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Volumn 38, Issue 8, 2010, Pages 2663-2675

Strategies for protein synthetic biology

Author keywords

[No Author keywords available]

Indexed keywords

DNA FRAGMENT; DNA; PROTEIN; SIGNAL PEPTIDE;

EID: 77952473769     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkq139     Document Type: Article
Times cited : (92)

References (136)
  • 1
    • 0034212551 scopus 로고    scopus 로고
    • Engineering stability in gene networks by autoregulation
    • Becskei,A. and Serrano,L. (2000) Engineering stability in gene networks by autoregulation. Nature, 405, 590-593.
    • (2000) Nature , vol.405 , pp. 590-593
    • Becskei, A.1    Serrano, L.2
  • 2
    • 17144456808 scopus 로고    scopus 로고
    • Positive feedback in eukaryotic gene networks: cell differentiation by graded to binary response conversion
    • Becskei,A., Seraphin,B. and Serrano,L. (2001) Positive feedback in eukaryotic gene networks: cell differentiation by graded to binary response conversion. EMBO J., 20, 2528-2535.
    • (2001) EMBO J. , vol.20 , pp. 2528-2535
    • Becskei, A.1    Seraphin, B.2    Serrano, L.3
  • 3
    • 0034688173 scopus 로고    scopus 로고
    • A synthetic oscillatory network of transcriptional regulators
    • Elowitz,M. and Leibler,S. (2000) A synthetic oscillatory network of transcriptional regulators. Nature, 403, 335-338.
    • (2000) Nature , vol.403 , pp. 335-338
    • Elowitz, M.1    Leibler, S.2
  • 4
    • 0034688174 scopus 로고    scopus 로고
    • Construction of a genetic toggle switch in Escherichia coli
    • Gardner,T.S., Cantor,C.R. and Collins,J.J. (2000) Construction of a genetic toggle switch in Escherichia coli. Nature, 403, 339-342.
    • (2000) Nature , vol.403 , pp. 339-342
    • Gardner, T.S.1    Cantor, C.R.2    Collins, J.J.3
  • 5
    • 22144452865 scopus 로고    scopus 로고
    • Hysteresis in a synthetic mammalian gene network
    • Kramer,B.P. and Fussenegger,M. (2005) Hysteresis in a synthetic mammalian gene network. Proc. Natl Acad. Sci. USA, 102, 9517-9522.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 9517-9522
    • Kramer, B.P.1    Fussenegger, M.2
  • 7
    • 67149138163 scopus 로고    scopus 로고
    • Protein sequestration generates a flexible ultrasensitive response in a genetic network
    • Buchler,N.E. and Cross,F.R. (2009) Protein sequestration generates a flexible ultrasensitive response in a genetic network. Mol. Syst. Biol., 5, 272-272.
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 272-1272
    • Buchler, N.E.1    Cross, F.R.2
  • 10
    • 70349308508 scopus 로고    scopus 로고
    • Cell regulation: determined to signal discrete cooperation
    • Gibson,T.J. (2009) Cell regulation: determined to signal discrete cooperation. Trends Biochem. Sci., 34, 471-482.
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 471-482
    • Gibson, T.J.1
  • 11
    • 9944237833 scopus 로고    scopus 로고
    • Complementarity of structure ensembles in protein-protein binding
    • Grünberg,R., Leckner,J. and Nilges,M. (2004) Complementarity of structure ensembles in protein-protein binding. Structure, 12, 2125-2136.
    • (2004) Structure , vol.12 , pp. 2125-2136
    • Grünberg, R.1    Leckner, J.2    Nilges, M.3
  • 12
    • 33645994825 scopus 로고    scopus 로고
    • Flexibility and conformational entropy in protein-protein binding
    • Grünberg,R., Nilges,M. and Leckner,J. (2006) Flexibility and conformational entropy in protein-protein binding. Structure, 14, 683-693.
    • (2006) Structure , vol.14 , pp. 683-693
    • Grünberg, R.1    Nilges, M.2    Leckner, J.3
  • 13
    • 28544451327 scopus 로고    scopus 로고
    • Foundations for engineering biology
    • Endy,D. (2005) Foundations for engineering biology. Nature, 438, 449-453.
    • (2005) Nature , vol.438 , pp. 449-453
    • Endy, D.1
  • 14
    • 46949091517 scopus 로고    scopus 로고
    • Refinement and standardization of synthetic biological parts and devices
    • Canton,B., Labno,A. and Endy,D. (2008) Refinement and standardization of synthetic biological parts and devices. Nat. Biotechnol., 26, 787-793.
    • (2008) Nat. Biotechnol. , vol.26 , pp. 787-793
    • Canton, B.1    Labno, A.2    Endy, D.3
  • 15
    • 33745454125 scopus 로고    scopus 로고
    • Synthetic biology: new engineering rules for an emerging discipline
    • 2006.0028
    • Andrianantoandro,E., Basu,S., Karig,D.K. and Weiss,R. (2006) Synthetic biology: new engineering rules for an emerging discipline. Mol. Syst. Biol., 2, 2006.0028.
    • (2006) Mol. Syst. Biol. , vol.2
    • Andrianantoandro, E.1    Basu, S.2    Karig, D.K.3    Weiss, R.4
  • 19
    • 64649101249 scopus 로고    scopus 로고
    • Long-timescale molecular dynamics simulations of protein structure and function
    • Klepeis,J.L., Lindorff-Larsen,K., Dror,R.O. and Shaw,D.E. (2009) Long-timescale molecular dynamics simulations of protein structure and function. Curr. Opin. Struct. Biol., 19, 120-127.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 120-127
    • Klepeis, J.L.1    Lindorff-Larsen, K.2    Dror, R.O.3    Shaw, D.E.4
  • 20
    • 77954102643 scopus 로고    scopus 로고
    • Protein design in biological networks: from manipulating the input to modifying the output
    • Van der Sloot,A.M., Kiel,C., Serrano,L. and Stricher,F. (2009) Protein design in biological networks: from manipulating the input to modifying the output. Protein Eng. Des. Sel., 22, 537-542.
    • (2009) Protein Eng. Des. Sel. , vol.22 , pp. 537-542
    • Van der Sloot, A.M.1    Kiel, C.2    Serrano, L.3    Stricher, F.4
  • 21
    • 41949132916 scopus 로고    scopus 로고
    • Flexible ligand docking to multiple receptor conformations: a practical alternative
    • Totrov,M. and Abagyan,R. (2008) Flexible ligand docking to multiple receptor conformations: a practical alternative. Curr. Opin. Struct. Biol., 18, 178-184.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 178-184
    • Totrov, M.1    Abagyan, R.2
  • 22
    • 74249119329 scopus 로고    scopus 로고
    • Critical assessment of methods of protein structure prediction - round VIII
    • Moult,J., Fidelis,K., Kryshtafovych,A., Rost,B. and Tramontano,A. (2009) Critical assessment of methods of protein structure prediction - round VIII. Proteins, 77(Suppl. 9), 1-4.
    • (2009) Proteins , vol.77 , Issue.SUPPL. 9 , pp. 1-4
    • Moult, J.1    Fidelis, K.2    Kryshtafovych, A.3    Rost, B.4    Tramontano, A.5
  • 23
    • 41949111630 scopus 로고    scopus 로고
    • Recent progress and future directions in protein-protein docking
    • Ritchie,D.W. (2008) Recent progress and future directions in protein-protein docking. Curr. Protein Pept. Sci., 9, 1-15.
    • (2008) Curr. Protein Pept. Sci. , vol.9 , pp. 1-15
    • Ritchie, D.W.1
  • 24
    • 62649171253 scopus 로고    scopus 로고
    • Frameworks for programming biological function through RNA parts and devices
    • Win,M.N., Liang,J.C. and Smolke,C.D. (2009) Frameworks for programming biological function through RNA parts and devices. Chem. Biol., 16, 298-310.
    • (2009) Chem. Biol. , vol.16 , pp. 298-310
    • Win, M.N.1    Liang, J.C.2    Smolke, C.D.3
  • 25
    • 36248972215 scopus 로고    scopus 로고
    • Engineering entropy-driven reactions and networks catalyzed by DNA
    • Zhang,D.Y., Turberfield,A.J., Yurke,B. and Winfree,E. (2007) Engineering entropy-driven reactions and networks catalyzed by DNA. Science, 318, 1121-1125.
    • (2007) Science , vol.318 , pp. 1121-1125
    • Zhang, D.Y.1    Turberfield, A.J.2    Yurke, B.3    Winfree, E.4
  • 26
    • 43049123356 scopus 로고    scopus 로고
    • Advances in laboratory evolution of enzymes
    • Bershtein,S. and Tawfik,D.S. (2008) Advances in laboratory evolution of enzymes. Curr. Opin. Chem. Biol., 12, 151-158.
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 151-158
    • Bershtein, S.1    Tawfik, D.S.2
  • 29
    • 0029064652 scopus 로고
    • Rational design of aromatic polyketide natural products by recombinant assembly of enzymatic subunits
    • McDaniel,R., Ebert-Khosla,S., Hopwood,D.A. and Khosla,C. (1995) Rational design of aromatic polyketide natural products by recombinant assembly of enzymatic subunits. Nature, 375, 549-554.
    • (1995) Nature , vol.375 , pp. 549-554
    • McDaniel, R.1    Ebert-Khosla, S.2    Hopwood, D.A.3    Khosla, C.4
  • 30
    • 23644452792 scopus 로고    scopus 로고
    • Engineered proteins as specific binding reagents
    • Binz,H.K. and Plückthun,A. (2005) Engineered proteins as specific binding reagents. Curr. Opin. Biotechnol., 16, 459-469.
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 459-469
    • Binz, H.K.1    Plückthun, A.2
  • 31
    • 34848919535 scopus 로고    scopus 로고
    • Multiple display of catalytic modules on a protein scaffold: nano-fabrication of enzyme particles
    • Heyman,A., Barak,Y., Caspi,J., Wilson,D.B., Altman,A., Bayer,E.A. and Shoseyov,O. (2007) Multiple display of catalytic modules on a protein scaffold: nano-fabrication of enzyme particles. J. Biotechnol., 131, 433-439.
    • (2007) J. Biotechnol. , vol.131 , pp. 433-439
    • Heyman, A.1    Barak, Y.2    Caspi, J.3    Wilson, D.B.4    Altman, A.5    Bayer, E.A.6    Shoseyov, O.7
  • 32
    • 39149098445 scopus 로고    scopus 로고
    • Designed armadillo repeat proteins as general peptide-binding scaffolds: consensus design and computational optimization of the hydrophobic core
    • Parmeggiani,F., Pellarin,R., Larsen,A.P., Varadamsetty,G., Stumpp,M.T., Zerbe,O., Caflisch,A. and Plückthun,A. (2008) Designed armadillo repeat proteins as general peptide-binding scaffolds: consensus design and computational optimization of the hydrophobic core. J. Mol. Biol., 376, 1282-1304.
    • (2008) J. Mol. Biol. , vol.376 , pp. 1282-1304
    • Parmeggiani, F.1    Pellarin, R.2    Larsen, A.P.3    Varadamsetty, G.4    Stumpp, M.T.5    Zerbe, O.6    Caflisch, A.7    Plückthun, A.8
  • 33
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • Pawson,T. and Nash,P. (2003) Assembly of cell regulatory systems through protein interaction domains. Science, 300, 445-452.
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 34
    • 20444414545 scopus 로고    scopus 로고
    • Linear motifs: evolutionary interaction switches
    • Neduva,V. and Russell,R.B. (2005) Linear motifs: evolutionary interaction switches. FEBS Lett., 579, 3342-3345.
    • (2005) FEBS Lett. , vol.579 , pp. 3342-3345
    • Neduva, V.1    Russell, R.B.2
  • 36
    • 62649096826 scopus 로고    scopus 로고
    • Designing new cellular signaling pathways
    • Pryciak,P.M. (2009) Designing new cellular signaling pathways. Chem. Biol., 16, 249-254.
    • (2009) Chem. Biol. , vol.16 , pp. 249-254
    • Pryciak, P.M.1
  • 37
    • 68549087161 scopus 로고    scopus 로고
    • Scaffolds: interaction platforms for cellular signalling circuits
    • Zeke,A., Lukács,M., Lim,W.A. and Reményi,A. (2009) Scaffolds: interaction platforms for cellular signalling circuits. Trends Cell Biol., 19, 364-374.
    • (2009) Trends Cell Biol. , vol.19 , pp. 364-374
    • Zeke, A.1    Lukács, M.2    Lim, W.A.3    Reményi, A.4
  • 38
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring and adaptor proteins
    • Pawson,T. and Scott,J.D. (1997) Signaling through scaffold, anchoring and adaptor proteins. Science, 278, 2075-2080.
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 39
    • 0035960710 scopus 로고    scopus 로고
    • Role of scaffolds in MAP kinase pathway specificity revealed by custom design of pathway-dedicated signaling proteins
    • Harris,K., Lamson,R.E., Nelson,B., Hughes,T.R., Marton,M.J., Roberts,C.J., Boone,C. and Pryciak,P.M. (2001) Role of scaffolds in MAP kinase pathway specificity revealed by custom design of pathway-dedicated signaling proteins. Curr. Biol., 11, 1815-1824.
    • (2001) Curr. Biol. , vol.11 , pp. 1815-1824
    • Harris, K.1    Lamson, R.E.2    Nelson, B.3    Hughes, T.R.4    Marton, M.J.5    Roberts, C.J.6    Boone, C.7    Pryciak, P.M.8
  • 40
    • 0037436155 scopus 로고    scopus 로고
    • Rewiring MAP kinase pathways using alternative scaffold assembly mechanisms
    • Park,S., Zarrinpar,A. and Lim,W.A. (2003) Rewiring MAP kinase pathways using alternative scaffold assembly mechanisms. Science, 299, 1061-1064.
    • (2003) Science , vol.299 , pp. 1061-1064
    • Park, S.1    Zarrinpar, A.2    Lim, W.A.3
  • 41
    • 26244444772 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase (MAPK)-docking sites in MAPK kinases function as tethers that are crucial for MAPK regulation in vivo
    • Grewal,S., Molina,D. and Bardwell,L. (2006) Mitogen-activated protein kinase (MAPK)-docking sites in MAPK kinases function as tethers that are crucial for MAPK regulation in vivo. Cell. Signal., 18, 123-134.
    • (2006) Cell. Signal. , vol.18 , pp. 123-134
    • Grewal, S.1    Molina, D.2    Bardwell, L.3
  • 42
    • 40849100220 scopus 로고    scopus 로고
    • Using engineered scaffold interactions to reshape MAP kinase pathway signaling dynamics
    • Bashor,C.J., Helman,N.C., Yan,S. and Lim,W.A. (2008) Using engineered scaffold interactions to reshape MAP kinase pathway signaling dynamics. Science, 319, 1539-1543.
    • (2008) Science , vol.319 , pp. 1539-1543
    • Bashor, C.J.1    Helman, N.C.2    Yan, S.3    Lim, W.A.4
  • 43
    • 41549124543 scopus 로고    scopus 로고
    • Membrane recruitment of scaffold proteins drives specific signaling
    • Pincet,F. (2007) Membrane recruitment of scaffold proteins drives specific signaling. PLoS ONE, 2, e977.
    • (2007) PLoS ONE , vol.2
    • Pincet, F.1
  • 44
    • 49649109812 scopus 로고    scopus 로고
    • Membrane localization of scaffold proteins promotes graded signaling in the yeast MAP kinase cascade
    • Takahashi,S. and Pryciak,P.M. (2008) Membrane localization of scaffold proteins promotes graded signaling in the yeast MAP kinase cascade. Curr. Biol. CB, 18, 1184-1191.
    • (2008) Curr. Biol. CB , vol.18 , pp. 1184-1191
    • Takahashi, S.1    Pryciak, P.M.2
  • 45
    • 0032168881 scopus 로고    scopus 로고
    • Membrane recruitment of the kinase cascade scaffold protein ste5 by the gbetagamma complex underlies activation of the yeast pheromone response pathway
    • Pryciak,P.M. and Huntress,F.A. (1998) Membrane recruitment of the kinase cascade scaffold protein ste5 by the gbetagamma complex underlies activation of the yeast pheromone response pathway. Genes Dev., 12, 2684-2697.
    • (1998) Genes Dev. , vol.12 , pp. 2684-2697
    • Pryciak, P.M.1    Huntress, F.A.2
  • 46
    • 0035203511 scopus 로고    scopus 로고
    • MAP kinase dynamics in response to pheromones in budding yeast
    • vanDrogen,F., Stucke,V.M., Jorritsma,G. and Peter,M. (2001) MAP kinase dynamics in response to pheromones in budding yeast. Nat. Cell Biol., 3, 1051-1059.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 1051-1059
    • vanDrogen, F.1    Stucke, V.M.2    Jorritsma, G.3    Peter, M.4
  • 47
    • 35748968807 scopus 로고    scopus 로고
    • Spatial regulation of fus3 MAP kinase activity through a reaction-diffusion mechanism in yeast pheromone signalling
    • Maeder,C.I., Hink,M.A., Kinkhabwala,A., Mayr,R., Bastiaens,P.I.H. and Knop,M. (2007) Spatial regulation of fus3 MAP kinase activity through a reaction-diffusion mechanism in yeast pheromone signalling. Nat. Cell Biol., 9, 1319-1326.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1319-1326
    • Maeder, C.I.1    Hink, M.A.2    Kinkhabwala, A.3    Mayr, R.4    Bastiaens, P.I.H.5    Knop, M.6
  • 48
    • 25844442435 scopus 로고    scopus 로고
    • A membrane binding domain in the ste5 scaffold synergizes with Gβγ binding to control localization and signaling in pheromone response
    • Winters,M.J., Lamson,R.E., Nakanishi,H., Neiman,A.M. and Pryciak,P.M. (2005) A membrane binding domain in the ste5 scaffold synergizes with Gβγ binding to control localization and signaling in pheromone response. Mol. Cell, 20, 21-32.
    • (2005) Mol. Cell , vol.20 , pp. 21-32
    • Winters, M.J.1    Lamson, R.E.2    Nakanishi, H.3    Neiman, A.M.4    Pryciak, P.M.5
  • 49
    • 37049012678 scopus 로고    scopus 로고
    • Identification of novel membrane-binding domains in multiple yeast cdc42 effectors
    • Takahashi,S. and Pryciak,P.M. (2007) Identification of novel membrane-binding domains in multiple yeast cdc42 effectors. Mol. Biol. Cell, 18, 4945-4956.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4945-4956
    • Takahashi, S.1    Pryciak, P.M.2
  • 50
    • 34547216984 scopus 로고    scopus 로고
    • Function and regulation in MAPK signaling pathways: lessons learned from the yeast saccharomyces cerevisiae
    • Chen,R.E. and Thorner,J. (2007) Function and regulation in MAPK signaling pathways: lessons learned from the yeast saccharomyces cerevisiae. Biochim. Biophys. Acta, 1773, 1311-1340.
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 1311-1340
    • Chen, R.E.1    Thorner, J.2
  • 51
    • 34047258309 scopus 로고    scopus 로고
    • Positive-feedback loops as a flexible biological module
    • Ingolia,N.T. and Murray,A.W. (2007) Positive-feedback loops as a flexible biological module. Curr. Biol. CB, 17, 668-677.
    • (2007) Curr. Biol. CB , vol.17 , pp. 668-677
    • Ingolia, N.T.1    Murray, A.W.2
  • 52
    • 0141483011 scopus 로고    scopus 로고
    • Redirecting tyrosine kinase signaling to an apoptotic caspase pathway through chimeric adaptor proteins
    • Howard,P.L., Chia,M.C., Rizzo,S.D., Liu,F. and Pawson,T. (2003) Redirecting tyrosine kinase signaling to an apoptotic caspase pathway through chimeric adaptor proteins. Proc. Natl Acad. Sci. USA, 100, 11267-11272.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 11267-11272
    • Howard, P.L.1    Chia, M.C.2    Rizzo, S.D.3    Liu, F.4    Pawson, T.5
  • 53
    • 0030013607 scopus 로고    scopus 로고
    • Controlling protein association and subcellular localization with a synthetic ligand that induces heterodimerization of proteins
    • Belshaw,P.J., Ho,S.N., Crabtree,G.R. and Schreiber,S.L. (1996) Controlling protein association and subcellular localization with a synthetic ligand that induces heterodimerization of proteins. Proc. Natl Acad. Sci. USA, 93, 4604-4607.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 4604-4607
    • Belshaw, P.J.1    Ho, S.N.2    Crabtree, G.R.3    Schreiber, S.L.4
  • 54
    • 0030878873 scopus 로고    scopus 로고
    • Inducible gene expression and protein translocation using nontoxic ligands identified by a mammalian three-hybrid screen
    • Liberles,S.D., Diver,S.T., Austin,D.J. and Schreiber,S.L. (1997) Inducible gene expression and protein translocation using nontoxic ligands identified by a mammalian three-hybrid screen. Proc. Natl Acad. Sci. USA, 94, 7825-7830.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 7825-7830
    • Liberles, S.D.1    Diver, S.T.2    Austin, D.J.3    Schreiber, S.L.4
  • 56
    • 16844385435 scopus 로고    scopus 로고
    • Characterization of the FKBP.rapamycin FRB ternary complex
    • Banaszynski,L.A., Liu,C.W. and Wandless,T.J. (2005) Characterization of the FKBP.rapamycin.FRB ternary complex. J. Am. Chem. Soc., 127, 4715-4721.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 4715-4721
    • Banaszynski, L.A.1    Liu, C.W.2    Wandless, T.J.3
  • 59
    • 0033535537 scopus 로고    scopus 로고
    • Inducible recruitment of cdc42 or WASP to a cell-surface receptor triggers actin polymerization and filopodium formation
    • Castellano,F., Montcourrier,P., Guillemot,J.C., Gouin,E., Machesky,L., Cossart,P. and Chavrier,P. (1999) Inducible recruitment of cdc42 or WASP to a cell-surface receptor triggers actin polymerization and filopodium formation. Curr. Biol. CB, 9, 351-360.
    • (1999) Curr. Biol. CB , vol.9 , pp. 351-360
    • Castellano, F.1    Montcourrier, P.2    Guillemot, J.C.3    Gouin, E.4    Machesky, L.5    Cossart, P.6    Chavrier, P.7
  • 60
    • 21444442055 scopus 로고    scopus 로고
    • An inducible translocation strategy to rapidly activate and inhibit small GTPase signaling pathways
    • Inoue,T., Heo,W.D., Grimley,J.S., Wandless,T.J. and Meyer,T. (2005) An inducible translocation strategy to rapidly activate and inhibit small GTPase signaling pathways. Nat. Methods, 2, 415-418.
    • (2005) Nat. Methods , vol.2 , pp. 415-418
    • Inoue, T.1    Heo, W.D.2    Grimley, J.S.3    Wandless, T.J.4    Meyer, T.5
  • 61
    • 33845310879 scopus 로고    scopus 로고
    • Rapid chemically induced changes of PtdIns(4,5)P2 gate KCNQ ion channels
    • Suh,B., Inoue,T., Meyer,T. and Hille,B. (2006) Rapid chemically induced changes of PtdIns(4,5)P2 gate KCNQ ion channels. Science, 314, 1454-1457.
    • (2006) Science , vol.314 , pp. 1454-1457
    • Suh, B.1    Inoue, T.2    Meyer, T.3    Hille, B.4
  • 62
    • 52449120635 scopus 로고    scopus 로고
    • Synthetic activation of endogenous PI3K and rac identifies an AND-Gate switch for cell polarization and migration
    • Inoue,T., Meyer,T. and Insall,R. (2008) Synthetic activation of endogenous PI3K and rac identifies an AND-Gate switch for cell polarization and migration. PLoS ONE, 3, e3068.
    • (2008) PLoS ONE , vol.3
    • Inoue, T.1    Meyer, T.2    Insall, R.3
  • 63
    • 70350070364 scopus 로고    scopus 로고
    • Spatiotemporal control of cell signalling using a light-switchable protein interaction
    • Levskaya,A., Weiner,O.D., Lim,W.A. and Voigt,C.A. (2009) Spatiotemporal control of cell signalling using a light-switchable protein interaction. Nature, 461, 997-1001.
    • (2009) Nature , vol.461 , pp. 997-1001
    • Levskaya, A.1    Weiner, O.D.2    Lim, W.A.3    Voigt, C.A.4
  • 65
    • 43749102294 scopus 로고    scopus 로고
    • Enhancement of cell type specificity by quantitative modulation of a chimeric ligand
    • Cironi,P., Swinburne,I.A. and Silver,P.A. (2008) Enhancement of cell type specificity by quantitative modulation of a chimeric ligand. J. Biol. Chem., 283, 8469-8476.
    • (2008) J. Biol. Chem. , vol.283 , pp. 8469-8476
    • Cironi, P.1    Swinburne, I.A.2    Silver, P.A.3
  • 66
    • 77954107275 scopus 로고    scopus 로고
    • Antiglycophorin single-chain fv fusion to low-affinity mutant erythropoietin improves red blood cell-lineage specificity
    • doi: 10.1093/protein/gzp085. [Epub ahead of print, 18 January 2010]
    • Taylor,N.D., Way,J.C., Silver,P.A. and Cironi,P. (2010) Antiglycophorin single-chain fv fusion to low-affinity mutant erythropoietin improves red blood cell-lineage specificity. Protein Eng. Des. Sel., doi: 10.1093/protein/gzp085 [Epub ahead of print, 18, January 2010].
    • (2010) Protein Eng. Des. Sel.
    • Taylor, N.D.1    Way, J.C.2    Silver, P.A.3    Cironi, P.4
  • 67
    • 0036441510 scopus 로고    scopus 로고
    • Autoinhibitory domains: modular effectors of cellular regulation
    • Pufall,M.A. and Graves,B.J. (2002) Autoinhibitory domains: modular effectors of cellular regulation. Annu. Rev. Cell Dev. Biol., 18, 421-462.
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 421-462
    • Pufall, M.A.1    Graves, B.J.2
  • 68
    • 0141757323 scopus 로고    scopus 로고
    • Reprogramming control of an allosteric signaling switch through modular recombination
    • Dueber,J.E., Yeh,B.J., Chak,K. and Lim,W.A. (2003) Reprogramming control of an allosteric signaling switch through modular recombination. Science, 301, 1904-1908.
    • (2003) Science , vol.301 , pp. 1904-1908
    • Dueber, J.E.1    Yeh, B.J.2    Chak, K.3    Lim, W.A.4
  • 69
    • 34249885757 scopus 로고    scopus 로고
    • Engineering synthetic signaling proteins with ultrasensitive input/output control
    • Dueber,J.E., Mirsky,E.A. and Lim,W.A. (2007) Engineering synthetic signaling proteins with ultrasensitive input/output control. Nat. Biotechnol., 25, 660-662.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 660-662
    • Dueber, J.E.1    Mirsky, E.A.2    Lim, W.A.3
  • 70
    • 34249894454 scopus 로고    scopus 로고
    • Rewiring cellular morphology pathways with synthetic guanine nucleotide exchange factors
    • Yeh,B.J., Rutigliano,R.J., Deb,A., Bar-Sagi,D. and Lim,W.A. (2007) Rewiring cellular morphology pathways with synthetic guanine nucleotide exchange factors. Nature, 447, 596-600.
    • (2007) Nature , vol.447 , pp. 596-600
    • Yeh, B.J.1    Rutigliano, R.J.2    Deb, A.3    Bar-Sagi, D.4    Lim, W.A.5
  • 72
    • 58549105950 scopus 로고    scopus 로고
    • Design and signaling mechanism of Light-Regulated histidine kinases
    • Möglich,A., Ayers,R.A. and Moffat,K. (2009) Design and signaling mechanism of Light-Regulated histidine kinases. J. Mol. Biol., 385, 1433-1444.
    • (2009) J. Mol. Biol. , vol.385 , pp. 1433-1444
    • Möglich, A.1    Ayers, R.A.2    Moffat, K.3
  • 73
    • 69249087672 scopus 로고    scopus 로고
    • Designing switchable enzymes
    • Ostermeier,M. (2009) Designing switchable enzymes. Curr. Opin. Struct. Biol., 19, 442-448.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 442-448
    • Ostermeier, M.1
  • 74
    • 0034754163 scopus 로고    scopus 로고
    • A yeast sensor of ligand binding
    • Tucker,C.L. and Fields,S. (2001) A yeast sensor of ligand binding. Nat. Biotechnol., 19, 1042-1046.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 1042-1046
    • Tucker, C.L.1    Fields, S.2
  • 75
    • 48349086462 scopus 로고    scopus 로고
    • Linking the functions of unrelated proteins using a novel directed evolution domain insertion method
    • Edwards,W.R., Busse,K., Allemann,R.K. and Jones,D.D. (2008) Linking the functions of unrelated proteins using a novel directed evolution domain insertion method. Nucl. Acids Res., 36, e78.
    • (2008) Nucl. Acids Res. , vol.36
    • Edwards, W.R.1    Busse, K.2    Allemann, R.K.3    Jones, D.D.4
  • 76
    • 0346500466 scopus 로고    scopus 로고
    • Creation of an allosteric enzyme by domain insertion
    • Guntas,G. and Ostermeier,M. (2004) Creation of an allosteric enzyme by domain insertion. J. Mol. Biol., 336, 263-273.
    • (2004) J. Mol. Biol. , vol.336 , pp. 263-273
    • Guntas, G.1    Ostermeier, M.2
  • 77
    • 23844465160 scopus 로고    scopus 로고
    • Directed evolution of protein switches and their application to the creation of ligand-binding proteins
    • Guntas,G., Mansell,T.J., Kim,J.R. and Ostermeier,M. (2005) Directed evolution of protein switches and their application to the creation of ligand-binding proteins. Proc. Natl Acad. Sci. USA, 102, 11224-11229.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 11224-11229
    • Guntas, G.1    Mansell, T.J.2    Kim, J.R.3    Ostermeier, M.4
  • 78
    • 34247465989 scopus 로고    scopus 로고
    • Engineering modular protein interaction switches by sequence overlap
    • Sallee,N.A., Yeh,B.J. and Lim,W.A. (2007) Engineering modular protein interaction switches by sequence overlap. J. Am. Chem. Soc., 129, 4606-4611.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 4606-4611
    • Sallee, N.A.1    Yeh, B.J.2    Lim, W.A.3
  • 79
    • 49449118042 scopus 로고    scopus 로고
    • Light-activated DNA binding in a designed allosteric protein
    • Strickland,D., Moffat,K. and Sosnick,T.R. (2008) Light-activated DNA binding in a designed allosteric protein. Proc. Natl Acad. Sci. USA, 105, 10709-10714.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 10709-10714
    • Strickland, D.1    Moffat, K.2    Sosnick, T.R.3
  • 81
  • 82
    • 15044360409 scopus 로고    scopus 로고
    • Seamless cloning and gene fusion
    • Lu,Q. (2005) Seamless cloning and gene fusion. Trends Biotechnol., 23, 199-207.
    • (2005) Trends Biotechnol. , vol.23 , pp. 199-207
    • Lu, Q.1
  • 83
    • 34248559599 scopus 로고    scopus 로고
    • Gene splicing and mutagenesis by PCR-driven overlap extension
    • Heckman,K.L. and Pease,L.R. (2007) Gene splicing and mutagenesis by PCR-driven overlap extension. Nat. Protocols, 2, 924-932.
    • (2007) Nat. Protocols , vol.2 , pp. 924-932
    • Heckman, K.L.1    Pease, L.R.2
  • 84
    • 33847608289 scopus 로고    scopus 로고
    • Harnessing homologous recombination in vitro to generate recombinant DNA via SLIC
    • Li,M.Z. and Elledge,S.J. (2007) Harnessing homologous recombination in vitro to generate recombinant DNA via SLIC. Nat. Meth., 4, 251-256.
    • (2007) Nat. Meth. , vol.4 , pp. 251-256
    • Li, M.Z.1    Elledge, S.J.2
  • 86
    • 45149118469 scopus 로고    scopus 로고
    • Engineering BioBrick vectors from BioBrick parts
    • Shetty,R., Endy,D. and Knight,T. (2008) Engineering BioBrick vectors from BioBrick parts. J. Biol. Eng., 2,5.
    • (2008) J. Biol. Eng. , vol.2 , pp. 5
    • Shetty, R.1    Endy, D.2    Knight, T.3
  • 90
    • 34548823802 scopus 로고    scopus 로고
    • Optimal encoding rules for synthetic genes: the need for a community effort
    • Wu,G., Dress,L. and Freeland,S.J. (2007) Optimal encoding rules for synthetic genes: the need for a community effort. Mol. Syst. Biol., 3, 134.
    • (2007) Mol. Syst. Biol. , vol.3 , pp. 134
    • Wu, G.1    Dress, L.2    Freeland, S.J.3
  • 91
    • 64849114915 scopus 로고    scopus 로고
    • Coding-sequence determinants of gene expression in escherichia coli
    • Kudla,G., Murray,A.W., Tollervey,D. and Plotkin,J.B. (2009) Coding-sequence determinants of gene expression in escherichia coli. Science, 324, 255-258.
    • (2009) Science , vol.324 , pp. 255-258
    • Kudla, G.1    Murray, A.W.2    Tollervey, D.3    Plotkin, J.B.4
  • 92
    • 70349964350 scopus 로고    scopus 로고
    • Automated design of synthetic ribosome binding sites to control protein expression
    • Salis,H.M., Mirsky,E.A. and Voigt,C.A. (2009) Automated design of synthetic ribosome binding sites to control protein expression. Nat. Biotechnol., 27, 946-950.
    • (2009) Nat. Biotechnol. , vol.27 , pp. 946-950
    • Salis, H.M.1    Mirsky, E.A.2    Voigt, C.A.3
  • 94
    • 0032699491 scopus 로고    scopus 로고
    • Synonymous codon substitutions affect ribosome traffic and protein folding during in vitro translation
    • Komar,A.A., Lesnik,T. and Reiss,C. (1999) Synonymous codon substitutions affect ribosome traffic and protein folding during in vitro translation. FEBS Lett., 462, 387-391.
    • (1999) FEBS Lett. , vol.462 , pp. 387-391
    • Komar, A.A.1    Lesnik, T.2    Reiss, C.3
  • 95
    • 33847076187 scopus 로고    scopus 로고
    • Experimental confirmation of a key role for non-optimal codons in protein export
    • Zalucki,Y.M. and Jennings,M.P. (2007) Experimental confirmation of a key role for non-optimal codons in protein export. Biochem. Biophys. Res. Commun., 355, 143-148.
    • (2007) Biochem. Biophys. Res. Commun. , vol.355 , pp. 143-148
    • Zalucki, Y.M.1    Jennings, M.P.2
  • 97
    • 32344448608 scopus 로고    scopus 로고
    • Protein aggregation and amyloidosis: confusion of the kinds?
    • Rousseau,F., Schymkowitz,J. and Serrano,L. (2006) Protein aggregation and amyloidosis: confusion of the kinds? Curr. Opin. Struct. Biol., 16, 118-126.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 118-126
    • Rousseau, F.1    Schymkowitz, J.2    Serrano, L.3
  • 98
    • 67649852558 scopus 로고    scopus 로고
    • Physicochemical principles that regulate the competition between functional and dysfunctional association of proteins
    • Pechmann,S., Levy,E.D., Tartaglia,G.G. and Vendruscolo,M. (2009) Physicochemical principles that regulate the competition between functional and dysfunctional association of proteins. Proc. Natl Acad. Sci. USA, 106, 10159-10164.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 10159-10164
    • Pechmann, S.1    Levy, E.D.2    Tartaglia, G.G.3    Vendruscolo, M.4
  • 99
    • 0029075822 scopus 로고
    • Co-regulation of two gene activities by tetracycline via a bidirectional promoter
    • Baron,U., Freundlieb,S., Gossen,M. and Bujard,H. (1995) Co-regulation of two gene activities by tetracycline via a bidirectional promoter. Nucleic Acids Res., 23, 3605-3606.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 3605-3606
    • Baron, U.1    Freundlieb, S.2    Gossen, M.3    Bujard, H.4
  • 100
    • 0023758546 scopus 로고
    • A segment of the 50 nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation
    • Jang,S.K., Krausslich,H.G., Nicklin,M.J., Duke,G.M., Palmenberg,A.C. and Wimmer,E. (1988) A segment of the 50 nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation. J. Virol., 62, 2636-2643.
    • (1988) J. Virol. , vol.62 , pp. 2636-2643
    • Jang, S.K.1    Krausslich, H.G.2    Nicklin, M.J.3    Duke, G.M.4    Palmenberg, A.C.5    Wimmer, E.6
  • 102
    • 0030296634 scopus 로고    scopus 로고
    • Three-part inventions: intracellular signaling and induced proximity
    • Crabtree,G.R. and Schreiber,S.L. (1996) Three-part inventions: intracellular signaling and induced proximity. Trends Biochem. Sci., 21, 418-422.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 418-422
    • Crabtree, G.R.1    Schreiber, S.L.2
  • 103
    • 0031892994 scopus 로고    scopus 로고
    • Dimerization as a regulatory mechanism in signal transduction
    • Klemm,J.D., Schreiber,S.L. and Crabtree,G.R. (1998) Dimerization as a regulatory mechanism in signal transduction. Annu. Rev. Immunol., 16, 569-592.
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 569-592
    • Klemm, J.D.1    Schreiber, S.L.2    Crabtree, G.R.3
  • 104
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields,S. and Song,O. (1989) A novel genetic system to detect protein-protein interactions. Nature, 340, 245-246.
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 105
    • 0035984722 scopus 로고    scopus 로고
    • [beta]-Lactamase protein fragment complementation assays as in vivo and in vitro sensors of protein-protein interactions
    • Galarneau,A., Primeau,M., Trudeau,L. and Michnick,S.W. (2002) [beta]-Lactamase protein fragment complementation assays as in vivo and in vitro sensors of protein-protein interactions. Nat. Biotechnol., 20, 619-622.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 619-622
    • Galarneau, A.1    Primeau, M.2    Trudeau, L.3    Michnick, S.W.4
  • 106
    • 33751213120 scopus 로고    scopus 로고
    • Complementary methods for studies of protein interactions in living cells
    • Kerppola,T.K. (2006) Complementary methods for studies of protein interactions in living cells. Nat. Methods, 3, 969-971.
    • (2006) Nat. Methods , vol.3 , pp. 969-971
    • Kerppola, T.K.1
  • 107
    • 34247629593 scopus 로고    scopus 로고
    • Application of proteinfragment complementation assays in cell biology
    • Remy,I. and Michnick,S.W. (2007) Application of proteinfragment complementation assays in cell biology. BioTechniques, 42, 137, 139, 141.
    • (2007) BioTechniques , vol.42 , pp. 141
    • Remy, I.1    Michnick, S.W.2
  • 108
    • 52049084405 scopus 로고    scopus 로고
    • The AnchorAway technique: rapid, conditional establishment of yeast mutant phenotypes
    • Haruki,H., Nishikawa,J. and Laemmli,U.K. (2008) The AnchorAway technique: rapid, conditional establishment of yeast mutant phenotypes. Mol. Cell, 31, 925-932.
    • (2008) Mol. Cell , vol.31 , pp. 925-932
    • Haruki, H.1    Nishikawa, J.2    Laemmli, U.K.3
  • 110
    • 3142734925 scopus 로고    scopus 로고
    • Switching desaturase enzyme specificity by alternate subcellular targeting
    • Heilmann,I., Pidkowich,M.S., Girke,T. and Shanklin,J. (2004) Switching desaturase enzyme specificity by alternate subcellular targeting. Proc. Natl Acad. Sci. USA, 101, 10266-10271.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 10266-10271
    • Heilmann, I.1    Pidkowich, M.S.2    Girke, T.3    Shanklin, J.4
  • 111
    • 4344575287 scopus 로고    scopus 로고
    • Coiled coil domains: stability, specificity and biological implications
    • Mason,J.M. and Arndt,K.M. (2004) Coiled coil domains: stability, specificity and biological implications. Chembiochem, 5, 170-176.
    • (2004) Chembiochem , vol.5 , pp. 170-176
    • Mason, J.M.1    Arndt, K.M.2
  • 112
    • 34548174444 scopus 로고    scopus 로고
    • Improved stability of the Jun-Fos activator protein-1 coiled coil motif: a stopped-flow circular dichroism kinetic analysis
    • Mason,J.M., Hagemann,U.B. and Arndt,K.M. (2007) Improved stability of the Jun-Fos activator protein-1 coiled coil motif: a stopped-flow circular dichroism kinetic analysis. J. Biol. Chem., 282, 23015-23024.
    • (2007) J. Biol. Chem. , vol.282 , pp. 23015-23024
    • Mason, J.M.1    Hagemann, U.B.2    Arndt, K.M.3
  • 113
    • 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., 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. J. Am. Chem. Soc., 125, 10561-10569.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 10561-10569
    • Mootz, H.D.1    Blum, E.S.2    Tyszkiewicz, A.B.3    Muir, T.W.4
  • 115
    • 0029868593 scopus 로고    scopus 로고
    • The interaction of coumarin antibiotics with fragments of the DNA gyrase b protein
    • Gormley,N.A., Orphanides,G., Meyer,A., Cullis,P.M. and Maxwell,A. (1996) The interaction of coumarin antibiotics with fragments of the DNA gyrase b protein. Biochemistry, 35, 5083-5092.
    • (1996) Biochemistry , vol.35 , pp. 5083-5092
    • Gormley, N.A.1    Orphanides, G.2    Meyer, A.3    Cullis, P.M.4    Maxwell, A.5
  • 116
    • 0344010997 scopus 로고    scopus 로고
    • A coumermycin/novobiocin-regulated gene expression system hum
    • Zhao,H.F., Boyd,J., Jolicoeur,N. and Shen,S.H. (2003) A coumermycin/novobiocin-regulated gene expression system hum. Gene Ther., 14, 1619-1629.
    • (2003) Gene Ther. , vol.14 , pp. 1619-1629
    • Zhao, H.F.1    Boyd, J.2    Jolicoeur, N.3    Shen, S.H.4
  • 117
    • 41449091908 scopus 로고    scopus 로고
    • Activation of protein splicing with light in yeast
    • Tyszkiewicz,A.B. and Muir,T.W. (2008) Activation of protein splicing with light in yeast. Nat. Meth., 5, 303-305.
    • (2008) Nat. Meth. , vol.5 , pp. 303-305
    • Tyszkiewicz, A.B.1    Muir, T.W.2
  • 119
    • 34250637961 scopus 로고    scopus 로고
    • Reverse MAPPIT detects disruptors of protein-protein interactions in human cells
    • Lemmens,I., Lievens,S., Eyckerman,S. and Tavernier,J. (2006) Reverse MAPPIT detects disruptors of protein-protein interactions in human cells. Nat. Protocols, 1, 92-97.
    • (2006) Nat. Protocols , vol.1 , pp. 92-97
    • Lemmens, I.1    Lievens, S.2    Eyckerman, S.3    Tavernier, J.4
  • 120
    • 0032514623 scopus 로고    scopus 로고
    • Oligomerization domain-directed reassembly of active dihydrofolate reductase from rationally designed fragments
    • Pelletier,J.N., Campbell-Valois,F. and Michnick,S.W. (1998) Oligomerization domain-directed reassembly of active dihydrofolate reductase from rationally designed fragments. Proc. Natl Acad. Sci. USA, 95, 12141-12146.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12141-12146
    • Pelletier, J.N.1    Campbell-Valois, F.2    Michnick, S.W.3
  • 121
    • 4344656346 scopus 로고    scopus 로고
    • Kinetics of regulated protein-protein interactions revealed with firefly luciferase complementation imaging in cells and living animals
    • Luker,K.E., Smith,M.C.P., Luker,G.D., Gammon,S.T., Piwnica-Worms,H. and Piwnica-Worms,D. (2004) Kinetics of regulated protein-protein interactions revealed with firefly luciferase complementation imaging in cells and living animals. Proc. Natl Acad. Sci. USA, 101, 12288-12293.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 12288-12293
    • Luker, K.E.1    Smith, M.C.P.2    Luker, G.D.3    Gammon, S.T.4    Piwnica-Worms, H.5    Piwnica-Worms, D.6
  • 122
    • 36749104291 scopus 로고    scopus 로고
    • Quantification of dynamic protein complexes using renilla luciferase fragment complementation applied to protein kinase a activities in vivo
    • Stefan,E., Aquin,S., Berger,N., Landry,C.R., Nyfeler,B., Bouvier,M. and Michnick,S.W. (2007) Quantification of dynamic protein complexes using renilla luciferase fragment complementation applied to protein kinase a activities in vivo. Proc. Natl Acad. Sci. USA, 104, 16916-16921.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 16916-16921
    • Stefan, E.1    Aquin, S.2    Berger, N.3    Landry, C.R.4    Nyfeler, B.5    Bouvier, M.6    Michnick, S.W.7
  • 123
    • 0037995710 scopus 로고    scopus 로고
    • Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis
    • Hu,C. and Kerppola,T.K. (2003) Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis. Nat. Biotechnol., 21, 539-545.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 539-545
    • Hu, C.1    Kerppola, T.K.2
  • 124
    • 2942559261 scopus 로고    scopus 로고
    • Visualization of Myc/Max/Mad family dimers and the competition for dimerization in living cells
    • Grinberg,A.V., Hu,C. and Kerppola,T.K. (2004) Visualization of Myc/Max/Mad family dimers and the competition for dimerization in living cells. Mol. Cell. Biol., 24, 4294-4308.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4294-4308
    • Grinberg, A.V.1    Hu, C.2    Kerppola, T.K.3
  • 125
    • 70350738339 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementation analysis of inducible protein interactions: Effects of factors affecting protein folding on fluorescent protein fragment association
    • Robida,A.M. and Kerppola,T.K. (2009) Bimolecular fluorescence complementation analysis of inducible protein interactions: Effects of factors affecting protein folding on fluorescent protein fragment association. J. Mol. Biol., 394, 391-409.
    • (2009) J. Mol. Biol. , vol.394 , pp. 391-409
    • Robida, A.M.1    Kerppola, T.K.2
  • 126
    • 0028080090 scopus 로고
    • Split ubiquitin as a sensor of protein interactions in vivo
    • Johnsson,N. and Varshavsky,A. (1994) Split ubiquitin as a sensor of protein interactions in vivo. Proc. Natl Acad. Sci. USA, 91, 10340-10344.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10340-10344
    • Johnsson, N.1    Varshavsky, A.2
  • 127
    • 34547421693 scopus 로고    scopus 로고
    • Exploiting protein destruction for constructive use
    • Stankunas,K. and Crabtree,G.R. (2007) Exploiting protein destruction for constructive use. Proc. Natl Acad. Sci. USA, 104, 11511-11512.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 11511-11512
    • Stankunas, K.1    Crabtree, G.R.2
  • 129
    • 70449449854 scopus 로고    scopus 로고
    • Rapid modification of proteins using a rapamycin-inducible tobacco etch virus protease system
    • Williams,D.J., Puhl,H.L. and Ikeda,S.R. (2009) Rapid modification of proteins using a rapamycin-inducible tobacco etch virus protease system. PLoS ONE, 4, e7474.
    • (2009) PLoS ONE , vol.4
    • Williams, D.J.1    Puhl, H.L.2    Ikeda, S.R.3
  • 130
    • 58549087359 scopus 로고    scopus 로고
    • Dynamic map of protein interactions in the escherichia coli chemotaxis pathway
    • doi: 10.1038/msb.2008.77
    • Kentner,D. and Sourjik,V. (2009) Dynamic map of protein interactions in the escherichia coli chemotaxis pathway. Mol. Syst. Biol., 5, doi: 10.1038/msb.2008.77.
    • (2009) Mol. Syst. Biol. , vol.5
    • Kentner, D.1    Sourjik, V.2
  • 132
    • 34347237194 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy: novel variations of an established technique
    • Haustein,E. and Schwille,P. (2007) Fluorescence correlation spectroscopy: novel variations of an established technique. Annu. Rev. Biophys. Biomol. Struct., 36, 151-169.
    • (2007) Annu. Rev. Biophys. Biomol. Struct. , vol.36 , pp. 151-169
    • Haustein, E.1    Schwille, P.2
  • 133
    • 77952963095 scopus 로고    scopus 로고
    • Engineered proteins pull double duty
    • Cochran,J.R. (2010) Engineered proteins pull double duty. Sci. Transl. Med., 2, 17ps5.
    • (2010) Sci. Transl. Med. , vol.2 , Issue.17
    • Cochran, J.R.1
  • 134
    • 0034225190 scopus 로고    scopus 로고
    • Enzyme-Based biosensors for in vivo measurements
    • Wilson,G.S. and Hu,Y. (2000) Enzyme-Based biosensors for in vivo measurements. Chem. Rev., 100, 2693-2704.
    • (2000) Chem. Rev. , vol.100 , pp. 2693-2704
    • Wilson, G.S.1    Hu, Y.2
  • 135
    • 42449161556 scopus 로고    scopus 로고
    • A review of biosensors and biologically-inspired systems for explosives detection
    • Smith,R.G., D'Souza,N. and Nicklin,S. (2008) A review of biosensors and biologically-inspired systems for explosives detection. Analyst, 133, 571-584.
    • (2008) Analyst , vol.133 , pp. 571-584
    • Smith, R.G.1    D'Souza, N.2    Nicklin, S.3
  • 136
    • 33746163862 scopus 로고    scopus 로고
    • Biopharmaceutical benchmarks 2006
    • Walsh,G. (2006) Biopharmaceutical benchmarks 2006. Nat. Biotechnol., 24, 769-776.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 769-776
    • Walsh, G.1


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