cysteine and 11-cis-retinal

cysteine has been researched along with 11-cis-retinal in 95 studies

Research

Studies (95)

Timeframe	Studies, this research(%)	All Research%
pre-1990	3 (3.16)	18.7374
1990's	34 (35.79)	18.2507
2000's	45 (47.37)	29.6817
2010's	11 (11.58)	24.3611
2020's	2 (2.11)	2.80

Authors

Authors	Studies
Büllesbach, EE; Crouch, RK; Knapp, DR; Papac, DI; Thornburg, KR	1
Cerione, RA; Phillips, WJ	1
Karnik, SS; Khorana, HG	1
Chen, HB; Karnik, SS; Khorana, HG; Sakmar, TP	1
Abdulaev, NG; Bogachuk, AS	1
Argos, P; Curtis, DR; Feldmann, RJ; Fong, SL; Hargrave, PA; Kühn, H; McDowell, JH; Mohana Rao, JK; Siemiatkowski-Juszczak, EC; Wang, JK	1
Kono, M; McKee, TD; Oprian, DD; Yu, H	1
Khorana, HG; Ridge, KD; Zhang, C	1
Dunlop, J; Finbow, ME; Jones, PC	1
Morrison, DF; O'Brien, PJ; Pepperberg, DR	1
Richards, JE; Scott, KM; Sieving, PA	1
Khorana, HG; Liu, X; Lu, Z; Ridge, KD	1
Farrens, DL; Khorana, HG	1
Boelens, R; Crielaard, W; Devreese, B; Düx, P; Hård, K; Hellingwerf, KJ; Hoff, WD; Kaptein, R; Nugteren-Roodzant, IM; van Beeumen, J	1
Bovee-Geurts, PH; DeGrip, WJ; Rath, P; Rothschild, KJ	1
Davidson, FF; Khorana, HG; Loewen, PC	1
Farahbakhsh, ZT; Hubbell, WL; Khorana, HG; Resek, JF	1
Bhattacharya, S; Karnik, SS; Khorana, HG; Ridge, KD	1
Farrens, DL; Hubbell, WL; Khorana, HG; Yang, K	1
Schwemer, J; Steinhoff, HJ	1
Altenbach, C; Farrens, DL; Hubbell, WL; Khorana, HG; Yang, K	1
Altenbach, C; Farahbakhsh, ZT; Farrens, DL; Hubbell, WL; Khorana, HG; Yang, K	1
Bazan, NG; Deretic, D; Papermaster, DS; Rodriguez de Turco, EB	1
Albert, AD; Groebner, G; Spooner, P; Watts, A; Yeagle, PL; Young, J	1
Benovic, JL; Loudon, RP	1
Cai, K; Hubbell, WL; Khorana, HG; Langen, R	1
Kono, M; Oprian, DD; Yu, H	2
Ball, LE; Busman, M; Chen, N; Cowden, LB; Crouch, RK; Dharmasiri, K; Galijatovic, A; Knapp, DR; Oatis, JE; Wang, J	1
Dunham, TD; Farrens, DL	1
Davidson, F; Hwa, J; Khorana, HG; Klein-Seetharaman, J; Reeves, PJ	1
Kono, M; Oprian, DD; Struthers, M; Yu, H	1
Altenbach, C; Cai, K; Hubbell, WL; Khorana, HG; Langen, R	1
Altenbach, C; Cai, K; Farrens, D; Hubbell, WL; Khorana, HG; Klein-Seetharaman, J; Zhang, C	1
Altenbach, C; Cai, K; Hubbell, WL; Hwa, J; Khorana, HG; Klein-Seetharaman, J	2
Oprian, DD; Yu, H	1
Getmanova, EV; Khorana, HG; Klein-Seetharaman, J; Loewen, MC; Reeves, PJ	1
Akhtar, M; McCarthy, NE	1
Oprian, DD; Struthers, M	1
Crouch, RK; Gelasco, A; Knapp, DR	1
Aris, L; Dratz, EA; Gilchrist, A; Hamm, HE; Meyer, C; Rens-Domiano, S; Schatz, PJ	1
Imamoto, Y; Kataoka, M; Palczewski, K; Tokunaga, F	1
Brown, LS; Lanyi, JK; Needleman, R; Shin, YK; Xiao, W	1
Birch, DG; Bowne, SJ; Daiger, SP; Heckenlively, JR; Lewis, RA; Mintz-Hittner, H; Northrup, H; Rodriquez, JA; Ruiz, RS; Saperstein, DA; Sohocki, MM; Sullivan, LS	1
Hwa, J; Khorana, HG; Klein-Seetharaman, J	1
Cai, K; Itoh, Y; Khorana, HG	2
Getmanova, EV; Khorana, HG; Klein-Seetharaman, J; Loewen, MC; Reeves, PJ; Schwalbe, H	1
Ballesteros, JA; Javitch, JA; Shi, L	1
Altenbach, C; Cai, K; Hubbell, WL; Khorana, HG; Klein-Seetharaman, J	3
Bubis, J; Möller, C; Ortiz, JO	1
Arimoto, R; Kisselev, OG; Makara, GM; Marshall, GR	1
Edwards, PC; Heyn, MP; Mielke, T; Schertler, GF; Villa, C	1
Alexiev, U; Braiman, MS; DeVita, AM; Krebs, RA; Partha, R	1
Alexiev, U; Gläsel, M; Heyn, MP; Mielke, T; Otto, H	1
Bovee-Geurts, PH; Breikers, G; DeGrip, WJ; Portier-VandeLuytgaarden, MJ	1
Klein-Seetharaman, J	1
Kobilka, BK	1
Gross, AK; Oprian, DD; Xie, G	1
Marshall, GR; Nikiforovich, GV	1
Colmenares, LU; Liu, RS	1
Friedman, N; Getmanova, E; Khorana, HG; Klein-Seetharaman, J; Loewen, MC; Patel, AB; Reeves, PJ; Sheves, M; Smith, SO	1
Belusic, G; Brenner-Weiss, G; Franz, C; Hartmann, K; Huber, A; Kühl, B; Paulsen, R; Schillo, S	1
Bezerra, AG; Brown, LS; Furutani, Y; Kandori, H; Sumii, M; Waschuk, S	1
Barnett-Norris, J; Hurst, DP; Reggio, PH; Song, ZH; Zhang, R	1
Ablonczy, Z; Crouch, RK; Lem, J; Makino, CL; Wang, Z; Wen, XH	1
Ablonczy, Z; Crouch, RK; Knapp, DR	1
Engel, A; Filipek, S; Müller, DJ; Palczewski, K; Park, PS; Tanuj Sapra, K	1
Francis, DJ; Gurevich, VV; Hanson, SM; Hubbell, WL; Klug, CS; Kolobova, EA; Vishnivetskiy, SA	1
Ayson, MJ; Hong, J; Jacobsen, RB; Kruppa, GH; Lane, P; Novak, P; Sale, KL; Schoeniger, JS; Wood, NL; Young, MM	1
Angel, TE; Dratz, EA; Kraft, PC	1
Berson, EL; Dryja, TP; Rivolta, C	1
Filipek, S; Koliński, M; Muller, DJ; Palczewski, K; Park, PS; Sapra, KT	1
Avlani, VA; Christopoulos, A; Gregory, KJ; Morton, CJ; Parker, MW; Sexton, PM	1
Farrens, DL; McDowell, JH; Smith, WC; Sommer, ME; Weber, LA	1
Barrett, R; Bush, RA; Dizhoor, AM; Fain, GL; Olshevskaya, EV; Peshenko, IV; Savchenko, AB; Sieving, PA; Woodruff, ML	1
Chen, Y; Holmes, AE; Nakanishi, K; Parr, T	1
Crouch, RK; Filipek, S; Jastrzebska, B; Kono, M; Lem, J; Maeda, A; Maeda, T; Müller, DJ; Palczewski, K; Park, PS; Pulawski, W; Sapra, KT	1
Alexiev, U; Dutta, A; Kim, TY; Klein-Seetharaman, J; Moeller, M; Wu, J	1
Khorana, HG; Kim, JM; Ou, WB; Yi, T	1
Brown, MF; Feller, SE; Grossfield, A; Olausson, BE; Pitman, MC; Vogel, A	1
Huber, T; Knepp, AM; Marrink, SJ; Periole, X; Sakmar, TP	1
Khorana, HG	1
Han, S; Junk, MJ; Kinnebrew, M; Pavlova, A; Stone, KM; Voska, J	1
Imamoto, Y; Kandori, H; Nagata, T; Shichida, Y; Terakita, A; Yamazaki, Y	1
Dempski, RE; Richards, R	1
Huber, T; Sakmar, TP; Tian, H	1
Hayashi, F; Seno, K	1
Demura, M; Kamo, N; Kikukawa, T; Kimura-Someya, T; Miyauchi, S; Nara, T; Ohkawa, K; Ohsawa, N; Shimono, K; Shirouzu, M; Tamogami, J; Yokoyama, S	1
Benaím, G; Bubis, J; Rodríguez, S; Silva, ML	1
Hamner, G; Kolandaivelu, S; Motipally, SI; Murphy, J; Myers, B; Sechrest, ER	1
Chang, CF; Inoue, K; Konno, M; Tahara, T	1

Reviews

3 review(s) available for cysteine and 11-cis-retinal

Article	Year
Structural mimicry in G protein-coupled receptors: implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors. Molecular pharmacology, 2001, Volume: 60, Issue:1 Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Binding Sites; Cysteine; Humans; Membrane Proteins; Molecular Sequence Data; Protein Conformation; Receptors, Dopamine D2; Rhodopsin; Sequence Homology, Amino Acid; Structure-Activity Relationship	2001
Dynamics in rhodopsin. Chembiochem : a European journal of chemical biology, 2002, Oct-04, Volume: 3, Issue:10 Topics: Amino Acid Sequence; Animals; Bacteriorhodopsins; Cattle; Cysteine; Dark Adaptation; Disulfides; Electron Spin Resonance Spectroscopy; Kinetics; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Protein Structure, Secondary; Rhodopsin; Sulfhydryl Compounds	2002
Agonist-induced conformational changes in the beta2 adrenergic receptor. The journal of peptide research : official journal of the American Peptide Society, 2002, Volume: 60, Issue:6 Topics: Adrenergic beta-Agonists; Binding Sites; Cysteine; Dobutamine; Fluoresceins; Humans; Isoproterenol; Protein Binding; Protein Conformation; Receptors, Adrenergic, beta-2; Receptors, Cell Surface; Rhodopsin; Spectrometry, Fluorescence	2002

Other Studies

92 other study(ies) available for cysteine and 11-cis-retinal

Article	Year
Palmitylation of a G-protein coupled receptor. Direct analysis by tandem mass spectrometry. The Journal of biological chemistry, 1992, Aug-25, Volume: 267, Issue:24 Topics: Amino Acid Sequence; Animals; Cattle; Chromatography, High Pressure Liquid; Cyanogen Bromide; Cysteine; GTP-Binding Proteins; Mass Spectrometry; Models, Structural; Molecular Sequence Data; Palmitic Acid; Palmitic Acids; Peptide Fragments; Protein Conformation; Rhodopsin; Rod Cell Outer Segment; Thermolysin	1992
Labeling of the beta gamma subunit complex of transducin with an environmentally sensitive cysteine reagent. Use of fluorescence spectroscopy to monitor transducin subunit interactions. The Journal of biological chemistry, 1991, Jun-15, Volume: 266, Issue:17 Topics: Aluminum; Aluminum Compounds; Anilino Naphthalenesulfonates; Animals; Cattle; Cysteine; Fluorides; Fluorine; GTP Phosphohydrolases; Guanosine 5'-O-(3-Thiotriphosphate); Guanosine Diphosphate; Kinetics; Macromolecular Substances; Rhodopsin; Rod Cell Outer Segment; Spectrometry, Fluorescence; Sulfhydryl Reagents; Transducin	1991
Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187. The Journal of biological chemistry, 1990, Oct-15, Volume: 265, Issue:29 Topics: Amino Acid Sequence; Animals; Cattle; Cysteine; Disulfides; Eye Proteins; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligonucleotide Probes; Protein Conformation; Rhodopsin; Rod Opsins	1990
Cysteine residues 110 and 187 are essential for the formation of correct structure in bovine rhodopsin. Proceedings of the National Academy of Sciences of the United States of America, 1988, Volume: 85, Issue:22 Topics: Amino Acid Sequence; Animals; Cattle; Cysteine; Molecular Sequence Data; Mutation; Phenotype; Protein Conformation; Retina; Retinal Pigments; Rhodopsin; Spectrophotometry; Transducin	1988
Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of bovine rhodopsin are palmitylated. FEBS letters, 1988, Mar-28, Volume: 230, Issue:1-2 Topics: Acylation; Animals; Cattle; Cell Membrane; Chromatography, Gas; Chromatography, High Pressure Liquid; Cysteine; Cytoplasm; Mass Spectrometry; Palmitic Acid; Palmitic Acids; Peptide Fragments; Protein Conformation; Retinal Pigments; Rhodopsin; Rod Cell Outer Segment	1988
The carboxyl-terminal one-third of bovine rhodopsin: its structure and function. Vision research, 1982, Volume: 22, Issue:12 Topics: Amino Acid Sequence; Amino Acids; Animals; Cattle; Cysteine; Models, Molecular; Phosphorylation; Protein Conformation; Retinal Pigments; Rhodopsin; Thermolysin	1982
A general method for mapping tertiary contacts between amino acid residues in membrane-embedded proteins. Biochemistry, 1995, Nov-21, Volume: 34, Issue:46 Topics: Amino Acids; Animals; Blotting, Western; Cattle; Cell Line; Cross-Linking Reagents; Cysteine; Disulfides; Macromolecular Substances; Membrane Proteins; Mutagenesis, Insertional; Peptide Mapping; Rhodopsin; Spectrophotometry; Transducin; Transfection	1995
Mapping of the amino acids in the cytoplasmic loop connecting helices C and D in rhodopsin. Chemical reactivity in the dark state following single cysteine replacements. Biochemistry, 1995, Jul-11, Volume: 34, Issue:27 Topics: Amino Acid Sequence; Animals; Cattle; Cysteine; Cytoplasm; Darkness; Ethylmaleimide; GTP-Binding Proteins; Molecular Sequence Data; Mutation; Protein Structure, Secondary; Rhodopsin	1995
Membrane insertion and assembly of ductin: a polytopic channel with dual orientations. The EMBO journal, 1995, Aug-01, Volume: 14, Issue:15 Topics: Amino Acid Sequence; Animals; Base Sequence; beta-Lactamases; Cysteine; Decapodiformes; Fluoresceins; Intracellular Membranes; Microsomes; Molecular Sequence Data; Mutation; Protein Biosynthesis; Protein Conformation; Proteolipids; Proton-Translocating ATPases; Recombinant Fusion Proteins; Rhodopsin; Vacuolar Proton-Translocating ATPases	1995
Depalmitoylation of rhodopsin with hydroxylamine. Methods in enzymology, 1995, Volume: 250 Topics: Acylation; Animals; Cattle; Cell Line; Chlorocebus aethiops; Chromatography, Affinity; Cysteine; Guanosine Triphosphate; Hydrogen-Ion Concentration; Hydrolysis; Hydroxylamine; Hydroxylamines; Isotope Labeling; Kinetics; Membrane Proteins; Mutagenesis, Site-Directed; Palmitic Acid; Palmitic Acids; Phosphates; Phosphorus Radioisotopes; Protein Processing, Post-Translational; Radioisotope Dilution Technique; Rats; Rats, Sprague-Dawley; Recombinant Proteins; Rhodopsin; Rod Cell Outer Segment; Transfection; Tritium	1995
Disruption of conserved rhodopsin disulfide bond by Cys187Tyr mutation causes early and severe autosomal dominant retinitis pigmentosa. Ophthalmology, 1995, Volume: 102, Issue:4 Topics: Adolescent; Adult; Amino Acid Sequence; Base Sequence; Child; Cysteine; Dark Adaptation; Disulfides; DNA Primers; Electroretinography; Female; Humans; Male; Middle Aged; Molecular Sequence Data; Pedigree; Phenotype; Point Mutation; Retina; Retinitis Pigmentosa; Rhodopsin; Tyrosine; Visual Fields	1995
Structure and function in rhodopsin. Separation and characterization of the correctly folded and misfolded opsins produced on expression of an opsin mutant gene containing only the native intradiscal cysteine codons. Biochemistry, 1995, Mar-14, Volume: 34, Issue:10 Topics: Amino Acid Sequence; Animals; Binding Sites; Cattle; Cell Line; Circular Dichroism; Codon; Cysteine; Gene Expression; Molecular Sequence Data; Molecular Structure; Mutation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Rhodopsin; Spectrophotometry; Spectrophotometry, Ultraviolet	1995
Structure and function in rhodopsin. Measurement of the rate of metarhodopsin II decay by fluorescence spectroscopy. The Journal of biological chemistry, 1995, Mar-10, Volume: 270, Issue:10 Topics: Amino Acid Sequence; Animals; Cattle; Cysteine; Hydroxylamine; Hydroxylamines; Kinetics; Light; Models, Structural; Molecular Sequence Data; Mutagenesis, Site-Directed; Photochemistry; Point Mutation; Protein Structure, Secondary; Recombinant Proteins; Rhodopsin; Rod Cell Outer Segment; Sensitivity and Specificity; Spectrometry, Fluorescence; Thermodynamics; Time Factors; Tryptophan	1995
Thiol ester-linked p-coumaric acid as a new photoactive prosthetic group in a protein with rhodopsin-like photochemistry. Biochemistry, 1994, Nov-29, Volume: 33, Issue:47 Topics: Chromatiaceae; Chromatography, High Pressure Liquid; Coumaric Acids; Cysteine; Disulfides; Dithiothreitol; Esters; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Photochemistry; Propionates; Rhodopsin; Sodium Hydroxide; Sulfhydryl Compounds	1994
Photoactivation of rhodopsin involves alterations in cysteine side chains: detection of an S-H band in the Meta I-->Meta II FTIR difference spectrum. Biophysical journal, 1994, Volume: 66, Issue:6 Topics: Amino Acid Sequence; Animals; Cattle; Cysteine; Disulfides; Ethylmaleimide; Rhodopsin; Rod Cell Outer Segment; Spectroscopy, Fourier Transform Infrared	1994
Structure and function in rhodopsin: replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state. Proceedings of the National Academy of Sciences of the United States of America, 1994, Apr-26, Volume: 91, Issue:9 Topics: Alanine; Amino Acid Sequence; Animals; Cattle; Cysteine; Disulfides; Guanine Nucleotides; Membrane Glycoproteins; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Denaturation; Recombinant Proteins; Rhodopsin; Rod Opsins; Structure-Activity Relationship; Temperature; Transducin	1994
Formation of the meta II photointermediate is accompanied by conformational changes in the cytoplasmic surface of rhodopsin. Biochemistry, 1993, Nov-16, Volume: 32, Issue:45 Topics: Amino Acid Sequence; Animals; Blotting, Western; Cattle; Cysteine; Cytoplasm; Digitonin; Electron Spin Resonance Spectroscopy; Glucosides; Molecular Sequence Data; Mutation; Photochemistry; Protein Structure, Secondary; Rhodopsin	1993
Palmitoylation of bovine opsin and its cysteine mutants in COS cells. Proceedings of the National Academy of Sciences of the United States of America, 1993, Jan-01, Volume: 90, Issue:1 Topics: Amino Acid Sequence; Animals; Cattle; Cell Line; Cell Membrane; Cysteine; Electrophoresis, Polyacrylamide Gel; Eye Proteins; G-Protein-Coupled Receptor Kinase 1; Molecular Sequence Data; Mutagenesis, Site-Directed; Palmitic Acid; Palmitic Acids; Phosphorylation; Protein Kinases; Protein Processing, Post-Translational; Protein Structure, Secondary; Recombinant Proteins; Rhodopsin; Rod Opsins; Serine; Spectrophotometry; Transfection	1993
Structure and function in rhodopsin. Single cysteine substitution mutants in the cytoplasmic interhelical E-F loop region show position-specific effects in transducin activation. Biochemistry, 1996, Sep-24, Volume: 35, Issue:38 Topics: Amino Acid Sequence; Animals; Cattle; COS Cells; Cysteine; Ethylmaleimide; Fluorescence; Gene Expression; Guanosine Triphosphate; Light; Molecular Sequence Data; Mutagenesis; Recombinant Proteins; Rhodopsin; Rod Opsins; Spectrophotometry; Transducin	1996
Spin-labeling analysis of structure and dynamics in octopus rhodopsin. Journal of photochemistry and photobiology. B, Biology, 1996, Volume: 35, Issue:1-2 Topics: Animals; Binding Sites; Cyclic N-Oxides; Cysteine; Electron Spin Resonance Spectroscopy; Light; Mesylates; Octopodiformes; Rhodopsin; Spin Labels	1996
Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science (New York, N.Y.), 1996, Nov-01, Volume: 274, Issue:5288 Topics: Amino Acid Sequence; Cysteine; Disulfides; Electron Spin Resonance Spectroscopy; Eye Proteins; G-Protein-Coupled Receptor Kinase 1; Light; Molecular Sequence Data; Mutation; Oxidation-Reduction; Phenanthrolines; Protein Kinases; Protein Structure, Secondary; Rhodopsin; Serine Endopeptidases; Spin Labels; Transducin	1996
Structure and function in rhodopsin. Cysteines 65 and 316 are in proximity in a rhodopsin mutant as indicated by disulfide formation and interactions between attached spin labels. Biochemistry, 1996, Nov-12, Volume: 35, Issue:45 Topics: Amino Acid Sequence; Animals; Cattle; Cysteine; Disulfides; DNA Mutational Analysis; Electron Spin Resonance Spectroscopy; Membrane Proteins; Molecular Sequence Data; Peptide Fragments; Protein Structure, Secondary; Rhodopsin; Sulfhydryl Compounds; Thermolysin	1996
Post-Golgi vesicles cotransport docosahexaenoyl-phospholipids and rhodopsin during frog photoreceptor membrane biogenesis. The Journal of biological chemistry, 1997, Apr-18, Volume: 272, Issue:16 Topics: Animals; Biological Transport; Cysteine; Docosahexaenoic Acids; Fatty Acids, Nonesterified; Golgi Apparatus; Methionine; Organelles; Phospholipids; Photoreceptor Cells; Ranidae; Retina; Rhodopsin; Rod Cell Outer Segment	1997
A distance measurement between specific sites on the cytoplasmic surface of bovine rhodopsin in rod outer segment disk membranes. Biochimica et biophysica acta, 1997, Aug-14, Volume: 1328, Issue:1 Topics: Animals; Binding Sites; Cattle; Cell Membrane; Cysteine; Disulfides; Eye Proteins; G-Protein-Coupled Receptor Kinase 1; Intracellular Membranes; Magnetic Resonance Spectroscopy; Membrane Proteins; Phosphorylation; Protein Kinases; Pyridines; Rhodopsin; Rod Cell Outer Segment; Spin Labels	1997
Altered activity of palmitoylation-deficient and isoprenylated forms of the G protein-coupled receptor kinase GRK6. The Journal of biological chemistry, 1997, Oct-24, Volume: 272, Issue:43 Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Base Sequence; Cattle; COS Cells; Cysteine; DNA Primers; Eye Proteins; G-Protein-Coupled Receptor Kinase 1; G-Protein-Coupled Receptor Kinases; GTP-Binding Proteins; Isoproterenol; Kinetics; Liposomes; Molecular Sequence Data; Mutagenesis, Site-Directed; Palmitic Acid; Phosphatidylcholines; Phosphorylation; Polymerase Chain Reaction; Protein Kinases; Protein Prenylation; Protein Serine-Threonine Kinases; Receptor Protein-Tyrosine Kinases; Receptors, Adrenergic, beta-2; Recombinant Proteins; Retina; Rhodopsin; Sequence Deletion; Serine; Transfection	1997
Structure and function in rhodopsin: topology of the C-terminal polypeptide chain in relation to the cytoplasmic loops. Proceedings of the National Academy of Sciences of the United States of America, 1997, Dec-23, Volume: 94, Issue:26 Topics: Amino Acid Sequence; Animals; Cysteine; Humans; Molecular Sequence Data; Mutagenesis; Protein Conformation; Rhodopsin; Signal Transduction	1997
Disulfide bond exchange in rhodopsin. Biochemistry, 1998, Feb-03, Volume: 37, Issue:5 Topics: Animals; Cattle; Cysteine; Disulfides; Electrophoresis, Polyacrylamide Gel; Ethylmaleimide; Mutagenesis; Photolysis; Protein Denaturation; Rhodopsin; Spectrophotometry; Transducin	1998
Mass spectrometric analysis of integral membrane proteins: application to complete mapping of bacteriorhodopsins and rhodopsin. Protein science : a publication of the Protein Society, 1998, Volume: 7, Issue:3 Topics: Amino Acid Sequence; Animals; Bacteriorhodopsins; Cattle; Chromatography, High Pressure Liquid; Cyanogen Bromide; Cysteine; Halobacterium salinarum; Mass Spectrometry; Membrane Proteins; Molecular Sequence Data; Peptide Fragments; Point Mutation; Rhodopsin	1998
Conformational changes in rhodopsin. Movement of helix f detected by site-specific chemical labeling and fluorescence spectroscopy. The Journal of biological chemistry, 1999, Jan-15, Volume: 274, Issue:3 Topics: Amino Acid Sequence; Animals; Bridged Bicyclo Compounds; COS Cells; Cysteine; Fluorescent Dyes; Molecular Sequence Data; Protein Conformation; Protein Structure, Secondary; Rhodopsin; Spectrometry, Fluorescence; Spin Labels	1999
Structure and function in rhodopsin: further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function. Proceedings of the National Academy of Sciences of the United States of America, 1999, Mar-02, Volume: 96, Issue:5 Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Cattle; Cysteine; Humans; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Folding; Protein Structure, Secondary; Recombinant Proteins; Retinitis Pigmentosa; Rhodopsin; Rod Opsins; Spectrophotometry	1999
Tertiary interactions between the fifth and sixth transmembrane segments of rhodopsin. Biochemistry, 1999, May-18, Volume: 38, Issue:20 Topics: Absorption; Amino Acid Substitution; Animals; Cattle; Cell Membrane; Cross-Linking Reagents; Cysteine; Membrane Proteins; Mutagenesis, Site-Directed; Peptide Fragments; Phenylalanine; Protein Structure, Tertiary; Rhodopsin; Spectrophotometry; Transducin	1999
Structural features of the C-terminal domain of bovine rhodopsin: a site-directed spin-labeling study. Biochemistry, 1999, Jun-22, Volume: 38, Issue:25 Topics: Amino Acid Sequence; Animals; Antibodies, Monoclonal; Binding Sites; Binding Sites, Antibody; Cattle; Cysteine; Electron Spin Resonance Spectroscopy; Light; Molecular Sequence Data; Mutagenesis, Site-Directed; Palmitic Acid; Peptide Fragments; Rhodopsin; Spin Labels	1999
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, 1999, Jun-22, Volume: 38, Issue:25 Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Binding Sites; Cattle; COS Cells; Cysteine; Cytoplasm; Disulfides; Leucine; Light; Molecular Sequence Data; Palmitic Acid; Peptide Fragments; Protein Structure, Secondary; Protein Structure, Tertiary; Pyridines; Rhodopsin; Spectrometry, Fluorescence; Sulfhydryl Reagents; Transducin; Tyrosine	1999
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 Biochemistry, 1999, Jun-22, Volume: 38, Issue:25 Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Cattle; Cysteine; Cytoplasm; Darkness; Disulfides; Light; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Peptide Fragments; Protein Structure, Secondary; Protein Structure, Tertiary; Pyridines; Rhodopsin; Sulfhydryl Reagents; Transducin	1999
State-dependent disulfide cross-linking in rhodopsin. Biochemistry, 1999, Sep-14, Volume: 38, Issue:37 Topics: Amino Acid Sequence; Animals; Cattle; COS Cells; Cross-Linking Reagents; Cysteine; Darkness; Disulfides; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptide Fragments; Photic Stimulation; Protein Structure, Tertiary; Retina; Rhodopsin; Rod Opsins	1999
Tertiary interactions between transmembrane segments 3 and 5 near the cytoplasmic side of rhodopsin. Biochemistry, 1999, Sep-14, Volume: 38, Issue:37 Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Cattle; COS Cells; Cross-Linking Reagents; Cysteine; Cytoplasm; Disulfides; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptide Fragments; Protein Structure, Tertiary; Retina; Rhodopsin	1999
NMR spectroscopy in studies of light-induced structural changes in mammalian rhodopsin: applicability of solution (19)F NMR. Proceedings of the National Academy of Sciences of the United States of America, 1999, Nov-23, Volume: 96, Issue:24 Topics: Amino Acid Sequence; Animals; Cattle; Cell Line, Transformed; Cysteine; Darkness; Detergents; Dimyristoylphosphatidylcholine; Fluorine Radioisotopes; Glucosides; Light; Memantine; Molecular Sequence Data; Mutagenesis; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Rhodopsin; Solutions	1999
Function of the farnesyl moiety in visual signalling. The Biochemical journal, 2000, Apr-01, Volume: 347 Pt 1 Topics: Amino Acid Sequence; Animals; Cattle; Cysteine; Eye Proteins; G-Protein-Coupled Receptor Kinase 1; Kinetics; Molecular Sequence Data; Peptide Fragments; Phosphorylation; Protein Kinases; Protein Prenylation; Rhodopsin; Rod Cell Outer Segment; Sheep; Signal Transduction; Spectrophotometry; Vision, Ocular	2000
Mapping tertiary contacts between amino acid residues within rhodopsin. Methods in enzymology, 2000, Volume: 315 Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Binding Sites; Concanavalin A; Consensus Sequence; COS Cells; Cysteine; Disulfides; Epitopes; Guanosine 5'-O-(3-Thiotriphosphate); Models, Molecular; Mutagenesis, Site-Directed; Peptide Fragments; Protein Structure, Tertiary; Recombinant Proteins; Rhodopsin; Transducin; Transfection	2000
Intrahelical arrangement in the integral membrane protein rhodopsin investigated by site-specific chemical cleavage and mass spectrometry. Biochemistry, 2000, Apr-25, Volume: 39, Issue:16 Topics: Amino Acid Sequence; Ascorbic Acid; Copper; Cyanogen Bromide; Cysteine; Membrane Proteins; Molecular Sequence Data; Mutagenesis, Site-Directed; Organometallic Compounds; Oxygen; Peptide Fragments; Phenanthrolines; Protein Structure, Secondary; Rhodopsin; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization	2000
Structural requirements for the stabilization of metarhodopsin II by the C terminus of the alpha subunit of transducin. The Journal of biological chemistry, 2001, Jan-26, Volume: 276, Issue:4 Topics: Amino Acid Sequence; Conserved Sequence; Cysteine; Glycine; Lysine; Peptide Fragments; Protein Binding; Protein Subunits; Rhodopsin; Transducin	2001
Light-induced conformational changes of rhodopsin probed by fluorescent alexa594 immobilized on the cytoplasmic surface. Biochemistry, 2000, Dec-12, Volume: 39, Issue:49 Topics: Amino Acid Sequence; Animals; Arrestin; Binding, Competitive; Cattle; Cell Membrane; Cysteine; Fluorescent Dyes; Hydrogen-Ion Concentration; Light; Models, Molecular; Molecular Sequence Data; Organic Chemicals; Phosphorylation; Photolysis; Protein Binding; Protein Conformation; Protein Structure, Secondary; Rhodopsin; Temperature; Transducin	2000
Light-induced rotation of a transmembrane alpha-helix in bacteriorhodopsin. Journal of molecular biology, 2000, Dec-15, Volume: 304, Issue:5 Topics: Animals; Bacterial Proteins; Bacteriorhodopsins; Cattle; Chemoreceptor Cells; Cysteine; Electron Spin Resonance Spectroscopy; Escherichia coli Proteins; Kinetics; Light; Membrane Proteins; Models, Molecular; Protein Structure, Secondary; Receptors, Cell Surface; Rhodopsin; Rotation; Spin Labels; Temperature	2000
Prevalence of mutations causing retinitis pigmentosa and other inherited retinopathies. Human mutation, 2001, Volume: 17, Issue:1 Topics: Amino Acid Substitution; Animals; Arginine; Cysteine; Genetic Variation; Glutamine; Homeodomain Proteins; Humans; Intermediate Filament Proteins; Leucine; Membrane Glycoproteins; Mutation; Nerve Tissue Proteins; Optic Atrophies, Hereditary; Peripherins; Prevalence; Proline; Retinal Degeneration; Retinal Diseases; Retinitis Pigmentosa; Rhodopsin; Trans-Activators; Tyrosine	2001
Structure and function in rhodopsin: Mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants. Proceedings of the National Academy of Sciences of the United States of America, 2001, Apr-24, Volume: 98, Issue:9 Topics: Amino Acid Sequence; Animals; COS Cells; Cysteine; Disulfides; Endopeptidase K; Humans; Lysine; Maleimides; Models, Molecular; Molecular Sequence Data; Mutation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Retinitis Pigmentosa; Rhodopsin; Rod Opsins; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Structure-Activity Relationship	2001
Mapping of contact sites in complex formation between transducin and light-activated rhodopsin by covalent crosslinking: use of a photoactivatable reagent. Proceedings of the National Academy of Sciences of the United States of America, 2001, Apr-24, Volume: 98, Issue:9 Topics: Amino Acid Sequence; Animals; Azides; Binding Sites; Cattle; COS Cells; Cross-Linking Reagents; Cysteine; Disulfides; Dithiothreitol; Ethylmaleimide; Guanosine Diphosphate; Light; Lysine; Maleimides; Models, Molecular; Molecular Sequence Data; Mutation; Photolysis; Protein Binding; Protein Structure, Secondary; Pyridines; Rhodopsin; Sepharose; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Transducin; Trypsin; Ultraviolet Rays	2001
Mapping of contact sites in complex formation between light-activated rhodopsin and transducin by covalent crosslinking: use of a chemically preactivated reagent. Proceedings of the National Academy of Sciences of the United States of America, 2001, Apr-24, Volume: 98, Issue:9 Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Azides; Binding Sites; Blotting, Western; Cattle; Cross-Linking Reagents; Cysteine; Hydrogen-Ion Concentration; Light; Models, Molecular; Molecular Sequence Data; Mutation; Peptide Fragments; Protein Binding; Protein Structure, Secondary; Protein Subunits; Pyridines; Rhodopsin; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Succinimides; Transducin	2001
Solution 19F nuclear Overhauser effects in structural studies of the cytoplasmic domain of mammalian rhodopsin. Proceedings of the National Academy of Sciences of the United States of America, 2001, Apr-24, Volume: 98, Issue:9 Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Cattle; Cysteine; Cytoplasm; Darkness; Detergents; Disulfides; Fluorine; Glucosides; Kinetics; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Mutation; Protein Structure, Tertiary; Recombinant Proteins; Rhodopsin; Solutions; Spectrophotometry, Ultraviolet	2001
Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: proximities between amino acids deduced from spontaneous disulfide bond formation between Cys316 and engineered cysteines in cytoplasmic loop 1. Biochemistry, 2001, Oct-23, Volume: 40, Issue:42 Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Cattle; Cysteine; Cytoplasm; Disulfides; Light; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Structure, Secondary; Protein Structure, Tertiary; Rhodopsin	2001
Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: proximities between amino acids deduced from spontaneous disulfide bond formation between cysteine pairs engineered in cytoplasmic loops 1, 3, and 4. Biochemistry, 2001, Oct-23, Volume: 40, Issue:42 Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Cattle; COS Cells; Cysteine; Cytoplasm; Disulfides; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Proteins; Rhodopsin; Spectrophotometry, Ultraviolet; Sulfhydryl Compounds	2001
Chemical modification of transducin with iodoacetic acid: transducin-alpha carboxymethylated at Cys(347) allows transducin binding to Light-activated rhodopsin but prevents its release in the presence of GTP. Archives of biochemistry and biophysics, 2001, Nov-15, Volume: 395, Issue:2 Topics: Animals; Cattle; Chromatography, High Pressure Liquid; Cysteine; Guanine; Guanosine Diphosphate; Guanosine Triphosphate; Iodoacetic Acid; Light; Magnetic Resonance Spectroscopy; Models, Molecular; Nucleotides; Peptides; Protein Binding; Protein Conformation; Retina; Rhodopsin; Thiocyanates; Time Factors; Transducin; Trypsin	2001
Rhodopsin-transducin interface: studies with conformationally constrained peptides. Biophysical journal, 2001, Volume: 81, Issue:6 Topics: Arginine; Binding Sites; Crystallography, X-Ray; Cysteine; Dose-Response Relationship, Drug; Leucine; Lysine; Magnetic Resonance Spectroscopy; Models, Molecular; Monte Carlo Method; Mutation; Peptide Biosynthesis; Peptides; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Rhodopsin; Spectrophotometry; Temperature; Transducin; Ultraviolet Rays; Valine	2001
Structure and function in rhodopsin: mapping light-dependent changes in distance between residue 65 in helix TM1 and residues in the sequence 306-319 at the cytoplasmic end of helix TM7 and in helix H8. Biochemistry, 2001, Dec-25, Volume: 40, Issue:51 Topics: Amino Acid Sequence; Animals; Cattle; Cysteine; Cytoplasm; Electron Spin Resonance Spectroscopy; Light; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptide Fragments; Protein Structure, Secondary; Rhodopsin; Spin Labels; Structure-Activity Relationship	2001
Structure and function in rhodopsin: mapping light-dependent changes in distance between residue 316 in helix 8 and residues in the sequence 60-75, covering the cytoplasmic end of helices TM1 and TM2 and their connection loop CL1. Biochemistry, 2001, Dec-25, Volume: 40, Issue:51 Topics: Amino Acid Sequence; Animals; Cattle; Crystallography, X-Ray; Cysteine; Cytoplasm; Electron Spin Resonance Spectroscopy; Light; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptide Fragments; Photochemistry; Protein Conformation; Protein Structure, Secondary; Rhodopsin; Solutions; Spin Labels; Structure-Activity Relationship	2001
X-ray diffraction of heavy-atom labelled two-dimensional crystals of rhodopsin identifies the position of cysteine 140 in helix 3 and cysteine 316 in helix 8. Journal of molecular biology, 2002, Feb-22, Volume: 316, Issue:3 Topics: Amino Acid Sequence; Animals; Cattle; Cholesterol; Cryoelectron Microscopy; Crystallization; Cysteine; Mercury; Models, Molecular; Molecular Sequence Data; p-Chloromercuribenzoic Acid; Protein Structure, Secondary; Retina; Rhodopsin; Sequence Alignment; Solvents; Spectrum Analysis; X-Ray Diffraction	2002
Detection of fast light-activated H+ release and M intermediate formation from proteorhodopsin. BMC physiology, 2002, Apr-09, Volume: 2 Topics: Cysteine; Electrophoresis, Polyacrylamide Gel; Hydrogen-Ion Concentration; Ion Transport; Kinetics; Light; Molecular Weight; Mutation; Proton Pumps; Protons; Rhodopsin; Rhodopsins, Microbial; Spectrum Analysis	2002
Light-induced changes in the structure and accessibility of the cytoplasmic loops of rhodopsin in the activated MII state. Biochemistry, 2002, Jun-25, Volume: 41, Issue:25 Topics: Animals; Cattle; Cysteine; Cytoplasm; Fluorescein; Fluorescence Polarization; Fluorescent Dyes; Light; Micelles; Photochemistry; Protein Structure, Secondary; Rhodopsin; Rod Cell Outer Segment; Spectrometry, Fluorescence; Xanthenes	2002
Retinitis pigmentosa-associated rhodopsin mutations in three membrane-located cysteine residues present three different biochemical phenotypes. Biochemical and biophysical research communications, 2002, Oct-04, Volume: 297, Issue:4 Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Cell Line; Cloning, Molecular; Cysteine; Darkness; Gene Expression; Humans; Light; Molecular Sequence Data; Phenotype; Protein Conformation; Protein Folding; Recombinant Proteins; Retinitis Pigmentosa; Rhodopsin; Spectrophotometry; Spodoptera; Transfection	2002
An opsin mutant with increased thermal stability. Biochemistry, 2003, Feb-25, Volume: 42, Issue:7 Topics: Amino Acid Sequence; Animals; Asparagine; Aspartic Acid; Cattle; COS Cells; Cross-Linking Reagents; Cysteine; Disulfides; Dithiothreitol; Light; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Denaturation; Recombinant Proteins; Retinaldehyde; Rhodopsin; Thermodynamics; Transducin; Transfection	2003
Three-dimensional model for meta-II rhodopsin, an activated G-protein-coupled receptor. Biochemistry, 2003, Aug-05, Volume: 42, Issue:30 Topics: Animals; Cattle; Computational Biology; Computer Simulation; Crystallography, X-Ray; Cysteine; Disulfides; Heterotrimeric GTP-Binding Proteins; Light; Membrane Proteins; Models, Chemical; Models, Molecular; Protein Conformation; Protein Structure, Secondary; Receptors, Cell Surface; Rhodopsin; Spin Labels; Thermodynamics	2003
The molecular basis for the high photosensitivity of rhodopsin. Proceedings of the National Academy of Sciences of the United States of America, 2003, Dec-09, Volume: 100, Issue:25 Topics: Animals; Bacteriorhodopsins; Binding Sites; Carbon; Crystallography, X-Ray; Cysteine; Hydrogen; Kinetics; Light; Magnetic Resonance Spectroscopy; Models, Chemical; Models, Molecular; Polyenes; Retina; Rhodopsin; Stereoisomerism	2003
NMR spectroscopy of phosphorylated wild-type rhodopsin: mobility of the phosphorylated C-terminus of rhodopsin in the dark and upon light activation. Biochemistry, 2004, Feb-03, Volume: 43, Issue:4 Topics: Amino Acid Sequence; Animals; Cattle; Cysteine; Darkness; Fluorine; Light; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Peptide Fragments; Phosphorus Isotopes; Phosphorylation; Rhodopsin; Solutions; Trifluoroethanol	2004
Targeted mutagenesis of the farnesylation site of Drosophila Ggammae disrupts membrane association of the G protein betagamma complex and affects the light sensitivity of the visual system. The Journal of biological chemistry, 2004, Aug-27, Volume: 279, Issue:35 Topics: Amino Acid Motifs; Animals; Animals, Genetically Modified; Blotting, Western; Cell Membrane; Crystallins; Cysteine; DNA; Drosophila; Electrophoresis, Polyacrylamide Gel; Electroretinography; gamma-Crystallins; Heterotrimeric GTP-Binding Proteins; Immunohistochemistry; Isoenzymes; Light; Mass Spectrometry; Models, Chemical; Mutagenesis, Site-Directed; Mutation; Phospholipase C beta; Photophobia; Photoreceptor Cells, Invertebrate; Point Mutation; Precipitin Tests; Protein Prenylation; Protein Processing, Post-Translational; Retina; Rhodopsin; Transgenes; Type C Phospholipases	2004
FTIR spectroscopy of the K photointermediate of Neurospora rhodopsin: structural changes of the retinal, protein, and water molecules after photoisomerization. Biochemistry, 2004, Aug-03, Volume: 43, Issue:30 Topics: Amino Acid Sequence; Archaeal Proteins; Bacteriorhodopsins; Carrier Proteins; Cysteine; Freezing; Fungal Proteins; Isomerism; Light; Molecular Sequence Data; Photoreceptors, Microbial; Recombinant Proteins; Retinaldehyde; Rhodopsin; Schiff Bases; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman; Water	2004
Cysteine 2.59(89) in the second transmembrane domain of human CB2 receptor is accessible within the ligand binding crevice: evidence for possible CB2 deviation from a rhodopsin template. Molecular pharmacology, 2005, Volume: 68, Issue:1 Topics: Amino Acid Sequence; Binding, Competitive; Cannabinoids; Cell Line; Cell Membrane; Cysteine; Dose-Response Relationship, Drug; Ethyl Methanesulfonate; Humans; Ligands; Molecular Sequence Data; Mutation; Protein Binding; Protein Structure, Secondary; Receptor, Cannabinoid, CB2; Rhodopsin	2005
Enhanced shutoff of phototransduction in transgenic mice expressing palmitoylation-deficient rhodopsin. The Journal of biological chemistry, 2005, Jul-01, Volume: 280, Issue:26 Topics: Amino Acid Sequence; Animals; Blotting, Western; Cysteine; Electrodes; Gene Library; Immunohistochemistry; Light; Mass Spectrometry; Mice; Mice, Transgenic; Models, Genetic; Models, Statistical; Molecular Sequence Data; Mutation; Palmitic Acid; Phosphorylation; Protein Processing, Post-Translational; Reactive Oxygen Species; Receptors, G-Protein-Coupled; Retina; Reverse Transcriptase Polymerase Chain Reaction; Rhodopsin; RNA; Time Factors	2005
Mass spectrometric analysis of integral membrane proteins at the subpicomolar level: application to rhodopsin. Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 2005, Oct-25, Volume: 825, Issue:2 Topics: Animals; Cattle; Cyanogen Bromide; Cysteine; Mass Spectrometry; Membrane Proteins; Nanotechnology; Peptide Fragments; Peptide Mapping; Rhodopsin; Sensitivity and Specificity	2005
Detecting molecular interactions that stabilize native bovine rhodopsin. Journal of molecular biology, 2006, Apr-21, Volume: 358, Issue:1 Topics: Animals; Cattle; Cell Membrane; Cysteine; Darkness; Imaging, Three-Dimensional; Models, Molecular; Models, Structural; Protein Folding; Protein Structure, Tertiary; Rhodopsin; Rod Cell Outer Segment; Thermodynamics	2006
Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin. Proceedings of the National Academy of Sciences of the United States of America, 2006, Mar-28, Volume: 103, Issue:13 Topics: Arrestin; Cysteine; Electron Spin Resonance Spectroscopy; Models, Molecular; Mutation; Phosphorylation; Protein Binding; Protein Structure, Quaternary; Rhodopsin	2006
Structure and dynamics of dark-state bovine rhodopsin revealed by chemical cross-linking and high-resolution mass spectrometry. Protein science : a publication of the Protein Society, 2006, Volume: 15, Issue:6 Topics: Amino Acid Sequence; Animals; Cattle; Chromatography, Liquid; Cross-Linking Reagents; Crystallography, X-Ray; Cysteine; Lysine; Mass Spectrometry; Molecular Sequence Data; Protein Conformation; Rhodopsin; Spectroscopy, Fourier Transform Infrared; Succinimides	2006
Metarhodopsin-II stabilization by crosslinked Gtalpha C-terminal peptides and implications for the mechanism of GPCR-G protein coupling. Vision research, 2006, Volume: 46, Issue:27 Topics: Animals; Cattle; Cross-Linking Reagents; Cysteine; Dark Adaptation; GTP-Binding Protein alpha Subunits; Peptide Fragments; Protein Binding; Receptors, G-Protein-Coupled; Rhodopsin; Rod Cell Outer Segment; Spectrum Analysis	2006
Mutation screening of the peropsin gene, a retinal pigment epithelium specific rhodopsin homolog, in patients with retinitis pigmentosa and allied diseases. Molecular vision, 2006, Dec-05, Volume: 12 Topics: Cysteine; DNA Mutational Analysis; Heterozygote; Humans; Mutation, Missense; Retinal Degeneration; Retinitis Pigmentosa; Rhodopsin; Tyrosine	2006
Stabilizing effect of Zn2+ in native bovine rhodopsin. The Journal of biological chemistry, 2007, Apr-13, Volume: 282, Issue:15 Topics: Amino Acid Sequence; Animals; Cations, Divalent; Cattle; Cysteine; Disulfides; Models, Molecular; Molecular Sequence Data; Protein Binding; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Rhodopsin; Rod Cell Outer Segment; Spectrum Analysis; Zinc	2007
Critical role for the second extracellular loop in the binding of both orthosteric and allosteric G protein-coupled receptor ligands. The Journal of biological chemistry, 2007, Aug-31, Volume: 282, Issue:35 Topics: Allosteric Regulation; Allosteric Site; Amino Acid Substitution; Animals; Cattle; Cysteine; Humans; Ligands; Models, Molecular; Protein Binding; Protein Structure, Tertiary; Receptor, Muscarinic M2; Rhodopsin; Structural Homology, Protein	2007
Dynamics of arrestin-rhodopsin interactions: loop movement is involved in arrestin activation and receptor binding. The Journal of biological chemistry, 2007, Aug-31, Volume: 282, Issue:35 Topics: Amino Acid Substitution; Animals; Arrestin; Binding Sites; Bridged Bicyclo Compounds; Cattle; Cysteine; Humans; Models, Molecular; Mutagenesis, Site-Directed; Phosphorylation; Protein Binding; Protein Structure, Secondary; Rhodopsin; Spectrometry, Fluorescence	2007
Constitutive excitation by Gly90Asp rhodopsin rescues rods from degeneration caused by elevated production of cGMP in the dark. The Journal of neuroscience : the official journal of the Society for Neuroscience, 2007, Aug-15, Volume: 27, Issue:33 Topics: Adaptation, Ocular; Animals; Aspartic Acid; Calcium; Cyclic GMP; Cysteine; Dark Adaptation; Disease Models, Animal; Electroretinography; Gene Expression Regulation; Glycine; Guanylate Cyclase-Activating Proteins; Mice; Mice, Transgenic; Microscopy, Electron, Transmission; Physical Stimulation; Retina; Retinal Degeneration; Retinal Rod Photoreceptor Cells; Rhodopsin; Tyrosine	2007
Porphyrinmaleimides: towards thiol probes for cysteine residues in proteins. Bioconjugate chemistry, 2008, Volume: 19, Issue:1 Topics: Cysteine; Electrophoresis, Polyacrylamide Gel; Light; Maleimides; Porphyrins; Rhodopsin; Sulfhydryl Compounds; Ultraviolet Rays	2008
Modulation of molecular interactions and function by rhodopsin palmitylation. Biochemistry, 2009, May-26, Volume: 48, Issue:20 Topics: Animals; Chlorocebus aethiops; COS Cells; Cysteine; Light; Mice; Mice, Inbred C57BL; Models, Molecular; Molecular Conformation; Palmitic Acid; Protein Binding; Protein Structure, Tertiary; Rhodopsin; Rod Cell Outer Segment; Transducin	2009
Characterization of membrane protein non-native states. 2. The SDS-unfolded states of rhodopsin. Biochemistry, 2010, Aug-03, Volume: 49, Issue:30 Topics: Animals; Cattle; Cysteine; Membrane Proteins; Micelles; Protein Denaturation; Protein Folding; Protein Structure, Tertiary; Rhodopsin; Sodium Dodecyl Sulfate; Spectrometry, Fluorescence; Tryptophan	2010
The roles of transmembrane domain helix-III during rhodopsin photoactivation. PloS one, 2011, Feb-25, Volume: 6, Issue:2 Topics: Amino Acid Sequence; Animals; Catalysis; Chlorocebus aethiops; COS Cells; Cysteine; Light; Membrane Proteins; Models, Biological; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutant Proteins; Photochemical Processes; Protein Interaction Domains and Motifs; Protein Structure, Secondary; Rhodopsin	2011
Molecular dynamics simulations reveal specific interactions of post-translational palmitoyl modifications with rhodopsin in membranes. Journal of the American Chemical Society, 2012, Mar-07, Volume: 134, Issue:9 Topics: Cysteine; Lipid Bilayers; Models, Molecular; Molecular Dynamics Simulation; Palmitic Acids; Protein Processing, Post-Translational; Rhodopsin	2012
Rhodopsin forms a dimer with cytoplasmic helix 8 contacts in native membranes. Biochemistry, 2012, Mar-06, Volume: 51, Issue:9 Topics: Binding Sites; Cell Membrane; Chromatography, Liquid; Cysteine; Cytoplasm; Dimerization; Mass Spectrometry; Protein Structure, Secondary; Proteolysis; Rhodopsin	2012
Molecular biology of light transduction by the Mammalian photoreceptor, rhodopsin. Journal of biomolecular structure & dynamics, 2000, Volume: 17 Suppl 1 Topics: Amino Acid Sequence; Animals; Cysteine; Mammals; Molecular Biology; Molecular Sequence Data; Protein Structure, Secondary; Receptors, G-Protein-Coupled; Rhodopsin	2000
Structural insight into proteorhodopsin oligomers. Biophysical journal, 2013, Jan-22, Volume: 104, Issue:2 Topics: Chromatography, Gel; Chromatography, Liquid; Cysteine; Detergents; Electron Spin Resonance Spectroscopy; Models, Molecular; Mutant Proteins; Protein Multimerization; Protein Structure, Quaternary; Protein Subunits; Refractometry; Rhodopsin; Rhodopsins, Microbial; Scattering, Radiation; Solubility; Spin Labels; Temperature	2013
Intramolecular interactions that induce helical rearrangement upon rhodopsin activation: light-induced structural changes in metarhodopsin IIa probed by cysteine S-H stretching vibrations. The Journal of biological chemistry, 2014, May-16, Volume: 289, Issue:20 Topics: Amino Acid Sequence; Cysteine; HEK293 Cells; Humans; Light; Liposomes; Models, Molecular; Molecular Sequence Data; Mutation; Phosphatidylcholines; Protein Binding; Protein Structure, Secondary; Rhodopsin; Vibration	2014
Cysteine Substitution and Labeling Provide Insight into Channelrhodopsin-2 Ion Conductance. Biochemistry, 2015, Sep-22, Volume: 54, Issue:37 Topics: Animals; Chlamydomonas reinhardtii; Cysteine; Electricity; Female; Indicators and Reagents; Ion Channel Gating; Kinetics; Light; Mesylates; Models, Molecular; Mutagenesis, Site-Directed; Oocytes; Patch-Clamp Techniques; Permeability; Protein Structure, Tertiary; Rhodopsin; Xenopus laevis	2015
A simple method for enhancing the bioorthogonality of cyclooctyne reagent. Chemical communications (Cambridge, England), 2016, Apr-07, Volume: 52, Issue:31 Topics: Alkynes; Animals; Azides; Cattle; Cycloaddition Reaction; Cyclooctanes; Cysteine; Mercaptoethanol; Models, Molecular; Rhodopsin; Sulfhydryl Compounds	2016
Palmitoylation is a prerequisite for dimerization-dependent raftophilicity of rhodopsin. The Journal of biological chemistry, 2017, 09-15, Volume: 292, Issue:37 Topics: Amphibian Proteins; Animals; Antibodies, Monoclonal; Cysteine; Cystine; Dark Adaptation; Dimerization; Hydrophobic and Hydrophilic Interactions; Kinetics; Light; Lipoylation; Membrane Microdomains; Models, Molecular; Oxidation-Reduction; Protein Conformation; Protein Multimerization; Protein Processing, Post-Translational; Protein Stability; Rana catesbeiana; Rhodopsin; Rod Cell Outer Segment; Transducin	2017
Interhelical interactions between D92 and C218 in the cytoplasmic domain regulate proton uptake upon N-decay in the proton transport of Acetabularia rhodopsin II. Journal of photochemistry and photobiology. B, Biology, 2018, Volume: 183 Topics: Acetabularia; Aspartic Acid; Cysteine; Hydrogen Bonding; Hydrogen-Ion Concentration; Kinetics; Light; Photolysis; Protein Domains; Protons; Rhodopsin; Spectrophotometry	2018
Phosphorylation-induced conformational changes of photoactivated rhodopsin probed by fluorescent labeling at Cys Biochimie, 2018, Volume: 150 Topics: Animals; Biofilms; Bridged Bicyclo Compounds; Cattle; Cysteine; Fluorescence; Molecular Conformation; Phosphorylation; Protein Conformation; Rhodopsin	2018
R17C Mutation in Photoreceptor Disc-Specific Protein, PRCD, Results in Additional Lipidation Altering Protein Stability and Subcellular Localization. International journal of molecular sciences, 2022, Sep-16, Volume: 23, Issue:18 Topics: Animals; Cysteine; Dogs; Eye Proteins; Humans; Membrane Proteins; Mice; Mutation; Protein Stability; Retinitis Pigmentosa; Rhodopsin	2022
Effects of the Unique Chromophore-Protein Interactions on the Primary Photoreaction of Schizorhodopsin. The journal of physical chemistry letters, 2023, Aug-10, Volume: 14, Issue:31 Topics: Cysteine; Isomerism; Protein Conformation; Rhodopsin; Rhodopsins, Microbial	2023