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Results: 1-11 |
Results: 11
Structure and function in rhodopsin: Mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants
Authors: Hwa, J Klein-Seetharaman, J Khorana, HG
Citation: J. Hwa et al., Structure and function in rhodopsin: Mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants, P NAS US, 98(9), 2001, pp. 4872-4876
Solution F-19 nuclear Overhauser effects in structural studies of the cytoplasmic domain of mammalian rhodopsin
Authors: Loewen, MC Klein-Seetharaman, J Getmanova, EV Reeves, PJ Schwalbe, H Khorana, HG
Citation: Mc. Loewen et al., Solution F-19 nuclear Overhauser effects in structural studies of the cytoplasmic domain of mammalian rhodopsin, P NAS US, 98(9), 2001, pp. 4888-4892
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
Authors: Klein-Seetharaman, J Hwa, J Cai, KW Altenbach, C Hubbell, WL Khorana, HG
Citation: J. Klein-seetharaman et al., 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, BIOCHEM, 40(42), 2001, pp. 12472-12478
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
Authors: Cai, KW Klein-Seetharaman, J Altenbach, C Hubbell, WL Khorana, HG
Citation: Kw. Cai et al., 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, BIOCHEM, 40(42), 2001, pp. 12479-12485
Expression and purification of rhodopsin and its mutants from stable mammalian cell lines: application to NMR studies
Authors: Reeves, PJ Klein-Seetharaman, J Getmanova, EV Eilers, M Loewen, MC Smith, SO Khorana, HG
Citation: Pj. Reeves et al., Expression and purification of rhodopsin and its mutants from stable mammalian cell lines: application to NMR studies, BIOCH SOC T, 27, 1999, pp. 950-955
Structure and function in rhodopsin: Further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function
Authors: Hwa, J Reeves, PJ Klein-Seetharaman, J Davidson, F Khorana, HG
Citation: J. Hwa et al., Structure and function in rhodopsin: Further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function, P NAS US, 96(5), 1999, pp. 1932-1935
NMR spectroscopy in studies of light-induced structural changes in mammalian rhodopsin: Applicability of solution F-19 NMR
Authors: Klein-Seetharaman, J Getmanova, EV Loewen, MC Reeves, PJ Khorana, HG
Citation: 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
Structure and function in rhodopsin: Effects of disulfide cross-links in the cytoplasmic face of rhodopsin on transducin activation and phosphorylation by rhodopsin kinase
Authors: Cai, K Klein-Seetharaman, J Hwa, J Hubbell, WL Khorana, HG
Citation: 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
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
Authors: Cai, KW Klein-Seetharaman, J Farrens, D Zhang, C Altenbach, C Hubbell, WL Khorana, HG
Citation: Kw. 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
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
Authors: Klein-Seetharaman, J Hwa, J Cai, KW Altenbach, C Hubbell, WL Khorana, HG
Citation: 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
Structural features and light-dependent changes in the sequence 59-75 connecting helices I and II in rhodopsin: A site-directed spin-labeling study
Authors: Altenbach, C Klein-Seetharaman, J Hwa, J Khorana, HG Hubbell, WL
Citation: 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
Risultati: 1-11 |