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Volumn 40, Issue 22, 2000, Pages 3039-3048

Effect of NADPH on formation and decay of human metarhodopsin III at physiological temperatures

Author keywords

Dark adaptation; Human rhodopsin; Metarhodopsin III; NADPH; Photoregeneration; Retinol dehydrogenase

Indexed keywords

REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; RETINOL; RETINOL DEHYDROGENASE; RHODOPSIN; VISUAL PIGMENT;

EID: 0033857249     PISSN: 00426989     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0042-6989(00)00148-6     Document Type: Article
Times cited : (7)

References (36)
  • 1
    • 0015122009 scopus 로고
    • Rhodopsin kinetics in the human eye
    • Alpern M. Rhodopsin kinetics in the human eye. Journal of Physiology. 217:1971;447-471.
    • (1971) Journal of Physiology , vol.217 , pp. 447-471
    • Alpern, M.1
  • 2
    • 0031911863 scopus 로고    scopus 로고
    • Rod opsin sequence in the John Dory: Further evidence for the spectral tuning of rhodopsin
    • Archer S.N., Hirano J. Rod opsin sequence in the John Dory: further evidence for the spectral tuning of rhodopsin. Journal of Fish Biology. 52:1998;209-212.
    • (1998) Journal of Fish Biology , vol.52 , pp. 209-212
    • Archer, S.N.1    Hirano, J.2
  • 3
    • 0015716256 scopus 로고
    • Kinetics of rhodopsin bleaching in the isolated human retina
    • Baumann C., Bender S. Kinetics of rhodopsin bleaching in the isolated human retina. Journal of Physiology. 235:1973;761-773.
    • (1973) Journal of Physiology , vol.235 , pp. 761-773
    • Baumann, C.1    Bender, S.2
  • 4
    • 0031850938 scopus 로고    scopus 로고
    • Control of rhodopsin activity in vision
    • Baylor D.A., Burns M.E. Control of rhodopsin activity in vision. Eye. 12:1999;521-525.
    • (1999) Eye , vol.12 , pp. 521-525
    • Baylor, D.A.1    Burns, M.E.2
  • 5
    • 0019175449 scopus 로고
    • Optical study of the light-induced protonation changes associated with the metarhodopsin H intermediate in rod-outer-segment membranes
    • Bennett N. Optical study of the light-induced protonation changes associated with the metarhodopsin H intermediate in rod-outer-segment membranes. European Journal of Biochemistry. 111:1980;99-103.
    • (1980) European Journal of Biochemistry , vol.111 , pp. 99-103
    • Bennett, N.1
  • 6
    • 0021265905 scopus 로고
    • Pathways in the hydrolysis of vertebrate rhodopsin
    • Blazynski C., Ostroy S.E. Pathways in the hydrolysis of vertebrate rhodopsin. Vision Research. 24:1984;459-470.
    • (1984) Vision Research , vol.24 , pp. 459-470
    • Blazynski, C.1    Ostroy, S.E.2
  • 7
    • 0018672648 scopus 로고
    • Biochemical aspects of the visual process XL. Spectral and chemical aspects of metarhodopsin III in photoreceptor membrane suspensions
    • van Breugel P.J.G.M., Bovee-Geurts P.H.M., Bonting S.L., Daemen F.J.M. Biochemical aspects of the visual process XL. Spectral and chemical aspects of metarhodopsin III in photoreceptor membrane suspensions. Biochimica et Biophysica Acta. 557:1979;188-198.
    • (1979) Biochimica et Biophysica Acta , vol.557 , pp. 188-198
    • Van Breugel, P.J.G.M.1    Bovee-Geurts, P.H.M.2    Bonting, S.L.3    Daemen, F.J.M.4
  • 8
    • 0018320164 scopus 로고
    • The orientation of the chrornophore of vertebrate rhodopsin in the "meta" intermediate states and the reversibility of the meta II-meta III transition
    • Chabre M., Breton J. The orientation of the chrornophore of vertebrate rhodopsin in the "meta" intermediate states and the reversibility of the meta II-meta III transition. Vision Research. 19:1979;1005-1018.
    • (1979) Vision Research , vol.19 , pp. 1005-1018
    • Chabre, M.1    Breton, J.2
  • 9
    • 0022336839 scopus 로고
    • Some properties of solubilized human rhodopsin
    • Crescitelli F. Some properties of solubilized human rhodopsin. Experimental Eye Research. 40:1985;521-535.
    • (1985) Experimental Eye Research , vol.40 , pp. 521-535
    • Crescitelli, F.1
  • 10
    • 0028351937 scopus 로고
    • Structure and function in rhodopsin.6. replacement by alanine of cysteine residues 110 and 187, components of a conserved disuffide bond in rhodopsin, affects the light-activated metarhodopsin II state
    • Davidson F.F., Loewen P.C., Khorana H.G. Structure and function in rhodopsin.6. replacement by alanine of cysteine residues 110 and 187, components of a conserved disuffide bond in rhodopsin, affects the light-activated metarhodopsin II state. Proceedings of the National Academy of Sciences of the United States of America. 91:1994;4029-4033.
    • (1994) Proceedings of the National Academy of Sciences of the United States of America , vol.91 , pp. 4029-4033
    • Davidson, F.F.1    Loewen, P.C.2    Khorana, H.G.3
  • 11
  • 12
    • 0027976593 scopus 로고
    • Deconvolutions based on singular value decomposition and the pseudoinverse: A guide for beginners
    • Hendler R.W., Shrager R.I. Deconvolutions based on singular value decomposition and the pseudoinverse: a guide for beginners. Journal of Biochemical and Biophysical Methods. 28:1994;1-33.
    • (1994) Journal of Biochemical and Biophysical Methods , vol.28 , pp. 1-33
    • Hendler, R.W.1    Shrager, R.I.2
  • 13
    • 0022869897 scopus 로고
    • Photoproducts of rhodopsin in the disc membrane
    • Hofmann K.P. Photoproducts of rhodopsin in the disc membrane. Photobiochemistry and Photobiophysics. 13:1986;309-327.
    • (1986) Photobiochemistry and Photobiophysics , vol.13 , pp. 309-327
    • Hofmann, K.P.1
  • 15
    • 0025105229 scopus 로고
    • Nanosecond photolysis of rhodopsin: Evidence for a new, blue-shifted intermediate
    • Hug S.J., Lewis J.W., Einterz C.M., Thorgeirsson T.E., Kliger D.S. Nanosecond photolysis of rhodopsin: evidence for a new, blue-shifted intermediate. Biochemistry. 29:1990;1475-1485.
    • (1990) Biochemistry , vol.29 , pp. 1475-1485
    • Hug, S.J.1    Lewis, J.W.2    Einterz, C.M.3    Thorgeirsson, T.E.4    Kliger, D.S.5
  • 16
    • 0038822850 scopus 로고    scopus 로고
    • Effects of pH on rhodopsin photointermediates from lurnirhodopsin to metarhodopsin II
    • Jäger S., Szundi I., Lewis J.W., Mah T.L., Kliger D.S. Effects of pH on rhodopsin photointermediates from lurnirhodopsin to metarhodopsin II. Biochemistry. 37:1998;6998-7005.
    • (1998) Biochemistry , vol.37 , pp. 6998-7005
    • Jäger, S.1    Szundi, I.2    Lewis, J.W.3    Mah, T.L.4    Kliger, D.S.5
  • 17
    • 0028887017 scopus 로고
    • Role of ligand in retinoid signaling. 9-cis-retinoic acid modulates the oligomeric: State of the retinoid X receptor
    • Kersten S., Pan L., Chambon P., Gronemeyer H., Noy N. Role of ligand in retinoid signaling. 9-cis-retinoic acid modulates the oligomeric: state of the retinoid X receptor. Biochemistry. 34:1995;13717-13721.
    • (1995) Biochemistry , vol.34 , pp. 13717-13721
    • Kersten, S.1    Pan, L.2    Chambon, P.3    Gronemeyer, H.4    Noy, N.5
  • 18
    • 0026716741 scopus 로고
    • Structural comparison of metarhodopsin II, metarhodopsin III and opsin based on kinetic analysis of Fourier transform infrared difference spectra
    • Klinger A.L., Braiman M.S. Structural comparison of metarhodopsin II, metarhodopsin III and opsin based on kinetic analysis of Fourier transform infrared difference spectra. Biophysical Journal. 63:1992;1244-1255.
    • (1992) Biophysical Journal , vol.63 , pp. 1244-1255
    • Klinger, A.L.1    Braiman, M.S.2
  • 19
    • 0027338310 scopus 로고
    • Preparative scale isolation and partial purification of human rod outer segments
    • van Kuijk F.J.G.M., Buck P., Lewis J.W., Kliger D.S. Preparative scale isolation and partial purification of human rod outer segments. Experimental Eye Research. 57:1993;249-252.
    • (1993) Experimental Eye Research , vol.57 , pp. 249-252
    • Van Kuijk, F.J.G.M.1    Buck, P.2    Lewis, J.W.3    Kliger, D.S.4
  • 20
    • 0019413494 scopus 로고
    • The involvement of rod photoreceptors in dark adaptation
    • Lamb T.D. The involvement of rod photoreceptors in dark adaptation. Vision Research. 21:1981;1773-1782.
    • (1981) Vision Research , vol.21 , pp. 1773-1782
    • Lamb, T.D.1
  • 22
    • 2642675217 scopus 로고    scopus 로고
    • Molecular basis of dark adaptation in rod photoreceptors
    • Leibrock C.S., Reuter T., Lamb T.D. Molecular basis of dark adaptation in rod photoreceptors. Eye. 12:1998;511-520.
    • (1998) Eye , vol.12 , pp. 511-520
    • Leibrock, C.S.1    Reuter, T.2    Lamb, T.D.3
  • 23
    • 0031017636 scopus 로고    scopus 로고
    • Metarhodopsin III formation and decay kinetics: Comparison of bovine and human rhodopsin
    • Lewis J.W., van Kuijk F.J.G.M., Carruthers J.A., Kliger D.S. Metarhodopsin III formation and decay kinetics: comparison of bovine and human rhodopsin. Vision Research. 37:1997;1-8.
    • (1997) Vision Research , vol.37 , pp. 1-8
    • Lewis, J.W.1    Van Kuijk, F.J.G.M.2    Carruthers, J.A.3    Kliger, D.S.4
  • 26
    • 0020133090 scopus 로고
    • Procedure for testing kinetic models of the photocycle of bacteriorhodopsin
    • Nagle J.F., Parodi L.A., Lozier R.H. Procedure for testing kinetic models of the photocycle of bacteriorhodopsin. Biophysical Journal. 38:1982;161-174.
    • (1982) Biophysical Journal , vol.38 , pp. 161-174
    • Nagle, J.F.1    Parodi, L.A.2    Lozier, R.H.3
  • 28
    • 0017182530 scopus 로고
    • Photoregeneration of rhodopsin and isorhodopsin from metarhodopsin III in the frog retina
    • Reuter T. Photoregeneration of rhodopsin and isorhodopsin from metarhodopsin III in the frog retina. Vision Research. 16:1976;909-917.
    • (1976) Vision Research , vol.16 , pp. 909-917
    • Reuter, T.1
  • 29
    • 0014689358 scopus 로고
    • Rhodopsin regeneration in man
    • Ripps H., Weale R.A. Rhodopsin regeneration in man. Nature (London). 222:1969;775-777.
    • (1969) Nature (London) , vol.222 , pp. 775-777
    • Ripps, H.1    Weale, R.A.2
  • 30
    • 0016168475 scopus 로고
    • Biochemical aspects of the visual process XXVI. Binding site and migration of retinaldehyde during rhodopsin photolysis
    • Rotmans J.P., Daemen F.J.M., Bonting S.L. Biochemical aspects of the visual process XXVI. Binding site and migration of retinaldehyde during rhodopsin photolysis. Biochimica et Biophysica Acta. 357:1974;151-158.
    • (1974) Biochimica et Biophysica Acta , vol.357 , pp. 151-158
    • Rotmans, J.P.1    Daemen, F.J.M.2    Bonting, S.L.3
  • 31
    • 33845555570 scopus 로고
    • Titration of individual components in a mixture with resolution of difference spectra, pKs and redox titrations
    • Shrager R.I., Hendler R.W. Titration of individual components in a mixture with resolution of difference spectra, pKs and redox titrations. Analytical Chemistry. 54:1982;1147-1152.
    • (1982) Analytical Chemistry , vol.54 , pp. 1147-1152
    • Shrager, R.I.1    Hendler, R.W.2
  • 32
    • 0030749599 scopus 로고    scopus 로고
    • Deriving reaction mechanisms from kinetic spectroscopy. Application to late rhodopsin intermediates
    • Szundi I., Lewis J.W., Kliger D.S. Deriving reaction mechanisms from kinetic spectroscopy. Application to late rhodopsin intermediates. Biophysical Journal. 73:1997;688-702.
    • (1997) Biophysical Journal , vol.73 , pp. 688-702
    • Szundi, I.1    Lewis, J.W.2    Kliger, D.S.3
  • 33
    • 0027757062 scopus 로고
    • Effects of temperature on rhodopsin photointermediates from lumirhodopsin to metarhodopsin II
    • Thorgeirsson T.E., Lewis J.W., Wallace-Williams S.E., Kliger D.S. Effects of temperature on rhodopsin photointermediates from lumirhodopsin to metarhodopsin II. Biochemistry. 32:1993;13861-13872.
    • (1993) Biochemistry , vol.32 , pp. 13861-13872
    • Thorgeirsson, T.E.1    Lewis, J.W.2    Wallace-Williams, S.E.3    Kliger, D.S.4
  • 35
    • 0033374434 scopus 로고    scopus 로고
    • IBMX, taurine and 9-cis retionoic acid all act to accelerate rhodopsin expression in postmitotic cells
    • Wallace V.A., Jensen A.M. IBMX, taurine and 9-cis retionoic acid all act to accelerate rhodopsin expression in postmitotic cells. Experimental Eye Research. 69:1999;617-627.
    • (1999) Experimental Eye Research , vol.69 , pp. 617-627
    • Wallace, V.A.1    Jensen, A.M.2
  • 36
    • 0027462158 scopus 로고
    • Movement of the retinylidene Schiff base counterion in rhodopsin by one helix turn reverses the pH dependence of the metarhodopsin I to metarhodopsin II transition
    • Zvyaga T.A., Min K.C., Beck M., Sakmar T.P. Movement of the retinylidene Schiff base counterion in rhodopsin by one helix turn reverses the pH dependence of the metarhodopsin I to metarhodopsin II transition. Journal of Biological Chemistry. 268:1993;4661-4667.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 4661-4667
    • Zvyaga, T.A.1    Min, K.C.2    Beck, M.3    Sakmar, T.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.