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Volumn 20, Issue 1, 2011, Pages 19-29

Converting a protein into a switch for biosensing and functional regulation

Author keywords

Allostery; Alternate frame folding; Circular permutation; Folding; Intrinsic disorder; Sensor; Unfolding

Indexed keywords

HELIX LOOP HELIX PROTEIN;

EID: 78650796409     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.541     Document Type: Review
Times cited : (38)

References (80)
  • 1
    • 70349774561 scopus 로고    scopus 로고
    • Directed evolution: New parts and optimized function
    • Dougherty MJ, Arnold FH (2009) Directed evolution: new parts and optimized function. Curr Opin Biotechnol 20:486-491.
    • (2009) Curr Opin Biotechnol , vol.20 , pp. 486-491
    • Dougherty, M.J.1    Arnold, F.H.2
  • 2
  • 4
    • 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 104:8311-8315.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 8311-8315
    • Hilser, V.J.1    Thompson, E.B.2
  • 5
    • 77951251659 scopus 로고    scopus 로고
    • Folding-based electrochemical biosensors: The case for responsive nucleic acid architectures
    • Lubin AA, Plaxco KW (2010) Folding-based electrochemical biosensors: the case for responsive nucleic acid architectures. Acc Chem Res 43:496-505.
    • (2010) Acc Chem Res , vol.43 , pp. 496-505
    • Lubin, A.A.1    Plaxco, K.W.2
  • 6
    • 75749127871 scopus 로고    scopus 로고
    • Exploiting binding-induced changes in probe flexibility for the optimization of electrochemical biosensors
    • White RJ, Plaxco KW (2010) Exploiting binding-induced changes in probe flexibility for the optimization of electrochemical biosensors. Anal Chem 82:73-76.
    • (2010) Anal Chem , vol.82 , pp. 73-76
    • White, R.J.1    Plaxco, K.W.2
  • 7
    • 51449088824 scopus 로고    scopus 로고
    • Biomolecule immobilization in biosensor development: Tailored strategies based on affinity interactions
    • Prieto-Simin B, Campas M, Marty JL (2008) Biomolecule immobilization in biosensor development: tailored strategies based on affinity interactions. Protein Pept Lett 15:757-763.
    • (2008) Protein Pept Lett , vol.15 , pp. 757-763
    • Prieto-Simin, B.1    Campas, M.2    Marty, J.L.3
  • 8
    • 77953477627 scopus 로고    scopus 로고
    • Critical aspects of biointerface design and their impact on biosensor development
    • North SH, Lock EH, Taitt CR, Walton SG (2010) Critical aspects of biointerface design and their impact on biosensor development. Anal Bioanal Chem 397: 925-933.
    • (2010) Anal Bioanal Chem , vol.397 , pp. 925-933
    • North, S.H.1    Lock, E.H.2    Taitt, C.R.3    Walton, S.G.4
  • 9
    • 46849092432 scopus 로고    scopus 로고
    • Biosensor technology: Technology push versus market pull
    • Luong JH, Male KB, Glennon JD (2008) Biosensor technology: technology push versus market pull. Biotechnol Adv 26:492-500.
    • (2008) Biotechnol Adv , vol.26 , pp. 492-500
    • Luong, J.H.1    Male, K.B.2    Glennon, J.D.3
  • 10
    • 33746635140 scopus 로고    scopus 로고
    • Design of protein conformational switches
    • Ambroggio XI, Kuhlman B (2006) Design of protein conformational switches. Curr Opin Struct Biol 16: 525-530.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 525-530
    • Ambroggio, X.I.1    Kuhlman, B.2
  • 11
    • 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
  • 12
    • 23944444109 scopus 로고    scopus 로고
    • Engineering allosteric protein switches by domain insertion
    • Ostermeier M (2005) Engineering allosteric protein switches by domain insertion. Protein Eng Des Sel 18: 359-364.
    • (2005) Protein Eng Des Sel , vol.18 , pp. 359-364
    • Ostermeier, M.1
  • 14
    • 77955984136 scopus 로고    scopus 로고
    • Structure-switching biosensors: Inspired by Nature
    • Vallee-Belisle A, Plaxco KW (2010) Structure-switching biosensors: inspired by Nature. Curr Opin Struct Biol 20:518-526.
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 518-526
    • Vallee-Belisle, A.1    Plaxco, K.W.2
  • 15
    • 70349770900 scopus 로고    scopus 로고
    • Generation of new protein functions by nonhomologous combinations and rearrangements of domains and modules
    • Koide S (2009) Generation of new protein functions by nonhomologous combinations and rearrangements of domains and modules. Curr Opin Biotech 20:398-404.
    • (2009) Curr Opin Biotech , vol.20 , pp. 398-404
    • Koide, S.1
  • 17
    • 0035910074 scopus 로고    scopus 로고
    • Genetically encoded reporters of protein kinase A activity reveal impact of substrate tethering
    • Zhang J, Ma Y, Taylor SS, Tsien RY (2001) Genetically encoded reporters of protein kinase A activity reveal impact of substrate tethering. Proc Natl Acad Sci USA 98:14997-15002.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14997-15002
    • Zhang, J.1    Ma, Y.2    Taylor, S.S.3    Tsien, R.Y.4
  • 18
    • 0035909994 scopus 로고    scopus 로고
    • Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells
    • Ting AY, Kain KH, Klemke RL, Tsien RY (2001) Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells. Proc Natl Acad Sci USA 98:15003-15008.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 15003-15008
    • Ting, A.Y.1    Kain, K.H.2    Klemke, R.L.3    Tsien, R.Y.4
  • 19
    • 77950434011 scopus 로고    scopus 로고
    • Visualization of JNK activity dynamics with a genetically encoded fluorescent biosensor
    • Fosbrink M, Aye-Han NN, Cheong R, Levchenko A, Zhang J (2010) Visualization of JNK activity dynamics with a genetically encoded fluorescent biosensor. Proc Natl Acad Sci USA 107:5459-5464.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 5459-5464
    • Fosbrink, M.1    Aye-Han, N.N.2    Cheong, R.3    Levchenko, A.4    Zhang, J.5
  • 21
    • 4143115810 scopus 로고    scopus 로고
    • Periplasmic binding proteins: A versatile superfamily for protein engineering
    • Dwyer MA, Hellinga HW (2004) Periplasmic binding proteins: a versatile superfamily for protein engineering. Curr Opin Struct Biol 14:495-504.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 495-504
    • Dwyer, M.A.1    Hellinga, H.W.2
  • 23
    • 2542523113 scopus 로고    scopus 로고
    • Computational design of receptors for an organophosphate surrogate of the nerve agent soman
    • Allert M, Rizk SS, Looger LL, Hellinga HW (2004) Computational design of receptors for an organophosphate surrogate of the nerve agent soman. Proc Natl Acad Sci USA 101:7907-7912.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7907-7912
    • Allert, M.1    Rizk, S.S.2    Looger, L.L.3    Hellinga, H.W.4
  • 24
    • 0038752617 scopus 로고    scopus 로고
    • Computational design of receptor and sensor proteins with novel functions
    • Looger LL, Dwyer MA, Smith JJ, Hellinga HW (2003) Computational design of receptor and sensor proteins with novel functions. Nature 423:185-190.
    • (2003) Nature , vol.423 , pp. 185-190
    • Looger, L.L.1    Dwyer, M.A.2    Smith, J.J.3    Hellinga, H.W.4
  • 25
    • 73249124179 scopus 로고    scopus 로고
    • Computational design of ligand binding is not a solved problem
    • Schreier B, Stumpp C, Wiesner S, Hocker B (2009) Computational design of ligand binding is not a solved problem. Proc Natl Acad Sci USA 106:18491-18496.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 18491-18496
    • Schreier, B.1    Stumpp, C.2    Wiesner, S.3    Hocker, B.4
  • 27
    • 77949808895 scopus 로고    scopus 로고
    • Rational conversion of affinity reagents into label-free sensors for peptide motifs by designed allostery
    • Huang J, Koide S (2010) Rational conversion of affinity reagents into label-free sensors for peptide motifs by designed allostery. ACS Chem Biol 5:273-277.
    • (2010) ACS Chem Biol , vol.5 , pp. 273-277
    • Huang, J.1    Koide, S.2
  • 28
    • 44349104094 scopus 로고    scopus 로고
    • Design of protein function leaps by directed domain interface evolution
    • Huang J, Koide A, Makabe K, Koide S (2008) Design of protein function leaps by directed domain interface evolution. Proc Natl Acad Sci USA 105:6578-6583.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 6578-6583
    • Huang, J.1    Koide, A.2    Makabe, K.3    Koide, S.4
  • 29
    • 70149092506 scopus 로고    scopus 로고
    • Structural basis for exquisite specificity of affinity clamps, synthetic binding proteins generated through directed domain-interface evolution
    • Huang J, Makabe K, Biancalana M, Koide A, Koide S (2009) Structural basis for exquisite specificity of affinity clamps, synthetic binding proteins generated through directed domain-interface evolution. J Mol Biol 392:1221-1231.
    • (2009) J Mol Biol , vol.392 , pp. 1221-1231
    • Huang, J.1    Makabe, K.2    Biancalana, M.3    Koide, A.4    Koide, S.5
  • 30
    • 70149112322 scopus 로고    scopus 로고
    • Semisynthetic fluorescent sensor proteins based on self-labeling protein tags
    • Brun MA, Tan KT, Nakata E, Hinner MJ, Johnsson K (2009) Semisynthetic fluorescent sensor proteins based on self-labeling protein tags. J Am Chem Soc 131: 5873-5884.
    • (2009) J Am Chem Soc , vol.131 , pp. 5873-5884
    • Brun, M.A.1    Tan, K.T.2    Nakata, E.3    Hinner, M.J.4    Johnsson, K.5
  • 35
    • 29444445833 scopus 로고    scopus 로고
    • Sequence determinants of a conformational switch in a protein structure
    • Anderson TA, Cordes MH, Sauer RT (2005) Sequence determinants of a conformational switch in a protein structure. Proc Natl Acad Sci USA 102:18344-18349.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 18344-18349
    • Anderson, T.A.1    Cordes, M.H.2    Sauer, R.T.3
  • 36
    • 0025712476 scopus 로고
    • Stable, monomeric variants of lambda Cro obtained by insertion of a designed beta-hairpin sequence
    • Mossing MC, Sauer RT (1990) Stable, monomeric variants of lambda Cro obtained by insertion of a designed beta-hairpin sequence. Science 250:1712-1715.
    • (1990) Science , vol.250 , pp. 1712-1715
    • Mossing, M.C.1    Sauer, R.T.2
  • 37
    • 0033815822 scopus 로고    scopus 로고
    • Understanding the sequence determinants of conformational switching using protein design
    • Dalal S, Regan L (2000) Understanding the sequence determinants of conformational switching using protein design. Protein Sci 9:1651-1659.
    • (2000) Protein Sci , vol.9 , pp. 1651-1659
    • Dalal, S.1    Regan, L.2
  • 39
    • 31944435091 scopus 로고    scopus 로고
    • Computational design of a single amino acid sequence that can switch between two distinct protein folds
    • Ambroggio XI, Kuhlman B (2006) Computational design of a single amino acid sequence that can switch between two distinct protein folds. J Am Chem Soc 128:1154-1161.
    • (2006) J Am Chem Soc , vol.128 , pp. 1154-1161
    • Ambroggio, X.I.1    Kuhlman, B.2
  • 40
    • 0037077678 scopus 로고    scopus 로고
    • Conversion of antennapedia homeodomain to zinc finger-like domain: Zn(II)-induced change in protein conformation and DNA binding
    • Hori Y, Sugiura Y (2002) Conversion of antennapedia homeodomain to zinc finger-like domain: Zn(II)-induced change in protein conformation and DNA binding. J Am Chem Soc 124:9362-9363.
    • (2002) J Am Chem Soc , vol.124 , pp. 9362-9363
    • Hori, Y.1    Sugiura, Y.2
  • 41
    • 27544509859 scopus 로고    scopus 로고
    • ZiCo: A peptide designed to switch folded state upon binding zinc
    • Cerasoli E, Sharpe BK, Woolfson DN (2005) ZiCo: a peptide designed to switch folded state upon binding zinc. J Am Chem Soc 127:15008-15009.
    • (2005) J Am Chem Soc , vol.127 , pp. 15008-15009
    • Cerasoli, E.1    Sharpe, B.K.2    Woolfson, D.N.3
  • 42
    • 77951215979 scopus 로고    scopus 로고
    • NMR characterization of an engineered domain fusion between maltose binding protein and TEM1 beta-lactamase provides insight into its structure and allosteric mechanism
    • Wright CM, Majumdar A, Tolman JR, Ostermeier M (2010) NMR characterization of an engineered domain fusion between maltose binding protein and TEM1 beta-lactamase provides insight into its structure and allosteric mechanism. Proteins 78:1423-1430.
    • (2010) Proteins , vol.78 , pp. 1423-1430
    • Wright, C.M.1    Majumdar, A.2    Tolman, J.R.3    Ostermeier, M.4
  • 45
    • 0033613235 scopus 로고    scopus 로고
    • Circular permutation and receptor insertion within green fluorescent protein
    • Baird GS, Zacharias DA, Tsien RY (1999) Circular permutation and receptor insertion within green fluorescent protein. Proc Natl Acad Sci USA 96:11241-11246.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11241-11246
    • Baird, G.S.1    Zacharias, D.A.2    Tsien, R.Y.3
  • 47
    • 8844263869 scopus 로고    scopus 로고
    • A molecular switch created by in vitro recombination of nonhomologous genes
    • Guntas G, Mitchell SF, Ostermeier M (2004) A molecular switch created by in vitro recombination of nonhomologous genes. Chem Biol 11:1483-1487.
    • (2004) Chem Biol , vol.11 , pp. 1483-1487
    • Guntas, G.1    Mitchell, S.F.2    Ostermeier, M.3
  • 48
    • 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 336:263-273.
    • (2004) J Mol Biol , vol.336 , pp. 263-273
    • Guntas, G.1    Ostermeier, M.2
  • 49
    • 23844465160 scopus 로고    scopus 로고
    • Directed evolution of protein switches and their application to the creation of ligand-binding proteins
    • Guntas G, Mansell TJ, Kim JR, 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
  • 50
    • 48349086462 scopus 로고    scopus 로고
    • Linking the functions of unrelated proteins using a novel directed evolution domain insertion method
    • Edwards WR, Busse K, Allemann RK, Jones DD (2008) Linking the functions of unrelated proteins using a novel directed evolution domain insertion method. Nucleic Acids Res 36:e78.
    • (2008) Nucleic Acids Res , vol.36
    • Edwards, W.R.1    Busse, K.2    Allemann, R.K.3    Jones, D.D.4
  • 52
    • 34447273196 scopus 로고    scopus 로고
    • Thermodynamic analysis of an antagonistic folding-unfolding equilibrium between two protein domains
    • Cutler T, Loh SN (2007) Thermodynamic analysis of an antagonistic folding-unfolding equilibrium between two protein domains. J Mol Biol 371:308-316.
    • (2007) J Mol Biol , vol.371 , pp. 308-316
    • Cutler, T.1    Loh, S.N.2
  • 53
    • 59649096956 scopus 로고    scopus 로고
    • Effect of interdomain linker length on an antagonistic folding-unfolding equilibrium between two protein domains
    • Cutler T, Mills BM, Lubin DJ, Chong LT, Loh SN (2009) Effect of interdomain linker length on an antagonistic folding-unfolding equilibrium between two protein domains. J Mol Biol 386:854-868.
    • (2009) J Mol Biol , vol.386 , pp. 854-868
    • Cutler, T.1    Mills, B.M.2    Lubin, D.J.3    Chong, L.T.4    Loh, S.N.5
  • 54
    • 33644831449 scopus 로고    scopus 로고
    • Modular enzyme design: Regulation by mutually exclusive protein folding
    • Ha J-H, Butler JS, Mitrea DM, Loh SN (2006) Modular enzyme design: regulation by mutually exclusive protein folding. J Mol Biol 357:1058-1062.
    • (2006) J Mol Biol , vol.357 , pp. 1058-1062
    • Ha, J.-H.1    Butler, J.S.2    Mitrea, D.M.3    Loh, S.N.4
  • 55
    • 70349386569 scopus 로고    scopus 로고
    • Direct observation of tug-of-war during the folding of a mutually exclusive protein
    • Peng Q, Li H (2009) Direct observation of tug-of-war during the folding of a mutually exclusive protein. J Am Chem Soc 131:13347-13354.
    • (2009) J Am Chem Soc , vol.131 , pp. 13347-13354
    • Peng, Q.1    Li, H.2
  • 56
    • 34247465989 scopus 로고    scopus 로고
    • Engineering modular protein interaction switches by sequence overlap
    • Sallee NA, Yeh BJ, Lim WA (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
  • 57
    • 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 105:10709-10714.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 10709-10714
    • Strickland, D.1    Moffat, K.2    Sosnick, T.R.3
  • 58
    • 78650790188 scopus 로고    scopus 로고
    • A photoswitchable DNA-binding protein based on a truncated GCN4-photoactive yellow protein chimera
    • Morgan SA, Woolley GA (2010) A photoswitchable DNA-binding protein based on a truncated GCN4-photoactive yellow protein chimera. Photochem Photobiol Sci.
    • (2010) Photochem Photobiol Sci
    • Morgan, S.A.1    Woolley, G.A.2
  • 59
    • 77953083303 scopus 로고    scopus 로고
    • Structure-based design of a photocontrolled DNA binding protein
    • Morgan SA, Al-Abdul-Wahid S, Woolley GA (2010) Structure-based design of a photocontrolled DNA binding protein. J Mol Biol 399:94-112.
    • (2010) J Mol Biol , vol.399 , pp. 94-112
    • Morgan, S.A.1    Al-Abdul-Wahid, S.2    Woolley, G.A.3
  • 60
    • 4143119033 scopus 로고    scopus 로고
    • Use of sequence duplication to engineer a ligand-triggered, long distance molecular switch in T4 lysozyme
    • Yousef MS, Baase WA, Matthews BW (2004) Use of sequence duplication to engineer a ligand-triggered, long distance molecular switch in T4 lysozyme. Proc Natl Acad Sci USA 101:11583-11586.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 11583-11586
    • Yousef, M.S.1    Baase, W.A.2    Matthews, B.W.3
  • 61
    • 0033028682 scopus 로고    scopus 로고
    • Structural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein folding
    • Sagermann M, Baase WA, Matthews BW (1999) Structural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein folding. Proc Natl Acad Sci USA 96:6078-6083.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6078-6083
    • Sagermann, M.1    Baase, W.A.2    Matthews, B.W.3
  • 63
    • 57049128294 scopus 로고    scopus 로고
    • Design and characterization of an HIV-specific ribonuclease zymogen
    • Turcotte RF, Raines RT (2008) Design and characterization of an HIV-specific ribonuclease zymogen. AIDS Res Human Retro 24:1357-1363.
    • (2008) AIDS Res Human Retro , vol.24 , pp. 1357-1363
    • Turcotte, R.F.1    Raines, R.T.2
  • 64
    • 33751112474 scopus 로고    scopus 로고
    • A ribonuclease zymogen activated by the NS3 protease of the hepatitis C virus
    • Johnson RJ, Lin SR, Raines RT (2006) A ribonuclease zymogen activated by the NS3 protease of the hepatitis C virus. FEBS J 273:5457-5465.
    • (2006) FEBS J , vol.273 , pp. 5457-5465
    • Johnson, R.J.1    Lin, S.R.2    Raines, R.T.3
  • 65
    • 65249094239 scopus 로고    scopus 로고
    • Structural and thermodynamic analysis of a conformationally-strained circular permutant of barnase
    • Butler JS, Mitrea DM, Mitrousis G, Cingolani G, Loh SN (2009) Structural and thermodynamic analysis of a conformationally-strained circular permutant of barnase. Biochemistry 48:3497-3507.
    • (2009) Biochemistry , vol.48 , pp. 3497-3507
    • Butler, J.S.1    Mitrea, D.M.2    Mitrousis, G.3    Cingolani, G.4    Loh, S.N.5
  • 66
    • 77649241924 scopus 로고    scopus 로고
    • Engineering an artificial zymogen by alternate frame protein folding
    • Mitrea DM, Parsons L, Loh SN (2010) Engineering an artificial zymogen by alternate frame protein folding. Proc Natl Acad Sci USA 107:2824-2829.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 2824-2829
    • Mitrea, D.M.1    Parsons, L.2    Loh, S.N.3
  • 67
    • 62349086577 scopus 로고    scopus 로고
    • Beyond molecular beacons: Optical sensors based on the binding-induced folding of proteins and polypeptides
    • Oh KJ, Cash KJ, Plaxco KW (2009) Beyond molecular beacons: optical sensors based on the binding-induced folding of proteins and polypeptides. Chemistry 15: 2244-2251.
    • (2009) Chemistry , vol.15 , pp. 2244-2251
    • Oh, K.J.1    Cash, K.J.2    Plaxco, K.W.3
  • 68
    • 0020520185 scopus 로고
    • Amino and carboxyterminal regions in globular proteins
    • Thornton JM, Sibanda BL (1983) Amino and carboxyterminal regions in globular proteins. J Mol Biol 167: 443-460.
    • (1983) J Mol Biol , vol.167 , pp. 443-460
    • Thornton, J.M.1    Sibanda, B.L.2
  • 69
    • 12844284527 scopus 로고    scopus 로고
    • The N-terminal to C-terminal motif in protein folding and function
    • Krishna MM, Englander SW (2005) The N-terminal to C-terminal motif in protein folding and function. Proc Natl Acad Sci USA 102:1053-1058.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 1053-1058
    • Krishna, M.M.1    Englander, S.W.2
  • 70
    • 34347353352 scopus 로고    scopus 로고
    • Peptide beacons: A new design for polypeptide-based optical biosensors
    • Oh KJ, Cash KJ, Hugenberg V, Plaxco KW (2007) Peptide beacons: a new design for polypeptide-based optical biosensors. Bioconjug Chem 18:607-609.
    • (2007) Bioconjug Chem , vol.18 , pp. 607-609
    • Oh, K.J.1    Cash, K.J.2    Hugenberg, V.3    Plaxco, K.W.4
  • 71
    • 37549022261 scopus 로고    scopus 로고
    • Chimeric peptide beacons: A direct polypeptide analog of DNA molecular beacons
    • Oh KJ, Cash KJ, Lubin AA, Plaxco KW (2007) Chimeric peptide beacons: a direct polypeptide analog of DNA molecular beacons. Chem Commun (Camb) 4869-4871.
    • (2007) Chem Commun (Camb) , pp. 4869-4871
    • Oh, K.J.1    Cash, K.J.2    Lubin, A.A.3    Plaxco, K.W.4
  • 72
    • 33750458342 scopus 로고    scopus 로고
    • Excimer-based peptide beacons: A convenient experimental approach for monitoring polypeptide-protein and polypeptide-oligonucleotide interactions
    • Oh KJ, Cash KJ, Plaxco KW (2006) Excimer-based peptide beacons: a convenient experimental approach for monitoring polypeptide-protein and polypeptide-oligonucleotide interactions. J Am Chem Soc 128:14018-14019.
    • (2006) J Am Chem Soc , vol.128 , pp. 14018-14019
    • Oh, K.J.1    Cash, K.J.2    Plaxco, K.W.3
  • 73
    • 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 102:10841-10845.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 10841-10845
    • Kohn, J.E.1    Plaxco, K.W.2
  • 74
    • 27444437925 scopus 로고    scopus 로고
    • Rational design of p53, an intrinsically unstructured protein, for the fabrication of novel molecular sensors
    • Geddie ML, O'Loughlin TL, Woods KK, Matsumura I (2005) Rational design of p53, an intrinsically unstructured protein, for the fabrication of novel molecular sensors. J Biol Chem 280:35641-35646.
    • (2005) J Biol Chem , vol.280 , pp. 35641-35646
    • Geddie, M.L.1    O'Loughlin, T.L.2    Woods, K.K.3    Matsumura, I.4
  • 76
    • 68649110959 scopus 로고    scopus 로고
    • Bridging the gap: From protein misfolding to protein misfolding diseases
    • Luheshi LM, Dobson CM (2009) Bridging the gap: from protein misfolding to protein misfolding diseases. FEBS Lett 583:2581-2586.
    • (2009) FEBS Lett , vol.583 , pp. 2581-2586
    • Luheshi, L.M.1    Dobson, C.M.2
  • 77
    • 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 3:723-732.
    • (2008) ACS Chem Biol , vol.3 , pp. 723-732
    • Stratton, M.M.1    Mitrea, D.M.2    Loh, S.N.3
  • 78
    • 78349276506 scopus 로고    scopus 로고
    • On the mechanism of protein fold-switching by a molecular sensor
    • Stratton MM, Loh SN (2010) On the mechanism of protein fold-switching by a molecular sensor. Proteins 78: 3260-3269.
    • (2010) Proteins , vol.78 , pp. 3260-3269
    • Stratton, M.M.1    Loh, S.N.2
  • 79
    • 0029017511 scopus 로고
    • Determination of the solution structure of apo calbindin D9k by NMR spectroscopy
    • Skelton NJ, Kordel J, Chazin WJ (1995) Determination of the solution structure of apo calbindin D9k by NMR spectroscopy. J Mol Biol 249:441-462.
    • (1995) J Mol Biol , vol.249 , pp. 441-462
    • Skelton, N.J.1    Kordel, J.2    Chazin, W.J.3
  • 80
    • 69549120468 scopus 로고    scopus 로고
    • Thermodynamic basis for the optimization of binding-induced biomolecular switches and structure-switching biosensors
    • Vallee-Belisle 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 106:13802-13807.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 13802-13807
    • Vallee-Belisle, A.1    Ricci, F.2    Plaxco, K.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.