Pure and Applied Chemistry

CrossRef Cited-by Linking

• Abramczyk Halina: Mechanisms of energy dissipation and ultrafast primary events in photostable systems: H-bond, excess electron, biological photoreceptors. Vib Spect 2012, 58, 1. <http://dx.doi.org/10.1016/j.vibspec.2011.10.008>
• Wand Amir, Friedman Noga, Sheves Mordechai, Ruhman Sanford: Ultrafast Photochemistry of Light-Adapted and Dark-Adapted Bacteriorhodopsin: Effects of the Initial Retinal Configuration. J. Phys. Chem. B 2012, 116, 10444. <http://dx.doi.org/10.1021/jp2125284>
• Murakami Midori, Kouyama Tsutomu: Crystallographic Analysis of the Primary Photochemical Reaction of Squid Rhodopsin. J Mol Bio 2011, 413, 615. <http://dx.doi.org/10.1016/j.jmb.2011.08.044>
• Fransen M. R., Palings I., Lugtenburg J., Jansen P. A. A., Groenendijk G. W. T.: Preparation and photolysis of deuterium-labelled rhodopsin analogues. Recl Trav Chim Pays-Bas 2010, 99, 384. <http://dx.doi.org/10.1002/recl.19800991204>
• Chen Xin, Batista Victor S.: The MP/SOFT methodology for simulations of quantum dynamics: Model study of the photoisomerization of the retinyl chromophore in visual rhodopsin. J Photochem Photobiol A Chem 2007, 190, 274. <http://dx.doi.org/10.1016/j.jphotochem.2007.05.015>
• Liu Robert S. H.: Introduction to the Symposium-in-print: Photoisomerization Pathways, Torsional Relaxation and the Hula Twist¶. Photochem Pholobiol 2007, 76, 580. <http://dx.doi.org/10.1562/0031-8655(2002)0760580ITTSIP2.0.CO2>
• Singh Anil K., Hota Prasanta K.: Development of Bacteriorhodopsin Analogues and Studies of Charge Separated Excited States in the Photoprocesses of Linear Polyenes†. Photochem Pholobiol 2007, 83, 50. <http://dx.doi.org/10.1562/2006-03-11-IR-844>
• Abramczyk Halina: Femtosecond primary events in bacteriorhodopsin and its retinal modified analogs: Revision of commonly accepted interpretation of electronic spectra of transient intermediates in the bacteriorhodopsin photocycle. J Chem Phys 2004, 120, 11120. <http://dx.doi.org/10.1063/1.1737731>
• Gascon Jose A., Batista Victor S.: QM/MM Study of Energy Storage and Molecular Rearrangements Due to the Primary Event in Vision. Biophysical Journal 2004, 87, 2931. <http://dx.doi.org/10.1529/biophysj.104.048264>
• Kuksa Vladimir, Imanishi Yoshikazu, Batten Matthew, Palczewski Krzysztof, Moise Alexander R.: Retinoid cycle in the vertebrate retina: experimental approaches and mechanisms of isomerization. vision res 2003, 43, 2959. <http://dx.doi.org/10.1016/S0042-6989(03)00482-6>
• KANDORI Hideki: Primary Photoreaction Processes in Vision. rle 2003, 31, 184. <http://dx.doi.org/10.2184/lsj.31.184>
• Liu Robert S. H.: Introduction to the Symposium-in-print: Photoisomerization Pathways, Torsional Relaxation and the Hula Twist¶. Photchem Photbio 2002, 76, 580. <http://dx.doi.org/10.1562/0031-8655(2002)076<0580:ITTSIP>2.0.CO;2>
• Kandori Hideki, Furutani Yuji, Nishimura Shoko, Shichida Yoshinori, Chosrowjan Haik, Shibata Yutaka, Mataga Noboru: Excited-state dynamics of rhodopsin probed by femtosecond fluorescence spectroscopy. chem phys letts 2001, 334, 271. <http://dx.doi.org/10.1016/S0009-2614(00)01457-3>
• McBee Joshua K, Palczewski Krzysztof, Baehr Wolfgang, Pepperberg David R: Confronting Complexity: the Interlink of Phototransduction and Retinoid Metabolism in the Vertebrate Retina. Prog Retin Eye Res 2001, 20, 469. <http://dx.doi.org/10.1016/S1350-9462(01)00002-7>
• Gonzalez-Luque R., Garavelli M., Bernardi F., Merchan M., Robb M. A., Olivucci M.: Computational evidence in favor of a two-state, two-mode model of the retinal chromophore photoisomerization. Proceedings of the National Academy of Sciences 2000, 97, 9379. <http://dx.doi.org/10.1073/pnas.97.17.9379>
• Tang Li, Ebrey Thomas G., Subramaniam Shankar: Sequences and Structures of Retinal Proteins. Isr. J. Chem. 1995, 35, 193. <http://dx.doi.org/10.1002/ijch.199500027>
• Kochendoerfer Gerd G., Mathies Richard A.: Ultrafast Spectroscopy of Rhodopsins - Photochemistry at Its Best!. Isr. J. Chem. 1995, 35, 211. <http://dx.doi.org/10.1002/ijch.199500028>
• Mah T. L., Lewis J. W., Sheves M., Ottolenghi M., Kliger D. S.: LOW-TEMPERATURE TRAPPING OF EARLY PHOTOINTERMEDIATES OF α-ISORHODOPSIN. Photchem Photbio 1995, 62, 356. <http://dx.doi.org/10.1111/j.1751-1097.1995.tb05282.x>
• Kakitani Toshiaki, Hatano Yasuyo, Shichida Yoshinori, Imamoto Yasushi, Tokunaga Fumio, Kakitani Hiroko: EXCITED STATE DYNAMICS OF RETINAL PROTEINS AS STUDIED BY FOURIER TRANSFORM OF OPTICAL ABSORPTION SPECTRUM—I. DEVELOPMENT OF ANALYTICAL METHOD. Photchem Photbio 1992, 56, 977. <http://dx.doi.org/10.1111/j.1751-1097.1992.tb09720.x>
• Warshel A., Chu Z.T., Hwang J.-K.: The dynamics of the primary event in rhodopsins revisited. Chemical Phys 1991, 158, 303. <http://dx.doi.org/10.1016/0301-0104(91)87074-6>
• Birge Robert R.: Nature of the primary photochemical events in rhodopsin and bacteriorhodopsin. Biochim Biophys Acta Bioenerg 1990, 1016, 293. <http://dx.doi.org/10.1016/0005-2728(90)90163-X>
• Beppu Yoshitaka, Kakitani Toshiaki: Comprehensive study of molecular conformation and adiabatic potential surface of all-trans retinal by the CNDO/2 method. Chemical Phys 1990, 148, 333. <http://dx.doi.org/10.1016/0301-0104(90)89029-P>
• Ottolenghi Michael, Sheves Mordechai: Synthetic retinals as probes for the binding site and photoreactions in rhodopsins. J Membrane Biol 1989, 112, 193. <http://dx.doi.org/10.1007/BF01870951>
• Holzwarth Alfred R.: Applications of ultrafast laser spectroscopy for the study of biological systems. Quart Rev Biophys 1989, 22, 239. <http://dx.doi.org/10.1017/S0033583500002985>
• Becker Ralph S.: THE VISUAL PROCESS: PHOTOPHYSICS and PHOTOISOMERIZATION OF MODEL VISUAL PIGMENTS and THE PRIMARY REACTION. Photchem Photbio 1988, 48, 369. <http://dx.doi.org/10.1111/j.1751-1097.1988.tb02836.x>
• Riveros Oscar J.: Motion of proton in double-well potential. biophys chem 1987, 28, 93. <http://dx.doi.org/10.1016/0301-4622(87)80078-9>
• Dixon Sheila F., Cooper Alan: QUANTUM EFFICIENCIES OF THE REVERSIBLE PHOTOREACTION OF OCTOPUS RHODOPSIN. Photchem Photbio 1987, 46, 115. <http://dx.doi.org/10.1111/j.1751-1097.1987.tb04744.x>
• Sharkov Andrey V., Pakulev Andrey V., Chekalin Sergey V., Matveetz Yuri A.: Primary events in bacteriorhodopsin probed by subpicosecond spectroscopy. Biochim Biophys Acta Bioenerg 1985, 808, 94. <http://dx.doi.org/10.1016/0005-2728(85)90031-3>
• Trissl H.-W.: I. Primary electrogenic processes in bacteriorhodopsin probed by photoelectric measurements with capacitative metal electrodes. Biochim Biophys Acta Bioenerg 1985, 806, 124. <http://dx.doi.org/10.1016/0005-2728(85)90088-X>
• Boucher François, Leblanc Roger M.: ENERGY STORAGE IN THE PRIMARY PHOTOREACTION OF BOVINE RHODOPSIN. A PHOTOACOUSTIC STUDY. Photchem Photbio 1985, 41, 459. <http://dx.doi.org/10.1111/j.1751-1097.1985.tb03512.x>
• Deng H., Pande C., Callender R. H., Ebrey T. G.: A DETAILED RESONANCE RAMAN STUDY OF THE M₄₁₂ INTERMEDIATE IN THE BACTERIORHODOPSIN PHOTOCYCLE. Photchem Photbio 1985, 41, 467. <http://dx.doi.org/10.1111/j.1751-1097.1985.tb03513.x>
• Kliger D.S., Horwitz J.S., Lewis J.W., Einterz C.M.: Evidence for a common batho-intermediate in the bleaching of rhodopsin and isorhodopsin. vision res 1984, 24, 1465. <http://dx.doi.org/10.1016/0042-6989(84)90307-9>
• Myers Anne B., Mathies Richard A.: Excited-state torsional dynamics of cis-stilbene from resonance Raman intensities. J Chem Phys 1984, 81, 1552. <http://dx.doi.org/10.1063/1.447884>
• WADDELL WALTER H., LECOMTE JULIETTE, WEST JOHN L., YOUNES USAMA E.: QUALITATIVE STUDIES OF THE LOW TEMPERATURE PHOTOCHEMISTRY OF RHODOPSIN AND RELATED PIGMENTS. Photchem Photbio 1984, 39, 213. <http://dx.doi.org/10.1111/j.1751-1097.1984.tb03430.x>
• Donahue Jean M., Waddell Walter H.: THE TRANS → CIS PHOTOISOMERIZATION OF PROTONATED RETINYL SCHIFF BASES. Photchem Photbio 1984, 40, 399. <http://dx.doi.org/10.1111/j.1751-1097.1984.tb04606.x>
• Trissl H.-W.: Charge displacements in purple membranes adsorbed to a heptane/water interface. Evidence for a primary charge separation in bacteriorhodopsin. Biochim Biophys Acta Bioenerg 1983, 723, 327. <http://dx.doi.org/10.1016/0005-2728(83)90133-0>
• Hilinski E. F., Rentzepis P. M.: Biological applications of picosecond spectroscopy. Appl Opt 1983, 302, 481. <http://dx.doi.org/10.1038/302481a0>
• Horwitz J. S., Lewis J. W., Powers M. A., Kliger D. S.: NANOSECOND LASER PHOTOLYSIS OF RHODOPSIN AND ISORHODOPSIN. Photchem Photbio 1983, 37, 181. <http://dx.doi.org/10.1111/j.1751-1097.1983.tb04456.x>
• Hsieh Chung-Lu, El-Sayed M. A., Nicol Malcolm, Nagumo Mark, Lee Jai-Hyung: TIME-RESOLVED RESONANCE RAMAN SPECTROSCOPY OF THE BACTERIORHODOPSIN PHOTOCYCLE ON THE PICOSECOND AND NANOSECOND TIME SCALES. Photchem Photbio 1983, 38, 83. <http://dx.doi.org/10.1111/j.1751-1097.1983.tb08370.x>
• Bacci M.: Spectroscopic and structural properties of metallo-proteins. La Rivista Del Nuovo Cimento Series 3 1982, 5, 1. <http://dx.doi.org/10.1007/BF02740883>
• Litman Burton J., Aton Bea, Hartley Jonathan B.: Functional domains of rhodopsin. vision res 1982, 22, 1439. <http://dx.doi.org/10.1016/0042-6989(82)90206-1>
• Cronin Thomas W., Goldsmith Timothy H.: QUANTUM EFFICIENCY AND PHOTOSENSITIVITY OF THE RHODOPSIN ⇌ METARHODOPSIN CONVERSION IN CRAYFISH PHOTORECEPTORS. Photchem Photbio 1982, 36, 447. <http://dx.doi.org/10.1111/j.1751-1097.1982.tb04401.x>
• Kakitani Toshiaki, Sarai Akinori, Kakitani Hiroko: Theoretical Studies of Photoisomerization in Visual Pigments. I. Formulation. J. Phys. Soc. Jpn. 1982, 51, 3302. <http://dx.doi.org/10.1143/JPSJ.51.3302>
• Kossi Christophe N, Leblanc Roger M: Rhodopsin in a new model bilayer membrane. Journal of Colloid and Interface Science 1981, 80, 426. <http://dx.doi.org/10.1016/0021-9797(81)90201-0>
• Darszon A., Schindler H., Montal M.: Functional reassembly of membrane proteins in planar lipid bilayers. Quart Rev Biophys 1981, 14, 1. <http://dx.doi.org/10.1017/S0033583500002079>
• Honig Barry: EXCITED STATE PROPERTIES OF VISUAL PIGMENTS AND BACTERIORHODOPSIN. Ann N Y Acad Sci 1981, 367, 269. <http://dx.doi.org/10.1111/j.1749-6632.1981.tb50573.x>
• Dinur U., Honig B., Ottolenghi M.: ANALYSIS OF PRIMARY PHOTOCHEMICAL PROCESSES IN BACTERIORHODOPSIN. Photchem Photbio 1981, 33, 523. <http://dx.doi.org/10.1111/j.1751-1097.1981.tb05455.x>
• Sarai Akinori, Kakitani Toshiaki, Kakitani Hiroko: PROTON TRANSFER IN THE PRIMARY PROCESS OF VISION. Photchem Photbio 1981, 33, 875. <http://dx.doi.org/10.1111/j.1751-1097.1981.tb05506.x>
• Tsuda Motoyuki, Glaccum Moira, Nelson Burr, Ebrey Thomas G.: Light isomerizes the chromophore of bacteriorhodopsin. Appl Opt 1980, 287, 351. <http://dx.doi.org/10.1038/287351a0>
• Iwasa Tatsuo, Tokunaga Fumio, Yoshizawa Tôru, Ebrey Thomas G.: QUANTUM EFFICIENCY FOR THE PHOTOCONVERSION OF BACTERIORHODOPSIN AT VERY LOW TEMPERATURES. Photchem Photbio 1980, 31, 83. <http://dx.doi.org/10.1111/j.1751-1097.1980.tb03686.x>
• Applebury M. L.: THE PRIMARY PROCESSES OF VISION: A VIEW FROM THE EXPERIMENTAL SIDE. Photchem Photbio 1980, 32, 425. <http://dx.doi.org/10.1111/j.1751-1097.1980.tb03784.x>
• Sarai Akinori, Kakitani Toshiaki, Shichida Yoshinori, Tokunaga Fumio, Yoshizawa Toru: SIMULATION ANALYSIS OF THE PHOTOCONVERSION PROCESS OF SQUID RHODOPSIN AT LIQUID HELIUM TEMPERATURE. Photchem Photbio 1980, 32, 199. <http://dx.doi.org/10.1111/j.1751-1097.1980.tb04010.x>
• Narva D., Callender R. H.: ON THE STATE OF CHROMOPHORE PROTONATION IN RHODOPSIN: IMPLICATION FOR PRIMARY PHOTOCHEMISTRY IN VISUAL PIGMENTS. Photchem Photbio 1980, 32, 273. <http://dx.doi.org/10.1111/j.1751-1097.1980.tb04021.x>
• Kakitani Toshiaki, Kakitani Hiroko: THEORETICAL STUDY OF OPTICAL SPECTRA AND CONFORMATION OF THE CHROMOPHORE OF HYPSORHODOPSIN. Photchem Photbio 1980, 32, 707. <http://dx.doi.org/10.1111/j.1751-1097.1980.tb04045.x>
• Kakitani T., Kakitani H.: Molecular mechanism for the initial process of visual excitation. Biophys Struct Mechanism 1979, 5, 55. <http://dx.doi.org/10.1007/BF00535773>
• Kakitani T.: Molecular mechanism for the initial process of visual excitation. IV. Energy surfaces of visual pigments and photoisomerization mechanism. Biophys Struct Mechanism 1979, 5, 293. <http://dx.doi.org/10.1007/BF02426664>
• Cooper Alan: Energetics of rhodopsin and isorhodopsin. FEBS Letters 1979, 100, 382. <http://dx.doi.org/10.1016/0014-5793(79)80375-0>
• Wallach Donald F.H., Verma Surendra P., Fookson Jeffrey, Montal M.: Application of laser Raman and infrared spectroscopy to the analysis of membrane structure. Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes 1979, 559, 153. <http://dx.doi.org/10.1016/0304-4157(79)90003-0>
• Cooper Alan: Energy uptake in the first step of visual excitation. Appl Opt 1979, 282, 531. <http://dx.doi.org/10.1038/282531a0>
• Kaufmann Kenneth J.: Picosecond spectroscopy applied to the study of chemical and biological reactions. Crit Rev Solid State Mater Sci 1979, 8, 265. <http://dx.doi.org/10.1080/10408437908243625>
• Warshel A., Ottoenghi M.: KINETIC AND SPECTROSCOPIC EFFECTS OF PROTEIN-CHROMOPHORE ELECTROSTATIC INTERACTIONS IN BACTERIORHODOPSIN. Photchem Photbio 1979, 30, 291. <http://dx.doi.org/10.1111/j.1751-1097.1979.tb07149.x>
• Gillbro T.: Flash kinetic study of the last steps in the photoinduced reaction cycle of bacteriorhodopsin. Biochim Biophys Acta Bioenerg 1978, 504, 175. <http://dx.doi.org/10.1016/0005-2728(78)90016-6>
• SCHULTEN KLAUS, TAVAN PAUL: A mechanism for the light-driven proton pump of Halobacterium halobium. Appl Opt 1978, 272, 85. <http://dx.doi.org/10.1038/272085a0>
• HURLEY JAMES B., BECHER BRIAN, EBREY THOMAS G.: More evidence that light isomerises the chromophore of purple membrane protein. Appl Opt 1978, 272, 87. <http://dx.doi.org/10.1038/272087a0>
• ATON B., CALLENDER R. H., HONIG B.: Photochemical cis–trans isomerisation of bovine rhodopsin at liquid helium temperatures. Appl Opt 1978, 273, 784. <http://dx.doi.org/10.1038/273784a0>
• PRESTI D., DELBRUCK M.: Photoreceptors for biosynthesis, energy storage and vision. Plant Cell Environ 1978, 1, 81. <http://dx.doi.org/10.1111/j.1365-3040.1978.tb00751.x>
• Kalisky Ofra, Lachish Uri, Ottolenghi Michael: TIME RESOLUTION OF A BACK PHOTOREACTION IN BACTERIORHODOPSIN. Photchem Photbio 1978, 28, 261. <http://dx.doi.org/10.1111/j.1751-1097.1978.tb07705.x>
• Kakitani Toshiaki, Kakitani Hiroko: Mechanism of Photoconversion among Rhodopsin, Bathorhodopsin and Isorhodopsin. J. Phys. Soc. Jpn. 1978, 44, 1403. <http://dx.doi.org/10.1143/JPSJ.44.1403>
• GREEN B. H., MONGER T. G., ALFANO R. R., ATON B., CALLENDER R. H.: Cis–trans isomerisation in rhodopsin occurs in picoseconds. Appl Opt 1977, 269, 179. <http://dx.doi.org/10.1038/269179a0>
• HURLEY JAMES B., EBREY THOMAS G., HONIG BARRY, OTTOLENGHI MICHAEL: Temperature and wavelength effects on the photochemistry of rhodopsin, isorhodopsin, bacteriorhodopsin and their photoproducts. Appl Opt 1977, 270, 540. <http://dx.doi.org/10.1038/270540a0>