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Reversible Photocontrol of Biological Systems by the Incorporation of Molecular Photoswitches
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ADVERTISEMENT RETURN TO ISSUEPREVReviewNEXTReversible Photocontrol of Biological Systems by the Incorporation of Molecular PhotoswitchesWiktor Szymański, John M. Beierle†, Hans A. V. Kistemaker‡, Willem A. Velema, and Ben L. Feringa*View Author Information Stratingh Institute for Chemistry, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands*E-mail: [email protected]Cite this: Chem. Rev. 2013, 113, 8, 6114–6178Publication Date (Web):April 25, 2013Publication History Received3 May 2012Published online25 April 2013Published inissue 14 August 2013https://doi.org/10.1021/cr300179fCopyright © 2013 American Chemical SocietyRIGHTS & PERMISSIONSACS Editors' ChoiceArticle Views42184Altmetric-Citations905LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (36 MB) Get e-AlertscloseSUBJECTS:Azobenzene,Genetics,Irradiation,Monomers,Peptides and proteins Get e-Alerts
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Citations
Cites
Characteristics of a human cell line transformed by DNA from human adenovirus type 5
Graham, F. L., Russell, W. C., Smiley, J., & Nairn, R. (1977) · Journal of General Virology · doi:10.1099/0022-1317-36-1-59 · Cited by 4,793
Diarylethenes for Memories and Switches
Irie, M. (2000) · Chemical Reviews · doi:10.1021/cr980069d · Cited by 4,157
The Leucine Zipper: A Hypothetical Structure Common to a New Class of DNA Binding Proteins
Landschulz, W. H., Johnson, P. F., & McKnight, S. L. (1988) · Science · doi:10.1126/science.3289117 · Cited by 3,443
RGD AND OTHER RECOGNITION SEQUENCES FOR INTEGRINS
Ruoslahti, E. (1996) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.12.1.697 · Cited by 3,191
Photoisomerization in different classes of azobenzene
Bandara, H. M. D., & Burdette, S. C. (2012) · Chem. Soc. Rev. · doi:10.1039/c1cs15179g · Cited by 3,095
Azobenzene photoswitches for biomolecules
Beharry, A. A., & Woolley, G. A. (2011) · Chemical Society Reviews · doi:10.1039/c1cs15023e · Cited by 1,851
Spiropyrans and Spirooxazines for Memories and Switches
Berkovic, G., Krongauz, V., & Weiss, V. (2000) · Chemical Reviews · doi:10.1021/cr9800715 · Cited by 1,588
Pabo, C. O., & Sauer, R. T. (1984) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.53.070184.001453 · Cited by 1,569
Biophysical and Molecular Mechanisms of Shaker Potassium Channel Inactivation
Hoshi, T., Zagotta, W. N., & Aldrich, R. W. (1990) · Science · doi:10.1126/science.2122519 · Cited by 1,538
Expanding the Genetic Code of Escherichia coli
Wang, L., Brock, A., Herberich, B., & Schultz, P. G. (2001) · Science · doi:10.1126/science.1060077 · Cited by 1,499
Photoisomerization dynamics of stilbenes
Waldeck, D. H. (1991) · Chemical Reviews · doi:10.1021/cr00003a007 · Cited by 1,348
Hulme, E. C., Birdsall, N. J. M., & Buckley, N. J. (1990) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.30.040190.003221 · Cited by 1,338
Sequence-Specific Cleavage of Double Helical DNA by Triple Helix Formation
Moser, H. E., & Dervan, P. B. (1987) · Science · doi:10.1126/science.3118463 · Cited by 1,284
CRF and CRF receptors: role in stress responsivity and other behaviors
Bale, T. L., & Vale, W. W. (2004) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.44.101802.121410 · Cited by 1,270
Fluorescent Labeling of Biomolecules with Organic Probes
Gonçalves, M. S. T. (2009) · Chemical Reviews · doi:10.1021/cr0783840 · Cited by 1,182
Glutamate receptors in the mammalian central nervous system
Ozawa, S., Kamiya, H., & Tsuzuki, K. (1998) · Progress in Neurobiology · doi:10.1016/s0301-0082(97)00085-3 · Cited by 1,122
Biologically Active Molecules with a “Light Switch”
Mayer, G., & Heckel, A. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200600387 · Cited by 1,119
From Mechanism to Mouse: A Tale of Two Bioorthogonal Reactions
Sletten, E. M., & Bertozzi, C. R. (2011) · Accounts of Chemical Research · doi:10.1021/ar200148z · Cited by 1,093
A genetically encoded photoactivatable Rac controls the motility of living cells
Wu, Y. I., Frey, D., Lungu, O. I., Jaehrig, A., Schlichting, I., Kuhlman, B., & Hahn, K. M. (2009) · Nature · doi:10.1038/nature08241 · Cited by 1,083
STRUCTURE AND FUNCTION OF G PROTEIN-COUPLED RECEPTORS
Strader, C. D., Fong, T. M., Tota, M. R., Underwood, D., & Dixon, R. A. F. (1994) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.63.070194.000533 · Cited by 1,079
DNA Recognition by Cys2His2 Zinc Finger Proteins
Wolfe, S. A., Nekludova, L., & Pabo, C. O. (2000) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.29.1.183 · Cited by 1,053
Reichlin, S. (1983) · New England Journal of Medicine · doi:10.1056/nejm198312153092406 · Cited by 1,044
Cis−Trans Isomerization of Organic Molecules and Biomolecules: Implications and Applications
Dugave, C., & Demange, L. (2003) · Chemical Reviews · doi:10.1021/cr0104375 · Cited by 1,032
Neuronal nicotinic receptors: from structure to pathology
Gotti, C., & Clementi, F. (2004) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2004.09.006 · Cited by 970
Bléger, D., Schwarz, J., Brouwer, A. M., & Hecht, S. (2012) · Journal of the American Chemical Society · doi:10.1021/ja310323y · Cited by 902
Wilkinson, B. M., & Gilbert, H. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.02.017 · Cited by 876
Fulgides for Memories and Switches
Yokoyama, Y. (2000) · Chemical Reviews · doi:10.1021/cr980070c · Cited by 874
Ionotropic and metabotropic glutamate receptor structure and pharmacology
Kew, J. N. C., & Kemp, J. A. (2005) · Psychopharmacology · doi:10.1007/s00213-005-2200-z · Cited by 788
Patch Clamp Techniques for Studying Ionic Channels in Excitable Membranes
Sakmann, B., & Neher, E. (1984) · Annual Review of Physiology · doi:10.1146/annurev.ph.46.030184.002323 · Cited by 755
Tryptophan zippers: Stable, monomeric β-hairpins
Cochran, A. G., Skelton, N. J., & Starovasnik, M. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.091100898 · Cited by 735
Calmodulin structure refined at 1.7 Å resolution
Chattopadhyaya, R., Meador, W. E., Means, A. R., & Quiocho, F. A. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90324-d · Cited by 729
Light-activated ion channels for remote control of neuronal firing
Banghart, M., Borges, K., Isacoff, E., Trauner, D., & Kramer, R. H. (2004) · Nature Neuroscience · doi:10.1038/nn1356 · Cited by 726
Levina, N. (1999) · The EMBO Journal · doi:10.1093/emboj/18.7.1730 · Cited by 721
The Discovery of Zinc Fingers and Their Applications in Gene Regulation and Genome Manipulation
Klug, A. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-010909-095056 · Cited by 710
Azobenzene Photoswitching without Ultraviolet Light
Beharry, A. A., Sadovski, O., & Woolley, G. A. (2011) · Journal of the American Chemical Society · doi:10.1021/ja209239m · Cited by 709
Stimuli-responsive surfaces for bio-applications
Mendes, P. M. (2008) · Chemical Society Reviews · doi:10.1039/b714635n · Cited by 661
TBP, a universal eukaryotic transcription factor?
Hernandez, N. (1993) · Genes & Development · doi:10.1101/gad.7.7b.1291 · Cited by 634
Protein Translocation Across the Bacterial Cytoplasmic Membrane
Driessen, A. J. M., & Nouwen, N. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.061606.160747 · Cited by 614
Siewertsen, R., Neumann, H., Buchheim-Stehn, B., Herges, R., Näther, C., Renth, F., & Temps, F. (2009) · Journal of the American Chemical Society · doi:10.1021/ja906547d · Cited by 594
MUSTACICH, D., & POWIS, G. (2000) · Biochemical Journal · doi:10.1042/bj3460001 · Cited by 592
Michaelis, E. K. (1998) · Progress in Neurobiology · doi:10.1016/s0301-0082(97)00055-5 · Cited by 580
Gilat, S. L., Kawai, S. H., & Lehn, J. (1995) · Chemistry - A European Journal · doi:10.1002/chem.19950010504 · Cited by 575
Allosteric control of an ionotropic glutamate receptor with an optical switch
Volgraf, M., Gorostiza, P., Numano, R., Kramer, R. H., Isacoff, E. Y., & Trauner, D. (2006) · Nature Chemical Biology · doi:10.1038/nchembio756 · Cited by 573
Mutations Affecting Tea Blockade and Ion Permeation in Voltage-activated K + Channels
MacKinnon, R., & Yellen, G. (1990) · Science · doi:10.1126/science.2218530 · Cited by 563
Simonelli, F., Maguire, A. M., Testa, F., Pierce, E. A., Mingozzi, F., Bennicelli, J. L., Rossi, S., Marshall, K., Banfi, S., Surace, E. M., et al. (2010) · Molecular Therapy · doi:10.1038/mt.2009.277 · Cited by 553
Unexpected Modes of PDZ Domain Scaffolding Revealed by Structure of nNOS-Syntrophin Complex
Hillier, B. J., Christopherson, K. S., Prehoda, K. E., Bredt, D. S., & Lim, W. A. (1999) · Science · doi:10.1126/science.284.5415.812 · Cited by 549
Protein−Protein Interactions: Interface Structure, Binding Thermodynamics, and Mutational Analysis
Stites, W. E. (1997) · Chemical Reviews · doi:10.1021/cr960387h · Cited by 491
Measurement of the penetration depths of red and near infrared light in human “ex vivo” tissues
Stolik, S., Delgado, J. A., Pérez, A., & Anasagasti, L. (2000) · Journal of Photochemistry and Photobiology B: Biology · doi:10.1016/s1011-1344(00)00082-8 · Cited by 468
Pharmacological and functional characteristics of metabotropic excitatory amino acid receptors
Schoepp, D., Bockaert, J., & Sladeczek, F. (1990) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(90)90052-a · Cited by 462
Glutamate and GABA receptor signalling in the developing brain
Luján, R., Shigemoto, R., & López-Bendito, G. (2005) · Neuroscience · doi:10.1016/j.neuroscience.2004.09.042 · Cited by 411
The gramicidin ion channel: A model membrane protein
Kelkar, D. A., & Chattopadhyay, A. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.05.011 · Cited by 380
Fehrentz, T., Schönberger, M., & Trauner, D. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201103236 · Cited by 377
Photoswitchable Biomaterials: En Route to Optobioelectronic Systems
Willner, I. (1997) · Accounts of Chemical Research · doi:10.1021/ar9700062 · Cited by 372
Finkelstein, A., & Andersen, O. S. (1981) · The Journal of Membrane Biology · doi:10.1007/bf01875422 · Cited by 371
Genetically Encodable Fluorescent Biosensors for Tracking Signaling Dynamics in Living Cells
Newman, R. H., Fosbrink, M. D., & Zhang, J. (2011) · Chemical Reviews · doi:10.1021/cr100002u · Cited by 353
Colquhoun, D., & Sakmann, B. (1981) · Nature · doi:10.1038/294464a0 · Cited by 353
Surface Sites for Engineering Allosteric Control in Proteins
Lee, J., Natarajan, M., Nashine, V. C., Socolich, M., Vo, T., Russ, W. P., Benkovic, S. J., & Ranganathan, R. (2008) · Science · doi:10.1126/science.1159052 · Cited by 344
Design and Signaling Mechanism of Light-Regulated Histidine Kinases
Möglich, A., Ayers, R. A., & Moffat, K. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.12.017 · Cited by 341
The triple helix: 50 years later, the outcome
Duca, M., Vekhoff, P., Oussedik, K., Halby, L., & Arimondo, P. B. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn493 · Cited by 341
Remote Control of Neuronal Activity with a Light-Gated Glutamate Receptor
Szobota, S., Gorostiza, P., Del Bene, F., Wyart, C., Fortin, D. L., Kolstad, K. D., Tulyathan, O., Volgraf, M., Numano, R., Aaron, H. L., et al. (2007) · Neuron · doi:10.1016/j.neuron.2007.05.010 · Cited by 333
Rhodopsin and phototransduction: a model system for G protein‐linked receptors
Hargrave, P. A., & McDowell, J. H. (1992) · The FASEB Journal · doi:10.1096/fasebj.6.6.1544542 · Cited by 326
Optical Switches for Remote and Noninvasive Control of Cell Signaling
Gorostiza, P., & Isacoff, E. Y. (2008) · Science · doi:10.1126/science.1166022 · Cited by 325
β-Hairpin Peptidomimetics: Design, Structures and Biological Activities
Robinson, J. A. (2008) · Accounts of Chemical Research · doi:10.1021/ar700259k · Cited by 321
Structure of the winged-helix protein hRFX1 reveals a new mode of DNA binding
Gajiwala, K. S., Chen, H., Cornille, F., Roques, B. P., Reith, W., Mach, B., & Burley, S. K. (2000) · Nature · doi:10.1038/35002634 · Cited by 317
The inactivation gate of the Shaker K+ channel behaves like an open-channel blocker
Demo, S. D., & Yellen, G. (1991) · Neuron · doi:10.1016/0896-6273(91)90277-7 · Cited by 313
Asanuma, H., Liang, X., Nishioka, H., Matsunaga, D., Liu, M., & Komiyama, M. (2007) · Nature Protocols · doi:10.1038/nprot.2006.465 · Cited by 311
MECHANOSENSITIVE CHANNELS OF ESCHERICHIA COLI:The MscL Gene, Protein, and Activities
Sukharev, S. I., Blount, P., Martinac, B., & Kung, A. C. (1997) · Annual Review of Physiology · doi:10.1146/annurev.physiol.59.1.633 · Cited by 299
Structure of Bam HI Endonuclease Bound to DNA: Partial Folding and Unfolding on DNA Binding
Newman, M., Strzelecka, T., Dorner, L. F., Schildkraut, I., & Aggarwal, A. K. (1995) · Science · doi:10.1126/science.7624794 · Cited by 298
Protein–protein interactions: PDZ domain networks
Fanning, A. S., & Anderson, J. M. (1996) · Current Biology · doi:10.1016/s0960-9822(96)00737-3 · Cited by 298
Photo-control of helix content in a short peptide
Kumita, J. R., Smart, O. S., & Woolley, G. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.8.3803 · Cited by 291
Cis-trans photoisomerization of azobenzene. Solvent and triplet donors effects
Bortolus, P., & Monti, S. (1979) · The Journal of Physical Chemistry · doi:10.1021/j100469a002 · Cited by 290
Azobenzene as Conformational Switch in Model Peptides
Renner, C., & Moroder, L. (2006) · ChemBioChem · doi:10.1002/cbic.200500531 · Cited by 260
Spectral Tuning of Azobenzene Photoswitches for Biological Applications
Sadovski, O., Beharry, A. A., Zhang, F., & Woolley, G. A. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200805013 · Cited by 254
Lefèvre, T., & Subirade, M. (2000) · Biopolymers · doi:10.1002/1097-0282(200012)54:7<489::aid-bip20>3.0.co;2-f · Cited by 253
Photochemical control of endogenous ion channels and cellular excitability
Fortin, D. L., Banghart, M. R., Dunn, T. W., Borges, K., Wagenaar, D. A., Gaudry, Q., Karakossian, M. H., Otis, T. S., Kristan, W. B., Trauner, D., et al. (2008) · Nature Methods · doi:10.1038/nmeth.1187 · Cited by 247
Photochromic Blockers of Voltage‐Gated Potassium Channels
Banghart, M. R., Mourot, A., Fortin, D. L., Yao, J. Z., Kramer, R. H., & Trauner, D. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200904504 · Cited by 241
Photochemical Restoration of Visual Responses in Blind Mice
Polosukhina, A., Litt, J., Tochitsky, I., Nemargut, J., Sychev, Y., De Kouchkovsky, I., Huang, T., Borges, K., Trauner, D., Van Gelder, R. N., et al. (2012) · Neuron · doi:10.1016/j.neuron.2012.05.022 · Cited by 238
Mazzoni, F., Novelli, E., & Strettoi, E. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.4968-08.2008 · Cited by 235
Liu, R. S., & Asato, A. E. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.2.259 · Cited by 230
Structures of the Prokaryotic Mechanosensitive Channels MscL and MscS
(2007) · Current Topics in Membranes · doi:10.1016/s1063-5823(06)58001-9 · Cited by 221
Photochromic Activators of the Acetylcholine Receptor
Bartels, E., Wassermann, N. H., & Erlanger, B. F. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.8.1820 · Cited by 214
Dynamic control over cell adhesive properties using molecular-based surface engineering strategies
Robertus, J., Browne, W. R., & Feringa, B. L. (2010) · Chem. Soc. Rev. · doi:10.1039/b906608j · Cited by 212
Self-citationSpörlein, S., Carstens, H., Satzger, H., Renner, C., Behrendt, R., Moroder, L., Tavan, P., Zinth, W., & Wachtveitl, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.122238799 · Cited by 211
Optogenetics: controlling cell function with light
Pastrana, E. (2011) · Nature Methods · doi:10.1038/nmeth.f.323 · Cited by 200
Bredenbeck, J., Helbing, J., Kumita, J. R., Woolley, G. A., & Hamm, P. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406948102 · Cited by 189
The Incorporation of a Photoisomerizable Amino Acid into Proteins in E. c oli
Bose, M., Groff, D., Xie, J., Brustad, E., & Schultz, P. G. (2006) · Journal of the American Chemical Society · doi:10.1021/ja055467u · Cited by 188
LiGluR restores visual responses in rodent models of inherited blindness
Caporale, N., Kolstad, K. D., Lee, T., Tochitsky, I., Dalkara, D., Trauner, D., Kramer, R., Dan, Y., Isacoff, E. Y., & Flannery, J. G. (2011) · Molecular Therapy · doi:10.1038/mt.2011.103 · Cited by 182
Mechanisms of photoswitch conjugation and light activation of an ionotropic glutamate receptor
Gorostiza, P., Volgraf, M., Numano, R., Szobota, S., Trauner, D., & Isacoff, E. Y. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701274104 · Cited by 181
Rapid optical control of nociception with an ion-channel photoswitch
Mourot, A., Fehrentz, T., Le Feuvre, Y., Smith, C. M., Herold, C., Dalkara, D., Nagy, F., Trauner, D., & Kramer, R. H. (2012) · Nature Methods · doi:10.1038/nmeth.1897 · Cited by 177
Stanfield, R. L., & Wilson, I. A. (1995) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(95)80015-s · Cited by 173
Optochemical control of genetically engineered neuronal nicotinic acetylcholine receptors
Tochitsky, I., Banghart, M. R., Mourot, A., Yao, J. Z., Gaub, B., Kramer, R. H., & Trauner, D. (2012) · Nature Chemistry · doi:10.1038/nchem.1234 · Cited by 172
Devillers-Thiéry, A., Galzi, J. L., Eiselé, J. L., Bertrand, S., Bertrand, D., & Changeux, J. P. (1993) · The Journal of Membrane Biology · doi:10.1007/bf02505755 · Cited by 170
Flint, D. G., Kumita, J. R., Smart, O. S., & Woolley, G. A. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00109-6 · Cited by 167
Photoswitchable Hydrogen-Bonding in Self-Organized Cylindrical Peptide Systems
Vollmer, M. S., Clark, T. D., Steinem, C., & Ghadiri, M. R. (1999) · Angewandte Chemie International Edition · doi:10.1002/(sici)1521-3773(19990601)38:11<1598::aid-anie1598>3.0.co;2-j · Cited by 165
Bidirectional Photocontrol of Peptide Conformation with a Bridged Azobenzene Derivative
Samanta, S., Qin, C., Lough, A. J., & Woolley, G. A. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201202383 · Cited by 165
Estimation of the available free energy in a LOV2-Jα photoswitch
Yao, X., Rosen, M. K., & Gardner, K. H. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.99 · Cited by 163
Incorporation of Nonnatural Amino Acids into Streptavidin through In Vitro Frame-Shift Suppression
Hohsaka, T., Ashizuka, Y., Murakami, H., & Sisido, M. (1996) · Journal of the American Chemical Society · doi:10.1021/ja9614225 · Cited by 163
A Light‐Driven DNA Nanomachine for the Efficient Photoswitching of RNA Digestion
Zhou, M., Liang, X., Mochizuki, T., & Asanuma, H. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.200907082 · Cited by 162
Principles and Applications of the Photochemical Control of Cellular Processes
Deiters, A. (2010) · ChemBioChem · doi:10.1002/cbic.200900529 · Cited by 160
Reduction and specific alkylation of the receptor for acetylcholine.
Karlin, A., & Winnik, M. (1968) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.60.2.668 · Cited by 158
Fluorescence Imaging of Azobenzene Photoswitching In Vivo
Beharry, A. A., Wong, L., Tropepe, V., & Woolley, G. A. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201006506 · Cited by 156
A DNA Nanomachine Powered by Light Irradiation
Liang, X., Nishioka, H., Takenaka, N., & Asanuma, H. (2008) · ChemBioChem · doi:10.1002/cbic.200700649 · Cited by 155
Photoregulation of cyclic peptide conformation.
Ulysse, L. G., Cubillos, J., & Chmielewski, J. A. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00137a023 · Cited by 153
Azo‐Propofols: Photochromic Potentiators of GABAAReceptors
Stein, M., Middendorp, S. J., Carta, V., Pejo, E., Raines, D. E., Forman, S. A., Sigel, E., & Trauner, D. H. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201205475 · Cited by 149
Engineering Light-Gated Ion Channels
Banghart, M. R., Volgraf, M., & Trauner, D. H. (2006) · Biochemistry · doi:10.1021/bi0618058 · Cited by 144
Liang, X., Mochizuki, T., & Asanuma, H. (2009) · Small · doi:10.1002/smll.200900223 · Cited by 144
Behrendt, R., Renner, C., Schenk, M., Wang, F., Wachtveitl, J., Oesterhelt, D., & Moroder, L. (1999) · Angewandte Chemie International Edition · doi:10.1002/(sici)1521-3773(19990917)38:18<2771::aid-anie2771>3.0.co;2-w · Cited by 141
Regulating gene expression with light-activated oligonucleotides
Tang, X., & Dmochowski, I. J. (2006) · Molecular BioSystems · doi:10.1039/b614349k · Cited by 141
A Light‐Driven DNA Nanomachine for the Efficient Photoswitching of RNA Digestion
Zhou, M., Liang, X., Mochizuki, T., & Asanuma, H. (2010) · Angewandte Chemie · doi:10.1002/ange.200907082 · Cited by 141
The protein-conducting channel SecYEG
Veenendaal, A. K. J., van der Does, C., & Driessen, A. J. M. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.02.009 · Cited by 139
A light-gated, potassium-selective glutamate receptor for the optical inhibition of neuronal firing
Janovjak, H., Szobota, S., Wyart, C., Trauner, D. H., & Isacoff, E. Y. (2010) · Nature Neuroscience · doi:10.1038/nn.2589 · Cited by 136
Aemissegger, A., Kräutler, V., A, W. F. V. G., & Hilvert, D. (2005) · Journal of the American Chemical Society · doi:10.1021/ja0442567 · Cited by 134
Wagenknecht, H. (2006) · Natural Product Reports · doi:10.1039/b504754b · Cited by 129
A Designedβ-Hairpin Containing a Natural Hydrophobic Cluster
Espinosa, J. F., & Gellman, S. H. (2000) · Angewandte Chemie International Edition · doi:10.1002/1521-3773(20000703)39:13<2330::aid-anie2330>3.0.co;2-c · Cited by 128
Lee, C. T., Smith, K. A., & Hatton, T. A. (2004) · Biochemistry · doi:10.1021/bi048556c · Cited by 126
Singer, M., & Jäschke, A. (2010) · Journal of the American Chemical Society · doi:10.1021/ja1024782 · Cited by 122
Acetylcholine Receptor: Covalent Attachment of Depolarizing Groups at the Active Site
Silman, I., & Karlin, A. (1969) · Science · doi:10.1126/science.164.3886.1420 · Cited by 122
Optical Control of Neuronal Activity
Szobota, S., & Isacoff, E. Y. (2010) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.093008.131400 · Cited by 122
Photocontrol of Coiled‐Coil Proteins in Living Cells
Zhang, F., Timm, K. A., Arndt, K. M., & Woolley, G. A. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201000909 · Cited by 117
Redox Potential of Azobenzene as an Amino Acid Residue in Peptides
Boulègue, C., Löweneck, M., Renner, C., & Moroder, L. (2007) · ChemBioChem · doi:10.1002/cbic.200600495 · Cited by 111
Photocontrolled Folding and Unfolding of a Collagen Triple Helix
Kusebauch, U., Cadamuro, S. A., Musiol, H., Lenz, M. O., Wachtveitl, J., Moroder, L., & Renner, C. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200601432 · Cited by 111
α-Helix folding in the presence of structural constraints
Ihalainen, J., Paoli, B., Muff, S., Backus, E. G. H., Bredenbeck, J., Woolley, G., Caflisch, A., & Hamm, P. (2008) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0712099105 · Cited by 105
A Photocontrolled β‐Hairpin Peptide
Dong, S., Löweneck, M., Schrader, T. E., Schreier, W. J., Zinth, W., Moroder, L., & Renner, C. (2005) · Chemistry - A European Journal · doi:10.1002/chem.200500986 · Cited by 105
Photomodulation of ionic current through hemithioindigo-modified gramicidin channels
Lougheed, T., Borisenko, V., Hennig, T., Rück‐Braun, K., & Woolley, G. A. (2004) · Organic & Biomolecular Chemistry · doi:10.1039/b408485c · Cited by 104
The lateral gate of SecYEG opens during protein translocation.
du Plessis, D. J. F., Berrelkamp, G., Nouwen, N., & Driessen, A. J. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m901855200 · Cited by 102
Reversible Photocontrol of DNA Binding by a Designed GCN4-bZIP Protein
Woolley, G. A., Jaikaran, A. S. I., Berezovski, M. V., Calarco, J. P., Krylov, S. N., Smart, O. S., & Kumita, J. R. (2006) · Biochemistry · doi:10.1021/bi060142r · Cited by 98
Lewis, F. D., Liu, X., Wu, Y., Miller, S. E., Wasielewski, M. R., Letsinger, R. L., Sanishvili, R., Joachimiak, A., Tereshko, V. A., & Egli, M. (1999) · Journal of the American Chemical Society · doi:10.1021/ja991934u · Cited by 97
Folding and unfolding of a photoswitchable peptide from picoseconds to microseconds
Ihalainen, J. A., Bredenbeck, J., Pfister, R., Helbing, J., Chi, L., van Stokkum, I. H. M., Woolley, G. A., & Hamm, P. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607748104 · Cited by 97
A Light-Modulated Sequence-Specific DNA-Binding Peptide
Caamaño, A. M., Vázquez, M. E., Martı́nez-Costas, J., Castedo, L., & Mascarenas, J. L. (2000) · Angewandte Chemie International Edition · Cited by 97
Light-triggered β-hairpin folding and unfolding
Schrader, T. E., Schreier, W. J., Cordes, T., Koller, F. O., Babitzki, G., Denschlag, R., Renner, C., Löweneck, M., Dong, S., Moroder, L., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707322104 · Cited by 96
A Water-Soluble Azobenzene Cross-Linker for Photocontrol of Peptide Conformation
Zhang, Z., Burns, D. C., Kumita, J. R., Smart, O. S., & Woolley, G. A. (2003) · Bioconjugate Chemistry · doi:10.1021/bc0340161 · Cited by 93
Photocontrollable Peptide‐Based Switches Target the Anti‐Apoptotic Protein Bcl‐xL
Kneissl, S., Loveridge, E. J., Williams, C., Crump, M. P., & Allemann, R. K. (2008) · ChemBioChem · doi:10.1002/cbic.200800502 · Cited by 93
Photocontrol of DNA Binding Specificity of a Miniature Engrailed Homeodomain
Guerrero, L., Smart, O. S., Woolley, G. A., & Allemann, R. K. (2005) · Journal of the American Chemical Society · doi:10.1021/ja0550428 · Cited by 93
Robust and Photocontrollable DNA Capsules Using Azobenzenes
Tanaka, F., Mochizuki, T., Liang, X., Asanuma, H., Tanaka, S., Suzuki, K., Kitamura, S., Nishikawa, A., Ui‐Tei, K., & Hagiya, M. (2010) · Nano Letters · doi:10.1021/nl101829m · Cited by 91
Light-regulated Catalysis by an RNA-cleaving Deoxyribozyme
Liu, Y., & Sen, D. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.06.060 · Cited by 91
Photoregulation of RNA Digestion by RNase H with Azobenzene-Tethered DNA
Matsunaga, D., Asanuma, H., & Komiyama, M. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0471976 · Cited by 88
A Light-Modulated Sequence-Specific DNA-Binding Peptide
Caamaño, A. M., Vázquez, M. E., Martı́nez-Costas, J., Castedo, L., & Mascarenas, J. L. (2000) · Angewandte Chemie · Cited by 87
Han, W., Lovell, T., Liu, T., & Noodleman, L. (2002) · ChemPhysChem · Cited by 87
Nanosculpting reversed wavelength sensitivity into a photoswitchable iGluR
Numano, R., Szobota, S., Lau, A. Y., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811899106 · Cited by 85
Ultrafast Conformational Dynamics in Cyclic Azobenzene Peptides of Increased Flexibility
Wachtveitl, J., Spörlein, S., Satzger, H., Fonrobert, B., Renner, C., Behrendt, R., Oesterhelt, D., Moroder, L., & Zinth, W. (2004) · Biophysical Journal · doi:10.1016/s0006-3495(04)74292-7 · Cited by 84
A Photochromic Agonist of AMPA Receptors
Erdmann, P. S., Sumser, M., & Trauner, D. H. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201109265 · Cited by 84
Photochemical Regulation of DNA‐Binding Specificity of MyoD
Guerrero, L., Smart, O. S., Weston, C. J., Burns, D. C., Woolley, G. A., & Allemann, R. K. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200502666 · Cited by 83
Synthesis and application of caged peptides and proteins
Shigeri, Y., Tatsu, Y., & Yumoto, N. (2001) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(01)00148-6 · Cited by 81
Nishioka, H., Liang, X., Kashida, H., & Asanuma, H. (2007) · Chemical Communications · doi:10.1039/b708952j · Cited by 80
Hemithioindigo-based photoswitches as ultrafast light trigger in chromopeptides
Cordes, T., Weinrich, D., Kempa, S., et al. (2006) · Chemical Physics Letters · doi:10.1016/j.cplett.2006.07.043 · Cited by 80
Azobenzene as photoresponsive conformational switch in cyclic peptides*
Renner, C., Kusebauch, U., Löweneck, M., Milbradt, A. G., & Moroder, L. (2005) · Journal of Peptide Research · doi:10.1111/j.1399-3011.2004.00203.x · Cited by 77
Behrendt, R., Schenk, M., Musiol, H., & Moroder, L. (1999) · Journal of Peptide Science · Cited by 77
Ostermeier, M. (2009) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2009.04.007 · Cited by 76
Straightforward and Reversible Photoregulation of Hybridization by Using a Photochromic Nucleoside
Ogasawara, S., & Maeda, M. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200803496 · Cited by 76
Bonardi, F., Halza, E., Walko, M., Du Plessis, F., Nouwen, N., Feringa, B. L., & Driessen, A. J. M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1101705108 · Cited by 72
Self-citationAll Optical Interface for Parallel, Remote, and Spatiotemporal Control of Neuronal Activity
Wang, S., Szobota, S., Wang, Y., Volgraf, M., Liu, Z., Sun, C., Trauner, D. H., Isacoff, E. Y., & Zhang, X. (2007) · Nano Letters · doi:10.1021/nl072783t · Cited by 72
Mismatch‐Binding Ligands Function as a Molecular Glue for DNA
Peng, T., Dohno, C., & Nakatani, K. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200601190 · Cited by 70
Optical switches and triggers for the manipulation of ion channels and pores
Gorostiza, P., & Isacoff, E. Y. (2007) · Molecular BioSystems · doi:10.1039/b710287a · Cited by 68
A Blue-Green Absorbing Cross-Linker for Rapid Photoswitching of Peptide Helix Content
Chi, L., Sadovski, O., & Woolley, G. A. (2006) · Bioconjugate Chemistry · doi:10.1021/bc050363u · Cited by 66
Reversible Photoswitching of a G‐Quadruplex
Ogasawara, S., & Maeda, M. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200902183 · Cited by 66
Chatani, E., Hayashi, R., Moriyama, H., & Ueki, T. (2002) · Protein Science · doi:10.1110/ps.31102 · Cited by 65
Regner, N., Herzog, T. T., Haiser, K., Hoppmann, C., Beyermann, M., Sauermann, J., Engelhard, M., Cordes, T., Rück‐Braun, K., & Zinth, W. (2012) · The Journal of Physical Chemistry B · doi:10.1021/jp300982a · Cited by 65
Muranaka, N., Hohsaka, T., & Sisido, M. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)03211-2 · Cited by 65
Photocontrol of Cell Adhesion Processes
Schütt, M., Krupka, S. S., Milbradt, A. G., Deindl, S., Sinner, E., Oesterhelt, D., Renner, C., & Moroder, L. (2003) · Chemistry & Biology · doi:10.1016/s1074-5521(03)00128-5 · Cited by 64
Lewis, F. D., Wu, Y., & Liu, X. (2002) · Journal of the American Chemical Society · doi:10.1021/ja026941o · Cited by 62
Light‐Induced Control of Protein Translocation by the SecYEG Complex
Bonardi, F., London, G., Nouwen, N. P., Feringa, B. L., & Driessen, A. J. M. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201002243 · Cited by 62
Self-citationOn the geometries and UV/Vis spectra of substituted trans-azobenzenes
Briquet, L., Vercauteren, D. P., André, J. M., Perpète, É. A., & Jacquemin, D. (2006) · Chemical Physics Letters · doi:10.1016/j.cplett.2006.12.065 · Cited by 61
Modulating PNA/DNA Hybridization by Light
Stafforst, T., & Hilvert, D. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201004548 · Cited by 61
Is solvated trans-azobenzene twisted or planar?
Briquet, L., Vercauteren, D. P., Perpète, É. A., & Jacquemin, D. (2005) · Chemical Physics Letters · doi:10.1016/j.cplett.2005.09.119 · Cited by 59
Fissi, A., Pieroni, O., Angelini, N., & Lenci, F. (1999) · Macromolecules · doi:10.1021/ma990796q · Cited by 57
Photocontrol of Contracting Muscle Fibers
Hoppmann, C., Schmieder, P., Domaing, P., Vogelreiter, G., Eichhorst, J., Wiesner, B., Morano, I. L., Rück‐Braun, K., & Beyermann, M. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201101398 · Cited by 56
Photocontrol of Kinesin ATPase Activity Using an Azobenzene Derivative
Yamada, M. D., Nakajima, Y., Maeda, H., & Maruta, S. (2007) · The Journal of Biochemistry · doi:10.1093/jb/mvm183 · Cited by 56
Site-specific incorporation of photoisomerizable azobenzene groups into ribonuclease S
Liu, D., Karanicolas, J., Yu, C., Zhang, Z., & Woolley, G. A. (1997) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(97)10044-0 · Cited by 55
Nakayama, K., Endo, M., & Majima, T. (2004) · Chemical Communications · doi:10.1039/b409844g · Cited by 54
Reversibility of conformational switching in light-sensitive peptides
Borisenko, V., & Woolley, G. A. (2005) · Journal of Photochemistry and Photobiology A Chemistry · doi:10.1016/j.jphotochem.2004.12.026 · Cited by 52
Control of Excimer Emission and Photochemistry of Stilbene Units by Oligonucleotide Hybridization
Letsinger, R. L., & Wu, T. (1994) · Journal of the American Chemical Society · doi:10.1021/ja00081a069 · Cited by 50
Origins of Helix−Coil Switching in a Light-Sensitive Peptide
Burns, D. C., Flint, D. G., Kumita, J. R., Feldman, H. J., Serrano, L., Zhang, Z., Smart, O. S., & Woolley, G. A. (2004) · Biochemistry · doi:10.1021/bi048152k · Cited by 50
Structure-Based Design of a Photocontrolled DNA Binding Protein
Morgan, S.-A., Al-Abdul-Wahid, S., & Woolley, G. A. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.03.053 · Cited by 47
Bis‐Azobenzene Crosslinkers for Photocontrol of Peptide Structure
Samanta, S., & Woolley, G. A. (2011) · ChemBioChem · doi:10.1002/cbic.201100204 · Cited by 46
Azobenzene Photoswitches for Staudinger–Bertozzi Ligation
Szymański, W., Wu, B., Poloni, C., Janssen, D. B., & Feringa, B. L. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201208596 · Cited by 46
Self-citationARTIFICIAL LIGHT‐SENSITIVE ENZYMATIC SYSTEMS AS CHEMICAL AMPLIFIERS OF WEAK LIGHT SIGNALS
Martínek, K., & Berezin, I. V. (1979) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1979.tb07104.x · Cited by 45
Engineering Protein Switches: Sensors, Regulators, and Spare Parts for Biology and Biotechnology
Golynskiy, M. V., Koay, M. S. T., Vinkenborg, J. L., et al. (2011) · ChemBioChem · doi:10.1002/cbic.201000642 · Cited by 45
Enlightened Enzymes: Strategies to Create Novel Photoresponsive Proteins
Krauß, U., Drepper, T., & Jaeger, K. (2011) · Chemistry - A European Journal · doi:10.1002/chem.201002716 · Cited by 43
A New Tool in Peptide Engineering: A Photoswitchable Stilbene‐type β‐Hairpin Mimetic
Erdélyi, M., Karlén, A., & Gogoll, A. (2005) · Chemistry - A European Journal · doi:10.1002/chem.200500648 · Cited by 42
Beharry, A. A., Sadovski, O., & Woolley, G. A. (2008) · Organic & Biomolecular Chemistry · doi:10.1039/b810533b · Cited by 42
Chatani, E. (2002) · Protein Science · doi:10.1110/ps.ps.31102 · Cited by 41
Kumita, J. R., Flint, D. G., Smart, O. S., & Woolley, G. A. (2002) · Protein Engineering Design and Selection · doi:10.1093/protein/15.7.561 · Cited by 40
A Hydrophilic Azobenzene-Bearing Amino Acid for Photochemical Control of a Restriction Enzyme BamHI
Nakayama, K., Endo, M., & Majima, T. (2005) · Bioconjugate Chemistry · doi:10.1021/bc049724g · Cited by 36
RNA Aptamers That Reversibly Bind Photoresponsive Azobenzene‐Containing Peptides
Hayashi, G., Hagihara, M., & Nakatani, K. (2008) · Chemistry - A European Journal · doi:10.1002/chem.200800936 · Cited by 35
Kusebauch, U., Cadamuro, S. A., Musiol, H., Moroder, L., & Renner, C. (2007) · Chemistry - A European Journal · doi:10.1002/chem.200601162 · Cited by 35
Correlation of membrane potential and potassium flux in the electroplax of electrophorus
Higman, H. B., Podleski, T. R., & Bartels, E. (1964) · Biochimica et Biophysica Acta (BBA) - Specialized Section on Biophysical Subjects · doi:10.1016/0926-6577(64)90047-6 · Cited by 34
Liem, L. K., Simard, J. M., Song, Y., & Tewari, K. P. (1995) · Neurosurgery · doi:10.1227/00006123-199502000-00020 · Cited by 33
Photoswitchable Click Amino Acids: Light Control of Conformation and Bioactivity
Hoppmann, C., Schmieder, P., Heinrich, N., & Beyermann, M. (2011) · ChemBioChem · doi:10.1002/cbic.201100578 · Cited by 31
Molecular Design for Reversing the Photoswitching Mode of Turning ON and OFF DNA Hybridization
Liang, X., Takenaka, N., Nishioka, H., & Asanuma, H. (2008) · Chemistry - An Asian Journal · doi:10.1002/asia.200700384 · Cited by 30
Exploring the Pharmacology and Action Spectra of Photochromic Open‐Channel Blockers
Fehrentz, T., Kuttruff, C. A., Huber, F. M. E., Kienzler, M. A., Mayer, P., & Trauner, D. H. (2012) · ChemBioChem · doi:10.1002/cbic.201200216 · Cited by 30
Ichimaru, N., Murai, M., Abe, M., Hamada, T., Yamada, Y., Makino, S., Nishioka, T., Makabe, H., Makino, A., Kobayashi, T., et al. (2004) · Biochemistry · doi:10.1021/bi0479003 · Cited by 30
Kumita, J. R., Flint, D. G., Woolley, G. A., & Smart, O. S. (2002) · Faraday Discussions · doi:10.1039/b200897a · Cited by 28
Mirarefi, P., & Lee, C. T. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.09.007 · Cited by 23
Flashy Science: Controlling Neural Function with Light
Thompson, S. M., Kao, J. P. Y., Krämer, R., Poskanzer, K. E., Silver, R. A., DiGregorio, D. A., & Wang, S. S. ‐. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3515-05.2005 · Cited by 22
Weston, D., Kirkham, J., & Cullen, D. C. (1999) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(99)00099-9 · Cited by 20
Photoresponsive tandem zinc finger peptide
Nomura, A., & Okamoto, A. (2009) · Chemical Communications · doi:10.1039/b819838a · Cited by 20
Parisot, J., Kurz, K., Hilbrig, F., & Freitag, R. (2009) · Journal of Separation Science · doi:10.1002/jssc.200800698 · Cited by 17
Photocontrol of Calmodulin Interaction with Target Peptides using Azobenzene Derivative
Shishido, H., Yamada, M. D., Kondo, K., & Maruta, S. (2009) · The Journal of Biochemistry · doi:10.1093/jb/mvp107 · Cited by 16
Varedian, M., Erdélyi, M., Persson, Å. H., & Gogoll, A. (2008) · Journal of Peptide Science · doi:10.1002/psc.1103 · Cited by 14
Photomodulation of the Redox and Folding Adjuvant Properties of Bis(cysteinyl) Peptides
Cabrele, C., Cattani‐Scholz, A., Renner, C., Behrendt, R., Oesterhelt, D., & Moroder, L. (2002) · European Journal of Organic Chemistry · doi:10.1002/1099-0690(200207)2002:13<2144::aid-ejoc2144>3.0.co;2-i · Cited by 13
Research works printed but not linked: 186
- Willner, 1996, Angew. Chem., Int. Ed., 35, 367, 10.1002/anie.199603671 · doi:10.1002/anie.199603671
- Curley, 1999, Pharmacol. Ther., 82, 347, 10.1016/S0163-7258(98)00055-2 · doi:10.1016/s0163-7258(98)00055-2
- Berg, 2002, Biochemistry
- Hamon, 2010, Tetrahedron, 66, 2538, 10.1016/j.tet.2010.01.057 · doi:10.1016/j.tet.2010.01.057
- Hamon, 2009, Tetrahedron, 65, 10105, 10.1016/j.tet.2009.08.063 · doi:10.1016/j.tet.2009.08.063
- Cattaneo, 1999, Phys. Chem. Chem. Phys., 1, 4739, 10.1039/a905055h · doi:10.1039/a905055h
- Zhang, 2009, J. Am. Chem. Soc., 131, 2283, 10.1021/ja807938v · doi:10.1021/ja807938v
- Nishimura, 1976, Bull. Chem. Soc. Jpn., 49, 1381, 10.1246/bcsj.49.1381 · doi:10.1246/bcsj.49.1381
- Wachtveitl, 2011, ChemBioChem, 12, 1169, 10.1002/cbic.201100185 · doi:10.1002/cbic.201100185
- Mendonça, 2011, Molecular Switches
- Han, 2002, ChemPhysChem, 3, 167, 10.1002/1439-7641(20020215)3:2<167::AID-CPHC167>3.0.CO;2-G · doi:10.1002/1439-7641(20020215)3:2<167::aid-cphc167>3.0.co;2-g
- Cammenga, 2009, Ind. Eng. Chem. Res., 48, 10120, 10.1021/ie900800q · doi:10.1021/ie900800q
- Minkin, 2011, Molecular Switches
- Lukyanov, 2005, Chem. Heterocycl. Compd., 41, 281, 10.1007/s10593-005-0148-x · doi:10.1007/s10593-005-0148-x
- Levitus, 1997, Chem. Phys. Lett., 277, 118, 10.1016/S0009-2614(97)00826-9 · doi:10.1016/s0009-2614(97)00826-9
- Bletz, 2002, J. Phys. Chem. A, 106, 2232, 10.1021/jp012562q · doi:10.1021/jp012562q
- Chibisov, 1997, J. Phys. Chem. A, 101, 4305, 10.1021/jp962569l · doi:10.1021/jp962569l
- Flannery, 1968, J. Am. Chem. Soc., 90, 5660, 10.1021/ja01023a003 · doi:10.1021/ja01023a003
- Wetzler, 1999, Phys. Chem. Chem. Phys., 1, 4955, 10.1039/a905273i · doi:10.1039/a905273i
- Aizawa, 1977, Arch. Biochem. Biophys., 180, 41, 10.1016/0003-9861(77)90006-6 · doi:10.1016/0003-9861(77)90006-6
- Namba, 1975, Chem. Lett., 4, 947, 10.1246/cl.1975.947 · doi:10.1246/cl.1975.947
- Sakata, 2005, Proc. Natl. Acad. Sci. U. S. A., 102, 4759, 10.1073/pnas.0405265102 · doi:10.1073/pnas.0405265102
- Warford, 2011, Molecular Switches
- Kellogg, 1967, J. Org. Chem., 32, 3093, 10.1021/jo01285a035 · doi:10.1021/jo01285a035
- Nakamura, 1988, J. Org. Chem., 53, 6136, 10.1021/jo00261a035 · doi:10.1021/jo00261a035
- Gilat, 1995, Chem.─Eur. J., 1, 275
- Yokoyama, 2011, Molecular Switches
- Santiago, 1968, J. Am. Chem. Soc., 90, 3654, 10.1021/ja01016a009 · doi:10.1021/ja01016a009
- Heller, 1981, J. Chem. Soc., Perkin Trans. 1, 197, 10.1039/P19810000197 · doi:10.1039/p19810000197
- Darcy, 1981, J. Chem. Soc., Perkin Trans. 1, 202, 10.1039/P19810000202 · doi:10.1039/p19810000202
- Ilge, 1990, J. Mol. Struct., 218, 39, 10.1016/0022-2860(90)80241-B · doi:10.1016/0022-2860(90)80241-b
- Yokoyama, 1996, Bull. Chem. Soc. Jpn., 69, 1605, 10.1246/bcsj.69.1605 · doi:10.1246/bcsj.69.1605
- Yamaguchi, 1992, Bull. Chem. Soc. Jpn., 65, 649, 10.1246/bcsj.65.649 · doi:10.1246/bcsj.65.649
- Cordes, 2008, Chem. Phys. Lett., 455, 197, 10.1016/j.cplett.2008.02.096 · doi:10.1016/j.cplett.2008.02.096
- Letsinger, 1995, J. Am. Chem. Soc., 117, 7323, 10.1021/ja00133a005 · doi:10.1021/ja00133a005
- Lewis, 1999, J. Am. Chem. Soc., 121, 11928, 10.1021/ja9932131 · doi:10.1021/ja9932131
- Yamana, 1996, Tetrahedron Lett., 37, 637, 10.1016/0040-4039(95)02220-1 · doi:10.1016/0040-4039(95)02220-1
- Yamana, 1998, Nucleosides Nucleotides Nucleic Acids, 17, 233, 10.1080/07328319808005172 · doi:10.1080/07328319808005172
- Yamana, 1999, Bioorg. Med. Chem., 7, 2977, 10.1016/S0968-0896(99)00244-8 · doi:10.1016/s0968-0896(99)00244-8
- Wang, 2008, Tetrahedron Lett., 49, 5087, 10.1016/j.tetlet.2008.06.027 · doi:10.1016/j.tetlet.2008.06.027
- Wu, 2009, Chem. Commun., 14, 1915, 10.1039/b819643e · doi:10.1039/b819643e
- Patnaik, 2007, Bioorg. Med. Chem., 15, 7840, 10.1016/j.bmc.2007.08.042 · doi:10.1016/j.bmc.2007.08.042
- Keiper, 2006, Angew. Chem., Int. Ed., 45, 3306, 10.1002/anie.200600164 · doi:10.1002/anie.200600164
- Ogasawara, 2008, Tetrahedron Lett., 49, 2479, 10.1016/j.tetlet.2008.01.124 · doi:10.1016/j.tetlet.2008.01.124
- Lena, 2010, Angew. Chem., Int. Ed., 49, 3657, 10.1002/anie.201000805 · doi:10.1002/anie.201000805
- Kashida, 2009, Curr. Org. Chem., 13, 1065, 10.2174/138527209788680736 · doi:10.2174/138527209788680736
- Asanuma, 1998, Tetrahedron Lett., 39, 9015, 10.1016/S0040-4039(98)02022-X · doi:10.1016/s0040-4039(98)02022-x
- Asanuma, 2001, Chem. Lett., 30, 108, 10.1246/cl.2001.108 · doi:10.1246/cl.2001.108
- Asanuma, 1999, Angew. Chem., Int. Ed., 38, 2393, 10.1002/(SICI)1521-3773(19990816)38:16<2393::AID-ANIE2393>3.0.CO;2-7 · doi:10.1002/(sici)1521-3773(19990816)38:16<2393::aid-anie2393>3.0.co;2-7
- Liang, 2003, J. Am. Chem. Soc., 125, 16408, 10.1021/ja037248j · doi:10.1021/ja037248j
- Asanuma, 2001, ChemBioChem, 2, 39, 10.1002/1439-7633(20010105)2:1<39::AID-CBIC39>3.0.CO;2-E · doi:10.1002/1439-7633(20010105)2:1<39::aid-cbic39>3.0.co;2-e
- Asanuma, 2000, Angew. Chem., Int. Ed., 39, 1316, 10.1002/(SICI)1521-3773(20000403)39:7<1316::AID-ANIE1316>3.0.CO;2-H · doi:10.1002/(sici)1521-3773(20000403)39:7<1316::aid-anie1316>3.0.co;2-h
- Liang, 2002, J. Am. Chem. Soc., 124, 1877, 10.1021/ja011988f · doi:10.1021/ja011988f
- Yamazawa, 2000, Angew. Chem., Int. Ed., 39, 2356, 10.1002/1521-3773(20000703)39:13<2356::AID-ANIE2356>3.0.CO;2-9 · doi:10.1002/1521-3773(20000703)39:13<2356::aid-anie2356>3.0.co;2-9
- Asanuma, 2001, Angew. Chem., Int. Ed., 40, 2671, 10.1002/1521-3773(20010716)40:14<2671::AID-ANIE2671>3.0.CO;2-Z · doi:10.1002/1521-3773(20010716)40:14<2671::aid-anie2671>3.0.co;2-z
- Asanuma, 2005, Nucleic Acids Symp. Ser., 49, 35, 10.1093/nass/49.1.35 · doi:10.1093/nass/49.1.35
- Liu, 2006, J. Am. Chem. Soc., 128, 1009, 10.1021/ja055983k · doi:10.1021/ja055983k
- Kim, 2009, Proc. Natl. Acad. Sci. U. S. A., 106, 6489, 10.1073/pnas.0812402106 · doi:10.1073/pnas.0812402106
- Andersson, 2008, J. Am. Chem. Soc., 130, 11836, 10.1021/ja801968f · doi:10.1021/ja801968f
- Dohno, 2007, J. Am. Chem. Soc., 129, 11898, 10.1021/ja074325s · doi:10.1021/ja074325s
- Uno, 2007, Nucleic Acids Symp. Ser., 51, 173, 10.1093/nass/nrm087 · doi:10.1093/nass/nrm087
- Dohno, 2011, Chem. Soc. Rev., 40, 5729, 10.1039/c1cs15062f · doi:10.1039/c1cs15062f
- Dohno, 2009, Bioorg. Med. Chem., 17, 2536, 10.1016/j.bmc.2009.01.053 · doi:10.1016/j.bmc.2009.01.053
- Ciardelli, 2011, Molecular Switches
- Goodman, 1966, J. Am. Chem. Soc., 88, 5010, 10.1021/ja00973a042 · doi:10.1021/ja00973a042
- Goodman, 1967, J. Am. Chem. Soc., 89, 3863, 10.1021/ja00991a031 · doi:10.1021/ja00991a031
- Benedetti, 1968, Biochemistry, 7, 4242, 10.1021/bi00852a015 · doi:10.1021/bi00852a015
- Benedetti, 1968, Biochemistry, 7, 4234, 10.1021/bi00852a014 · doi:10.1021/bi00852a014
- Goodman, 1968, Biochemistry, 7, 4226, 10.1021/bi00852a013 · doi:10.1021/bi00852a013
- Pieroni, 1980, J. Am. Chem. Soc., 102, 5913, 10.1021/ja00538a039 · doi:10.1021/ja00538a039
- Pieroni, 1992, J. Photochem. Photobiol. B, 12, 125, 10.1016/1011-1344(92)85002-C · doi:10.1016/1011-1344(92)85002-c
- Pieroni, 1988, Makromol. Chem., Rapid Commun., 9, 637, 10.1002/marc.1988.030090907 · doi:10.1002/marc.1988.030090907
- Ciardelli, 1989, J. Am. Chem. Soc., 111, 3470, 10.1021/ja00191a076 · doi:10.1021/ja00191a076
- Pieroni, 1992, J. Am. Chem. Soc., 114, 2734, 10.1021/ja00033a067 · doi:10.1021/ja00033a067
- Fissi, 1996, Macromolecules, 29, 4680, 10.1021/ma960280w · doi:10.1021/ma960280w
- Fissi, 1995, Macromolecules, 28, 302, 10.1021/ma00105a042 · doi:10.1021/ma00105a042
- Ueno, 1981, Chem. Lett., 10, 113, 10.1246/cl.1981.113 · doi:10.1246/cl.1981.113
- Ueno, 1981, J. Am. Chem. Soc., 103, 6410, 10.1021/ja00411a025 · doi:10.1021/ja00411a025
- Ulysse, 2006, Chem. Biol. Drug Des., 67, 127, 10.1111/j.1747-0285.2005.00337.x · doi:10.1111/j.1747-0285.2005.00337.x
- Behrendt, 1999, J. Pept. Sci., 5, 519, 10.1002/(SICI)1099-1387(199911)5:11<519::AID-PSC223>3.0.CO;2-3 · doi:10.1002/(sici)1099-1387(199911)5:11<519::aid-psc223>3.0.co;2-3
- Renner, 2000, Biopolymers, 54, 501, 10.1002/1097-0282(200012)54:7<501::AID-BIP30>3.0.CO;2-8 · doi:10.1002/1097-0282(200012)54:7<501::aid-bip30>3.0.co;2-8
- Renner, 2002, Biopolymers, 63, 382, 10.1002/bip.10127 · doi:10.1002/bip.10127
- Cattani-Scholz, 2002, Angew. Chem., Int. Ed., 41, 289, 10.1002/1521-3773(20020118)41:2<289::AID-ANIE289>3.0.CO;2-2 · doi:10.1002/1521-3773(20020118)41:2<289::aid-anie289>3.0.co;2-2
- Wilkinson, 2004, Biochim. Biophys. Acta: Proteins Proteomics, 1699, 35, 10.1016/S1570-9639(04)00063-9 · doi:10.1016/s1570-9639(04)00063-9
- Loweneck, 2006, Biophys. J., 90, 2099, 10.1529/biophysj.105.067363 · doi:10.1529/biophysj.105.067363
- Satzger, 2004, Chem. Phys. Lett., 396, 191, 10.1016/j.cplett.2004.08.024 · doi:10.1016/j.cplett.2004.08.024
- Bredenbeck, 2003, Proc. Natl. Acad. Sci. U. S. A., 100, 10580, 10.1073/pnas.1036583100 · doi:10.1073/pnas.1036583100
- Bredenbeck, 2003, Proc. Natl. Acad. Sci. U. S. A., 100, 6452, 10.1073/pnas.1036583100 · doi:10.1073/pnas.1036583100
- Koller, 2007, J. Phys. Chem. B, 111, 10481, 10.1021/jp072117g · doi:10.1021/jp072117g
- Denschlag, 2010, Phys. Chem. Chem. Phys., 12, 6204, 10.1039/b921803c · doi:10.1039/b921803c
- Pfister, 2008, Org. Biomol. Chem., 6, 3508, 10.1039/b804568b · doi:10.1039/b804568b
- Milbradt, 2005, Biopolymers, 77, 304, 10.1002/bip.20226 · doi:10.1002/bip.20226
- Hoppmann, 2009, Angew. Chem., Int. Ed., 48, 6636, 10.1002/anie.200901933 · doi:10.1002/anie.200901933
- Krautler, 2005, J. Am. Chem. Soc., 127, 4935, 10.1021/ja044253u · doi:10.1021/ja044253u
- Jurt, 2006, Angew. Chem., Int. Ed., 45, 6297, 10.1002/anie.200602084 · doi:10.1002/anie.200602084
- Dong, 2006, Chem.─Eur. J., 12, 1114
- Erdelyi, 2008, Org. Biomol. Chem., 6, 4356, 10.1039/b812001c · doi:10.1039/b812001c
- Erdelyi, 2006, Chem.─Eur. J, 12, 403
- Lindgren, 2009, Chem.─Eur. J., 15, 501
- Caamaño, 2000, Angew. Chem., Int. Ed., 39, 3104, 10.1002/1521-3773(20000901)39:17<3104::AID-ANIE3104>3.0.CO;2-0 · doi:10.1002/1521-3773(20000901)39:17<3104::aid-anie3104>3.0.co;2-0
- Harada, 1991, FEBS Lett., 286, 6, 10.1016/0014-5793(91)80928-V · doi:10.1016/0014-5793(91)80928-v
- Hayashi, 2007, Nucleic Acids Symp. Ser., 51, 93, 10.1093/nass/nrm047 · doi:10.1093/nass/nrm047
- Hayashi, 2009, Chem.─Eur. J., 15, 424
- Sinicropi, 2009, Photochem. Photobiol. Sci., 8, 1639, 10.1039/b906271h · doi:10.1039/b906271h
- Cordes, 2009, Chem. Phys., 358, 103, 10.1016/j.chemphys.2008.12.027 · doi:10.1016/j.chemphys.2008.12.027
- Chen, 2003, J. Am. Chem. Soc., 125, 12443, 10.1021/ja030277+ · doi:10.1021/ja030277+
- Backus, 2010, J. Phys. Chem. B, 114, 3735, 10.1021/jp911849n · doi:10.1021/jp911849n
- Zhang, 2008, ChemBioChem, 9, 2147, 10.1002/cbic.200800196 · doi:10.1002/cbic.200800196
- Pozhidaeva, 2004, Bioconjugate Chem, 15, 1297, 10.1021/bc049855h · doi:10.1021/bc049855h
- Kusebauch, 2007, Chem.─Eur. J., 13, 2966
- Rivado-Casas, 2009, J. Org. Chem., 74, 4666, 10.1021/jo802792j · doi:10.1021/jo802792j
- Varfolomeyev, 1996, BioSystems, 39, 35, 10.1016/0303-2647(95)01576-0 · doi:10.1016/0303-2647(95)01576-0
- Willner, 1993, React. Polym., 21, 177, 10.1016/0923-1137(93)90120-5 · doi:10.1016/0923-1137(93)90120-5
- Bieth, 1969, Proc. Natl. Acad. Sci. U. S. A., 64, 1103, 10.1073/pnas.64.3.1103 · doi:10.1073/pnas.64.3.1103
- Wilson, 1962, J. Biol. Chem., 237, 1323, 10.1016/S0021-9258(18)60328-X · doi:10.1016/s0021-9258(18)60328-x
- Bieth, 1970, Proc. Natl. Acad. Sci. U. S. A., 66, 850, 10.1073/pnas.66.3.850 · doi:10.1073/pnas.66.3.850
- Deal, 1969, Proc. Natl. Acad. Sci. U. S. A., 64, 1230, 10.1073/pnas.64.4.1230 · doi:10.1073/pnas.64.4.1230
- Hohsaka, 1994, J. Am. Chem. Soc., 116, 413, 10.1021/ja00080a064 · doi:10.1021/ja00080a064
- Westmark, 1993, J. Am. Chem. Soc., 115, 3416, 10.1021/ja00062a003 · doi:10.1021/ja00062a003
- Harvey, 2000, Tetrahedron, 56, 9763, 10.1016/S0040-4020(00)00883-8 · doi:10.1016/s0040-4020(00)00883-8
- Pearson, 2006, Org. Biomol. Chem., 4, 3618, 10.1039/B609320P · doi:10.1039/b609320p
- Pearson, 2008, Chem.─Eur. J., 14, 7358
- Abell, 2007, J. Med. Chem., 50, 2916, 10.1021/jm061455n · doi:10.1021/jm061455n
- Pearson, 2010, Chem.─Eur. J., 16, 6983
- Pearson, 2007, J. Am. Chem. Soc., 129, 14862, 10.1021/ja0766674 · doi:10.1021/ja0766674
- Robertson, 2005, Invest. Ophthalmol. Vis. Sci., 46, 4634, 10.1167/iovs.04-1291 · doi:10.1167/iovs.04-1291
- Fujita, 2006, Biochemistry, 45, 6581, 10.1021/bi060544z · doi:10.1021/bi060544z
- Vomasta, 2008, Angew. Chem., Int. Ed., 47, 7644, 10.1002/anie.200802242 · doi:10.1002/anie.200802242
- Vomasta, 2009, Bioorg. Med. Chem. Lett., 19, 1283, 10.1016/j.bmcl.2009.01.079 · doi:10.1016/j.bmcl.2009.01.079
- Banerjee, 2005, Biochemistry, 44, 3211, 10.1021/bi047737b · doi:10.1021/bi047737b
- Kuil, 2008, Bioorg. Med. Chem., 16, 1393, 10.1016/j.bmc.2007.10.049 · doi:10.1016/j.bmc.2007.10.049
- Kuil, 2009, J. Pept. Sci., 15, 685, 10.1002/psc.1173 · doi:10.1002/psc.1173
- Karube, 1976, Biochim. Biophys. Acta, 445, 774, 10.1016/0005-2744(76)90127-3 · doi:10.1016/0005-2744(76)90127-3
- Nakamoto, 1975, J. Ferment. Technol., 53, 595
- Willner, 1991, J. Am. Chem. Soc., 113, 4013, 10.1021/ja00010a065 · doi:10.1021/ja00010a065
- Willner, 1993, J. Am. Chem. Soc., 115, 8690, 10.1021/ja00072a023 · doi:10.1021/ja00072a023
- Wang, 2007, Biochemistry, 46, 14557, 10.1021/bi701073d · doi:10.1021/bi701073d
- Wang, 2006, J. Phys. Chem. B, 110, 16117, 10.1021/jp060981n · doi:10.1021/jp060981n
- Erlanger, 1976, Eur. J. Biochem., 61, 287, 10.1111/j.1432-1033.1976.tb10021.x · doi:10.1111/j.1432-1033.1976.tb10021.x
- Karube, 1976, Biochim. Biophys. Acta, 429, 975, 10.1016/0005-2744(76)90342-9 · doi:10.1016/0005-2744(76)90342-9
- Aizawa, 1977, Arch. Biochem. Biophys., 182, 305, 10.1016/0003-9861(77)90311-3 · doi:10.1016/0003-9861(77)90311-3
- Willner, 1991, J. Am. Chem. Soc., 113, 3321, 10.1021/ja00009a016 · doi:10.1021/ja00009a016
- Willner, 1994, Photochem. Photobiol., 59, 491, 10.1111/j.1751-1097.1994.tb05070.x · doi:10.1111/j.1751-1097.1994.tb05070.x
- Willner, 1995, J. Am. Chem. Soc., 117, 6581, 10.1021/ja00129a023 · doi:10.1021/ja00129a023
- Harvey, 2008, ChemBioChem, 9, 191, 10.1002/cbic.200700570 · doi:10.1002/cbic.200700570
- Ueda, 1994, J. Chem. Soc., Perkin Trans. 1, 225, 10.1039/p19940000225 · doi:10.1039/p19940000225
- van Dam-Mieras, 1975, Biochemistry, 14, 5387, 10.1021/bi00696a001 · doi:10.1021/bi00696a001
- Imperiali, 1994, J. Am. Chem. Soc., 116, 12083, 10.1021/ja00105a071 · doi:10.1021/ja00105a071
- Chatani, 2002, Protein Sci., 11, 72
- Hamachi, 1998, Chem. Lett., 27, 537, 10.1246/cl.1998.537 · doi:10.1246/cl.1998.537
- James, 2001, Protein Eng., 14, 983, 10.1093/protein/14.12.983 · doi:10.1093/protein/14.12.983
- Schierling, 2010, Proc. Natl. Acad. Sci. U. S. A., 107, 1361, 10.1073/pnas.0909444107 · doi:10.1073/pnas.0909444107
- Hien, 2011, Bioconjugate Chem., 22, 1366, 10.1021/bc200063m · doi:10.1021/bc200063m
- Krauss, 2010, Microb. Biotechnol., 3, 15, 10.1111/j.1751-7915.2009.00140.x · doi:10.1111/j.1751-7915.2009.00140.x
- Krauss, 2011, Chem.─Eur. J., 17, 2552
- Morgan, 2010, Photochem. Photobiol. Sci., 9, 1320, 10.1039/c0pp00214c · doi:10.1039/c0pp00214c
- Willner, 1992, J. Am. Chem. Soc., 114, 3150, 10.1021/ja00034a078 · doi:10.1021/ja00034a078
- Willner, 1993, J. Am. Chem. Soc., 115, 4937, 10.1021/ja00064a084 · doi:10.1021/ja00064a084
- Zahavy, 1993, J. Chem. Soc., Chem. Commun., 23, 1753, 10.1039/c39930001753 · doi:10.1039/c39930001753
- Zahavy, 1994, Mol. Cryst. Liq. Cryst. Sci. Technol., Sect A: Mol. Cryst. Liq. Cryst., 246, 195, 10.1080/10587259408037813 · doi:10.1080/10587259408037813
- Shimoboji, 2002, Bioconjugate Chem., 13, 915, 10.1021/bc010057q · doi:10.1021/bc010057q
- Gorostiza, 2008, Physiology, 23, 238, 10.1152/physiol.00018.2008 · doi:10.1152/physiol.00018.2008
- Volgraf, 2011, Molecular Switches
- Karczmar, 1993, Neuropsychopharmacology, 9, 181, 10.1038/npp.1993.81 · doi:10.1038/npp.1993.81
- Schoffeniels, 1957, Biochim. Biophys. Acta, 26, 1, 10.1016/0006-3002(57)90047-1 · doi:10.1016/0006-3002(57)90047-1
- Higman, 1964, Biochim. Biophys. Acta, 79, 138
- Lester, 1980, J. Gen. Physiol., 75, 207, 10.1085/jgp.75.2.207 · doi:10.1085/jgp.75.2.207
- Lester, 1980, Ann. N. Y. Acad. Sci., 346, 475, 10.1111/j.1749-6632.1980.tb22118.x · doi:10.1111/j.1749-6632.1980.tb22118.x
- Chabala, 1986, J. Physiol.-London, 379, 83, 10.1113/jphysiol.1986.sp016242 · doi:10.1113/jphysiol.1986.sp016242
- Lester, 1977, Nature, 266, 373, 10.1038/266373a0 · doi:10.1038/266373a0
- Wassermann, 1979, Proc. Natl. Acad. Sci. U. S. A., 76, 256, 10.1073/pnas.76.1.256 · doi:10.1073/pnas.76.1.256
- Nargeot, 1982, J. Gen. Physiol., 79, 657, 10.1085/jgp.79.4.657 · doi:10.1085/jgp.79.4.657
- Stankovic, 1991, Biochim. Biophys. Acta, 1061, 163, 10.1016/0005-2736(91)90281-C · doi:10.1016/0005-2736(91)90281-c
- Koeppe, 1996, Annu. Rev. Biophys. Biomol. Struct., 25, 231, 10.1146/annurev.bb.25.060196.001311 · doi:10.1146/annurev.bb.25.060196.001311
- Andersen, 1984, Annu. Rev. Physiol., 46, 531, 10.1146/annurev.ph.46.030184.002531 · doi:10.1146/annurev.ph.46.030184.002531
- Lien, 1996, J. Am. Chem. Soc., 118, 12222, 10.1021/ja962217s · doi:10.1021/ja962217s
- Ketchem, 1996, J. Biomol. NMR, 8, 1, 10.1007/BF00198135 · doi:10.1007/bf00198135
- Woolley, 1995, J. Am. Chem. Soc., 117, 4448, 10.1021/ja00121a002 · doi:10.1021/ja00121a002
- Blount, 2007, Curr. Top. Membr., 58, 201, 10.1016/S1063-5823(06)58008-1 · doi:10.1016/s1063-5823(06)58008-1
- Yoshimura, 2001, Biophys. J., 80, 2198, 10.1016/S0006-3495(01)76192-9 · doi:10.1016/s0006-3495(01)76192-9
- Kocer, 2005, Science, 309, 755, 10.1126/science.1114760 · doi:10.1126/science.1114760
- Steinbacher, 2007, Curr. Top. Membr., 58, 1
- Kocer, 2007, Nat. Protoc., 2, 1426, 10.1038/nprot.2007.196 · doi:10.1038/nprot.2007.196
- Mourot, 2011, ACS Chem. Neurosci., 2, 536, 10.1021/cn200037p · doi:10.1021/cn200037p
- Cahová, 2013, Angew. Chem., Int. Ed., 52, 3186, 10.1002/anie.201209943 · doi:10.1002/anie.201209943
- Fujimoto, 2012, Chem.─Eur. J., 18, 9834
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Metadata
- Authors
- Szymański, W., Beierle, J. M., Kistemaker, H. A. V., Velema, W. A., & Feringa, B. L.
- Venue
- Chemical Reviews
- Publisher
- American Chemical Society (ACS)
- Published
- 2013-04-25
- Volume
- 113
- Issue
- 8
- Pages
- 6114-6178
- ISSN
- 0009-2665 (ISSN-L)
- 1520-6890
- OpenAlex
- W2326558292
- Cited by
- 1,239
- References
- 203
- FWCI
- 2.74
- Type
- journal article
- Language
- en
- Open access
- hybrid
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