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Volumn 33, Issue 2, 2015, Pages 101-110

Synthetic protein switches: Design principles and applications

Author keywords

Biosensors; Molecular diagnostics; Protein engineering; Protein switches; Signaling; Synthetic biology

Indexed keywords

BIOSENSORS; MACHINERY; PROTEINS; SIGNAL TRANSDUCTION; SIGNALING; TIME SWITCHES;

EID: 84921565935     PISSN: 01677799     EISSN: 18793096     Source Type: Journal    
DOI: 10.1016/j.tibtech.2014.11.010     Document Type: Review
Times cited : (128)

References (98)
  • 1
    • 77952944052 scopus 로고    scopus 로고
    • Designing customized cell signalling circuits
    • Lim W.A. Designing customized cell signalling circuits. Nat. Rev. Mol. Cell Biol. 2010, 11:393-403.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 393-403
    • Lim, W.A.1
  • 2
    • 84894534641 scopus 로고    scopus 로고
    • Synthetic biology in mammalian cells: next generation research tools and therapeutics
    • Lienert F., et al. Synthetic biology in mammalian cells: next generation research tools and therapeutics. Nat. Rev. Mol. Cell Biol. 2014, 15:95-107.
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 95-107
    • Lienert, F.1
  • 3
    • 84862081641 scopus 로고    scopus 로고
    • Foundations for the design and implementation of synthetic genetic circuits
    • Slusarczyk A.L., et al. Foundations for the design and implementation of synthetic genetic circuits. Nat. Rev. Genet. 2012, 13:406-420.
    • (2012) Nat. Rev. Genet. , vol.13 , pp. 406-420
    • Slusarczyk, A.L.1
  • 4
    • 84890178034 scopus 로고    scopus 로고
    • Advances in genetic circuit design: novel biochemistries, deep part mining, and precision gene expression
    • Nielsen A.A., et al. Advances in genetic circuit design: novel biochemistries, deep part mining, and precision gene expression. Curr. Opin. Chem. Biol. 2013, 17:878-892.
    • (2013) Curr. Opin. Chem. Biol. , vol.17 , pp. 878-892
    • Nielsen, A.A.1
  • 5
    • 84902590850 scopus 로고    scopus 로고
    • Diagnostic applications of nucleic acid circuits
    • Jung C., Ellington A.D. Diagnostic applications of nucleic acid circuits. Acc. Chem. Res. 2014, 47:1825-1835.
    • (2014) Acc. Chem. Res. , vol.47 , pp. 1825-1835
    • Jung, C.1    Ellington, A.D.2
  • 6
    • 84865297453 scopus 로고    scopus 로고
    • Synthetic biology with RNA: progress report
    • Benenson Y. Synthetic biology with RNA: progress report. Curr. Opin. Chem. Biol. 2012, 16:278-284.
    • (2012) Curr. Opin. Chem. Biol. , vol.16 , pp. 278-284
    • Benenson, Y.1
  • 7
    • 84865283318 scopus 로고    scopus 로고
    • Post-translational tools expand the scope of synthetic biology
    • Olson E.J., Tabor J.J. Post-translational tools expand the scope of synthetic biology. Curr. Opin. Chem. Biol. 2012, 16:300-306.
    • (2012) Curr. Opin. Chem. Biol. , vol.16 , pp. 300-306
    • Olson, E.J.1    Tabor, J.J.2
  • 9
    • 79959451416 scopus 로고    scopus 로고
    • Reporting from the field: genetically encoded fluorescent reporters uncover signaling dynamics in living biological systems
    • Mehta S., Zhang J. Reporting from the field: genetically encoded fluorescent reporters uncover signaling dynamics in living biological systems. Annu. Rev. Biochem. 2011, 80:375-401.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 375-401
    • Mehta, S.1    Zhang, J.2
  • 10
    • 84892898809 scopus 로고    scopus 로고
    • Protein folding and de novo protein design for biotechnological applications
    • Khoury G.A., et al. Protein folding and de novo protein design for biotechnological applications. Trends Biotechnol. 2014, 32:99-109.
    • (2014) Trends Biotechnol. , vol.32 , pp. 99-109
    • Khoury, G.A.1
  • 11
    • 84904916503 scopus 로고    scopus 로고
    • Computational protein design of ligand binding and catalysis
    • Feldmeier K., Hocker B. Computational protein design of ligand binding and catalysis. Curr. Opin. Chem. Biol. 2013, 17:929-933.
    • (2013) Curr. Opin. Chem. Biol. , vol.17 , pp. 929-933
    • Feldmeier, K.1    Hocker, B.2
  • 12
    • 0030610646 scopus 로고    scopus 로고
    • 2+ based on green fluorescent proteins and calmodulin
    • 2+ based on green fluorescent proteins and calmodulin. Nature 1997, 388:882-887.
    • (1997) Nature , vol.388 , pp. 882-887
    • Miyawaki, A.1
  • 14
    • 73349108496 scopus 로고    scopus 로고
    • Imaging neural activity in worms, flies and mice with improved GCaMP calcium indicators
    • Tian L., et al. Imaging neural activity in worms, flies and mice with improved GCaMP calcium indicators. Nat. Methods 2009, 6:875-881.
    • (2009) Nat. Methods , vol.6 , pp. 875-881
    • Tian, L.1
  • 15
    • 84880427381 scopus 로고    scopus 로고
    • Ultrasensitive fluorescent proteins for imaging neuronal activity
    • Chen T.W., et al. Ultrasensitive fluorescent proteins for imaging neuronal activity. Nature 2013, 499:295-300.
    • (2013) Nature , vol.499 , pp. 295-300
    • Chen, T.W.1
  • 16
    • 84867026349 scopus 로고    scopus 로고
    • Optimization of a GCaMP calcium indicator for neural activity imaging
    • Akerboom J., et al. Optimization of a GCaMP calcium indicator for neural activity imaging. J. Neurosci. 2012, 32:13819-13840.
    • (2012) J. Neurosci. , vol.32 , pp. 13819-13840
    • Akerboom, J.1
  • 17
    • 84884623859 scopus 로고    scopus 로고
    • Rational design of FRET sensor proteins based on mutually exclusive domain interactions
    • Merkx M., et al. Rational design of FRET sensor proteins based on mutually exclusive domain interactions. Biochem. Soc. Trans. 2013, 41:1201-1205.
    • (2013) Biochem. Soc. Trans. , vol.41 , pp. 1201-1205
    • Merkx, M.1
  • 18
    • 79951671135 scopus 로고    scopus 로고
    • Design and application of genetically encoded biosensors
    • Palmer A.E., et al. Design and application of genetically encoded biosensors. Trends Biotechnol. 2011, 29:144-152.
    • (2011) Trends Biotechnol. , vol.29 , pp. 144-152
    • Palmer, A.E.1
  • 19
    • 84884617349 scopus 로고    scopus 로고
    • Opportunities for bioprocess monitoring using FRET biosensors
    • Constantinou A., Polizzi K.M. Opportunities for bioprocess monitoring using FRET biosensors. Biochem. Soc. Trans. 2013, 41:1146-1151.
    • (2013) Biochem. Soc. Trans. , vol.41 , pp. 1146-1151
    • Constantinou, A.1    Polizzi, K.M.2
  • 20
    • 44349104094 scopus 로고    scopus 로고
    • Design of protein function leaps by directed domain interface evolution
    • Huang J., et al. Design of protein function leaps by directed domain interface evolution. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:6578-6583.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 6578-6583
    • Huang, J.1
  • 21
    • 70149092506 scopus 로고    scopus 로고
    • Structural basis for exquisite specificity of affinity clamps, synthetic binding proteins generated through directed domain-interface evolution
    • Huang J., et al. Structural basis for exquisite specificity of affinity clamps, synthetic binding proteins generated through directed domain-interface evolution. J. Mol. Biol. 2009, 392:1221-1231.
    • (2009) J. Mol. Biol. , vol.392 , pp. 1221-1231
    • Huang, J.1
  • 22
    • 77949808895 scopus 로고    scopus 로고
    • Rational conversion of affinity reagents into label-free sensors for Peptide motifs by designed allostery
    • Huang J., Koide S. Rational conversion of affinity reagents into label-free sensors for Peptide motifs by designed allostery. ACS Chem. Biol. 2010, 5:273-277.
    • (2010) ACS Chem. Biol. , vol.5 , pp. 273-277
    • Huang, J.1    Koide, S.2
  • 23
    • 84902665495 scopus 로고    scopus 로고
    • Directed network wiring identifies a key protein interaction in embryonic stem cell differentiation
    • Yasui N., et al. Directed network wiring identifies a key protein interaction in embryonic stem cell differentiation. Mol. Cell 2014, 54:1034-1041.
    • (2014) Mol. Cell , vol.54 , pp. 1034-1041
    • Yasui, N.1
  • 24
    • 80053525802 scopus 로고    scopus 로고
    • Semisynthesis of fluorescent metabolite sensors on cell surfaces
    • Brun M.A., et al. Semisynthesis of fluorescent metabolite sensors on cell surfaces. J. Am. Chem. Soc. 2011, 133:16235-16242.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 16235-16242
    • Brun, M.A.1
  • 25
    • 84860871322 scopus 로고    scopus 로고
    • A semisynthetic fluorescent sensor protein for glutamate
    • Brun M.A., et al. A semisynthetic fluorescent sensor protein for glutamate. J. Am. Chem. Soc. 2012, 134:7676-7678.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 7676-7678
    • Brun, M.A.1
  • 26
    • 84869461900 scopus 로고    scopus 로고
    • A fluorescent sensor for GABA and synthetic GABA(B) receptor ligands
    • Masharina A., et al. A fluorescent sensor for GABA and synthetic GABA(B) receptor ligands. J. Am. Chem. Soc. 2012, 134:19026-19034.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 19026-19034
    • Masharina, A.1
  • 27
    • 84893903976 scopus 로고    scopus 로고
    • Sensing acetylcholine and anticholinesterase compounds
    • Schena A., Johnsson K. Sensing acetylcholine and anticholinesterase compounds. Angew. Chem. 2014, 53:1302-1305.
    • (2014) Angew. Chem. , vol.53 , pp. 1302-1305
    • Schena, A.1    Johnsson, K.2
  • 28
    • 84902839007 scopus 로고    scopus 로고
    • Bioluminescent sensor proteins for point-of-care therapeutic drug monitoring
    • Griss R., et al. Bioluminescent sensor proteins for point-of-care therapeutic drug monitoring. Nat. Chem. Biol. 2014, 10:598-603.
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 598-603
    • Griss, R.1
  • 29
    • 84869455585 scopus 로고    scopus 로고
    • Engineered luciferase reporter from a deep sea shrimp utilizing a novel imidazopyrazinone substrate
    • Hall M.P., et al. Engineered luciferase reporter from a deep sea shrimp utilizing a novel imidazopyrazinone substrate. ACS Chem. Biol. 2012, 7:1848-1857.
    • (2012) ACS Chem. Biol. , vol.7 , pp. 1848-1857
    • Hall, M.P.1
  • 30
    • 84898993517 scopus 로고    scopus 로고
    • The ensemble nature of allostery
    • Motlagh H.N., et al. The ensemble nature of allostery. Nature 2014, 508:331-339.
    • (2014) Nature , vol.508 , pp. 331-339
    • Motlagh, H.N.1
  • 31
    • 78650413957 scopus 로고    scopus 로고
    • Circular permutation: a different way to engineer enzyme structure and function
    • Yu Y., Lutz S. Circular permutation: a different way to engineer enzyme structure and function. Trends Biotechnol. 2011, 29:18-25.
    • (2011) Trends Biotechnol. , vol.29 , pp. 18-25
    • Yu, Y.1    Lutz, S.2
  • 32
    • 58149164666 scopus 로고    scopus 로고
    • 2+-sensing molecular switch based on alternate frame protein folding
    • 2+-sensing molecular switch based on alternate frame protein folding. ACS Chem. Biol. 2008, 3:723-732.
    • (2008) ACS Chem. Biol. , vol.3 , pp. 723-732
    • Stratton, M.M.1
  • 33
    • 84873867172 scopus 로고    scopus 로고
    • Stepwise conversion of a binding protein to a fluorescent switch: application to Thermoanaerobacter tengcongensis ribose binding protein
    • Ha J.H., et al. Stepwise conversion of a binding protein to a fluorescent switch: application to Thermoanaerobacter tengcongensis ribose binding protein. Biochemistry 2013, 52:600-612.
    • (2013) Biochemistry , vol.52 , pp. 600-612
    • Ha, J.H.1
  • 34
    • 84906861542 scopus 로고    scopus 로고
    • Converting a binding protein into a biosensing conformational switch using protein fragment exchange
    • Zheng H., et al. Converting a binding protein into a biosensing conformational switch using protein fragment exchange. Biochemistry 2014, 53:5505-5514.
    • (2014) Biochemistry , vol.53 , pp. 5505-5514
    • Zheng, H.1
  • 35
    • 77649241924 scopus 로고    scopus 로고
    • Engineering an artificial zymogen by alternate frame protein folding
    • Mitrea D.M., et al. Engineering an artificial zymogen by alternate frame protein folding. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:2824-2829.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 2824-2829
    • Mitrea, D.M.1
  • 36
    • 84880348332 scopus 로고    scopus 로고
    • GFP variants with alternative beta-strands and their application as light-driven protease sensors: a tale of two tails
    • Do K., Boxer S.G. GFP variants with alternative beta-strands and their application as light-driven protease sensors: a tale of two tails. J. Am. Chem. Soc. 2013, 135:10226-10229.
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 10226-10229
    • Do, K.1    Boxer, S.G.2
  • 37
    • 8844263869 scopus 로고    scopus 로고
    • A molecular switch created by in vitro recombination of nonhomologous genes
    • Guntas G., et al. A molecular switch created by in vitro recombination of nonhomologous genes. Chem. Biol. 2004, 11:1483-1487.
    • (2004) Chem. Biol. , vol.11 , pp. 1483-1487
    • Guntas, G.1
  • 38
    • 23844465160 scopus 로고    scopus 로고
    • Directed evolution of protein switches and their application to the creation of ligand-binding proteins
    • Guntas G., et al. Directed evolution of protein switches and their application to the creation of ligand-binding proteins. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:11224-11229.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 11224-11229
    • Guntas, G.1
  • 39
    • 84881613098 scopus 로고    scopus 로고
    • An engineered calmodulin-based allosteric switch for peptide biosensing
    • Meister G.E., Joshi N.S. An engineered calmodulin-based allosteric switch for peptide biosensing. Chembiochem 2013, 14:1460-1467.
    • (2013) Chembiochem , vol.14 , pp. 1460-1467
    • Meister, G.E.1    Joshi, N.S.2
  • 40
    • 34948822244 scopus 로고    scopus 로고
    • Molecular imaging of Akt kinase activity
    • Zhang L., et al. Molecular imaging of Akt kinase activity. Nat. Med. 2007, 13:1114-1119.
    • (2007) Nat. Med. , vol.13 , pp. 1114-1119
    • Zhang, L.1
  • 41
    • 84865408770 scopus 로고    scopus 로고
    • Crystal structure of firefly luciferase in a second catalytic conformation supports a domain alternation mechanism
    • Sundlov J.A., et al. Crystal structure of firefly luciferase in a second catalytic conformation supports a domain alternation mechanism. Biochemistry 2012, 51:6493-6495.
    • (2012) Biochemistry , vol.51 , pp. 6493-6495
    • Sundlov, J.A.1
  • 42
    • 84894278611 scopus 로고    scopus 로고
    • Improved protein-protein interaction assay FlimPIA by the entrapment of luciferase conformation
    • Ohmuro-Matsuyama Y., et al. Improved protein-protein interaction assay FlimPIA by the entrapment of luciferase conformation. Anal. Chem. 2014, 86:2013-2018.
    • (2014) Anal. Chem. , vol.86 , pp. 2013-2018
    • Ohmuro-Matsuyama, Y.1
  • 43
    • 84882705992 scopus 로고    scopus 로고
    • A protein-protein interaction assay based on the functional complementation of mutant firefly luciferases
    • Ohmuro-Matsuyama Y., et al. A protein-protein interaction assay based on the functional complementation of mutant firefly luciferases. Anal. Chem. 2013, 85:7935-7940.
    • (2013) Anal. Chem. , vol.85 , pp. 7935-7940
    • Ohmuro-Matsuyama, Y.1
  • 44
    • 84875291004 scopus 로고    scopus 로고
    • Demonstration of protein-fragment complementation assay using purified firefly luciferase fragments
    • Ohmuro-Matsuyama Y., et al. Demonstration of protein-fragment complementation assay using purified firefly luciferase fragments. BMC Biotechnol. 2013, 13:31.
    • (2013) BMC Biotechnol. , vol.13 , pp. 31
    • Ohmuro-Matsuyama, Y.1
  • 45
    • 80053651953 scopus 로고    scopus 로고
    • A protein therapeutic modality founded on molecular regulation
    • Wright C.M., et al. A protein therapeutic modality founded on molecular regulation. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:16206-16211.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 16206-16211
    • Wright, C.M.1
  • 46
    • 0037219686 scopus 로고    scopus 로고
    • Evolutionarily conserved networks of residues mediate allosteric communication in proteins
    • Suel G.M., et al. Evolutionarily conserved networks of residues mediate allosteric communication in proteins. Nat. Struct. Biol. 2003, 10:59-69.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 59-69
    • Suel, G.M.1
  • 47
    • 0033923044 scopus 로고    scopus 로고
    • Systematic circular permutation of an entire protein reveals essential folding elements
    • Iwakura M., et al. Systematic circular permutation of an entire protein reveals essential folding elements. Nat. Struct. Biol. 2000, 7:580-585.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 580-585
    • Iwakura, M.1
  • 48
    • 54249105941 scopus 로고    scopus 로고
    • Surface sites for engineering allosteric control in proteins
    • Lee J., et al. Surface sites for engineering allosteric control in proteins. Science 2008, 322:438-442.
    • (2008) Science , vol.322 , pp. 438-442
    • Lee, J.1
  • 49
    • 84455167671 scopus 로고    scopus 로고
    • Hot spots for allosteric regulation on protein surfaces
    • Reynolds K.A., et al. Hot spots for allosteric regulation on protein surfaces. Cell 2011, 147:1564-1575.
    • (2011) Cell , vol.147 , pp. 1564-1575
    • Reynolds, K.A.1
  • 50
    • 0034754163 scopus 로고    scopus 로고
    • A yeast sensor of ligand binding
    • Tucker C.L., Fields S. A yeast sensor of ligand binding. Nat. Biotechnol. 2001, 19:1042-1046.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 1042-1046
    • Tucker, C.L.1    Fields, S.2
  • 51
    • 0033545844 scopus 로고    scopus 로고
    • Clonal selection and in vivo quantitation of protein interactions with protein-fragment complementation assays
    • Remy I., Michnick S.W. Clonal selection and in vivo quantitation of protein interactions with protein-fragment complementation assays. Proc. Natl. Acad. Sci. U.S.A. 1999, 96:5394-5399.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 5394-5399
    • Remy, I.1    Michnick, S.W.2
  • 52
    • 84886496265 scopus 로고    scopus 로고
    • Switchable reporter enzymes based on mutually exclusive domain interactions allow antibody detection directly in solution
    • Banala S., et al. Switchable reporter enzymes based on mutually exclusive domain interactions allow antibody detection directly in solution. ACS Chem. Biol. 2013, 8:2127-2132.
    • (2013) ACS Chem. Biol. , vol.8 , pp. 2127-2132
    • Banala, S.1
  • 53
    • 84876467576 scopus 로고    scopus 로고
    • A generic scaffold for conversion of peptide ligands into homogenous biosensors
    • Nirantar S.R., et al. A generic scaffold for conversion of peptide ligands into homogenous biosensors. Biosens. Bioelectron. 2013, 47:421-428.
    • (2013) Biosens. Bioelectron. , vol.47 , pp. 421-428
    • Nirantar, S.R.1
  • 54
    • 84929591267 scopus 로고    scopus 로고
    • DNA-directed control of enzyme-inhibitor complex formation: a modular approach to reversibly switch enzyme activity
    • Published online September 12, 2014.
    • Janssen B.M., et al. DNA-directed control of enzyme-inhibitor complex formation: a modular approach to reversibly switch enzyme activity. ACS Synth. Biol. 2014, Published online September 12, 2014. http://dx.doi.org/10.1021/sb500278z.
    • (2014) ACS Synth. Biol.
    • Janssen, B.M.1
  • 55
    • 84905560978 scopus 로고    scopus 로고
    • Engineering beta-lactamase zymogens for use in protease activity assays
    • Kim H., et al. Engineering beta-lactamase zymogens for use in protease activity assays. Chem. Commun. (Camb.) 2014, 50:10155-10157.
    • (2014) Chem. Commun. (Camb.) , vol.50 , pp. 10155-10157
    • Kim, H.1
  • 56
    • 78049318476 scopus 로고    scopus 로고
    • Antibody detection by using a FRET-based protein conformational switch
    • Golynskiy M.V., et al. Antibody detection by using a FRET-based protein conformational switch. Chembiochem 2010, 11:2264-2267.
    • (2010) Chembiochem , vol.11 , pp. 2264-2267
    • Golynskiy, M.V.1
  • 57
    • 84909619329 scopus 로고    scopus 로고
    • Protease-based synthetic sensing and signal amplification
    • Stein V., Alexandrov A. Protease-based synthetic sensing and signal amplification. Proc. Natl. Acad. Sci. U.S.A. 2014, 111:15934-15939.
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 15934-15939
    • Stein, V.1    Alexandrov, A.2
  • 58
    • 84904995490 scopus 로고    scopus 로고
    • Illuminating cell signalling with optogenetic tools
    • Tischer D., Weiner O.D. Illuminating cell signalling with optogenetic tools. Nat. Rev. Mol. Cell Biol. 2014, 15:551-558.
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 551-558
    • Tischer, D.1    Weiner, O.D.2
  • 59
    • 69949104482 scopus 로고    scopus 로고
    • A genetically encoded photoactivatable Rac controls the motility of living cells
    • Wu Y.I., et al. A genetically encoded photoactivatable Rac controls the motility of living cells. Nature 2009, 461:104-108.
    • (2009) Nature , vol.461 , pp. 104-108
    • Wu, Y.I.1
  • 60
    • 84908057379 scopus 로고    scopus 로고
    • Manipulation of endogenous kinase activity in living cells using photoswitchable inhibitory peptides
    • Yi J.J., et al. Manipulation of endogenous kinase activity in living cells using photoswitchable inhibitory peptides. ACS Synth. Biol. 2014, 3:788-795.
    • (2014) ACS Synth. Biol. , vol.3 , pp. 788-795
    • Yi, J.J.1
  • 61
    • 84862777445 scopus 로고    scopus 로고
    • TULIPs: tunable, light-controlled interacting protein tags for cell biology
    • Strickland D., et al. TULIPs: tunable, light-controlled interacting protein tags for cell biology. Nat. Methods 2012, 9:379-384.
    • (2012) Nat. Methods , vol.9 , pp. 379-384
    • Strickland, D.1
  • 62
    • 84912094108 scopus 로고    scopus 로고
    • Orthogonal optogenetic triple-gene control in mammalian cells
    • Muller K., et al. Orthogonal optogenetic triple-gene control in mammalian cells. ACS Synth. Biol. 2014, 3:796-801.
    • (2014) ACS Synth. Biol. , vol.3 , pp. 796-801
    • Muller, K.1
  • 63
    • 84892142058 scopus 로고    scopus 로고
    • A fully genetically encoded protein architecture for optical control of peptide ligand concentration
    • Schmidt D., et al. A fully genetically encoded protein architecture for optical control of peptide ligand concentration. Nat. Commun. 2014, 5:3019.
    • (2014) Nat. Commun. , vol.5 , pp. 3019
    • Schmidt, D.1
  • 64
    • 84860133612 scopus 로고    scopus 로고
    • Designing photoswitchable peptides using the AsLOV2 domain
    • Lungu O.I., et al. Designing photoswitchable peptides using the AsLOV2 domain. Chem. Biol. 2012, 19:507-517.
    • (2012) Chem. Biol. , vol.19 , pp. 507-517
    • Lungu, O.I.1
  • 65
    • 84904480201 scopus 로고    scopus 로고
    • Engineering light-inducible nuclear localization signals for precise spatiotemporal control of protein dynamics in living cells
    • Niopek D., et al. Engineering light-inducible nuclear localization signals for precise spatiotemporal control of protein dynamics in living cells. Nat. Commun. 2014, 5:4404.
    • (2014) Nat. Commun. , vol.5 , pp. 4404
    • Niopek, D.1
  • 66
    • 84868556564 scopus 로고    scopus 로고
    • Optical control of protein activity by fluorescent protein domains
    • Zhou X.X., et al. Optical control of protein activity by fluorescent protein domains. Science 2012, 338:810-814.
    • (2012) Science , vol.338 , pp. 810-814
    • Zhou, X.X.1
  • 67
    • 70350070364 scopus 로고    scopus 로고
    • Spatiotemporal control of cell signalling using a light-switchable protein interaction
    • Levskaya A., et al. Spatiotemporal control of cell signalling using a light-switchable protein interaction. Nature 2009, 461:997-1001.
    • (2009) Nature , vol.461 , pp. 997-1001
    • Levskaya, A.1
  • 68
    • 84890036078 scopus 로고    scopus 로고
    • Using optogenetics to interrogate the dynamic control of signal transmission by the Ras/Erk module
    • Toettcher J.E., et al. Using optogenetics to interrogate the dynamic control of signal transmission by the Ras/Erk module. Cell 2013, 155:1422-1434.
    • (2013) Cell , vol.155 , pp. 1422-1434
    • Toettcher, J.E.1
  • 69
    • 84900874407 scopus 로고    scopus 로고
    • Optogenetic control of protein kinase activity in mammalian cells
    • Wend S., et al. Optogenetic control of protein kinase activity in mammalian cells. ACS Synth. Biol. 2014, 3:280-285.
    • (2014) ACS Synth. Biol. , vol.3 , pp. 280-285
    • Wend, S.1
  • 70
    • 77954519891 scopus 로고    scopus 로고
    • Engineered allosteric activation of kinases in living cells
    • Karginov A.V., et al. Engineered allosteric activation of kinases in living cells. Nat. Biotechnol. 2010, 28:743-747.
    • (2010) Nat. Biotechnol. , vol.28 , pp. 743-747
    • Karginov, A.V.1
  • 71
    • 84906679884 scopus 로고    scopus 로고
    • Engineered kinase activation reveals unique morphodynamic phenotypes and associated trafficking for Src family isoforms
    • Chu P.H., et al. Engineered kinase activation reveals unique morphodynamic phenotypes and associated trafficking for Src family isoforms. Proc. Natl. Acad. Sci. U.S.A. 2014, 111:12420-12425.
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 12420-12425
    • Chu, P.H.1
  • 72
    • 84897021544 scopus 로고    scopus 로고
    • Dissecting motility signaling through activation of specific Src-effector complexes
    • Karginov A.V., et al. Dissecting motility signaling through activation of specific Src-effector complexes. Nat. Chem. Biol. 2014, 10:286-290.
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 286-290
    • Karginov, A.V.1
  • 73
    • 84876882853 scopus 로고    scopus 로고
    • Rational design of a ligand-controlled protein conformational switch
    • Dagliyan O., et al. Rational design of a ligand-controlled protein conformational switch. Proc. Natl. Acad. Sci. U.S.A. 2013, 110:6800-6804.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 6800-6804
    • Dagliyan, O.1
  • 74
    • 0041854719 scopus 로고    scopus 로고
    • Conditional protein splicing: a new tool to control protein structure and function in vitro and in vivo
    • Mootz H.D., et al. Conditional protein splicing: a new tool to control protein structure and function in vitro and in vivo. J. Am. Chem. Soc. 2003, 125:10561-10569.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 10561-10569
    • Mootz, H.D.1
  • 75
    • 6044271721 scopus 로고    scopus 로고
    • Activation of an autoregulated protein kinase by conditional protein splicing
    • Mootz H.D., et al. Activation of an autoregulated protein kinase by conditional protein splicing. Angew. Chem. 2004, 43:5189-5192.
    • (2004) Angew. Chem. , vol.43 , pp. 5189-5192
    • Mootz, H.D.1
  • 76
    • 84907366061 scopus 로고    scopus 로고
    • A designer cell-based histamine-specific human allergy profiler
    • Auslander D., et al. A designer cell-based histamine-specific human allergy profiler. Nat. Commun. 2014, 5:4408.
    • (2014) Nat. Commun. , vol.5 , pp. 4408
    • Auslander, D.1
  • 77
    • 84905569769 scopus 로고    scopus 로고
    • 2 transgene-control device
    • 2 transgene-control device. Mol. Cell 2014, 55:397-408.
    • (2014) Mol. Cell , vol.55 , pp. 397-408
    • Auslander, D.1
  • 78
    • 84872001455 scopus 로고    scopus 로고
    • Pharmaceutically controlled designer circuit for the treatment of the metabolic syndrome
    • Ye H., et al. Pharmaceutically controlled designer circuit for the treatment of the metabolic syndrome. Proc. Natl. Acad. Sci. U.S.A. 2013, 110:141-146.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 141-146
    • Ye, H.1
  • 79
    • 84887315800 scopus 로고    scopus 로고
    • Reward-based hypertension control by a synthetic brain-dopamine interface
    • Rossger K., et al. Reward-based hypertension control by a synthetic brain-dopamine interface. Proc. Natl. Acad. Sci. U.S.A. 2013, 110:18150-18155.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 18150-18155
    • Rossger, K.1
  • 80
    • 77951159012 scopus 로고    scopus 로고
    • Rapid diversification of cell signaling phenotypes by modular domain recombination
    • Peisajovich S.G., et al. Rapid diversification of cell signaling phenotypes by modular domain recombination. Science 2010, 328:368-372.
    • (2010) Science , vol.328 , pp. 368-372
    • Peisajovich, S.G.1
  • 81
    • 40849100220 scopus 로고    scopus 로고
    • Using engineered scaffold interactions to reshape MAP kinase pathway signaling dynamics
    • Bashor C.J., et al. Using engineered scaffold interactions to reshape MAP kinase pathway signaling dynamics. Science 2008, 319:1539-1543.
    • (2008) Science , vol.319 , pp. 1539-1543
    • Bashor, C.J.1
  • 82
    • 0037436155 scopus 로고    scopus 로고
    • Rewiring MAP kinase pathways using alternative scaffold assembly mechanisms
    • Park S.H., et al. Rewiring MAP kinase pathways using alternative scaffold assembly mechanisms. Science 2003, 299:1061-1064.
    • (2003) Science , vol.299 , pp. 1061-1064
    • Park, S.H.1
  • 83
    • 84868087234 scopus 로고    scopus 로고
    • Engineering robust control of two-component system phosphotransfer using modular scaffolds
    • Whitaker W.R., et al. Engineering robust control of two-component system phosphotransfer using modular scaffolds. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:18090-18095.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 18090-18095
    • Whitaker, W.R.1
  • 84
    • 34249894454 scopus 로고    scopus 로고
    • Rewiring cellular morphology pathways with synthetic guanine nucleotide exchange factors
    • Yeh B.J., et al. Rewiring cellular morphology pathways with synthetic guanine nucleotide exchange factors. Nature 2007, 447:596-600.
    • (2007) Nature , vol.447 , pp. 596-600
    • Yeh, B.J.1
  • 85
    • 84913557652 scopus 로고    scopus 로고
    • A set of computationally designed orthogonal antiparallel homodimers that expands the synthetic coiled-coil toolkit
    • Negron C., Keating A.E. A set of computationally designed orthogonal antiparallel homodimers that expands the synthetic coiled-coil toolkit. J. Am. Chem. Soc. 2014, 136:16544-16556.
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 16544-16556
    • Negron, C.1    Keating, A.E.2
  • 86
    • 84868149942 scopus 로고    scopus 로고
    • SYNZIP protein interaction toolbox: in vitro and in vivo specifications of heterospecific coiled-coil interaction domains
    • Thompson K.E., et al. SYNZIP protein interaction toolbox: in vitro and in vivo specifications of heterospecific coiled-coil interaction domains. ACS Synth. Biol. 2012, 1:118-129.
    • (2012) ACS Synth. Biol. , vol.1 , pp. 118-129
    • Thompson, K.E.1
  • 87
    • 0141483011 scopus 로고    scopus 로고
    • Redirecting tyrosine kinase signaling to an apoptotic caspase pathway through chimeric adaptor proteins
    • Howard P.L., et al. Redirecting tyrosine kinase signaling to an apoptotic caspase pathway through chimeric adaptor proteins. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:11267-11272.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 11267-11272
    • Howard, P.L.1
  • 88
    • 38349092683 scopus 로고    scopus 로고
    • The genetic design of signaling cascades to record receptor activation
    • Barnea G., et al. The genetic design of signaling cascades to record receptor activation. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:64-69.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 64-69
    • Barnea, G.1
  • 89
    • 79953214378 scopus 로고    scopus 로고
    • Studying G protein-coupled receptor activation using split-tobacco etch virus assays
    • Djannatian M.S., et al. Studying G protein-coupled receptor activation using split-tobacco etch virus assays. Anal. Biochem. 2011, 412:141-152.
    • (2011) Anal. Biochem. , vol.412 , pp. 141-152
    • Djannatian, M.S.1
  • 90
    • 74049115093 scopus 로고    scopus 로고
    • Integrated analysis of receptor activation and downstream signaling with EXTassays
    • Botvinnik A., et al. Integrated analysis of receptor activation and downstream signaling with EXTassays. Nat. Methods 2010, 7:74-80.
    • (2010) Nat. Methods , vol.7 , pp. 74-80
    • Botvinnik, A.1
  • 91
    • 48249132027 scopus 로고    scopus 로고
    • Analysis of transient phosphorylation-dependent protein-protein interactions in living mammalian cells using split-TEV
    • Wehr M.C., et al. Analysis of transient phosphorylation-dependent protein-protein interactions in living mammalian cells using split-TEV. BMC Biotechnol. 2008, 8:55.
    • (2008) BMC Biotechnol. , vol.8 , pp. 55
    • Wehr, M.C.1
  • 92
    • 33751217186 scopus 로고    scopus 로고
    • Monitoring regulated protein-protein interactions using split TEV
    • Wehr M.C., et al. Monitoring regulated protein-protein interactions using split TEV. Nat. Methods 2006, 3:985-993.
    • (2006) Nat. Methods , vol.3 , pp. 985-993
    • Wehr, M.C.1
  • 93
    • 84871721147 scopus 로고    scopus 로고
    • Salt-inducible kinases regulate growth through the Hippo signalling pathway in Drosophila
    • Wehr M.C., et al. Salt-inducible kinases regulate growth through the Hippo signalling pathway in Drosophila. Nat. Cell Biol. 2013, 15:61-71.
    • (2013) Nat. Cell Biol. , vol.15 , pp. 61-71
    • Wehr, M.C.1
  • 94
    • 84916202038 scopus 로고    scopus 로고
    • Modular extracellular sensor architecture for engineering mammalian cell-based devices
    • Published online February 25, 2014.
    • Daringer N.M., et al. Modular extracellular sensor architecture for engineering mammalian cell-based devices. ACS Synth. Biol. 2014, Published online February 25, 2014. http://dx.doi.org/10.1021/sb400128g.
    • (2014) ACS Synth. Biol.
    • Daringer, N.M.1
  • 95
    • 77955620283 scopus 로고    scopus 로고
    • Activation of specific apoptotic caspases with an engineered small-molecule-activated protease
    • Gray D.C., et al. Activation of specific apoptotic caspases with an engineered small-molecule-activated protease. Cell 2010, 142:637-646.
    • (2010) Cell , vol.142 , pp. 637-646
    • Gray, D.C.1
  • 96
    • 84858189214 scopus 로고    scopus 로고
    • TIPI: TEV protease-mediated induction of protein instability
    • Taxis C., Knop M. TIPI: TEV protease-mediated induction of protein instability. Methods Mol. Biol. 2012, 832:611-626.
    • (2012) Methods Mol. Biol. , vol.832 , pp. 611-626
    • Taxis, C.1    Knop, M.2
  • 97
    • 84861210856 scopus 로고    scopus 로고
    • The N-end rule pathway
    • Tasaki T., et al. The N-end rule pathway. Annu. Rev. Biochem. 2012, 81:261-289.
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 261-289
    • Tasaki, T.1
  • 98
    • 84880962137 scopus 로고    scopus 로고
    • Building robust functionality in synthetic circuits using engineered feedback regulation
    • Chen S., et al. Building robust functionality in synthetic circuits using engineered feedback regulation. Curr. Opin. Biotechnol. 2013, 24:790-796.
    • (2013) Curr. Opin. Biotechnol. , vol.24 , pp. 790-796
    • Chen, S.1


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