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Volumn 15, Issue 5, 2007, Pages 611-623

The Signaling Pathway of Rhodopsin

Author keywords

SIGNALING

Indexed keywords

ASPARTIC ACID; GLUTAMIC ACID; RETINAL; RHODOPSIN;

EID: 34247847854     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2007.04.002     Document Type: Article
Times cited : (46)

References (58)
  • 1
    • 36749107785 scopus 로고
    • Molecular dynamics simulations at constant pressure and/or temperature
    • Andersen H.C. Molecular dynamics simulations at constant pressure and/or temperature. J. Chem. Phys. 72 (1980) 2384-2393
    • (1980) J. Chem. Phys. , vol.72 , pp. 2384-2393
    • Andersen, H.C.1
  • 2
    • 0029156621 scopus 로고
    • Photoregeneration of bovine rhodopsin from its signaling state
    • Arnis S., and Hofmann K.P. Photoregeneration of bovine rhodopsin from its signaling state. Biochemistry 34 (1995) 9333-9340
    • (1995) Biochemistry , vol.34 , pp. 9333-9340
    • Arnis, S.1    Hofmann, K.P.2
  • 3
    • 0031467960 scopus 로고    scopus 로고
    • Molecular determinants of selectivity in 5-hydroxytryptamine1B receptor-G protein interactions
    • Bae H., Anderson K., Flood L.A., Skiba N.P., Hamm H.E., and Graber S.G. Molecular determinants of selectivity in 5-hydroxytryptamine1B receptor-G protein interactions. J. Biol. Chem. 272 (1997) 32071-32077
    • (1997) J. Biol. Chem. , vol.272 , pp. 32071-32077
    • Bae, H.1    Anderson, K.2    Flood, L.A.3    Skiba, N.P.4    Hamm, H.E.5    Graber, S.G.6
  • 4
    • 0033591051 scopus 로고    scopus 로고
    • Two amino acids within the α4 helix of Gαi1 mediate coupling with 5-hydroxytryptamine1B receptors
    • Bae H., Cabrera-Vera T.M., Depree K.M., Graber S.G., and Hamm H.E. Two amino acids within the α4 helix of Gαi1 mediate coupling with 5-hydroxytryptamine1B receptors. J. Biol. Chem. 274 (1999) 14963-14971
    • (1999) J. Biol. Chem. , vol.274 , pp. 14963-14971
    • Bae, H.1    Cabrera-Vera, T.M.2    Depree, K.M.3    Graber, S.G.4    Hamm, H.E.5
  • 5
    • 0018333003 scopus 로고
    • Responses of retinal rods to single photons
    • Baylor D.A., Lamb T.D., and Yau K.W. Responses of retinal rods to single photons. J. Physiol. 288 (1979) 613-634
    • (1979) J. Physiol. , vol.288 , pp. 613-634
    • Baylor, D.A.1    Lamb, T.D.2    Yau, K.W.3
  • 7
    • 0035942238 scopus 로고    scopus 로고
    • Mapping of contact sites in complex formation between transducin and light-activated rhodopsin by covalent crosslinking: use of a photoactivatable reagent
    • Cai K., Itoh Y., and Khorana H.G. Mapping of contact sites in complex formation between transducin and light-activated rhodopsin by covalent crosslinking: use of a photoactivatable reagent. Proc. Natl. Acad. Sci. USA 98 (2001) 4877-4882
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4877-4882
    • Cai, K.1    Itoh, Y.2    Khorana, H.G.3
  • 8
    • 0031910020 scopus 로고    scopus 로고
    • Locally accessible conformations of proteins: multiple molecular dynamics simulations of crambin
    • Caves L.S., Evanseck J.D., and Karplus M. Locally accessible conformations of proteins: multiple molecular dynamics simulations of crambin. Protein Sci. 7 (1998) 649-666
    • (1998) Protein Sci. , vol.7 , pp. 649-666
    • Caves, L.S.1    Evanseck, J.D.2    Karplus, M.3
  • 9
    • 20344370764 scopus 로고    scopus 로고
    • Allosteric mechanisms of signal transduction
    • Changeux J.P., and Edelstein S.J. Allosteric mechanisms of signal transduction. Science 308 (2005) 1424-1428
    • (2005) Science , vol.308 , pp. 1424-1428
    • Changeux, J.P.1    Edelstein, S.J.2
  • 10
    • 0141927102 scopus 로고    scopus 로고
    • Molecular dynamics simulation of dark-adapted rhodopsin in an explicit membrane bilayer: coupling between local retinal and larger scale conformational change
    • Crozier P.S., Stevens M.J., Forrest L.R., and Woolf T.B. Molecular dynamics simulation of dark-adapted rhodopsin in an explicit membrane bilayer: coupling between local retinal and larger scale conformational change. J. Mol. Biol. 333 (2003) 493-514
    • (2003) J. Mol. Biol. , vol.333 , pp. 493-514
    • Crozier, P.S.1    Stevens, M.J.2    Forrest, L.R.3    Woolf, T.B.4
  • 11
    • 33846218265 scopus 로고    scopus 로고
    • How a small change in retinal leads to G-protein activation: initial events suggested by molecular dynamics calculations
    • Crozier P.S., Stevens M.J., and Woolf T.B. How a small change in retinal leads to G-protein activation: initial events suggested by molecular dynamics calculations. Proteins 66 (2007) 559-574
    • (2007) Proteins , vol.66 , pp. 559-574
    • Crozier, P.S.1    Stevens, M.J.2    Woolf, T.B.3
  • 13
    • 0034730097 scopus 로고    scopus 로고
    • Transducin-dependent protonation of glutamic acid 134 in rhodopsin
    • Fahmy K., Sakmar T.P., and Siebert F. Transducin-dependent protonation of glutamic acid 134 in rhodopsin. Biochemistry 39 (2000) 10607-10612
    • (2000) Biochemistry , vol.39 , pp. 10607-10612
    • Fahmy, K.1    Sakmar, T.P.2    Siebert, F.3
  • 14
    • 0029035661 scopus 로고
    • Mapping light-dependent structural changes in the cytoplasmic loop connecting helices C and D in rhodopsin: a site-directed spin labeling study
    • Farahbakhsh Z.T., Ridge K.D., Khorana H.G., and Hubbell W.L. Mapping light-dependent structural changes in the cytoplasmic loop connecting helices C and D in rhodopsin: a site-directed spin labeling study. Biochemistry 34 (1995) 8812-8819
    • (1995) Biochemistry , vol.34 , pp. 8812-8819
    • Farahbakhsh, Z.T.1    Ridge, K.D.2    Khorana, H.G.3    Hubbell, W.L.4
  • 19
    • 0021051045 scopus 로고
    • Hemoglobin tertiary structural change on ligand binding. Its role in the co-operative mechanism
    • Gelin B.R., Lee A.W., and Karplus M. Hemoglobin tertiary structural change on ligand binding. Its role in the co-operative mechanism. J. Mol. Biol. 171 (1983) 489-559
    • (1983) J. Mol. Biol. , vol.171 , pp. 489-559
    • Gelin, B.R.1    Lee, A.W.2    Karplus, M.3
  • 20
    • 0032541084 scopus 로고    scopus 로고
    • G protein-coupled receptors. II. Mechanism of agonist activation
    • Gether U., and Kobilka B.K. G protein-coupled receptors. II. Mechanism of agonist activation. J. Biol. Chem. 273 (1998) 17979-17982
    • (1998) J. Biol. Chem. , vol.273 , pp. 17979-17982
    • Gether, U.1    Kobilka, B.K.2
  • 21
    • 33847361456 scopus 로고    scopus 로고
    • Convergence of molecular dynamics simulations of membrane proteins
    • Grossfield A., Feller S.E., and Pitman M.C. Convergence of molecular dynamics simulations of membrane proteins. Proteins 67 (2007) 31-40
    • (2007) Proteins , vol.67 , pp. 31-40
    • Grossfield, A.1    Feller, S.E.2    Pitman, M.C.3
  • 22
    • 0001538909 scopus 로고
    • Canonical dynamics: equilibrium phase-space distributions
    • Hoover W.G. Canonical dynamics: equilibrium phase-space distributions. Phys. Rev. A. 31 (1984) 1695-1697
    • (1984) Phys. Rev. A. , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 23
    • 0001575530 scopus 로고
    • Cis-trans isomers of vitamin A and retinene in the rhodopsin system
    • Hubbard R., and Wald G. Cis-trans isomers of vitamin A and retinene in the rhodopsin system. J. Gen. Physiol. 36 (1952) 269-315
    • (1952) J. Gen. Physiol. , vol.36 , pp. 269-315
    • Hubbard, R.1    Wald, G.2
  • 24
    • 0037285444 scopus 로고    scopus 로고
    • Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking
    • Hubbell W.L., Altenbach C., Hubbell C.M., and Khorana H.G. Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking. Adv. Protein Chem. 63 (2003) 243-290
    • (2003) Adv. Protein Chem. , vol.63 , pp. 243-290
    • Hubbell, W.L.1    Altenbach, C.2    Hubbell, C.M.3    Khorana, H.G.4
  • 25
    • 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
  • 26
    • 33751094833 scopus 로고    scopus 로고
    • Predisposition of the dark state of rhodopsin to functional changes in structure
    • Isin B., Rader A.J., Dhiman H.K., Klein-Seetharaman J., and Bahar I. Predisposition of the dark state of rhodopsin to functional changes in structure. Proteins 65 (2006) 970-983
    • (2006) Proteins , vol.65 , pp. 970-983
    • Isin, B.1    Rader, A.J.2    Dhiman, H.K.3    Klein-Seetharaman, J.4    Bahar, I.5
  • 27
    • 0035942229 scopus 로고    scopus 로고
    • Mapping of contact sites in complex formation between light-activated rhodopsin and transducin by covalent crosslinking: use of a chemically preactivated reagent
    • Itoh Y., Cai K., and Khorana H.G. Mapping of contact sites in complex formation between light-activated rhodopsin and transducin by covalent crosslinking: use of a chemically preactivated reagent. Proc. Natl. Acad. Sci. USA 98 (2001) 4883-4887
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4883-4887
    • Itoh, Y.1    Cai, K.2    Khorana, H.G.3
  • 28
    • 1842861561 scopus 로고    scopus 로고
    • Biomolecular motors: the F1-ATPase paradigm
    • Karplus M., and Gao Y.Q. Biomolecular motors: the F1-ATPase paradigm. Curr. Opin. Struct. Biol. 14 (2004) 250-259
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 250-259
    • Karplus, M.1    Gao, Y.Q.2
  • 29
    • 0031446595 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: rhodopsin mutants with a neutral amino acid at E134 have a partially activated conformation in the dark state
    • Kim J.M., Altenbach C., Thurmond R.L., Khorana H.G., and Hubbell W.L. Structure and function in rhodopsin: rhodopsin mutants with a neutral amino acid at E134 have a partially activated conformation in the dark state. Proc. Natl. Acad. Sci. USA 94 (1997) 14273-14278
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14273-14278
    • Kim, J.M.1    Altenbach, C.2    Thurmond, R.L.3    Khorana, H.G.4    Hubbell, W.L.5
  • 30
    • 0031016906 scopus 로고    scopus 로고
    • Molecular basis of receptor/G protein coupling selectivity studied by coexpression of wild type and mutant m2 muscarinic receptors with mutant G α(q) subunits
    • Kostenis E., Conklin B.R., and Wess J. Molecular basis of receptor/G protein coupling selectivity studied by coexpression of wild type and mutant m2 muscarinic receptors with mutant G α(q) subunits. Biochemistry 36 (1997) 1487-1495
    • (1997) Biochemistry , vol.36 , pp. 1487-1495
    • Kostenis, E.1    Conklin, B.R.2    Wess, J.3
  • 31
    • 0035498356 scopus 로고    scopus 로고
    • Kinetics and pH dependence of light-induced deprotonation of the Schiff base of rhodopsin: possible coupling to proton uptake and formation of the active form of Meta II
    • Kuwata O., Yuan C., Misra S., Govindjee R., and Ebrey T.G. Kinetics and pH dependence of light-induced deprotonation of the Schiff base of rhodopsin: possible coupling to proton uptake and formation of the active form of Meta II. Biochemistry (Mosc.) 66 (2001) 1283-1299
    • (2001) Biochemistry (Mosc.) , vol.66 , pp. 1283-1299
    • Kuwata, O.1    Yuan, C.2    Misra, S.3    Govindjee, R.4    Ebrey, T.G.5
  • 32
    • 25444478851 scopus 로고    scopus 로고
    • Molecular dynamics simulations of retinal in rhodopsin: from the dark-adapted state towards lumirhodopsin
    • Lemaitre V., Yeagle P., and Watts A. Molecular dynamics simulations of retinal in rhodopsin: from the dark-adapted state towards lumirhodopsin. Biochemistry 44 (2005) 12667-12680
    • (2005) Biochemistry , vol.44 , pp. 12667-12680
    • Lemaitre, V.1    Yeagle, P.2    Watts, A.3
  • 33
    • 0000961995 scopus 로고
    • Evaluation of the configurational entropy for proteins: application to molecular dynamics simulations of an α-helix
    • Levy R.M., Martin K., Kushick J., and Perahia D. Evaluation of the configurational entropy for proteins: application to molecular dynamics simulations of an α-helix. Macromolecules 17 (1984) 1370-1374
    • (1984) Macromolecules , vol.17 , pp. 1370-1374
    • Levy, R.M.1    Martin, K.2    Kushick, J.3    Perahia, D.4
  • 34
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • Lockless S.W., and Ranganathan R. Evolutionarily conserved pathways of energetic connectivity in protein families. Science 286 (1999) 295-299
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 35
    • 0035498937 scopus 로고    scopus 로고
    • Receptor activation: what does the rhodopsin structure tell us?
    • Meng E.C., and Bourne H.R. Receptor activation: what does the rhodopsin structure tell us?. Trends Pharmacol. Sci. 22 (2001) 587-593
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 587-593
    • Meng, E.C.1    Bourne, H.R.2
  • 36
    • 0034784920 scopus 로고    scopus 로고
    • Rhodopsin: structural basis of molecular physiology
    • Menon S.T., Han M., and Sakmar T.P. Rhodopsin: structural basis of molecular physiology. Physiol. Rev. 81 (2001) 1659-1688
    • (2001) Physiol. Rev. , vol.81 , pp. 1659-1688
    • Menon, S.T.1    Han, M.2    Sakmar, T.P.3
  • 37
    • 33746321096 scopus 로고    scopus 로고
    • Crystallographic analysis of primary visual photochemistry
    • Nakamichi H., and Okada T. Crystallographic analysis of primary visual photochemistry. Angew. Chem. Int. Ed. Engl. 45 (2006) 4270-4273
    • (2006) Angew. Chem. Int. Ed. Engl. , vol.45 , pp. 4270-4273
    • Nakamichi, H.1    Okada, T.2
  • 38
    • 33748079137 scopus 로고    scopus 로고
    • Local peptide movement in the photoreaction intermediate of rhodopsin
    • Nakamichi H., and Okada T. Local peptide movement in the photoreaction intermediate of rhodopsin. Proc. Natl. Acad. Sci. USA 103 (2006) 12729-12734
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 12729-12734
    • Nakamichi, H.1    Okada, T.2
  • 39
    • 84926811618 scopus 로고
    • Constant pressure molecular-dynamics for molecular-systems
    • Nose S., and Klein M.L. Constant pressure molecular-dynamics for molecular-systems. Mol. Phys. 50 (1983) 1055-1076
    • (1983) Mol. Phys. , vol.50 , pp. 1055-1076
    • Nose, S.1    Klein, M.L.2
  • 40
    • 0035336676 scopus 로고    scopus 로고
    • Activation of rhodopsin: new insights from structural and biochemical studies
    • Okada T., Ernst O.P., Palczewski K., and Hofmann K.P. Activation of rhodopsin: new insights from structural and biochemical studies. Trends Biochem. Sci. 26 (2001) 318-324
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 318-324
    • Okada, T.1    Ernst, O.P.2    Palczewski, K.3    Hofmann, K.P.4
  • 41
    • 4344581120 scopus 로고    scopus 로고
    • The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure
    • Okada T., Sugihara M., Bondar A.N., Elstner M., Entel P., and Buss V. The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure. J. Mol. Biol. 342 (2004) 571-583
    • (2004) J. Mol. Biol. , vol.342 , pp. 571-583
    • Okada, T.1    Sugihara, M.2    Bondar, A.N.3    Elstner, M.4    Entel, P.5    Buss, V.6
  • 42
  • 45
    • 0037015153 scopus 로고    scopus 로고
    • Early steps of the intramolecular signal transduction in rhodopsin explored by molecular dynamics simulations
    • Rohrig U.F., Guidoni L., and Rothlisberger U. Early steps of the intramolecular signal transduction in rhodopsin explored by molecular dynamics simulations. Biochemistry 41 (2002) 10799-10809
    • (2002) Biochemistry , vol.41 , pp. 10799-10809
    • Rohrig, U.F.1    Guidoni, L.2    Rothlisberger, U.3
  • 46
    • 5044235587 scopus 로고    scopus 로고
    • Electron crystallography reveals the structure of metarhodopsin I
    • Ruprecht J.J., Mielke T., Vogel R., Villa C., and Schertler G.F. Electron crystallography reveals the structure of metarhodopsin I. EMBO J. 23 (2004) 3609-3620
    • (2004) EMBO J. , vol.23 , pp. 3609-3620
    • Ruprecht, J.J.1    Mielke, T.2    Vogel, R.3    Villa, C.4    Schertler, G.F.5
  • 47
    • 0036930078 scopus 로고    scopus 로고
    • Molecular dynamics investigation of primary photoinduced events in the activation of rhodopsin
    • Saam J., Tajkhorshid E., Hayashi S., and Schulten K. Molecular dynamics investigation of primary photoinduced events in the activation of rhodopsin. Biophys. J. 83 (2002) 3097-3112
    • (2002) Biophys. J. , vol.83 , pp. 3097-3112
    • Saam, J.1    Tajkhorshid, E.2    Hayashi, S.3    Schulten, K.4
  • 48
    • 0029897495 scopus 로고    scopus 로고
    • Constitutively active mutants of the α 1B-adrenergic receptor: role of highly conserved polar amino acids in receptor activation
    • Scheer A., Fanelli F., Costa T., De Benedetti P.G., and Cotecchia S. Constitutively active mutants of the α 1B-adrenergic receptor: role of highly conserved polar amino acids in receptor activation. EMBO J. 15 (1996) 3566-3578
    • (1996) EMBO J. , vol.15 , pp. 3566-3578
    • Scheer, A.1    Fanelli, F.2    Costa, T.3    De Benedetti, P.G.4    Cotecchia, S.5
  • 49
    • 23244431748 scopus 로고    scopus 로고
    • Probing the ultrafast charge translocation of photoexcited retinal in bacteriorhodopsin
    • Schenkl S., van Mourik F., van der Zwan G., Haacke S., and Chergui M. Probing the ultrafast charge translocation of photoexcited retinal in bacteriorhodopsin. Science 309 (2005) 917-920
    • (2005) Science , vol.309 , pp. 917-920
    • Schenkl, S.1    van Mourik, F.2    van der Zwan, G.3    Haacke, S.4    Chergui, M.5
  • 50
    • 21844469248 scopus 로고    scopus 로고
    • Rhodopsin: a structural primer for G-protein coupled receptors
    • Stenkamp R.E., Teller D.C., and Palczewski K. Rhodopsin: a structural primer for G-protein coupled receptors. Arch. Pharm. (Weinheim) 338 (2005) 209-216
    • (2005) Arch. Pharm. (Weinheim) , vol.338 , pp. 209-216
    • Stenkamp, R.E.1    Teller, D.C.2    Palczewski, K.3
  • 51
    • 0037219686 scopus 로고    scopus 로고
    • Evolutionarily conserved networks of residues mediate allosteric communication in proteins
    • Suel G.M., Lockless S.W., Wall M.A., and Ranganathan R. Evolutionarily conserved networks of residues mediate allosteric communication in proteins. Nat. Struct. Biol. 10 (2003) 59-69
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 59-69
    • Suel, G.M.1    Lockless, S.W.2    Wall, M.A.3    Ranganathan, R.4
  • 52
    • 0001649232 scopus 로고    scopus 로고
    • Role of isomerization barriers in the pKa control of the retinal Schiff base: a density functional study
    • Tajkhorshid E., Paizs B., and Suhai S. Role of isomerization barriers in the pKa control of the retinal Schiff base: a density functional study. J. Phys. Chem. B 103 (1997) 4518-4527
    • (1997) J. Phys. Chem. B , vol.103 , pp. 4518-4527
    • Tajkhorshid, E.1    Paizs, B.2    Suhai, S.3
  • 53
    • 0034128699 scopus 로고    scopus 로고
    • Molecular dynamics study of the nature and origin of retinal's twisted structure in bacteriorhodopsin
    • Tajkhorshid E., Baudry J., Schulten K., and Suhai S. Molecular dynamics study of the nature and origin of retinal's twisted structure in bacteriorhodopsin. Biophys. J. 78 (2000) 683-693
    • (2000) Biophys. J. , vol.78 , pp. 683-693
    • Tajkhorshid, E.1    Baudry, J.2    Schulten, K.3    Suhai, S.4
  • 54
    • 0035800032 scopus 로고    scopus 로고
    • Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs)
    • Teller D.C., Okada T., Behnke C.A., Palczewski K., and Stenkamp R.E. Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs). Biochemistry 40 (2001) 7761-7772
    • (2001) Biochemistry , vol.40 , pp. 7761-7772
    • Teller, D.C.1    Okada, T.2    Behnke, C.A.3    Palczewski, K.4    Stenkamp, R.E.5
  • 55
    • 0014411230 scopus 로고
    • Molecular basis of visual excitation
    • Wald G. Molecular basis of visual excitation. Science 162 (1968) 230-239
    • (1968) Science , vol.162 , pp. 230-239
    • Wald, G.1
  • 56
    • 0027723278 scopus 로고
    • Rhodopsin activation: effects on the metarhodopsin I-metarhodopsin II equilibrium of neutralization or introduction of charged amino acids within putative transmembrane segments
    • Weitz C.J., and Nathans J. Rhodopsin activation: effects on the metarhodopsin I-metarhodopsin II equilibrium of neutralization or introduction of charged amino acids within putative transmembrane segments. Biochemistry 32 (1993) 14176-14182
    • (1993) Biochemistry , vol.32 , pp. 14176-14182
    • Weitz, C.J.1    Nathans, J.2
  • 58
    • 22144459357 scopus 로고    scopus 로고
    • Ultrafast excited state dynamics of the protonated Schiff base of all-trans retinal in solvents
    • Zgrablic G., Voitchovsky K., Kindermann M., Haacke S., and Chergui M. Ultrafast excited state dynamics of the protonated Schiff base of all-trans retinal in solvents. Biophys. J. 88 (2005) 2779-2788
    • (2005) Biophys. J. , vol.88 , pp. 2779-2788
    • Zgrablic, G.1    Voitchovsky, K.2    Kindermann, M.3    Haacke, S.4    Chergui, M.5


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