[1]
|
Kerppola, T.K. (2009) Visualization of Molecular Interactions Using Bimolecular Fluorescence Complementation Analysis: Characteristics of Protein Fragment Complementation. Chemical Society Reviews, 38, 2876-2886.
https://doi.org/10.1039/b909638h
|
[2]
|
Lalonde, S., Ehrhardt, D.W., Loque, D., Chen, J., Rhee, S.Y. and Frommer, W.B. (2008) Molecular and Cellular Approaches for the Detection of Protein-Protein Interactions: Latest Techniques and Current Limitations. The Plant Journal, 53, 610-635.
https://doi.org/10.1111/j.1365-313X.2007.03332.x
|
[3]
|
Shekhawat, S.S. and Ghosh, I. (2011) Split-Protein Systems: Beyond Binary Protein-Protein Interactions. Current Opinion in Chemical Biology, 15, 789-797.
https://doi.org/10.1016/j.cbpa.2011.10.014
|
[4]
|
Ventura, S. (2011) Bimolecular Fluorescence Complementation: Illuminating Cellular Protein Interactions. Current Molecular Medicine, 11, 582-598.
https://doi.org/10.2174/156652411800615117
|
[5]
|
Cabantous, S., Thomas, C.T. and Waldo, G.S. (2005) Protein Tagging and Detection with Engineered Self-Assembling Fragments of Green Fluorescent Protein. Nature Biotechnology, 23, 102-107. https://doi.org/10.1038/nbt1044
|
[6]
|
Johnsson, N. and Varshavsky, A. (1994) Split Ubiquitin as a Sensor of Protein Interactions in Vivo. Proceedings of the National Academy of Sciences of the United States of America, 91, 10340-10344. https://doi.org/10.1073/pnas.91.22.10340
|
[7]
|
Ghosh, I., Hamilton, A.D. and Regan, L. (2000) Antiparallel Leucine Zipper-Directed Protein Reassembly: Application to the Green Fluorescent Protein. Journal of the American Chemical Society, 122, 5658-5659. https://doi.org/10.1021/ja994421w
|
[8]
|
Hu, C.D. and Kerppola, T.K. (2003) Simultaneous Visualization of Multiple Protein Interactions in Living Cells Using Multicolor Fluorescence Complementation Analysis. Nature Biotechnology, 21, 539-545. https://doi.org/10.1038/nbt816
|
[9]
|
Pelletier, J.N., Campbell-Valois, F.X. and Michnick, S.W. (1998) Oligomerization Domain-Directed Reassembly of Active Dihydrofolate Reductase from Rationally Designed Fragments. Proceedings of the National Academy of Sciences of the United States of America, 95, 12141-12146. https://doi.org/10.1073/pnas.95.21.12141
|
[10]
|
Galarneau, A., Primeau, M., Trudeau, L.E. and Michnick, S.W. (2002) β-Lactamase Protein Fragment Complementation Assays as in Vivo and in Vitro Sensors of Protein-Protein Interactions. Nature Biotechnology, 20, 619-622.
https://doi.org/10.1038/nbt0602-619
|
[11]
|
Luker, K.E., Smith, M.C. P., Luker, G.D., Gammon, S.T., Piwnica-Worms, H. and Piwnica-Worms, D.P. (2004) Kinetics of Regulated Protein-Protein Interactions Revealed with Firefly Luciferase Complementation Imaging in Cells and Living Animals. Proceedings of the National Academy of Sciences of the United States of America, 101, 12288-12293. https://doi.org/10.1073/pnas.0404041101
|
[12]
|
Paulmurugan, R. and Gambhir, S.S. (2003) Monitoring Protein-Protein Interactions Using Split Synthetic Renilla Luciferase Protein-Fragment-Assisted Complementation. Analytical Chemistry, 75, 1584-1589. https://doi.org/10.1021/ac020731c
|
[13]
|
Remy, I. and Michnick, S.W. (2006) A Highly Sensitive Protein-Protein Interaction Assay Based on Gaussia Luciferase. Nature Methods, 3, 977-979.
https://doi.org/10.1038/nmeth979
|
[14]
|
Wehr, M.C., Laage, R., Bolz, U., Fischer, T.M., Grunewald, S., Scheek, S., Bach, A., Nave, K.A. and Rossner, M.J. (2006) Monitoring Regulated Protein-Protein Interactions using Split TEV. Nature Methods, 3, 985-993.
https://doi.org/10.1038/nmeth967
|
[15]
|
Massoud, T.F., Paulmurugan, R. and Gambhir, S.S. (2010) A Molecularly Engineered Split Reporter for Imaging Protein-Protein Interactions with Positron Emission Tomography. Nature Medicine, 16, 921-926. https://doi.org/10.1038/nm.2185
|
[16]
|
Muller, M.M., Kries, H., Csuhai, E., Kast, P. and Hilvert, D. (2010) Design, Selection, and Characterization of a Split Chorismate Mutase. Protein Science, 19, 1000-1010.
https://doi.org/10.1002/pro.377
|
[17]
|
Zetsche, B., Volz, S.E. and Zhang, F. (2015) A Split-Cas9 Architecture for Inducible Genome Editing and Transcription Modulation. Nature Biotechnology, 33, 139-142.
https://doi.org/10.1038/nbt.3149
|
[18]
|
Martell, J.D., Yamagata, M., Deerinck, T.J., Phan, S., Kwa, C.G., Ellisman, M.H., Sanes, J.R. and Ting, A.Y. (2016) A Split Horseradish Peroxidase for the Detection of Intercellular Protein-Protein Interactions and Sensitive Visualization of Synapses. Nature Biotechnology, 34, 774-780. https://doi.org/10.1038/nbt.3563
|
[19]
|
Pu, J., Zinkus-Boltz, J. and Dickinson, B.C. (2017) Evolution of a Split RNA Polymerase as a Versatile Biosensor Platform. Nature Chemical Biology, 13, 432-438.
https://doi.org/10.1038/nchembio.2299
|
[20]
|
Thomas, E.E., Pandey, N., Knudsen, S., Ball, Z.T. and Silberg, J.J. (2017) Programming Post-Translational Control over the Metabolic Labeling of Cellular Proteins with a Noncanonical Amino Acid. ACS Synthetic Biology, 6, 1572-1583.
https://doi.org/10.1021/acssynbio.7b00100
|
[21]
|
Stains, C.I., Porter, J.R., Ooi, A.T., Segal, D.J. and Ghosh, I. (2005) DNA Sequence-Enabled Reassembly of the Green Fluorescent Protein. Journal of the American Chemical Society, 127, 10782-10783. https://doi.org/10.1021/ja051969w
|
[22]
|
Stains, C.I., Furman, J.L., Segal, D.J. and Ghosh, I. (2006) Site-Specific Detection of DNA Methylation Utilizing mCpG-SEER. Journal of the American Chemical Society, 128, 9761-9765. https://doi.org/10.1021/ja060681j
|
[23]
|
Porter, J.R., Stains, C.I., Segal, D.J. and Ghosh, I. (2007) Split β-Lactamase Sensor for the Sequence-Specific Detection of DNA Methylation. Analytical Chemistry, 79, 6702-6708. https://doi.org/10.1021/ac071163+
|
[24]
|
Porter, J.R., Stains, C.I., Jester, B.W. and Ghosh, I. (2008) A General and Rapid Cell-Free Approach for the Interrogation of Protein-Protein, Protein-DNA, and Protein-RNA Interactions and their Antagonists Utilizing Split-Protein Reporters. Journal of the American Chemical Society, 130, 6488-6497.
https://doi.org/10.1021/ja7114579
|
[25]
|
Shekhawat, S.S., Porter, J.R., Sriprasad, A. and Ghosh, I. (2009) An Autoinhibited Coiled-Coil Design Strategy for Split-Protein Protease Sensors. Journal of the American Chemical Society, 131, 15284-15290. https://doi.org/10.1021/ja9050857
|
[26]
|
Jester, B.W., Cox, K.J., Gaj, A., Shomin, C.D., Porter, J.R. and Ghosh, I. (2010) A Coiled-Coil Enabled Split-Luciferase Three-Hybrid System: Applied Toward Profiling Inhibitors of Protein Kinases. Journal of the American Chemical Society, 132, 11727-11735. https://doi.org/10.1021/ja104491h
|
[27]
|
Furman, J.L., Badran, A.H., Ajulo, O., Porter, J.R., Stains, C.I., Segal, D.J. and Ghosh, I. (2010) Toward a General Approach for RNA-Templated Hierarchical Assembly of Split-Proteins. Journal of the American Chemical Society, 132, 11692-11701.
https://doi.org/10.1021/ja104395b
|
[28]
|
Stains, C.I., Furman, J.L., Porter, J.R., Rajagopal, S., Li, Y.X., Wyatt, R.T. and Ghosh, I. (2010) A General Approach for Receptor and Antibody-Targeted Detection of Native Proteins Utilizing Split-Luciferase Reassembly. ACS Chemical Biology, 5, 943-952. https://doi.org/10.1021/cb100143m
|
[29]
|
Jester, B.W., Gaj, A., Shomin, C.D., Cox, K.J. and Ghosh, I. (2012) Testing the Promiscuity of Commercial Kinase Inhibitors against the AGC Kinase Group Using a Split-Luciferase Screen. Journal of Medicinal Chemistry, 55, 1526-1537.
https://doi.org/10.1021/jm201265f
|
[30]
|
Furman, J.L., Mok, P.W., Badran, A.H. and Ghosh, I. (2011) Turn-On DNA Damage Sensors for the Direct Detection of 8-Oxoguanine and Photoproducts in Native DNA. Journal of the American Chemical Society, 133, 12518-12527.
https://doi.org/10.1021/ja1116606
|
[31]
|
Badran, A.H., Furman, J.L., Ma, A.S., Comi, T.J., Porter, J.R. and Ghosh, I. (2011) Evaluating the Global CpG Methylation Status of Native DNA Utilizing a Bipartite Split-Luciferase Sensor. Analytical Chemistry, 83, 7151-7157.
https://doi.org/10.1021/ac2015239
|
[32]
|
Porter, J.R., Helmers, M.R., Wang, P., Furman, J.L., Joy, S.T., Arora, P.S. and Ghosh, I. (2010) Profiling Small Molecule Inhibitors against Helix-Receptor Interactions: The Bcl-2 Family Inhibitor BH3I-1 Potently Inhibits p53/hDM2. Chemical Communications, 46, 8020-8022. https://doi.org/10.1039/c0cc02969f
|
[33]
|
Furman, J.L., Badran, A.H., Shen, S.Y., Stains, C.I., Hannallah, J., Segal, D.J. and Ghosh, I. (2009) Systematic Evaluation of Split-Fluorescent Proteins for the Direct Detection of Native and Methylated DNA. Bioorganic & Medicinal Chemistry Letters, 19, 3748-3751. https://doi.org/10.1016/j.bmcl.2009.04.141
|
[34]
|
Zhang, J., Campbell, R.E., Ting, A.Y. and Tsien, R.Y. (2002) Creating New Fluorescent Probes for Cell Biology. Nature Reviews Molecular Cell Biology, 3, 906-918.
https://doi.org/10.1038/nrm976
|
[35]
|
Ozawa, T., Kaihara, A., Sato, M., Tachihara, K. and Umezawa, Y. (2001) Split Luciferase as an Optical Probe for Detecting Protein-Protein Interactions in Mammalian Cells Based on Protein Splicing. Analytical Chemistry, 73, 2516-2521.
https://doi.org/10.1021/ac0013296
|
[36]
|
Wehrman, T., Kleaveland, B., Her, J.H., Balint, R.F. and Blau, H.M. (2002) Protein-Protein Interactions Monitored in Mammalian Cells via Complementation of β-Lactamase Enzyme Fragments. Proceedings of the National Academy of Sciences of the United States of America, 99, 3469-3474.
https://doi.org/10.1073/pnas.062043699
|
[37]
|
Avitabile, E., Forghieri, C. and Campadelli-Fiume, G. (2007) Complexes between Herpes Simplex Virus Glycoproteins gD, gB, and gH Detected in Cells by Complementation of Split Enhanced Green Fluorescent Protein. Journal of Virology, 81, 11532-11537. https://doi.org/10.1128/JVI.01343-07
|
[38]
|
Morell, M., Espargaró, A., Avilés, F.X. and Ventura, S. (2007) Detection of Transient Protein-Protein Interactions by Bimolecular Fluorescence Complementation: The Abl-SH3 Case. Proteomics, 7, 1023-1036.
https://doi.org/10.1002/pmic.200600966
|
[39]
|
Magliery, T.J., Wilson, C.G.M., Pan, W.L., Mishler, D., Ghosh, I., Hamilton, A.D. and Regan, L. (2005) Detecting Protein-Protein Interactions with a Green Fluorescent Protein Fragment Reassembly Trap: Scope and Mechanism. Journal of the American Chemical Society, 127, 146-157. https://doi.org/10.1021/ja046699g
|
[40]
|
Hu, C.D., Chinenov, Y. and Kerppola, T.K. (2002) Visualization of Interactions among bZIP and Rel Family Proteins in Living Cells Using Bimolecular Fluorescence Complementation. Molecular Cell, 9, 789-798.
https://doi.org/10.1016/S1097-2765(02)00496-3
|
[41]
|
Tchekanda, E., Sivanesan, D. and Michnick, S.W. (2014) An Infrared Reporter to Detect Spatiotemporal Dynamics of Protein-Protein Interactions. Nature Methods, 11, 641-644. https://doi.org/10.1038/nmeth.2934
|
[42]
|
To, T.L., Zhang, Q. and Shu, X. (2016) Structure-Guided Design of a Reversible Fluorogenic Reporter of Protein-Protein Interactions. Protein Science, 25, 748-753.
https://doi.org/10.1002/pro.2866
|
[43]
|
Pedelacq, J.D., Cabantous, S., Tran, T., Terwilliger, T.C. and Waldo, G.S. (2006) Engineering and Characterization of a Superfolder Green Fluorescent Protein. Nature Biotechnology, 24, 79-88. https://doi.org/10.1038/nbt1172
|
[44]
|
Cabantous, S. and Wald, G.S. (2006) In Vivo and in Vitro Protein Solubility Assays Using Split GFP. Nature Methods, 3, 845-854. https://doi.org/10.1038/nmeth932
|
[45]
|
Callahan, B.P., Stanger, M.J. and Belfort, M. (2010) Protease Activation of Split Green Fluorescent Protein. ChemBioChem, 11, 2259-2263.
https://doi.org/10.1002/cbic.201000453
|
[46]
|
Sakamoto, S., Terauchi, M., Hugo, A., Kim, T., Araki, Y. and Wada, T. (2013) Creation of a Caspase-3 Sensing System Using a Combination of Split-GFP and Split-Intein. Chemical Communications, 49, 10323-10325. https://doi.org/10.1039/c3cc43389g
|
[47]
|
To, T.L., Schepis, A., Ruiz-Gonzalez, R., Zhang, Q., Yu, D., Dong, Z., Coughlin, S. R. and Shu, X. (2016) Rational Design of a GFP-Based Fluorogenic Caspase Reporter for Imaging Apoptosis in Vivo. Cell Chemical Biology, 23, 875-882.
https://doi.org/10.1016/j.chembiol.2016.06.007
|
[48]
|
Yin, C., Wang, M., Lei, C., Wang, Z., Li, P., Li, Y., Li, W., Huang, Y., Nie, Z. and Yao, S. (2015) Phosphorylation-Mediated Assembly of a Semisynthetic Fluorescent Protein for Label-Free Detection of Protein Kinase Activity. Analytical Chemistry, 87, 6311-6318. https://doi.org/10.1021/acs.analchem.5b01160
|
[49]
|
Milech, N., Longville, B.A.C., Cunningham, P.T., Scobie, M.N., Bogdawa, H.M., Winslow, S., Anastasas, M., Connor, T., Ong, F., Stone, S.R., Kerfoot, M., Heinrich, T., Kroeger, K.M., Tan, Y., Hoffmann, K., Thomas, W.R., Watt, P.M. and Hopkins, R.M. (2015) GFP-Complementation Assay to Detect Functional CPP and Protein Delivery into Living Cells. Scientific Report, 5, Article No. 18329.
https://doi.org/10.1038/srep18329
|
[50]
|
Park, E., Lee, H.Y., Woo, J., Choi, D. and Dinesh-Kuma, S.P. (2017) Spatiotemporal Monitoring of Pseudomonas syringae Effectors via Type III Secretion Using Split Fluorescent Protein Fragments. Plant Cell, 29, 1571-1584.
https://doi.org/10.1105/tpc.17.00047
|
[51]
|
Schmit, S., Adjobo-Hermans, M.J., Wallbrecher, R., Verdurmen, W.P., Bovée-Geurts, P.H.M., van Oostrum, J., Milletti, F., Enderle, T. and Brock, R. (2015) Detecting Cytosolic Peptide Delivery with the GFP Complementation Assay in the Low Micromolar Range. Angewandte Chemie International Edition, 54, 15105-15108.
https://doi.org/10.1002/anie.201505913
|
[52]
|
Cabantous, S., Nguyen, H.B., Pédelacq, J.D., Koraichi, F., Chaudhary, A., Ganguly, K., Lockard, M.A., Favre, G., Terwilliger, T.C. and Waldo, G.S. (2013) A New Protein-Protein Interaction Sensor Based on Tripartite Split-GFP Association. Scientific Reports, 3, Article No. 2854. https://doi.org/10.1038/srep02854
|
[53]
|
Koraichi, F., Gence, R., Bouchenot, C., Grosjean, S., Lajoie-Mazenc, I., Favre, G. and Cabantous, S. (2018) High-Content Tripartite Split-GFP Cell-Based Assays to Screen for Modulators of Small GTPase Activation. Journal of Cell Science, 131, Article ID: jcs210419. https://doi.org/10.1242/jcs.210419
|
[54]
|
Zhang, J., Wang, M., Tang, R., Liu, Y., Lei, C., Huang, Y., Nie, Z. and Yao, S. (2018) Transpeptidation-Mediated Assembly of Tripartite Split Green Fluorescent Protein for Label-Free Assay of Sortase Activity. Analytical Chemistry, 90, 3245-3252.
https://doi.org/10.1021/acs.analchem.7b04756
|
[55]
|
Leibly, D.J., Arbing, M.A., Pashkov, I., De Vore, N., Waldo, G.S., Terwilliger, T.C. and Yeates, T.O. (2015) A Suite of Engineered GFP Molecules for Oligomeric Scaffolding. Structure, 23, 1754-1768. https://doi.org/10.1016/j.str.2015.07.008
|
[56]
|
Nguyen, H.B., Hung, L.W., Yeates, T.O., Terwilliger, T.C. and Waldo, G.S. (2013) Split Green Fluorescent Protein as a Modular Binding Partner for Protein Crystallization. Acta Crystallographic Section D, 69, 2513-2523.
https://doi.org/10.1107/S0907444913024608
|
[57]
|
Paulmurugan, R. and Gambhir, S.S. (2006) An Intramolecular Folding Sensor for Imaging Estrogen Receptor-Ligand Interactions. Proceedings of the National Academy of Sciences of the United States of America, 103, 15883-15888.
https://doi.org/10.1073/pnas.0607385103
|
[58]
|
Paulmurugan, R., Tamrazi, A., Katzenellenbogen, J.A., Katzenellenbogen, B.S. and Gambhir, S.S. (2008) A Human Estrogen Receptor (ER) α Mutation with Differential Responsiveness to Nonsteroidal Ligands: Novel Approaches for Studying Mechanism of ER action. Molecular Endocrinology, 22, 1552-1564.
https://doi.org/10.1210/me.2007-0570
|
[59]
|
Kim, S.B., Awais, M., Sato, M., Umezawa, Y. and Tao, H. (2007)Integrated Molecule-Format Bioluminescent Probe for Visualizing Androgenicity of Ligands Based on the Intramolecular Association of Androgen Receptor with Its Recognition Peptide. Analytical Chemistry, 79, 1874-1880. https://doi.org/10.1021/ac061934u
|
[60]
|
Kim, S.B., Umezawa, Y., Kanno, K.A. and Tao, H. (2008) An Integrated Molecule-Format Multicolor Probe for Monitoring Multiple Activities of a Bioactive Small Molecule. ACS Chemical Biology, 3, 359-372. https://doi.org/10.1021/cb800004s
|
[61]
|
Paulmurugan, R., Tamrazi, A., Massoud, T.F., Katzenellenbogen, J.A. and Gambhir, S.S. (2011) In Vitro and in Vivo Molecular Imaging of Estrogen Receptor α and β Homo- and Heterodimerization: Exploration of New Modes of Receptor Regulation. Molecular Endocrinology, 25, 2029-2040.
https://doi.org/10.1210/me.2011-1145
|
[62]
|
Fan-Minogue, H., Cao, Z., Paulmurugan, R., Chan, C.T., Massoud, T.F., Felsher, D.W. and Gambhir, S.S. (2010) Noninvasive Molecular Imaging of c-Myc Activation in Living Mice. Proceedings of the National Academy of Sciences of the United States of America, 107, 15892-15897. https://doi.org/10.1073/pnas.1007443107
|
[63]
|
Dang, C.V., O’Donnell, K.A., Zeller, K.I., Nguyen, T., Osthus, R.C. and Li, F. (2006) The c-Myc Target Gene Network. Seminars Cancer Biology, 16, 253-264.
https://doi.org/10.1016/j.semcancer.2006.07.014
|
[64]
|
Ilagan, M.X.G., Lim, S., Fulbright, M., Piwnica-Worms, D. and Kopan, R. (2011) Real-Time Imaging of Notch Activation with a Luciferase Complementation-Based Reporter. Science Signaling, 4, rs7. https://doi.org/10.1126/scisignal.2001656
|
[65]
|
Kopan, R. and Ilagan, M.X.G. (2009) The Canonical Notch Signaling Pathway: Unfolding the Activation Mechanism. Cell, 137, 216-233.
https://doi.org/10.1016/j.cell.2009.03.045
|
[66]
|
Macdonald-Obermann, J.L., Piwnica-Worms, D. and Pike, L.J. (2012) Mechanics of EGF Receptor/ErbB2 Kinase Activation Revealed by Luciferase Fragment Complementation Imaging. Proceedings of the National Academy of Sciences of the United States of America, 109, 137-142. https://doi.org/10.1073/pnas.1111316109
|
[67]
|
Yang, K.S., Ilagan, M.X.G., Piwnica-Worms, D. and Pike, L.J. (2009) Luciferase Fragment Complementation Imaging of Conformational Changes in the Epidermal Growth Factor Receptor. Journal of Biological Chemistry, 284, 7474-7482.
https://doi.org/10.1074/jbc.M808041200
|
[68]
|
Misawa, N., Kafi, A., Hattori, M., Miura, K., Masuda, K. and Ozawa, T. (2010) Rapid and High-Sensitivity Cell-Based Assays of Protein-Protein Interactions Using Split Click Beetle Luciferase Complementation: An Approach to the Study of G-Protein-Coupled Receptors. Analytical Chemistry, 82, 2552-2560.
https://doi.org/10.1021/ac100104q
|
[69]
|
Hattori, M., Tanaka, M., Takakura, H., Aoki, K., Miura, K., Anzai, T. and Ozawa, T. (2013) Analysis of Temporal Patterns of GPCR-β-Arrestin Interactions Using Split Luciferase-Fragment Complementation. Molecular Biosystems, 9, 957-964.
https://doi.org/10.1039/c2mb25443c
|
[70]
|
Wolf, F., Li, W., Li, F. and Li, C.-Y. (2011)Novel Luciferase-Based Reporter System to Monitor Activation of ErbB2/Her2/neu Pathway Noninvasively during Radiotherapy. International Journal of Radiation Oncology, Biology, Physics, 79, 233-238.
https://doi.org/10.1016/j.ijrobp.2010.08.001
|
[71]
|
Yu, S.W., Wang, H.M., Poitras, M.F., Coombs, C., Bowers, W.J., Federoff, H.J., Poirier, G.G., Dawson, T.M. and Dawson, V.L. (2002) Mediation of Poly(ADP-Ribose) Polymerase-1-Dependent Cell Death by Apoptosis-Inducing Factor. Science, 297, 259-263.
https://doi.org/10.1126/science.1072221
|
[72]
|
Furman, J.L., Mok, P.-W., Shen, S., Stains, C.I. and Ghosh, I. (2010) A Turn-on Split-Luciferase Sensor for the Direct Detection of Poly(ADP-Ribose) as a Marker for DNA Repair and Cell Death. Chemical Communications, 47, 397-399.
https://doi.org/10.1039/C0CC02229B
|
[73]
|
Eustermann, S., Brockmann, C., Mehrotra, P.V., Yang, J.C., Loakes, D., West, S. C., Ahel, I. and Neuhaus, D. (2010) Solution Structures of the Two PBZ Domains from Human APLF and Their Interaction with Poly(ADP-Ribose). Nature Structral & Molecular Biology, 17, 241-243. https://doi.org/10.1038/nsmb.1747
|
[74]
|
Spencer, D.M., Wandless, T.J., Schreiber, S.L. and Crabtree, G.R. (1993) Controlling Signal Transduction with Synthetic Ligands. Science, 262, 1019-1024.
https://doi.org/10.1126/science.7694365
|
[75]
|
Fegan, A., White, B., Carlson, J.C.T. and Wagner, C.R. (2010) Chemically Controlled Protein Assembly: Techniques and Applications. Chemical Reviews, 110, 3315-3336.
https://doi.org/10.1021/cr8002888
|
[76]
|
Spencer, D.M., Belshaw, P.J., Chen, L., Ho, S.N., Randazzo, F., Crabtree, G.R. and Schreiber, S.L. (1996) Functional Analysis of Fas Signaling in Vivo Using Synthetic Inducers of Dimerization. Current Biology, 6, 839-847.
https://doi.org/10.1016/S0960-9822(02)00607-3
|
[77]
|
Nyanguile, O., Uesugi, M., Austin, D.J. and Verdine, G.L. (1997) A Nonnatural Transcriptional Coactivator. Proceedings of the National Academy of Sciences of the United States of America, 94, 13402-13406.
https://doi.org/10.1073/pnas.94.25.13402
|
[78]
|
Cheng, J.K., Yu, L., Zhang, D.Y., Huang, Q.J., Spencer, D. and Su, B. (2005) Dimerization through the Catalytic Domain Is Essential for MEKK2 Activation. Journal of Biological Chemistry, 280, 13477-13482. https://doi.org/10.1074/jbc.M414258200
|
[79]
|
Freiberg, R.A., Spencer, D.M., Choate, K.A., Peng, P.D., Schreiber, S.L., Crabtree, G.R. and Khavari, P.A. (1996) Specific Triggering of the Fas Signal Transduction Pathway in Normal Human Keratinocytes. Journal Biological Chemistry, 271, 31666-31669. https://doi.org/10.1074/jbc.271.49.31666
|
[80]
|
Schwartz, E.C., Saez, L., Young, M.W. and Muir, T.W. (2007) Post-Translational Enzyme Activation in an Animal via Optimized Conditional Protein Splicing. Nature Chemical Biology, 3, 50-54. https://doi.org/10.1038/nchembio832
|
[81]
|
Mootz, H.D., Blum, E.S., Tyszkiewicz, A.B. and Muir, T.W. (2003) Conditional Protein Splicing: A New Tool to Control Protein Structure and Function in Vitro and in Vivo. Journal of the American Chemical Society, 125, 10561-10569.
https://doi.org/10.1021/ja0362813
|
[82]
|
Mootz, H.D. and Muir, T.W. (2002) Protein Splicing Triggered by a Small Molecule. Journal of the American Chemical Society, 124, 9044-9045.
https://doi.org/10.1021/ja026769o
|
[83]
|
Sakamoto, K.M., Kim, K.B., Kumagai, A., Mercurio, F., Crews, C.M. and Deshaies, R.J. (2001) Protacs: Chimeric Molecules that Target Proteins to the Skp1-Cullin-F Box Complex for Ubiquitination and Degradation. Proceedings of the National Academy of Sciences of the United States of America, 98, 8554-8559.
https://doi.org/10.1073/pnas.141230798
|
[84]
|
Schneekloth, A.R., Pucheault, M., Tae, H.S. and Crews, C.M. (2008) Targeted Intracellular Protein Degradation Induced by a Small Molecule: En Route to Chemical Proteomics. Bioorganic & Medicinal Chemistry Letter, 18, 5904-5908.
https://doi.org/10.1016/j.bmcl.2008.07.114
|
[85]
|
Pratt, M.R., Schwartz, E.C. and Muir, T.W. (2007) Small-Molecule-Mediated Rescue of Protein Function by an Inducible Proteolytic Shunt. Proceedings of the National Academy of Sciences of the United States of America, 104, 11209-11214.
https://doi.org/10.1073/pnas.0700816104
|
[86]
|
Hunter, T. (1995) Protein Kinases and Phosphatases: The Yin and Yang of Protein Phosphorylation and Signaling. Cell, 80, 225-236.
https://doi.org/10.1016/0092-8674(95)90405-0
|
[87]
|
Manning, G., Whyte, D.B., Martinez, R., Hunter, T. and Sudarsanam, S. (2002) The Protein Kinase Complement of the Human Genome. Science, 298, 1912-1934.
https://doi.org/10.1126/science.1075762
|
[88]
|
Alonso, A., Sasin, J., Bottini, N., Friedberg, I., Friedberg, I., Osterman, A., Godzik, A., Hunter, T., Dixon, J. and Mustelin, T. (2004) Protein Tyrosine Phosphatases in the Human Genome. Cell, 117, 699-711. https://doi.org/10.1016/j.cell.2004.05.018
|
[89]
|
Camacho-Soto, K., Castillo-Montaya, J., Tye, B.W. and Ghosh, I. (2014) Ligand-Gated Split-Kinases. Journal of the American Chemical Society, 136, 3995-4002.
https://doi.org/10.1021/ja4130803
|
[90]
|
Camacho-Soto, K., Castillo-Montaya, J., Tye, B.W., Ogunleye, L.O. and Ghosh, I. (2014) Small Molecule Gated Split-Tyrosine Phosphatases and Orthogonal Split-Tyrosine Kinases. Journal of the American Chemical Society, 136, 17078-17086.
https://doi.org/10.1021/ja5080745
|