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Volumn 377, Issue 4, 2008, Pages 1067-1081

Rapid Incorporation of Functional Rhodopsin into Nanoscale Apolipoprotein Bound Bilayer (NABB) Particles

Author keywords

electron microscopy; G protein coupled receptor; high density lipoprotein; rhodopsin; single particle imaging

Indexed keywords

APOLIPOPROTEIN; RHODOPSIN;

EID: 40849130624     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.01.066     Document Type: Article
Times cited : (102)

References (57)
  • 2
    • 0020490523 scopus 로고
    • Micellar complexes of human apolipoprotein A-I with phosphatidylcholines and cholesterol prepared from cholate-lipid dispersions
    • Matz C.E., and Jonas A. Micellar complexes of human apolipoprotein A-I with phosphatidylcholines and cholesterol prepared from cholate-lipid dispersions. J. Biol. Chem. 257 (1982) 4535-4540
    • (1982) J. Biol. Chem. , vol.257 , pp. 4535-4540
    • Matz, C.E.1    Jonas, A.2
  • 3
    • 0020490580 scopus 로고
    • Reaction of human lecithin cholesterol acyltransferase with synthetic micellar complexes of apolipoprotein A-I, phosphatidylcholine, and cholesterol
    • Matz C.E., and Jonas A. Reaction of human lecithin cholesterol acyltransferase with synthetic micellar complexes of apolipoprotein A-I, phosphatidylcholine, and cholesterol. J. Biol. Chem. 257 (1982) 4541-4546
    • (1982) J. Biol. Chem. , vol.257 , pp. 4541-4546
    • Matz, C.E.1    Jonas, A.2
  • 4
    • 0024523877 scopus 로고
    • Defined apolipoprotein A-I conformations in reconstituted high-density lipoprotein disks
    • Jonas A., Kezdy K.E., and Wald J.H. Defined apolipoprotein A-I conformations in reconstituted high-density lipoprotein disks. J. Biol. Chem. 264 (1989) 4818-4824
    • (1989) J. Biol. Chem. , vol.264 , pp. 4818-4824
    • Jonas, A.1    Kezdy, K.E.2    Wald, J.H.3
  • 5
    • 0035942337 scopus 로고    scopus 로고
    • Arrangement of apolipoprotein A-I in reconstituted high-density lipoprotein disks: an alternative model based on fluorescence resonance energy transfer experiments
    • Tricerri M.A., Agree A.K.B., Sanchez S.A., Bronski J., and Jonas A. Arrangement of apolipoprotein A-I in reconstituted high-density lipoprotein disks: an alternative model based on fluorescence resonance energy transfer experiments. Biochemistry 40 (2001) 5065-5074
    • (2001) Biochemistry , vol.40 , pp. 5065-5074
    • Tricerri, M.A.1    Agree, A.K.B.2    Sanchez, S.A.3    Bronski, J.4    Jonas, A.5
  • 6
    • 34547927446 scopus 로고    scopus 로고
    • The structure of apolipoprotein A-I in high density lipoproteins
    • Davidson W.S., and Thompson T.B. The structure of apolipoprotein A-I in high density lipoproteins. J. Biol. Chem. 282 (2007) 22249-22253
    • (2007) J. Biol. Chem. , vol.282 , pp. 22249-22253
    • Davidson, W.S.1    Thompson, T.B.2
  • 8
    • 34250666273 scopus 로고    scopus 로고
    • A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein
    • Whorton M.R., Bokoch M.P., Rasmussen S.G., Huang B., Zare R.N., Kobilka B., and Sunahara R.K. A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein. Proc. Natl. Acad. Sci. USA 104 (2007) 7682-7687
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 7682-7687
    • Whorton, M.R.1    Bokoch, M.P.2    Rasmussen, S.G.3    Huang, B.4    Zare, R.N.5    Kobilka, B.6    Sunahara, R.K.7
  • 9
    • 34447509986 scopus 로고    scopus 로고
    • Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins
    • Bayburt T.H., Leitz A.J., Xie G., Oprian D.D., and Sligar S.G. Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins. J. Biol. Chem. 282 (2007) 14875-14881
    • (2007) J. Biol. Chem. , vol.282 , pp. 14875-14881
    • Bayburt, T.H.1    Leitz, A.J.2    Xie, G.3    Oprian, D.D.4    Sligar, S.G.5
  • 10
    • 0043007514 scopus 로고    scopus 로고
    • Self-assembly of discoidal phospholipid bilayer nanoparticles with membrane scaffold proteins
    • Bayburt T.H., Grinkova Y.V., and Sligar S.G. Self-assembly of discoidal phospholipid bilayer nanoparticles with membrane scaffold proteins. Nano Lett. 2 (2002) 853-856
    • (2002) Nano Lett. , vol.2 , pp. 853-856
    • Bayburt, T.H.1    Grinkova, Y.V.2    Sligar, S.G.3
  • 11
    • 0037076392 scopus 로고    scopus 로고
    • Single-molecule height measurements on microsomal cytochrome P450 in nanometer-scale phospholipid bilayer disks
    • Bayburt T.H., and Sligar S.G. Single-molecule height measurements on microsomal cytochrome P450 in nanometer-scale phospholipid bilayer disks. Proc. Natl. Acad. Sci. USA 99 (2002) 6725-6730
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6725-6730
    • Bayburt, T.H.1    Sligar, S.G.2
  • 12
    • 33744830288 scopus 로고    scopus 로고
    • Novel changes in discoidal high density lipoprotein morphology: a molecular dynamics study
    • Catte A., Patterson J.C., Jones M.K., Jerome W.G., Bashtovyy D., Su Z., et al. Novel changes in discoidal high density lipoprotein morphology: a molecular dynamics study. Biophys. J. 90 (2006) 4345-4360
    • (2006) Biophys. J. , vol.90 , pp. 4345-4360
    • Catte, A.1    Patterson, J.C.2    Jones, M.K.3    Jerome, W.G.4    Bashtovyy, D.5    Su, Z.6
  • 13
    • 25444491569 scopus 로고    scopus 로고
    • Intermolecular contact between globular N-terminal fold and C-terminal domain of apoA-I stabilizes its lipid-bound conformation: studies employing chemical cross-linking and mass spectrometry
    • Bhat S., Sorci-Thomas M.G., Alexander E.T., Samuel M.P., and Thomas M.J. Intermolecular contact between globular N-terminal fold and C-terminal domain of apoA-I stabilizes its lipid-bound conformation: studies employing chemical cross-linking and mass spectrometry. J. Biol. Chem. 280 (2005) 33015-33025
    • (2005) J. Biol. Chem. , vol.280 , pp. 33015-33025
    • Bhat, S.1    Sorci-Thomas, M.G.2    Alexander, E.T.3    Samuel, M.P.4    Thomas, M.J.5
  • 14
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., and Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157 (1982) 105-132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 16
    • 0036926084 scopus 로고    scopus 로고
    • Molecular dynamics simulations on discoidal HDL particles suggest a mechanism for rotation in the apo A-I belt model
    • Klon A.E., Segrest J.P., and Harvey S.C. Molecular dynamics simulations on discoidal HDL particles suggest a mechanism for rotation in the apo A-I belt model. J. Mol. Biol. 324 (2002) 703-721
    • (2002) J. Mol. Biol. , vol.324 , pp. 703-721
    • Klon, A.E.1    Segrest, J.P.2    Harvey, S.C.3
  • 17
    • 17444381547 scopus 로고    scopus 로고
    • Apolipoprotein A-I could be a significant determinant of epithelial integrity in rainbow trout gill cell cultures: a study in functional proteomics
    • Smith R.W., Wood C.M., Cash P., Diao L., and Part P. Apolipoprotein A-I could be a significant determinant of epithelial integrity in rainbow trout gill cell cultures: a study in functional proteomics. Biochim. Biophys. Acta 1749 (2005) 81-93
    • (2005) Biochim. Biophys. Acta , vol.1749 , pp. 81-93
    • Smith, R.W.1    Wood, C.M.2    Cash, P.3    Diao, L.4    Part, P.5
  • 18
    • 0037102326 scopus 로고    scopus 로고
    • On-column tris(2-carboxyethyl)phosphine reduction and IC5-maleimide labeling during purification of a RpoC fragment on a nickel-nitrilotriacetic acid column
    • Bergendahl V., Anthony L.C., Heyduk T., and Burgess R.R. On-column tris(2-carboxyethyl)phosphine reduction and IC5-maleimide labeling during purification of a RpoC fragment on a nickel-nitrilotriacetic acid column. Anal. Biochem. 307 (2002) 368-374
    • (2002) Anal. Biochem. , vol.307 , pp. 368-374
    • Bergendahl, V.1    Anthony, L.C.2    Heyduk, T.3    Burgess, R.R.4
  • 19
    • 0030732162 scopus 로고    scopus 로고
    • Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation
    • Borhani D.W., Rogers D.P., Engler J.A., and Brouillette C.G. Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation. Proc. Natl. Acad. Sci. USA 94 (1997) 12291-12296
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12291-12296
    • Borhani, D.W.1    Rogers, D.P.2    Engler, J.A.3    Brouillette, C.G.4
  • 20
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: physical principles
    • White S.H., and Wimley W.C. Membrane protein folding and stability: physical principles. Annu. Rev. Biophys. Biomol. Struct. 28 (1999) 319-365
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 21
    • 7044235790 scopus 로고    scopus 로고
    • Thermodynamics of lipid-peptide interactions
    • Seelig J. Thermodynamics of lipid-peptide interactions. Biochim. Biophys. Acta, Biomembr. 1666 (2004) 40-50
    • (2004) Biochim. Biophys. Acta, Biomembr. , vol.1666 , pp. 40-50
    • Seelig, J.1
  • 22
    • 4644262024 scopus 로고    scopus 로고
    • Enthalpy-driven apolipoprotein A-I and lipid bilayer interaction indicating protein penetration upon lipid binding
    • Arnulphi C., Jin L.H., Tricerri M.A., and Jonas A. Enthalpy-driven apolipoprotein A-I and lipid bilayer interaction indicating protein penetration upon lipid binding. Biochemistry 43 (2004) 12258-12264
    • (2004) Biochemistry , vol.43 , pp. 12258-12264
    • Arnulphi, C.1    Jin, L.H.2    Tricerri, M.A.3    Jonas, A.4
  • 23
    • 0030614601 scopus 로고    scopus 로고
    • Truncation of the amino terminus of human apolipoprotein A-I substantially alters only the lipid-free conformation
    • Rogers D.P., Brouillette C.G., Engler J.A., Tendian S.W., Roberts L., Mishra V.K., et al. Truncation of the amino terminus of human apolipoprotein A-I substantially alters only the lipid-free conformation. Biochemistry 36 (1997) 288-300
    • (1997) Biochemistry , vol.36 , pp. 288-300
    • Rogers, D.P.1    Brouillette, C.G.2    Engler, J.A.3    Tendian, S.W.4    Roberts, L.5    Mishra, V.K.6
  • 24
    • 0026254055 scopus 로고
    • Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water
    • Scholtz J.M., Hong Q., York E.J., Stewart J.M., and Baldwin R.L. Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water. Biopolymers 31 (1991) 1463-1470
    • (1991) Biopolymers , vol.31 , pp. 1463-1470
    • Scholtz, J.M.1    Hong, Q.2    York, E.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 25
    • 6344248642 scopus 로고    scopus 로고
    • Double belt structure of discoidal high density lipoproteins: molecular basis for size heterogeneity
    • Li L., Chen J.G., Mishra V.K., Kurtz J.A., Cao D.F., Klon A.E., et al. Double belt structure of discoidal high density lipoproteins: molecular basis for size heterogeneity. J. Mol. Biol. 343 (2004) 1293-1311
    • (2004) J. Mol. Biol. , vol.343 , pp. 1293-1311
    • Li, L.1    Chen, J.G.2    Mishra, V.K.3    Kurtz, J.A.4    Cao, D.F.5    Klon, A.E.6
  • 26
    • 0016529701 scopus 로고
    • d-Pantolactone as a circular dichroism (CD) calibration
    • Konno T., Meguro H., and Tuzimura K. d-Pantolactone as a circular dichroism (CD) calibration. Anal. Biochem. 67 (1975) 226-232
    • (1975) Anal. Biochem. , vol.67 , pp. 226-232
    • Konno, T.1    Meguro, H.2    Tuzimura, K.3
  • 27
    • 0036192245 scopus 로고    scopus 로고
    • Interaction of apolipoprotein A-I in three different conformations with palmitoyl oleoyl phosphatidylcholine vesicles
    • Tricerri M.A., Sanchez S.A., Arnulphi C., Durbin D.M., Gratton E., and Jonas A. Interaction of apolipoprotein A-I in three different conformations with palmitoyl oleoyl phosphatidylcholine vesicles. J. Lipid Res. 43 (2002) 187-197
    • (2002) J. Lipid Res. , vol.43 , pp. 187-197
    • Tricerri, M.A.1    Sanchez, S.A.2    Arnulphi, C.3    Durbin, D.M.4    Gratton, E.5    Jonas, A.6
  • 28
    • 0029101114 scopus 로고
    • Reconstitution of membrane-proteins into liposomes-application to energy-transducing membrane-proteins
    • Rigaud J.L., Pitard B., and Levy D. Reconstitution of membrane-proteins into liposomes-application to energy-transducing membrane-proteins. Biochim. Biophys. Acta 1231 (1995) 223-246
    • (1995) Biochim. Biophys. Acta , vol.1231 , pp. 223-246
    • Rigaud, J.L.1    Pitard, B.2    Levy, D.3
  • 29
    • 0027848788 scopus 로고
    • 3-Dimensional immunoelectron microscopy of scorpion hemocyanin labeled with a monoclonal Fab fragment
    • Boisset N., Radermacher M., Grassucci R., Taveau J.C., Liu W.P., Lamy J., et al. 3-Dimensional immunoelectron microscopy of scorpion hemocyanin labeled with a monoclonal Fab fragment. J. Struct. Biol. 111 (1993) 234-244
    • (1993) J. Struct. Biol. , vol.111 , pp. 234-244
    • Boisset, N.1    Radermacher, M.2    Grassucci, R.3    Taveau, J.C.4    Liu, W.P.5    Lamy, J.6
  • 31
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high-resolution single-particle reconstructions
    • Lüdtke S.J., Baldwin P.R., and Chiu W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128 (1999) 82-97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Lüdtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 32
    • 0008882006 scopus 로고
    • The thermal stability of rhodopsin and opsin
    • Hubbard R. The thermal stability of rhodopsin and opsin. J. Gen. Physiol. 42 (1958) 259-280
    • (1958) J. Gen. Physiol. , vol.42 , pp. 259-280
    • Hubbard, R.1
  • 33
    • 0018208522 scopus 로고
    • Stability of rhodopsin in detergent solutions
    • Knudsen P., and Hubbell W.L. Stability of rhodopsin in detergent solutions. Membr. Biochem. 1 (1978) 297-322
    • (1978) Membr. Biochem. , vol.1 , pp. 297-322
    • Knudsen, P.1    Hubbell, W.L.2
  • 34
    • 0019827661 scopus 로고
    • The asymmetric transmembrane distribution of phosphatidylethanolamine, phosphatidylserine, and fatty acids of the bovine retinal rod outer segment disk membrane
    • Miljanich G.P., Nemes P.P., White D.L., and Dratz E.A. The asymmetric transmembrane distribution of phosphatidylethanolamine, phosphatidylserine, and fatty acids of the bovine retinal rod outer segment disk membrane. J. Membr. Biol. 60 (1981) 249-255
    • (1981) J. Membr. Biol. , vol.60 , pp. 249-255
    • Miljanich, G.P.1    Nemes, P.P.2    White, D.L.3    Dratz, E.A.4
  • 35
    • 0020020857 scopus 로고
    • Fatty acid composition and pairing in phospholipids of rod outer segments
    • Miljanich G.P., and Dratz E.A. Fatty acid composition and pairing in phospholipids of rod outer segments. Methods Enzymol. 81 (1982) 806-815
    • (1982) Methods Enzymol. , vol.81 , pp. 806-815
    • Miljanich, G.P.1    Dratz, E.A.2
  • 36
    • 0038729667 scopus 로고    scopus 로고
    • Signaling states of rhodopsin-formation of the storage form, metarhodopsin III, from active metarhodopsin II
    • Heck M., Schädel S.A., Maretzki D., Bartl F.J., Ritter E., Palczewski K., and Hofmann K.P. Signaling states of rhodopsin-formation of the storage form, metarhodopsin III, from active metarhodopsin II. J. Biol. Chem. 278 (2003) 3162-3169
    • (2003) J. Biol. Chem. , vol.278 , pp. 3162-3169
    • Heck, M.1    Schädel, S.A.2    Maretzki, D.3    Bartl, F.J.4    Ritter, E.5    Palczewski, K.6    Hofmann, K.P.7
  • 37
    • 10844243995 scopus 로고    scopus 로고
    • Functional characterization of rhodopsin monomers and dimers in detergents
    • Jastrzebska B., Maeda T., Zhu L., Fotiadis D., Filipek S., Engel A., et al. Functional characterization of rhodopsin monomers and dimers in detergents. J. Biol. Chem. 279 (2004) 54663-54675
    • (2004) J. Biol. Chem. , vol.279 , pp. 54663-54675
    • Jastrzebska, B.1    Maeda, T.2    Zhu, L.3    Fotiadis, D.4    Filipek, S.5    Engel, A.6
  • 38
    • 40849089587 scopus 로고
    • Turnover number
    • Wiley-Interscience, New York, NY
    • Segel I.H. Turnover number. Enzyme Kinetics vol. 1 (1993), Wiley-Interscience, New York, NY 79-80
    • (1993) Enzyme Kinetics , vol.1 , pp. 79-80
    • Segel, I.H.1
  • 39
    • 15444376596 scopus 로고    scopus 로고
    • Solubilization, stabilization, and purification of chemokine receptors using biosensor technology
    • Navratilova I., Sodroski J., and Myszka D.G. Solubilization, stabilization, and purification of chemokine receptors using biosensor technology. Anal. Biochem. 339 (2005) 271-281
    • (2005) Anal. Biochem. , vol.339 , pp. 271-281
    • Navratilova, I.1    Sodroski, J.2    Myszka, D.G.3
  • 40
    • 1942519744 scopus 로고    scopus 로고
    • Membrane model for the G-protein-coupled receptor rhodopsin: hydrophobic interface and dynamical structure
    • Huber T., Botelho A.V., Beyer K., and Brown M.F. Membrane model for the G-protein-coupled receptor rhodopsin: hydrophobic interface and dynamical structure. Biophys. J. 86 (2004) 2078-2100
    • (2004) Biophys. J. , vol.86 , pp. 2078-2100
    • Huber, T.1    Botelho, A.V.2    Beyer, K.3    Brown, M.F.4
  • 41
    • 33845930555 scopus 로고    scopus 로고
    • Evidence for specificity in lipid-rhodopsin interactions
    • Soubias O., Teague W.E., and Gawrisch K. Evidence for specificity in lipid-rhodopsin interactions. J. Biol. Chem. 281 (2006) 33233-33241
    • (2006) J. Biol. Chem. , vol.281 , pp. 33233-33241
    • Soubias, O.1    Teague, W.E.2    Gawrisch, K.3
  • 42
    • 0028124422 scopus 로고
    • Modulation of rhodopsin function by properties of the membrane bilayer
    • Brown M.F. Modulation of rhodopsin function by properties of the membrane bilayer. Chem. Phys. Lipids 73 (1994) 159-180
    • (1994) Chem. Phys. Lipids , vol.73 , pp. 159-180
    • Brown, M.F.1
  • 43
    • 33845505655 scopus 로고    scopus 로고
    • Curvature and hydrophobic forces drive oligomerization and modulate activity of rhodopsin in membranes
    • Botelho A.V., Huber T., Sakmar T.P., and Brown M.F. Curvature and hydrophobic forces drive oligomerization and modulate activity of rhodopsin in membranes. Biophys. J. 91 (2006) 4464-4477
    • (2006) Biophys. J. , vol.91 , pp. 4464-4477
    • Botelho, A.V.1    Huber, T.2    Sakmar, T.P.3    Brown, M.F.4
  • 44
    • 34548146523 scopus 로고    scopus 로고
    • G protein-coupled receptors self-assemble in dynamics simulations of model bilayers
    • Periole X., Huber T., Marrink S.J., and Sakmar T.P. G protein-coupled receptors self-assemble in dynamics simulations of model bilayers. J. Am. Chem. Soc. 129 (2007) 10126-10132
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 10126-10132
    • Periole, X.1    Huber, T.2    Marrink, S.J.3    Sakmar, T.P.4
  • 46
    • 0242581698 scopus 로고    scopus 로고
    • Biophysics-is rhodopsin dimeric in native rods?
    • Chabre M., Cone R., and Saibil H. Biophysics-is rhodopsin dimeric in native rods?. Nature 426 (2003) 30-31
    • (2003) Nature , vol.426 , pp. 30-31
    • Chabre, M.1    Cone, R.2    Saibil, H.3
  • 47
    • 34547434085 scopus 로고    scopus 로고
    • Monomeric G protein-coupled receptor rhodopsin in solution activates its G protein transducin at the diffusion limit
    • Ernst O.P., Gramse V., Kolbe M., Hofmann K.P., and Heck M. Monomeric G protein-coupled receptor rhodopsin in solution activates its G protein transducin at the diffusion limit. Proc. Natl. Acad. Sci. USA 104 (2007) 10859-10864
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 10859-10864
    • Ernst, O.P.1    Gramse, V.2    Kolbe, M.3    Hofmann, K.P.4    Heck, M.5
  • 49
    • 21844441860 scopus 로고    scopus 로고
    • Monomeric G-protein-coupled receptor as a functional unit
    • Chabre M., and le Maire M. Monomeric G-protein-coupled receptor as a functional unit. Biochemistry 44 (2005) 9395-9403
    • (2005) Biochemistry , vol.44 , pp. 9395-9403
    • Chabre, M.1    le Maire, M.2
  • 50
    • 0038159530 scopus 로고    scopus 로고
    • Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes
    • Liang Y., Fotiadis D., Filipek S., Saperstein D.A., Palczewski K., and Engel A. Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes. J. Biol. Chem. 278 (2003) 21655-21662
    • (2003) J. Biol. Chem. , vol.278 , pp. 21655-21662
    • Liang, Y.1    Fotiadis, D.2    Filipek, S.3    Saperstein, D.A.4    Palczewski, K.5    Engel, A.6
  • 54
    • 38349107042 scopus 로고    scopus 로고
    • Site-specific incorporation of keto amino acids into functional G protein-coupled receptors using unnatural amino acid mutagenesis
    • Ye S., Köhrer C., Huber T., Kazmi M., Sachdev P., Yan E.C., et al. Site-specific incorporation of keto amino acids into functional G protein-coupled receptors using unnatural amino acid mutagenesis. J. Biol. Chem. 283 (2008) 1525-1533
    • (2008) J. Biol. Chem. , vol.283 , pp. 1525-1533
    • Ye, S.1    Köhrer, C.2    Huber, T.3    Kazmi, M.4    Sachdev, P.5    Yan, E.C.6
  • 55
    • 0020020855 scopus 로고
    • Preparation of retinal rod outer segments
    • Papermaster D.S. Preparation of retinal rod outer segments. Methods Enzymol. 81 (1982) 48-52
    • (1982) Methods Enzymol. , vol.81 , pp. 48-52
    • Papermaster, D.S.1
  • 56
    • 0028957661 scopus 로고
    • Structure and function in rhodopsin. Measurement of the rate of metarhodopsin II decay by fluorescence spectroscopy
    • Farrens D.L., and Khorana H.G. Structure and function in rhodopsin. Measurement of the rate of metarhodopsin II decay by fluorescence spectroscopy. J. Biol. Chem. 270 (1995) 5073-5076
    • (1995) J. Biol. Chem. , vol.270 , pp. 5073-5076
    • Farrens, D.L.1    Khorana, H.G.2
  • 57
    • 0027820508 scopus 로고
    • Light-dependent transducin activation by an ultraviolet-absorbing rhodopsin mutant
    • Fahmy K., and Sakmar T.P. Light-dependent transducin activation by an ultraviolet-absorbing rhodopsin mutant. Biochemistry 32 (1993) 9165-9171
    • (1993) Biochemistry , vol.32 , pp. 9165-9171
    • Fahmy, K.1    Sakmar, T.P.2


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