Biophysical approaches to G protein-coupled receptors: Structure, function and dynamics
暂无分享,去创建一个
[1] H. Macleod,et al. Conformational changes in rhodopsin probed by surface plasmon resonance spectroscopy. , 1994, Biochemistry.
[2] Stephen H. White,et al. Membrane protein structure: experimental approaches , 1994 .
[3] H G Khorana,et al. Structure and function in rhodopsin. Single cysteine substitution mutants in the cytoplasmic interhelical E-F loop region show position-specific effects in transducin activation. , 1996, Biochemistry.
[4] G. Turcatti,et al. Fluorescent labeling of NK2 receptor at specific sites in vivo and fluorescence energy transfer analysis of NK2 ligand-receptor complexes. , 1997, Receptors & channels.
[5] S. White. Membrane Protein Structure , 1994, Methods in Physiology Series.
[6] M. Lyttle,et al. Site-specific incorporation of nonnatural residues during in vitro protein biosynthesis with semisynthetic aminoacyl-tRNAs. , 1991, Biochemistry.
[7] Dewey Tg,et al. Fluorescence labeling of the palmitoylation sites of rhodopsin. , 1994 .
[8] K. Hideg,et al. Photoactivated conformational changes in rhodopsin: a time-resolved spin label study. , 1993, Science.
[9] H. Khorana,et al. Mapping light-dependent structural changes in the cytoplasmic loop connecting helices C and D in rhodopsin: a site-directed spin labeling study. , 1995, Biochemistry.
[10] G. Turcatti,et al. Synthesis and characterization of selective fluorescent ligands for the neurokinin NK2 receptor. , 1994, Journal of medicinal chemistry.
[11] Manuel Peitsch,et al. Probing the Structure and Function of the Tachykinin Neurokinin-2 Receptor through Biosynthetic Incorporation of Fluorescent Amino Acids at Specific Sites* , 1996, The Journal of Biological Chemistry.
[12] L. Stryer. Fluorescence energy transfer as a spectroscopic ruler. , 1978, Annual review of biochemistry.
[13] B. Seligmann,et al. Fluorescence analysis of the size of a binding pocket of a peptide receptor at natural abundance. , 1990, Biochemistry.
[14] C. Strader,et al. Characterization of the binding domain of the beta-adrenergic receptor with the fluorescent antagonist carazolol. Evidence for a buried ligand binding site. , 1990, The Journal of biological chemistry.
[15] G. Turcatti,et al. Characterization of Non-peptide Antagonist and Peptide Agonist Binding Sites of the NK1 Receptor with Fluorescent Ligands* , 1997, The Journal of Biological Chemistry.
[16] H. Khorana,et al. Transmembrane protein structure: spin labeling of bacteriorhodopsin mutants. , 1990, Science.
[17] P G Schultz,et al. A general method for site-specific incorporation of unnatural amino acids into proteins. , 1989, Science.
[18] H. Khorana,et al. Structural features and light-dependent changes in the cytoplasmic interhelical E-F loop region of rhodopsin: a site-directed spin-labeling study. , 1996, Biochemistry.
[19] G. Turcatti,et al. Probing the binding domain of the NK2 receptor with fluorescent ligands: evidence that heptapeptide agonists and antagonists bind differently. , 1995, Biochemistry.
[20] B. Kobilka,et al. Fluorescent labeling of purified beta 2 adrenergic receptor. Evidence for ligand-specific conformational changes. , 1995, The Journal of biological chemistry.
[21] C. Altenbach,et al. Investigation of structure and dynamics in membrane proteins using site-directed spin labeling , 1994 .
[22] H. Khorana,et al. Formation of the meta II photointermediate is accompanied by conformational changes in the cytoplasmic surface of rhodopsin. , 1993, Biochemistry.
[23] L. Sklar,et al. Evidence for protonation in the human neutrophil formyl peptide receptor binding pocket. , 1993, Biochemistry.
[24] Gebhard F. X. Schertler,et al. Projection structure of rhodopsin , 1993, Nature.
[25] O. Lichtarge,et al. Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F , 1996, Nature.