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Volumn 111, Issue 42, 2014, Pages 15048-15053

Intrinsic disorder as a generalizable strategy for the rational design of highly responsive, allosterically cooperative receptors

Author keywords

Biosensors; Intrinsically disordered proteins; Ribozymes; Synthetic biology; Ultrasensitivity

Indexed keywords

APTAMER; INTRINSICALLY DISORDERED PROTEIN; RIBOZYME; 6-CARBOXYFLUORESCEIN; COCAINE; DNA; DOXORUBICIN; FLUORESCEIN DERIVATIVE; LIGAND; OXYGEN; PROTEIN BINDING;

EID: 84908061195     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1410796111     Document Type: Article
Times cited : (68)

References (42)
  • 1
    • 84877783519 scopus 로고    scopus 로고
    • Ultrasensitive response motifs: Basic amplifiers in molecular signalling networks
    • Zhang Q, Bhattacharya S, Andersen ME (2013) Ultrasensitive response motifs: Basic amplifiers in molecular signalling networks. Open Biol 3(4):130031.
    • (2013) Open Biol , vol.3 , Issue.4 , pp. 130031
    • Zhang, Q.1    Bhattacharya, S.2    Andersen, M.E.3
  • 2
    • 49449118042 scopus 로고    scopus 로고
    • Light-activated DNA binding in a designed allosteric protein
    • Strickland D, Moffat K, Sosnick TR (2008) Light-activated DNA binding in a designed allosteric protein. Proc Natl Acad Sci USA 105(31):10709-10714.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.31 , pp. 10709-10714
    • Strickland, D.1    Moffat, K.2    Sosnick, T.R.3
  • 3
    • 0042736856 scopus 로고    scopus 로고
    • Allosteric switching by mutually exclusive folding of protein domains
    • Radley TL, Markowska AI, Bettinger BT, Ha JH, Loh SN (2003) Allosteric switching by mutually exclusive folding of protein domains. J Mol Biol 332(3):529-536.
    • (2003) J Mol Biol , vol.332 , Issue.3 , pp. 529-536
    • Radley, T.L.1    Markowska, A.I.2    Bettinger, B.T.3    Ha, J.H.4    Loh, S.N.5
  • 4
    • 0346500466 scopus 로고    scopus 로고
    • Creation of an allosteric enzyme by domain insertion
    • Guntas G, Ostermeier M (2004) Creation of an allosteric enzyme by domain insertion. J Mol Biol 336(1):263-273.
    • (2004) J Mol Biol , vol.336 , Issue.1 , pp. 263-273
    • Guntas, G.1    Ostermeier, M.2
  • 5
    • 18044371235 scopus 로고    scopus 로고
    • Artificial allosteric control of maltose binding protein
    • Choi B, et al. (2005) Artificial allosteric control of maltose binding protein. Phys Rev Lett 94(3):038103.
    • (2005) Phys Rev Lett , vol.94 , Issue.3 , pp. 038103
    • Choi, B.1
  • 6
    • 0031171217 scopus 로고    scopus 로고
    • Rational design of allosteric ribozymes
    • Tang J, Breaker RR (1997) Rational design of allosteric ribozymes. Chem Biol 4(6): 453-459.
    • (1997) Chem Biol , vol.4 , Issue.6 , pp. 453-459
    • Tang, J.1    Breaker, R.R.2
  • 7
    • 84866521002 scopus 로고    scopus 로고
    • Rational design of allosteric inhibitors and activators using the population-shift model: In vitro validation and application to an artificial biosensor
    • Ricci F, Vallée-Bélisle A, Porchetta A, Plaxco KW (2012) Rational design of allosteric inhibitors and activators using the population-shift model: In vitro validation and application to an artificial biosensor. J Am Chem Soc 134(37):15177-15180.
    • (2012) J Am Chem Soc , vol.134 , Issue.37 , pp. 15177-15180
    • Ricci, F.1    Vallée-Bélisle, A.2    Porchetta, A.3    Plaxco, K.W.4
  • 8
    • 84871546095 scopus 로고    scopus 로고
    • Using distal-site mutations and allosteric inhibition to tune, extend, and narrow the useful dynamic range of aptamer-based sensors
    • Porchetta A, Vallée-Bélisle A, Plaxco KW, Ricci F (2012) Using distal-site mutations and allosteric inhibition to tune, extend, and narrow the useful dynamic range of aptamer-based sensors. J Am Chem Soc 134(51):20601-20604.
    • (2012) J Am Chem Soc , vol.134 , Issue.51 , pp. 20601-20604
    • Porchetta, A.1    Vallée-Bélisle, A.2    Plaxco, K.W.3    Ricci, F.4
  • 9
    • 34249885757 scopus 로고    scopus 로고
    • Engineering synthetic signaling proteins with ultrasensitive input/output control
    • Dueber JE, Mirsky EA, Lim WA (2007) Engineering synthetic signaling proteins with ultrasensitive input/output control. Nat Biotechnol 25(6):660-662.
    • (2007) Nat Biotechnol , vol.25 , Issue.6 , pp. 660-662
    • Dueber, J.E.1    Mirsky, E.A.2    Lim, W.A.3
  • 10
    • 84871956143 scopus 로고    scopus 로고
    • Decrease in RNA folding cooperativity by deliberate population of intermediates in RNA G-quadruplexes
    • Kwok CK, Sherlock ME, Bevilacqua PC (2013) Decrease in RNA folding cooperativity by deliberate population of intermediates in RNA G-quadruplexes. Angew Chem Int Ed Engl 52(2):683-686.
    • (2013) Angew Chem Int Ed Engl , vol.52 , Issue.2 , pp. 683-686
    • Kwok, C.K.1    Sherlock, M.E.2    Bevilacqua, P.C.3
  • 11
    • 56749183344 scopus 로고    scopus 로고
    • 2+ in aqueous solution based on structure-switching DNA
    • 2+ in aqueous solution based on structure-switching DNA. Chem Commun (Camb) 45: 6005-6007.
    • (2008) Chem Commun (Camb) , vol.45 , pp. 6005-6007
    • Wang, Z.1    Heon Lee, J.2    Lu, Y.3
  • 12
    • 84906947812 scopus 로고    scopus 로고
    • Using the population-shift mechanism to rationally introduce Hill-type cooperativity into a biomolecular receptor
    • Simon AJ, Vallée-Bélisle A, Ricci F, Watkins H, Plaxco KW (2014) Using the population-shift mechanism to rationally introduce Hill-type cooperativity into a biomolecular receptor. Angew Chem 53(36):9471-9475.
    • (2014) Angew Chem , vol.53 , Issue.36 , pp. 9471-9475
    • Simon, A.J.1    Vallée-Bélisle, A.2    Ricci, F.3    Watkins, H.4    Plaxco, K.W.5
  • 13
    • 47649098600 scopus 로고    scopus 로고
    • Cooperativity and biological complexity
    • Whitty A (2008) Cooperativity and biological complexity. Nat Chem Biol 4(8):435-439.
    • (2008) Nat Chem Biol , vol.4 , Issue.8 , pp. 435-439
    • Whitty, A.1
  • 14
    • 84863451993 scopus 로고    scopus 로고
    • Multianalyte digital enzyme biosensors with built-in Boolean logic
    • Katz E, Wang J, Privman M, Halámek J (2012) Multianalyte digital enzyme biosensors with built-in Boolean logic. Anal Chem 84(13):5463-5469.
    • (2012) Anal Chem , vol.84 , Issue.13 , pp. 5463-5469
    • Katz, E.1    Wang, J.2    Privman, M.3    Halámek, J.4
  • 15
    • 80055106927 scopus 로고    scopus 로고
    • High-precision, in vitro validation of the sequestration mechanism for generating ultrasensitive dose-response curves in regulatory networks
    • Ricci F, Vallée-Bélisle A, Plaxco KW (2011) High-precision, in vitro validation of the sequestration mechanism for generating ultrasensitive dose-response curves in regulatory networks. PLoS Comput Biol 7(10):e1002171.
    • (2011) PLoS Comput Biol , vol.7 , Issue.10 , pp. e1002171
    • Ricci, F.1    Vallée-Bélisle, A.2    Plaxco, K.W.3
  • 16
    • 84862277231 scopus 로고    scopus 로고
    • Digital switching of local arginine density in a genetically encoded self-assembled polypeptide nanoparticle controls cellular uptake
    • MacEwan SR, Chilkoti A (2012) Digital switching of local arginine density in a genetically encoded self-assembled polypeptide nanoparticle controls cellular uptake. Nano Lett 12(6):3322-3328.
    • (2012) Nano Lett , vol.12 , Issue.6 , pp. 3322-3328
    • MacEwan, S.R.1    Chilkoti, A.2
  • 17
    • 79959518231 scopus 로고    scopus 로고
    • Nanoparticles that communicate in vivo to amplify tumour targeting
    • von Maltzahn G, et al. (2011) Nanoparticles that communicate in vivo to amplify tumour targeting. Nat Mater 10(7):545-552.
    • (2011) Nat Mater , vol.10 , Issue.7 , pp. 545-552
    • Von Maltzahn, G.1
  • 18
    • 79952832701 scopus 로고    scopus 로고
    • High-fidelity determination of security threats via a Boolean biocatalytic cascade
    • Chuang M-C, et al. (2011) High-fidelity determination of security threats via a Boolean biocatalytic cascade. Chem Commun (Camb) 47(11):3087-3089.
    • (2011) Chem Commun (Camb) , vol.47 , Issue.11 , pp. 3087-3089
    • Chuang, M.-C.1
  • 20
    • 77949860707 scopus 로고    scopus 로고
    • Designing artificial enzymes by intuition and computation
    • Nanda V, Koder RL (2010) Designing artificial enzymes by intuition and computation. Nat Chem 2(1):15-24.
    • (2010) Nat Chem , vol.2 , Issue.1 , pp. 15-24
    • Nanda, V.1    Koder, R.L.2
  • 22
    • 84859765617 scopus 로고    scopus 로고
    • Role of the biomolecular energy gap in protein design, structure, and evolution
    • Fleishman SJ, Baker D (2012) Role of the biomolecular energy gap in protein design, structure, and evolution. Cell 149(2):262-273.
    • (2012) Cell , vol.149 , Issue.2 , pp. 262-273
    • Fleishman, S.J.1    Baker, D.2
  • 23
    • 34347235156 scopus 로고    scopus 로고
    • Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins
    • Hilser VJ, Thompson EB (2007) Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins. Proc Natl Acad Sci USA 104(20):8311-8315.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.20 , pp. 8311-8315
    • Hilser, V.J.1    Thompson, E.B.2
  • 24
    • 84879327823 scopus 로고    scopus 로고
    • Modulation of allostery by protein intrinsic disorder
    • Ferreon AC, Ferreon JC, Wright PE, Deniz AA (2013) Modulation of allostery by protein intrinsic disorder. Nature 498:390-394.
    • (2013) Nature , vol.498 , pp. 390-394
    • Ferreon, A.C.1    Ferreon, J.C.2    Wright, P.E.3    Deniz, A.A.4
  • 25
    • 84899638075 scopus 로고    scopus 로고
    • Intrinsic disorder mediates cooperative signal transduction in STIM1
    • Furukawa Y, et al. (2014) Intrinsic disorder mediates cooperative signal transduction in STIM1. J Mol Biol 426(10):2082-2097.
    • (2014) J Mol Biol , vol.426 , Issue.10 , pp. 2082-2097
    • Furukawa, Y.1
  • 26
    • 0003043542 scopus 로고
    • The possible effects of the aggregation of the molecules of hæmoglobin on its dissociation curves
    • Hill AV (1910) The possible effects of the aggregation of the molecules of hæmoglobin on its dissociation curves. J Physiol 40:IV-VII.
    • (1910) J Physiol , vol.40 , pp. IV-VII
    • Hill, A.V.1
  • 27
    • 0017917985 scopus 로고
    • The meaning of Scatchard and Hill plots
    • Dahlquist FW (1978) The meaning of Scatchard and Hill plots. Methods Enzymol 48: 270-299.
    • (1978) Methods Enzymol , vol.48 , pp. 270-299
    • Dahlquist, F.W.1
  • 28
    • 79951800443 scopus 로고    scopus 로고
    • Allosteric, chelate, and interannular cooperativity: A mise au point
    • Ercolani G, Schiaffino L (2011) Allosteric, chelate, and interannular cooperativity: A mise au point. Angew Chem Int Ed Engl 50(8):1762-1768.
    • (2011) Angew Chem Int Ed Engl , vol.50 , Issue.8 , pp. 1762-1768
    • Ercolani, G.1    Schiaffino, L.2
  • 29
    • 33644515626 scopus 로고    scopus 로고
    • MercuryII-mediated formation of thymine-HgII-thymine base pairs in DNA duplexes
    • Miyake Y, et al. (2006) MercuryII-mediated formation of thymine-HgII-thymine base pairs in DNA duplexes. J Am Chem Soc 128(7):2172-2173.
    • (2006) J Am Chem Soc , vol.128 , Issue.7 , pp. 2172-2173
    • Miyake, Y.1
  • 31
    • 36549094651 scopus 로고
    • Intrachain loops in polymers
    • Chan HS, Dill KA (1989) Intrachain loops in polymers. J Chem Phys 90(1):492-509.
    • (1989) J Chem Phys , vol.90 , Issue.1 , pp. 492-509
    • Chan, H.S.1    Dill, K.A.2
  • 32
    • 0032539693 scopus 로고    scopus 로고
    • A unified view of polymer, dumbbell, and oligonucleotide DNA nearest-neighbor thermodynamics
    • SantaLucia J, Jr (1998) A unified view of polymer, dumbbell, and oligonucleotide DNA nearest-neighbor thermodynamics. Proc Natl Acad Sci USA 95(4):1460-1465.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.4 , pp. 1460-1465
    • SantaLucia, J.1
  • 33
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker M (2003) Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res 31(13):3406-3415.
    • (2003) Nucleic Acids Res , vol.31 , Issue.13 , pp. 3406-3415
    • Zuker, M.1
  • 34
    • 69549120468 scopus 로고    scopus 로고
    • Thermodynamic basis for the optimization of binding-induced biomolecular switches and structure-switching biosensors
    • Vallée-Bélisle A, Ricci F, Plaxco KW (2009) Thermodynamic basis for the optimization of binding-induced biomolecular switches and structure-switching biosensors. Proc Natl Acad Sci USA 106(33):13802-13807.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.33 , pp. 13802-13807
    • Vallée-Bélisle, A.1    Ricci, F.2    Plaxco, K.W.3
  • 35
    • 0036835759 scopus 로고    scopus 로고
    • Efficiencies of fluorescence resonance energy transfer and contact-mediated quenching in oligonucleotide probes
    • Marras SAE, Kramer FR, Tyagi S (2002) Efficiencies of fluorescence resonance energy transfer and contact-mediated quenching in oligonucleotide probes. Nucleic Acids Res 30(21):e122.
    • (2002) Nucleic Acids Res , vol.30 , Issue.21 , pp. e122
    • Marras, S.A.E.1    Kramer, F.R.2    Tyagi, S.3
  • 36
    • 37049008251 scopus 로고    scopus 로고
    • A DNA aptamer with high affinity and specificity for therapeutic anthracyclines
    • Wochner A, et al. (2008) A DNA aptamer with high affinity and specificity for therapeutic anthracyclines. Anal Biochem 373(1):34-42.
    • (2008) Anal Biochem , vol.373 , Issue.1 , pp. 34-42
    • Wochner, A.1
  • 37
    • 0034813846 scopus 로고    scopus 로고
    • Aptamer-based folding fluorescent sensor for cocaine
    • Stojanovic MN, de Prada P, Landry DW (2001) Aptamer-based folding fluorescent sensor for cocaine. J Am Chem Soc 123(21):4928-4931.
    • (2001) J Am Chem Soc , vol.123 , Issue.21 , pp. 4928-4931
    • Stojanovic, M.N.1    De Prada, P.2    Landry, D.W.3
  • 38
    • 70149101545 scopus 로고    scopus 로고
    • High specificity, electrochemical sandwich assays based on single aptamer sequences and suitable for the direct detection of small-molecule targets in blood and other complex matrices
    • Zuo X, Xiao Y, Plaxco KW (2009) High specificity, electrochemical sandwich assays based on single aptamer sequences and suitable for the direct detection of small-molecule targets in blood and other complex matrices. J Am Chem Soc 131(20): 6944-6945.
    • (2009) J Am Chem Soc , vol.131 , Issue.20 , pp. 6944-6945
    • Zuo, X.1    Xiao, Y.2    Plaxco, K.W.3
  • 39
    • 84900390627 scopus 로고    scopus 로고
    • A comparison of the folding kinetics of a small, artificially selected DNA aptamer with those of equivalently simple naturally occurring proteins
    • Lawrence C, et al. (2014) A comparison of the folding kinetics of a small, artificially selected DNA aptamer with those of equivalently simple naturally occurring proteins. Protein Sci 23(1):56-66.
    • (2014) Protein Sci , vol.23 , Issue.1 , pp. 56-66
    • Lawrence, C.1
  • 40
    • 84908059314 scopus 로고    scopus 로고
    • Enzymatically amplified SPR imaging for biosensor microarrays: Fighting the tyranny of the Langmuir isotherm
    • Corn RM (2005) Enzymatically amplified SPR imaging for biosensor microarrays: Fighting the tyranny of the Langmuir isotherm. Abstr Pap Am Chem Soc 230: U330-U331.
    • (2005) Abstr Pap Am Chem Soc , vol.230 , pp. U330-U331
    • Corn, R.M.1
  • 41
    • 84862526773 scopus 로고    scopus 로고
    • Protein conformational switches: From nature to design
    • Ha J-H, Loh SN (2012) Protein conformational switches: From nature to design. Chemistry 18(26):7984-7999.
    • (2012) Chemistry , vol.18 , Issue.26 , pp. 7984-7999
    • Ha, J.-H.1    Loh, S.N.2
  • 42
    • 23344433223 scopus 로고    scopus 로고
    • Engineering a signal transduction mechanism for protein-based biosensors
    • Kohn JE, Plaxco KW (2005) Engineering a signal transduction mechanism for protein-based biosensors. Proc Natl Acad Sci USA 102(31):10841-10845.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.31 , pp. 10841-10845
    • Kohn, J.E.1    Plaxco, K.W.2


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