; Ngo, T; Chen, RW; Lu, ZJ; Ridge, KD
   Functionally discrete mimics of light-activated rhodopsin identified through expression of soluble cytoplasmic domains
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6. Bofill-Cardona, E; Kudlacek, O; Yang, Q; Ahorn, H; Freissmuth, M; Nanoff, C
   Binding of calmodulin to the D-2-dopamine receptor reduces receptor signaling by arresting the G protein activation switch
   JOURNAL OF BIOLOGICAL CHEMISTRY
   
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7. Gelasco, A; Crouch, RK; Knapp, DR
   Intrahelical arrangement in the integral membrane protein rhodopsin investigated by site-specific chemical cleavage and mass spectrometry
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   Biophysical approaches to G protein-coupled receptors: Structure, functionand dynamics
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9. Klein-Seetharaman, J; Getmanova, EV; Loewen, MC; Reeves, PJ; Khorana, HG
   NMR spectroscopy in studies of light-induced structural changes in mammalian rhodopsin: Applicability of solution F-19 NMR
   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
   
   J. Klein-Seetharaman et al., "NMR spectroscopy in studies of light-induced structural changes in mammalian rhodopsin: Applicability of solution F-19 NMR", P NAS US, 96(24), 1999, pp. 13744-13749
10. Cai, K; Klein-Seetharaman, J; Hwa, J; Hubbell, WL; Khorana, HG
    Structure and function in rhodopsin: Effects of disulfide cross-links in the cytoplasmic face of rhodopsin on transducin activation and phosphorylation by rhodopsin kinase
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    K. Cai et al., "Structure and function in rhodopsin: Effects of disulfide cross-links in the cytoplasmic face of rhodopsin on transducin activation and phosphorylation by rhodopsin kinase", BIOCHEM, 38(39), 1999, pp. 12893-12898
11. Yu, HB; Oprian, DD
    Tertiary interactions between transmembrane segments 3 and 5 near the cytoplasmic side of rhodopsin
    BIOCHEMISTRY
    
    H.B. Yu e D.D. Oprian, "Tertiary interactions between transmembrane segments 3 and 5 near the cytoplasmic side of rhodopsin", BIOCHEM, 38(37), 1999, pp. 12033-12040
12. Langen, R; Cai, KW; Altenbach, C; Khorana, HG; Hubbell, WL
    Structural features of the C-terminal domain of bovine rhodopsin: A site-directed spin-labeling study
    BIOCHEMISTRY
    
    R. Langen et al., "Structural features of the C-terminal domain of bovine rhodopsin: A site-directed spin-labeling study", BIOCHEM, 38(25), 1999, pp. 7918-7924
13. Cai, KW; Klein-Seetharaman, J; Farrens, D; Zhang, C; Altenbach, C; Hubbell, WL; Khorana, HG
    Single-cysteine substitution mutants at amino acid positions 306-321 in rhodopsin, the sequence between the cytoplasmic end of helix VII and the palmitoylation sites: Sulfhydryl reactivity and transducin activation reveal a tertiary structure
    BIOCHEMISTRY
    
    K.W. Cai et al., "Single-cysteine substitution mutants at amino acid positions 306-321 in rhodopsin, the sequence between the cytoplasmic end of helix VII and the palmitoylation sites: Sulfhydryl reactivity and transducin activation reveal a tertiary structure", BIOCHEM, 38(25), 1999, pp. 7925-7930
14. Altenbach, C; Cai, KW; Khorana, HG; Hubbell, WL
    Structural features and light-dependent changes in the sequence 306-322 extending from helix VII to the palmitoylation sites in rhodopsin: A site-directed spin-labeling study
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    C. Altenbach et al., "Structural features and light-dependent changes in the sequence 306-322 extending from helix VII to the palmitoylation sites in rhodopsin: A site-directed spin-labeling study", BIOCHEM, 38(25), 1999, pp. 7931-7937
15. Klein-Seetharaman, J; Hwa, J; Cai, KW; Altenbach, C; Hubbell, WL; Khorana, HG
    Single-cysteine substitution mutants at amino acid positions 55-75, the sequence connecting the cytoplasmic ends of helices I and II in rhodopsin: Reactivity of the sulfhydryl groups and their derivatives identifies a tertiary structure that changes upon light-activation
    BIOCHEMISTRY
    
    J. Klein-Seetharaman et al., "Single-cysteine substitution mutants at amino acid positions 55-75, the sequence connecting the cytoplasmic ends of helices I and II in rhodopsin: Reactivity of the sulfhydryl groups and their derivatives identifies a tertiary structure that changes upon light-activation", BIOCHEM, 38(25), 1999, pp. 7938-7944
16. Altenbach, C; Klein-Seetharaman, J; Hwa, J; Khorana, HG; Hubbell, WL
    Structural features and light-dependent changes in the sequence 59-75 connecting helices I and II in rhodopsin: A site-directed spin-labeling study
    BIOCHEMISTRY
    
    C. Altenbach et al., "Structural features and light-dependent changes in the sequence 59-75 connecting helices I and II in rhodopsin: A site-directed spin-labeling study", BIOCHEM, 38(25), 1999, pp. 7945-7949
17. ABDULAEV NG; RIDGE KD
    LIGHT-INDUCED EXPOSURE OF THE CYTOPLASMIC END OF TRANSMEMBRANE HELIX-7 IN RHODOPSIN
    Proceedings of the National Academy of Sciences of the United Statesof America
    
    N.G. Abdulaev e K.D. Ridge, "LIGHT-INDUCED EXPOSURE OF THE CYTOPLASMIC END OF TRANSMEMBRANE HELIX-7 IN RHODOPSIN", Proceedings of the National Academy of Sciences of the United Statesof America, 95(22), 1998, pp. 12854-12859
18. KONVICKA K; GUARNIERI F; BALLESTEROS JA; WEINSTEIN H
    A PROPOSED STRUCTURE FOR TRANSMEMBRANE SEGMENT-7 OF G-PROTEIN-COUPLEDRECEPTORS INCORPORATING AN ASN-PRO ASP-PRO MOTIF/
    Biophysical journal
    
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19. KIM JM; ALTENBACH C; THURMOND RL; KHORANA HG; HUBBELL WL
    STRUCTURE AND FUNCTION IN RHODOPSIN - RHODOPSIN MUTANTS WITH A NEUTRAL AMINO-ACID AT E134 HAVE A PARTIALLY ACTIVATED CONFORMATION IN THE DARK STATE
    Proceedings of the National Academy of Sciences of the United Statesof America
    
    J.M. Kim et al., "STRUCTURE AND FUNCTION IN RHODOPSIN - RHODOPSIN MUTANTS WITH A NEUTRAL AMINO-ACID AT E134 HAVE A PARTIALLY ACTIVATED CONFORMATION IN THE DARK STATE", Proceedings of the National Academy of Sciences of the United Statesof America, 94(26), 1997, pp. 14273-14278