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Protein Splicing Triggered by a Small Molecule

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Laboratory of Synthetic Protein Chemistry, The Rockefeller University, 1230 York Avenue, New York, New York 10021
Cite this: J. Am. Chem. Soc. 2002, 124, 31, 9044-9045
Publication Date (Web):July 11, 2002
https://doi.org/10.1021/ja026769o
Copyright © 2002 American Chemical Society
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The use of small molecules that turn specific proteins on or off provides a level of temporal control that is difficult to achieve using standard genetic approaches. Consequently, the development of small-molecule switches of protein function is a very active area of chemical biology, sometimes referred to as chemical genetics. Most studies in this area rely on the identification of small molecules that bind directly to the active site of a target protein, thereby acting as agonists or antagonists of function. Strategies have also been described in which the small molecule triggers a change in the secondary, tertiary, or ternary structure of the protein, in so doing changing the functional state of the molecule. Another approach to this problem would be to alter the primary structure of a target protein in response to a small-molecule trigger; a dramatic change in primary sequence would be directly coupled to function. In principle, this can be achieved by harnessing protein splicing, a posttranslational editing process that results in the precise removal of an internal domain (termed an intein) from two flanking sequences termed the N- and C-exteins. In this communication we introduce a technique that allows protein splicing to occur only in the presence of the small molecule, rapamycin. This approach is expected to be independent of the nature of the two exteins and so should provide a general vehicle for controlling protein function using small molecules.

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  1. Robert E. Thompson, Tom W. Muir. Chemoenzymatic Semisynthesis of Proteins. Chemical Reviews 2019, Article ASAP.
  2. Josef A. Gramespacher, Antony J. Burton, Luis F. Guerra, Tom W. Muir. Proximity Induced Splicing Utilizing Caged Split Inteins. Journal of the American Chemical Society 2019, 141 (35) , 13708-13712. DOI: 10.1021/jacs.9b05721.
  3. Josef A. Gramespacher, Adam J. Stevens, Duy P. Nguyen, Jason W. Chin, and Tom W. Muir . Intein Zymogens: Conditional Assembly and Splicing of Split Inteins via Targeted Proteolysis. Journal of the American Chemical Society 2017, 139 (24) , 8074-8077. DOI: 10.1021/jacs.7b02618.
  4. Julie N. Reitter, Christopher E. Cousin, Michael C. Nicastri, Mario V. Jaramillo, and Kenneth V. Mills . Salt-Dependent Conditional Protein Splicing of an Intein from Halobacterium salinarum. Biochemistry 2016, 55 (9) , 1279-1282. DOI: 10.1021/acs.biochem.6b00128.
  5. Michael C. Nicastri, Kristina Xega, Lingyun Li, Jian Xie, Chunyu Wang, Robert J. Linhardt, Julie N. Reitter, and Kenneth V. Mills . Internal Disulfide Bond Acts as a Switch for Intein Activity. Biochemistry 2013, 52 (34) , 5920-5927. DOI: 10.1021/bi400736c.
  6. Adrian Fegan, Brian White, Jonathan C. T. Carlson and Carston R. Wagner . Chemically Controlled Protein Assembly: Techniques and Applications. Chemical Reviews 2010, 110 (6) , 3315-3336. DOI: 10.1021/cr8002888.
  7. Seiji Sakamoto and Kazuaki Kudo. Supramolecular Control of Split-GFP Reassembly by Conjugation of β-Cyclodextrin and Coumarin Units. Journal of the American Chemical Society 2008, 130 (29) , 9574-9582. DOI: 10.1021/ja802313a.
  8. Courtney M. Yuen,, Stephen J. Rodda,, Steven A. Vokes,, Andrew P. McMahon, and, David R. Liu. Control of Transcription Factor Activity and Osteoblast Differentiation in Mammalian Cells Using an Evolved Small-Molecule-Dependent Intein. Journal of the American Chemical Society 2006, 128 (27) , 8939-8946. DOI: 10.1021/ja062980e.
  9. Daniel P. Walsh and, Young-Tae Chang. Chemical Genetics. Chemical Reviews 2006, 106 (6) , 2476-2530. DOI: 10.1021/cr0404141.
  10. Steffen Brenzel,, Thomas Kurpiers, and, Henning D. Mootz. Engineering Artificially Split Inteins for Applications in Protein Chemistry:  Biochemical Characterization of the Split Ssp DnaB Intein and Comparison to the Split Sce VMA Intein. Biochemistry 2006, 45 (6) , 1571-1578. DOI: 10.1021/bi051697+.
  11. Jianxin Shi and, Tom W. Muir. Development of a Tandem Protein Trans-Splicing System Based on Native and Engineered Split Inteins. Journal of the American Chemical Society 2005, 127 (17) , 6198-6206. DOI: 10.1021/ja042287w.
  12. Steffen Brenzel and, Henning D. Mootz. Design of an Intein that Can Be Inhibited with a Small Molecule Ligand. Journal of the American Chemical Society 2005, 127 (12) , 4176-4177. DOI: 10.1021/ja043501j.
  13. Smita S. Muddana and, Blake R. Peterson. Facile Synthesis of CIDs:  Biotinylated Estrone Oximes Efficiently Heterodimerize Estrogen Receptor and Streptavidin Proteins in Yeast Three Hybrid Systems. Organic Letters 2004, 6 (9) , 1409-1412. DOI: 10.1021/ol0497537.
  14. Henning D. Mootz,, Elyse S. Blum,, Amy B. Tyszkiewicz, and, Tom W. Muir. Conditional Protein Splicing:  A New Tool to Control Protein Structure and Function in Vitro and in Vivo. Journal of the American Chemical Society 2003, 125 (35) , 10561-10569. DOI: 10.1021/ja0362813.
  15. Nicole Magnasco Nichols,, Jack S. Benner,, Deana D. Martin, and, Thomas C. Evans, Jr.. Zinc Ion Effects on Individual Ssp DnaE Intein Splicing Steps:  Regulating Pathway Progression. Biochemistry 2003, 42 (18) , 5301-5311. DOI: 10.1021/bi020679e.
  16. Thomas C. Evans, Jr. and, Ming-Qun Xu. Mechanistic and Kinetic Considerations of Protein Splicing. Chemical Reviews 2002, 102 (12) , 4869-4884. DOI: 10.1021/cr9601369.
  17. Alain Mazé, Yaakov Benenson. Artificial signaling in mammalian cells enabled by prokaryotic two-component system. Nature Chemical Biology 2020, 16 (2) , 179-187. DOI: 10.1038/s41589-019-0429-9.
  18. Maniraj Bhagawati, Tobias M. E. Terhorst, Friederike Füsser, Simon Hoffmann, Tim Pasch, Shmuel Pietrokovski, Henning D. Mootz. A mesophilic cysteine-less split intein for protein trans -splicing applications under oxidizing conditions. Proceedings of the National Academy of Sciences 2019, 116 (44) , 22164-22172. DOI: 10.1073/pnas.1909825116.
  19. Barbara Di Ventura, Henning D. Mootz. Switchable inteins for conditional protein splicing. Biological Chemistry 2019, 400 (4) , 467-475. DOI: 10.1515/hsz-2018-0309.
  20. Ashwin Lahiry, Yamin Fan, Samuel D Stimple, Mitch Raith, David W Wood. Inteins as tools for tagless and traceless protein purification. Journal of Chemical Technology & Biotechnology 2018, 93 (7) , 1827-1835. DOI: 10.1002/jctb.5415.
  21. Skander Elleuche, Stefanie Pöggeler. Fungal Inteins: Distribution, Evolution, and Applications. 2018,,, 57-85. DOI: 10.1007/978-3-319-71740-1_2.
  22. Hideo Iwaï, A. Sesilja Aranko. Protein Ligation by HINT Domains. 2017,,, 421-445. DOI: 10.1002/9781119044116.ch12.
  23. Scott A. Walper, Kendrick B. Turner, Igor L. Medintz. Bioorthogonal Labeling of Cellular Proteins by Enzymatic and Related Mechanisms. 2017,,, 165-230. DOI: 10.1002/9783527683451.ch7.
  24. Spencer C. Alford, Connor O’Sullivan, Perry L. Howard. Conditional Toxin Splicing Using a Split Intein System. 2017,,, 197-216. DOI: 10.1007/978-1-4939-6451-2_13.
  25. Annika Ciragan, A. Sesilja Aranko, Igor Tascon, Hideo Iwaï. Salt-inducible Protein Splicing in cis and trans by Inteins from Extremely Halophilic Archaea as a Novel Protein-Engineering Tool. Journal of Molecular Biology 2016, 428 (23) , 4573-4588. DOI: 10.1016/j.jmb.2016.10.006.
  26. I. Cody MacDonald, Tara L. Deans. Tools and applications in synthetic biology. Advanced Drug Delivery Reviews 2016, 105, 20-34. DOI: 10.1016/j.addr.2016.08.008.
  27. Skander Elleuche, Stefanie Pöggeler. Inteins and Their Use in Protein Synthesis with Fungi. 2016,,, 289-307. DOI: 10.1007/978-3-319-27951-0_13.
  28. D. C. Jones, I. N. Mistry, A. Tavassoli. Post-translational control of protein function with light using a LOV-intein fusion protein. Molecular BioSystems 2016, 12 (4) , 1388-1393. DOI: 10.1039/C6MB00007J.
  29. Yifeng Li. Split-inteins and their bioapplications. Biotechnology Letters 2015, 37 (11) , 2121-2137. DOI: 10.1007/s10529-015-1905-2.
  30. Shimyn Slomovic, James J Collins. DNA sense-and-respond protein modules for mammalian cells. Nature Methods 2015, 12 (11) , 1085-1090. DOI: 10.1038/nmeth.3585.
  31. Stephanie Voß, Laura Klewer, Yao-Wen Wu. Chemically induced dimerization: reversible and spatiotemporal control of protein function in cells. Current Opinion in Chemical Biology 2015, 28, 194-201. DOI: 10.1016/j.cbpa.2015.09.003.
  32. Jonathan C Y Tang, Stephanie Rudolph, Onkar S Dhande, Victoria E Abraira, Seungwon Choi, Sylvain W Lapan, Iain R Drew, Eugene Drokhlyansky, Andrew D Huberman, Wade G Regehr, Constance L Cepko. Cell type–specific manipulation with GFP-dependent Cre recombinase. Nature Neuroscience 2015, 18 (9) , 1334-1341. DOI: 10.1038/nn.4081.
  33. Dong-Jiunn Jeffery Truong, Karin Kühner, Ralf Kühn, Stanislas Werfel, Stefan Engelhardt, Wolfgang Wurst, Oskar Ortiz. Development of an intein-mediated split–Cas9 system for gene therapy. Nucleic Acids Research 2015, 43 (13) , 6450-6458. DOI: 10.1093/nar/gkv601.
  34. Zoltán Kis, Hugo Sant'Ana Pereira, Takayuki Homma, Ryan M. Pedrigi, Rob Krams. Mammalian synthetic biology: emerging medical applications. Journal of The Royal Society Interface 2015, 12 (106) , 20141000. DOI: 10.1098/rsif.2014.1000.
  35. Jana K. Böcker, Kristina Friedel, Julian C. J. Matern, Anne-Lena Bachmann, Henning D. Mootz. Generation of a Genetically Encoded, Photoactivatable Intein for the Controlled Production of Cyclic Peptides. Angewandte Chemie 2015, 127 (7) , 2144-2148. DOI: 10.1002/ange.201409848.
  36. Jana K. Böcker, Kristina Friedel, Julian C. J. Matern, Anne-Lena Bachmann, Henning D. Mootz. Generation of a Genetically Encoded, Photoactivatable Intein for the Controlled Production of Cyclic Peptides. Angewandte Chemie International Edition 2015, 54 (7) , 2116-2120. DOI: 10.1002/anie.201409848.
  37. Max C. Waldhauer, Silvan N. Schmitz, Constantin Ahlmann-Eltze, Jan G. Gleixner, Carolin C. Schmelas, Anna G. Huhn, Charlotte Bunne, Magdalena Büscher, Max Horn, Nils Klughammer, Jakob Kreft, Elisabeth Schäfer, Philipp A. Bayer, Stephen G. Krämer, Julia Neugebauer, Pierre Wehler, Matthias P. Mayer, Roland Eils, Barbara Di Ventura. Backbone circularization of Bacillus subtilis family 11 xylanase increases its thermostability and its resistance against aggregation. Molecular BioSystems 2015, 11 (12) , 3231-3243. DOI: 10.1039/C5MB00341E.
  38. Rishi Rakhit, Raul Navarro, Thomas J. Wandless. Chemical Biology Strategies for Posttranslational Control of Protein Function. Chemistry & Biology 2014, 21 (9) , 1238-1252. DOI: 10.1016/j.chembiol.2014.08.011.
  39. Olga Novikova, Natalya Topilina, Marlene Belfort. Enigmatic Distribution, Evolution, and Function of Inteins. Journal of Biological Chemistry 2014, 289 (21) , 14490-14497. DOI: 10.1074/jbc.R114.548255.
  40. Xiongfeng Dai, Manlu Zhu, Yi-Ping Wang. Circular permutation of E. coli EPSP synthase: increased inhibitor resistance, improved catalytic activity, and an indicator for protein fragment complementation. Chem. Commun. 2014, 50 (15) , 1830-1832. DOI: 10.1039/C3CC48722A.
  41. Neel H. Shah, Tom W. Muir. Inteins: nature's gift to protein chemists. Chem. Sci. 2014, 5 (2) , 446-461. DOI: 10.1039/C3SC52951G.
  42. Spencer C. Alford, Connor O'Sullivan, Jon Obst, Jennifer Christie, Perry L. Howard. Conditional protein splicing of α-sarcin in live cells. Molecular BioSystems 2014, 10 (4) , 831. DOI: 10.1039/c3mb70387h.
  43. Natalya I Topilina, Kenneth V Mills. Recent advances in in vivo applications of intein-mediated protein splicing. Mobile DNA 2014, 5 (1) , 5. DOI: 10.1186/1759-8753-5-5.
  44. James A. J. Arpino, Edward J. Hancock, James Anderson, Mauricio Barahona, Guy-Bart V. Stan, Antonis Papachristodoulou, Karen Polizzi. Tuning the dials of Synthetic Biology. Microbiology 2013, 159 (Pt_7) , 1236-1253. DOI: 10.1099/mic.0.067975-0.
  45. Gerrit Volkmann, Henning D. Mootz. Recent progress in intein research: from mechanism to directed evolution and applications. Cellular and Molecular Life Sciences 2013, 70 (7) , 1185-1206. DOI: 10.1007/s00018-012-1120-4.
  46. Kenneth V. Mills. Self-Splicing Proteins. 2013,,, 315-321. DOI: 10.1016/B978-0-12-382219-2.00076-4.
  47. William Bacchus, Martin Fussenegger. The use of light for engineered control and reprogramming of cellular functions. Current Opinion in Biotechnology 2012, 23 (5) , 695-702. DOI: 10.1016/j.copbio.2011.12.004.
  48. Xudong Huang, Rammohan Narayanaswamy, Kathleen Fenn, Sebastian Szpakowski, Clarence Sasaki, Jose Costa, Pilar Blancafort, Paul M. Lizardi. Sequence-Specific Biosensors Report Drug-Induced Changes in Epigenetic Silencing in Living Cells. DNA and Cell Biology 2012, 31 (S1) , S-2-S-10. DOI: 10.1089/dna.2011.1537.
  49. Mateusz Putyrski, Carsten Schultz. Protein translocation as a tool: The current rapamycin story. FEBS Letters 2012, 586 (15) , 2097-2105. DOI: 10.1016/j.febslet.2012.04.061.
  50. Brian R. White, Jonathan C. T. Carlson, Jessie L. Kerns, Carston R. Wagner. Protein interface remodeling in a chemically induced protein dimer. Journal of Molecular Recognition 2012, 25 (7) , 393-403. DOI: 10.1002/jmr.2196.
  51. James Apgar, Mary Ross, Xiao Zuo, Sarah Dohle, Derek Sturtevant, Binzhang Shen, Humberto de la Vega, Philip Lessard, Gabor Lazar, R. Michael Raab, . A Predictive Model of Intein Insertion Site for Use in the Engineering of Molecular Switches. PLoS ONE 2012, 7 (5) , e37355. DOI: 10.1371/journal.pone.0037355.
  52. Fu-Sen Liang, Gerald R. Crabtree. Small Molecule-Induced Proximity. 2012,,, 115-126. DOI: 10.1007/978-4-431-54038-0_11.
  53. Philip T. Shemella, Natalya I. Topilina, Ikko Soga, Brian Pereira, Georges Belfort, Marlene Belfort, Saroj K. Nayak. Electronic Structure of Neighboring Extein Residue Modulates Intein C-Terminal Cleavage Activity. Biophysical Journal 2011, 100 (9) , 2217-2225. DOI: 10.1016/j.bpj.2011.02.037.
  54. Sun H. Peck, Irwin Chen, David R. Liu. Directed Evolution of a Small-Molecule-Triggered Intein with Improved Splicing Properties in Mammalian Cells. Chemistry & Biology 2011, 18 (5) , 619-630. DOI: 10.1016/j.chembiol.2011.02.014.
  55. Bokai Liu, Qi Wu, Deshui Lv, Xianfu Lin. Modulating the synthetase activity of penicillin G acylase in organic media by addition of N-methylimidazole: Using vinyl acetate as activated acyl donor. Journal of Biotechnology 2011, 153 (3-4) , 111-115. DOI: 10.1016/j.jbiotec.2011.03.009.
  56. Alison R. Gillies, David W. Wood. Inteins in Protein Engineering. 2011,,, 271-293. DOI: 10.1002/9783527634026.ch10.
  57. Tim Sonntag, Henning D. Mootz. An intein-cassette integration approach used for the generation of a split TEV protease activated by conditional protein splicing. Molecular BioSystems 2011, 7 (6) , 2031. DOI: 10.1039/c1mb05025g.
  58. Richard Ramsden, Luther Arms, Trisha N Davis, Eric GD Muller. An intein with genetically selectable markers provides a new approach to internally label proteins with GFP. BMC Biotechnology 2011, 11 (1) , 71. DOI: 10.1186/1472-6750-11-71.
  59. A. Sesilja Aranko, Gerrit Volkmann. Protein trans-splicing as a protein ligation tool to study protein structure and function. BioMolecular Concepts 2011, 2 (3) DOI: 10.1515/bmc.2011.014.
  60. Núria Sancho Oltra, Jeffrey Bos, Gerard Roelfes. Control over Enzymatic Activity by DNA-Directed Split Enzyme Reassembly. ChemBioChem 2010, 11 (16) , 2255-2258. DOI: 10.1002/cbic.201000517.
  61. Luis Berrade, Youngeun Kwon , Julio A. Camarero. Photomodulation of Protein Trans-Splicing Through Backbone Photocaging of the DnaE Split Intein. ChemBioChem 2010, 11 (10) , 1368-1372. DOI: 10.1002/cbic.201000157.
  62. Skander Elleuche, Stefanie Pöggeler. Inteins, valuable genetic elements in molecular biology and biotechnology. Applied Microbiology and Biotechnology 2010, 87 (2) , 479-489. DOI: 10.1007/s00253-010-2628-x.
  63. Xiaohu Ouyang, James K. Chen. Synthetic Strategies for Studying Embryonic Development. Chemistry & Biology 2010, 17 (6) , 590-606. DOI: 10.1016/j.chembiol.2010.04.013.
  64. Philip T. Shemella, Saroj K. Nayak. Identifying the Reaction Mechanisms of Inteins with QM/MM Multiscale Methods. 2010,,, 469-489. DOI: 10.1007/978-90-481-3575-2_16.
  65. M.K. Pastuszka, J.A. Mackay. Biomolecular engineering of intracellular switches in eukaryotes. Journal of Drug Delivery Science and Technology 2010, 20 (3) , 163-169. DOI: 10.1016/S1773-2247(10)50025-X.
  66. Henning D. Mootz. Split Inteins as Versatile Tools for Protein Semisynthesis. ChemBioChem 2009, 10 (16) , 2579-2589. DOI: 10.1002/cbic.200900370.
  67. Skander Elleuche, Stefanie Pöggeler. Inteins – Selfish Elements in Fungal Genomes. 2009,,, 41-61. DOI: 10.1007/978-3-642-00286-1_3.
  68. Toshihisa Mizuno, Kumiko Suzuki, Tatsuya Imai, Yuya Kitade, Yuji Furutani, Motonori Kudou, Masayuki Oda, Hideki Kandori, Kouhei Tsumoto, Toshiki Tanaka. Manipulation of protein-complex function by using an engineered heterotrimeric coiled-coil switch. Organic & Biomolecular Chemistry 2009, 7 (15) , 3102. DOI: 10.1039/b901118h.
  69. Thomas Kurpiers, Henning D. Mootz. Site-Specific Chemical Modification of Proteins with a Prelabelled Cysteine Tag Using the Artificially Split Mxe GyrA Intein. ChemBioChem 2008, 9 (14) , 2317-2325. DOI: 10.1002/cbic.200800319.
  70. Judith Müller, Nils Johnsson. Split-Ubiquitin and the Split-Protein Sensors: Chessman for the Endgame. ChemBioChem 2008, , NA-NA. DOI: 10.1002/cbic.200800190.
  71. Christian F. W. Becker, Roger S. Goody. Synthetic Peptides and Proteins to Elucidate Biological Function. 2008,, DOI: 10.1002/9780470048672.wecb583.
  72. Amy B Tyszkiewicz, Tom W Muir. Activation of protein splicing with light in yeast. Nature Methods 2008, DOI: 10.1038/nmeth.1189.
  73. Tom W. Muir. Studying protein structure and function using semisynthesis. Biopolymers 2008, 90 (6) , 743-750. DOI: 10.1002/bip.21102.
  74. Mathieu Pucheault. Natural products: chemical instruments to apprehend biological symphony. Org. Biomol. Chem. 2008, 6 (3) , 424-432. DOI: 10.1039/B713022H.
  75. Mathieu Pucheault. . Organic & Biomolecular Chemistry 2008,,, 424. DOI: 10.1039/b713022h.
  76. Carsten Schultz. Molecular tools for cell and systems biology. HFSP Journal 2007, 1 (4) , 230-248. DOI: 10.2976/1.2812442.
  77. Kryn Stankunas, J. Henri Bayle, James J. Havranek, Thomas J. Wandless, David Baker, Gerald R. Crabtree, Jason E. Gestwicki. Rescue of Degradation-Prone Mutants of the FK506-Rapamycin Binding (FRB) Protein with Chemical Ligands. ChemBioChem 2007, 8 (10) , 1162-1169. DOI: 10.1002/cbic.200700087.
  78. Thomas Kurpiers, Henning D. Mootz. Regioselektive Cysteinbiokonjugation durch Anhängen eines modifizierten Cystein-tags an ein Protein mithilfe vontrans-Proteinspleißen. Angewandte Chemie 2007, 119 (27) , 5327-5330. DOI: 10.1002/ange.200700719.
  79. Thomas Kurpiers, Henning D. Mootz. Regioselective Cysteine Bioconjugation by Appending a Labeled Cystein Tag to a Protein by Using Protein Splicing intrans. Angewandte Chemie International Edition 2007, 46 (27) , 5234-5237. DOI: 10.1002/anie.200700719.
  80. Daniel Evanko. Controlling proteins the intein way. Nature Methods 2007, 4 (2) , 112-113. DOI: 10.1038/nmeth0207-112a.
  81. Daniel Rauh, Herbert Waldmann. Symbiose aus Chemie und Biologie zum Studium von Proteinfunktionen. Angewandte Chemie 2007, 119 (6) , 840-844. DOI: 10.1002/ange.200602979.
  82. Daniel Rauh, Herbert Waldmann. Linking Chemistry and Biology for the Study of Protein Function. Angewandte Chemie International Edition 2007, 46 (6) , 826-829. DOI: 10.1002/anie.200602979.
  83. Francine B Perler. Shining a light on protein expression in living organisms. Nature Chemical Biology 2007, 3 (1) , 17-18. DOI: 10.1038/nchembio0107-17.
  84. Edmund C Schwartz, Lino Saez, Michael W Young, Tom W Muir. Post-translational enzyme activation in an animal via optimized conditional protein splicing. Nature Chemical Biology 2007, 3 (1) , 50-54. DOI: 10.1038/nchembio832.
  85. Tomomi Ando, Shinya Tsukiji, Tsutomu Tanaka, Teruyuki Nagamune. Construction of a small-molecule-integrated semisynthetic split intein for in vivo protein ligation. Chemical Communications 2007, (47) , 4995. DOI: 10.1039/b712843f.
  86. Satoshi Yuzawa, Toshihisa Mizuno, Toshiki Tanaka. Activating an Enzyme by an Engineered Coiled Coil Switch. Chemistry - A European Journal 2006, 12 (28) , 7345-7352. DOI: 10.1002/chem.200600007.
  87. Christina Ludwig, Martina Pfeiff, Uwe Linne, Henning D. Mootz. Ligation eines synthetischen Peptids an den N-Terminus eines rekombinanten Proteins durch semisynthetischestrans-Proteinspleißen. Angewandte Chemie 2006, 118 (31) , 5343-5347. DOI: 10.1002/ange.200600570.
  88. Christina Ludwig, Martina Pfeiff, Uwe Linne, Henning D. Mootz. Ligation of a Synthetic Peptide to the N Terminus of a Recombinant Protein Using Semisynthetic Proteintrans-Splicing. Angewandte Chemie International Edition 2006, 45 (31) , 5218-5221. DOI: 10.1002/anie.200600570.
  89. Tom W. Muir. Chemical biology: Cutting out the middle man. Nature 2006, 442 (7102) , 517-518. DOI: 10.1038/442517a.
  90. Sumitaka Hasegawa, Gayatri Gowrishankar, Jianghong Rao. Detection of mRNA in Mammalian Cells with a Split Ribozyme Reporter. ChemBioChem 2006, 7 (6) , 925-928. DOI: 10.1002/cbic.200600061.
  91. Vasant Muralidharan, Tom W Muir. Protein ligation: an enabling technology for the biophysical analysis of proteins. Nature Methods 2006, 3 (6) , 429-438. DOI: 10.1038/nmeth886.
  92. Jeong Jin Choi, Ki Hoon Nam, Bokkee Min, Sang-Jin Kim, Dieter Söll, Suk-Tae Kwon. Protein Trans-splicing and Characterization of a Split Family B-type DNA Polymerase from the Hyperthermophilic Archaeal Parasite Nanoarchaeum equitans. Journal of Molecular Biology 2006, 356 (5) , 1093-1106. DOI: 10.1016/j.jmb.2005.12.036.
  93. Takeaki Ozawa. Designing split reporter proteins for analytical tools. Analytica Chimica Acta 2006, 556 (1) , 58-68. DOI: 10.1016/j.aca.2005.06.026.
  94. Thomas Durek, Christian F.W. Becker. Protein semi-synthesis: New proteins for functional and structural studies. Biomolecular Engineering 2005, 22 (5-6) , 153-172. DOI: 10.1016/j.bioeng.2005.07.004.
  95. Tom W. Muir. 2005 Irving Sigal Young Investigator Award. Protein Science 2005, 14 (12) , 3140-3144. DOI: 10.1110/ps.051848105.
  96. D. Dafydd Jones, Paul D. Barker. Controlling Self-Assembly by Linking Protein Folding, DNA Binding, and the Redox Chemistry of Heme. Angewandte Chemie 2005, 117 (39) , 6495-6499. DOI: 10.1002/ange.200463035.
  97. D. Dafydd Jones, Paul D. Barker. Controlling Self-Assembly by Linking Protein Folding, DNA Binding, and the Redox Chemistry of Heme. Angewandte Chemie International Edition 2005, 44 (39) , 6337-6341. DOI: 10.1002/anie.200463035.
  98. David E. Paschon, Zarana S. Patel, Marc Ostermeier. Enhanced Catalytic Efficiency of Aminoglycoside Phosphotransferase (3′)-IIa Achieved Through Protein Fragmentation and Reassembly. Journal of Molecular Biology 2005, 353 (1) , 26-37. DOI: 10.1016/j.jmb.2005.08.026.
  99. Ming-Qun Xu, Thomas C Evans. Recent advances in protein splicing: manipulating proteins in vitro and in vivo. Current Opinion in Biotechnology 2005, 16 (4) , 440-446. DOI: 10.1016/j.copbio.2005.06.012.
  100. Masato Oikawa, Minoru Ikoma, Makoto Sasaki. Simultaneous accumulation of both skeletal and appendage-based diversities on tandem Ugi/Diels–Alder products. Tetrahedron Letters 2005, 46 (35) , 5863-5866. DOI: 10.1016/j.tetlet.2005.06.147.
  101. Allison Doerr. Frankenstein's protein. Nature Methods 2005, 2 (6) , 408-408. DOI: 10.1038/nmeth0605-408.
  102. Thomas C. Evans, Ming-Qun Xu, Sriharsa Pradhan. PROTEIN SPLICING ELEMENTS AND PLANTS: From Transgene Containment to Protein Purification. Annual Review of Plant Biology 2005, 56 (1) , 375-392. DOI: 10.1146/annurev.arplant.56.032604.144242.
  103. Bradley L. Nilsson, Matthew B. Soellner, Ronald T. Raines. Chemical Synthesis of Proteins. Annual Review of Biophysics and Biomolecular Structure 2005, 34 (1) , 91-118. DOI: 10.1146/annurev.biophys.34.040204.144700.
  104. Allen R. Buskirk, David R. Liu. Creating Small-Molecule-Dependent Switches to Modulate Biological Functions. Chemistry & Biology 2005, 12 (2) , 151-161. DOI: 10.1016/j.chembiol.2004.11.012.
  105. Michael E. Hahn, Tom W. Muir. Manipulating proteins with chemistry: a cross-section of chemical biology. Trends in Biochemical Sciences 2005, 30 (1) , 26-34. DOI: 10.1016/j.tibs.2004.10.010.
  106. Gurkan Guntas, Sarah F. Mitchell, Marc Ostermeier. A Molecular Switch Created by In Vitro Recombination of Nonhomologous Genes. Chemistry & Biology 2004, 11 (11) , 1483-1487. DOI: 10.1016/j.chembiol.2004.08.020.
  107. A. R. Buskirk, Y.-C. Ong, Z. J. Gartner, D. R. Liu. Directed evolution of ligand dependence: Small-molecule-activated protein splicing. Proceedings of the National Academy of Sciences 2004, 101 (29) , 10505-10510. DOI: 10.1073/pnas.0402762101.
  108. Francine B Perler. The ins and outs of gene expression control. Nature Biotechnology 2004, 22 (7) , 824-826. DOI: 10.1038/nbt0704-824.
  109. Ralf David, Michael P.O. Richter, Annette G. Beck-Sickinger. . European Journal of Biochemistry 2004,,, 663. DOI: 10.1111/j.1432-1033.2004.03978.x.
  110. Sonalee Athavankar, Blake R Peterson. Control of Gene Expression with Small Molecules. Chemistry & Biology 2003, 10 (12) , 1245-1253. DOI: 10.1016/j.chembiol.2003.11.007.
  111. Tom W. Muir. SEMISYNTHESIS OF PROTEINS BY EXPRESSED PROTEIN LIGATION. Annual Review of Biochemistry 2003, 72 (1) , 249-289. DOI: 10.1146/annurev.biochem.72.121801.161900.
  112. Edmund C. Schwartz, Tom W. Muir, Amy B. Tyszkiewicz. “The splice is right”: how protein splicing is opening new doors in protein science. Chem. Commun. 2003, 265 (17) , 2087-2090. DOI: 10.1039/B304989M.
  113. Jonathan Caspi, Gil Amitai, Olga Belenkiy, Shmuel Pietrokovski. . Molecular Microbiology 2003,,, 1569. DOI: 10.1046/j.1365-2958.2003.03825.x.
  114. Takeaki Ozawa, Yoshio Umezawa. Inteins for Split-Protein Reconstitutions and Their Applications. ,,, 307-323. DOI: 10.1007/3-540-29474-0_18.
  115. Steffen Brenzel, Christina Ludwig, Henning D. Mootz. Switchable Inteins: New Tools to Control Protein Function by using Regulated Protein Splicing. ,,, 754-758. DOI: 10.1007/978-0-387-26575-9_332.

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