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Volumn 110, Issue 14, 2013, Pages 5315-5320

Catalytic DNA with phosphatase activity

Author keywords

[No Author keywords available]

Indexed keywords

DEOXYRIBOZYME; DNA; PHOSPHATASE; PHOSPHOSERINE; SERINE; TYROSINE;

EID: 84875856674     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1221946110     Document Type: Article
Times cited : (49)

References (40)
  • 1
    • 0028918401 scopus 로고
    • A proficient enzyme
    • Radzicka A, Wolfenden R (1995) A proficient enzyme. Science 267(5194):90-93.
    • (1995) Science , vol.267 , Issue.5194 , pp. 90-93
    • Radzicka, A.1    Wolfenden, R.2
  • 2
    • 0038286174 scopus 로고    scopus 로고
    • The rate of hydrolysis of phosphomonoester dianions and the exceptional catalytic proficiencies of protein and inositol phosphatases
    • Lad C, Williams NH, Wolfenden R (2003) The rate of hydrolysis of phosphomonoester dianions and the exceptional catalytic proficiencies of protein and inositol phosphatases. Proc Natl Acad Sci USA 100(10):5607-5610.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.10 , pp. 5607-5610
    • Lad, C.1    Williams, N.H.2    Wolfenden, R.3
  • 3
    • 34548311711 scopus 로고    scopus 로고
    • Forty years of in vitro evolution
    • Joyce GF (2007) Forty years of in vitro evolution. Angew Chem Int Ed 46(34): 6420-6436.
    • (2007) Angew Chem Int Ed , vol.46 , Issue.34 , pp. 6420-6436
    • Joyce, G.F.1
  • 4
    • 77951731728 scopus 로고    scopus 로고
    • Deoxyribozymes: Selection design and serendipity in the development of DNA catalysts
    • Silverman SK (2009) Deoxyribozymes: Selection design and serendipity in the development of DNA catalysts. Acc Chem Res 42(10):1521-1531.
    • (2009) Acc Chem Res , vol.42 , Issue.10 , pp. 1521-1531
    • Silverman, S.K.1
  • 5
    • 62649161589 scopus 로고    scopus 로고
    • Biologically inspired synthetic enzymes made from DNA
    • Schlosser K, Li Y (2009) Biologically inspired synthetic enzymes made from DNA. Chem Biol 16(3):311-322.
    • (2009) Chem Biol , vol.16 , Issue.3 , pp. 311-322
    • Schlosser, K.1    Li, Y.2
  • 6
    • 77957362844 scopus 로고    scopus 로고
    • DNA as a versatile chemical component for catalysis, encoding, and stereocontrol
    • Silverman SK (2010) DNA as a versatile chemical component for catalysis, encoding, and stereocontrol. Angew Chem Int Ed 49(40):7180-7201.
    • (2010) Angew Chem Int Ed , vol.49 , Issue.40 , pp. 7180-7201
    • Silverman, S.K.1
  • 7
    • 80052102623 scopus 로고    scopus 로고
    • Strategy and success for the directed evolution of enzymes
    • Dalby PA (2011) Strategy and success for the directed evolution of enzymes. Curr Opin Struct Biol 21(4):473-480.
    • (2011) Curr Opin Struct Biol , vol.21 , Issue.4 , pp. 473-480
    • Dalby, P.A.1
  • 8
    • 0035810165 scopus 로고    scopus 로고
    • Functional proteins from a random-sequence library
    • Keefe AD, Szostak JW (2001) Functional proteins from a random-sequence library. Nature 410(6829):715-718.
    • (2001) Nature , vol.410 , Issue.6829 , pp. 715-718
    • Keefe, A.D.1    Szostak, J.W.2
  • 9
    • 70349327390 scopus 로고    scopus 로고
    • DNA-catalyzed sequence-specific hydrolysis of DNA
    • Chandra M, Sachdeva A, Silverman SK (2009) DNA-catalyzed sequence-specific hydrolysis of DNA. Nat Chem Biol 5(10):718-720.
    • (2009) Nat Chem Biol , vol.5 , Issue.10 , pp. 718-720
    • Chandra, M.1    Sachdeva, A.2    Silverman, S.K.3
  • 10
    • 84857807846 scopus 로고    scopus 로고
    • Establishing broad generality of DNA catalysts for site-specific hydrolysis of single-stranded DNA
    • Xiao Y, Wehrmann RJ, Ibrahim NA, Silverman SK (2012) Establishing broad generality of DNA catalysts for site-specific hydrolysis of single-stranded DNA. Nucleic Acids Res 40(4):1778-1786.
    • (2012) Nucleic Acids Res , vol.40 , Issue.4 , pp. 1778-1786
    • Xiao, Y.1    Wehrmann, R.J.2    Ibrahim, N.A.3    Silverman, S.K.4
  • 11
    • 0037062949 scopus 로고    scopus 로고
    • The chemical repertoire of natural ribozymes
    • Doudna JA, Cech TR (2002) The chemical repertoire of natural ribozymes. Nature 418(6894):222-228.
    • (2002) Nature , vol.418 , Issue.6894 , pp. 222-228
    • Doudna, J.A.1    Cech, T.R.2
  • 13
    • 0041305819 scopus 로고    scopus 로고
    • A common speed limit for RNA-cleaving ribozymes and deoxyribozymes
    • Breaker RR, et al. (2003) A common speed limit for RNA-cleaving ribozymes and deoxyribozymes. RNA 9(8):949-957.
    • (2003) RNA , vol.9 , Issue.8 , pp. 949-957
    • Breaker, R.R.1
  • 15
    • 77949583070 scopus 로고    scopus 로고
    • DNA-catalyzed serine side chain reactivity and selectivity
    • Sachdeva A, Silverman SK (2010) DNA-catalyzed serine side chain reactivity and selectivity. Chem Commun 46(13):2215-2217.
    • (2010) Chem Commun , vol.46 , Issue.13 , pp. 2215-2217
    • Sachdeva, A.1    Silverman, S.K.2
  • 16
    • 79958105696 scopus 로고    scopus 로고
    • DNA-catalyzed covalent modification of amino acid side chains in tethered and free peptide substrates
    • Wong OY, Pradeepkumar PI, Silverman SK (2011) DNA-catalyzed covalent modification of amino acid side chains in tethered and free peptide substrates. Biochemistry 50(21):4741-4749.
    • (2011) Biochemistry , vol.50 , Issue.21 , pp. 4741-4749
    • Wong, O.Y.1    Pradeepkumar, P.I.2    Silverman, S.K.3
  • 17
    • 84858311242 scopus 로고    scopus 로고
    • Covalent tagging of phosphorylated peptides by phosphate-specific deoxyribozymes
    • Sachdeva A, Chandra M, Chandrasekar J, Silverman SK (2012) Covalent tagging of phosphorylated peptides by phosphate-specific deoxyribozymes. ChemBioChem 13(5): 654-657.
    • (2012) ChemBioChem , vol.13 , Issue.5 , pp. 654-657
    • Sachdeva, A.1    Chandra, M.2    Chandrasekar, J.3    Silverman, S.K.4
  • 18
    • 77953742146 scopus 로고    scopus 로고
    • Catalytic promiscuity in the biosynthesis of cyclic peptide secondary metabolites in planktonic marine cyanobacteria
    • Li B, et al. (2010) Catalytic promiscuity in the biosynthesis of cyclic peptide secondary metabolites in planktonic marine cyanobacteria. Proc Natl Acad Sci USA 107(23): 10430-10435.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.23 , pp. 10430-10435
    • Li, B.1
  • 19
    • 33645212804 scopus 로고    scopus 로고
    • The time required for water attack at the phosphorus atom of simple phosphodiesters and of DNA
    • Schroeder GK, Lad C, Wyman P, Williams NH, Wolfenden R (2006) The time required for water attack at the phosphorus atom of simple phosphodiesters and of DNA. Proc Natl Acad Sci USA 103(11):4052-4055.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.11 , pp. 4052-4055
    • Schroeder, G.K.1    Lad, C.2    Wyman, P.3    Williams, N.H.4    Wolfenden, R.5
  • 20
    • 79959432785 scopus 로고    scopus 로고
    • Biological phosphoryl-transfer reactions: Understanding mechanism and catalysis
    • Lassila JK, Zalatan JG, Herschlag D (2011) Biological phosphoryl-transfer reactions: understanding mechanism and catalysis. Annu Rev Biochem 80:669-702.
    • (2011) Annu Rev Biochem , vol.80 , pp. 669-702
    • Lassila, J.K.1    Zalatan, J.G.2    Herschlag, D.3
  • 21
    • 0032952507 scopus 로고    scopus 로고
    • Crystal structure of an 82-nucleotide RNA-DNA complex formed by the 10-23 DNA enzyme
    • Nowakowski J, Shim PJ, Prasad GS, Stout CD, Joyce GF (1999) Crystal structure of an 82-nucleotide RNA-DNA complex formed by the 10-23 DNA enzyme. Nat Struct Biol 6(2):151-156.
    • (1999) Nat Struct Biol , vol.6 , Issue.2 , pp. 151-156
    • Nowakowski, J.1    Shim, P.J.2    Prasad, G.S.3    Stout, C.D.4    Joyce, G.F.5
  • 22
    • 0031860103 scopus 로고    scopus 로고
    • The structure and mechanism of protein phosphatases: Insights into catalysis and regulation
    • Barford D, Das AK, Egloff MP (1998) The structure and mechanism of protein phosphatases: insights into catalysis and regulation. Annu Rev Biophys Biomol Struct 27: 133-164.
    • (1998) Annu Rev Biophys Biomol Struct , vol.27 , pp. 133-164
    • Barford, D.1    Das, A.K.2    Egloff, M.P.3
  • 23
    • 0035413604 scopus 로고    scopus 로고
    • Molecular reactions of protein phosphatases-Insights from structure and chemistry
    • Jackson MD, Denu JM (2001) Molecular reactions of protein phosphatases-Insights from structure and chemistry. Chem Rev 101(8):2313-2340.
    • (2001) Chem Rev , vol.101 , Issue.8 , pp. 2313-2340
    • Jackson, M.D.1    Denu, J.M.2
  • 24
    • 0029043627 scopus 로고
    • A catalytic mechanism for the dual-specific phosphatases
    • Denu JM, Dixon JE (1995) A catalytic mechanism for the dual-specific phosphatases. Proc Natl Acad Sci USA 92(13):5910-5914.
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.13 , pp. 5910-5914
    • Denu, J.M.1    Dixon, J.E.2
  • 25
    • 33750299450 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: From genes, to function, to disease
    • Tonks NK (2006) Protein tyrosine phosphatases: From genes, to function, to disease. Nat Rev Mol Cell Biol 7(11):833-846.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , Issue.11 , pp. 833-846
    • Tonks, N.K.1
  • 26
    • 4344585269 scopus 로고    scopus 로고
    • Phosphoryl group transfer: Evolution of a catalytic scaffold
    • Allen KN, Dunaway-Mariano D (2004) Phosphoryl group transfer: Evolution of a catalytic scaffold. Trends Biochem Sci 29(9):495-503.
    • (2004) Trends Biochem Sci , vol.29 , Issue.9 , pp. 495-503
    • Allen, K.N.1    Dunaway-Mariano, D.2
  • 27
    • 70549106287 scopus 로고    scopus 로고
    • Markers of fitness in a successful enzyme superfamily
    • Allen KN, Dunaway-Mariano D (2009) Markers of fitness in a successful enzyme superfamily. Curr Opin Struct Biol 19(6):658-665.
    • (2009) Curr Opin Struct Biol , vol.19 , Issue.6 , pp. 658-665
    • Allen, K.N.1    Dunaway-Mariano, D.2
  • 28
    • 84872817040 scopus 로고    scopus 로고
    • Human HAD phosphatases: Structure, mechanism, and roles in health and disease
    • Seifried A, Schultz J, Gohla A (2013) Human HAD phosphatases: structure, mechanism, and roles in health and disease. FEBS J 280(2):549-571.
    • (2013) FEBS J , vol.280 , Issue.2 , pp. 549-571
    • Seifried, A.1    Schultz, J.2    Gohla, A.3
  • 29
    • 70350340056 scopus 로고    scopus 로고
    • Serine/threonine phosphatases: Mechanism through structure
    • Shi Y (2009) Serine/threonine phosphatases: Mechanism through structure. Cell 139(3):468-484.
    • (2009) Cell , vol.139 , Issue.3 , pp. 468-484
    • Shi, Y.1
  • 30
    • 4644314829 scopus 로고    scopus 로고
    • Do electrostatic interactions with positively charged active site groups tighten the transition state for enzymatic phosphoryl transfer?
    • Nikolic-Hughes I, Rees DC, Herschlag D (2004) Do electrostatic interactions with positively charged active site groups tighten the transition state for enzymatic phosphoryl transfer? J Am Chem Soc 126(38):11814-11819.
    • (2004) J Am Chem Soc , vol.126 , Issue.38 , pp. 11814-11819
    • Nikolic-Hughes, I.1    Rees, D.C.2    Herschlag, D.3
  • 31
    • 0028105959 scopus 로고
    • Structural studies of metal binding by inositol monophosphatase: Evidence for two-metal ion catalysis
    • Bone R, Frank L, Springer JP, Atack JR (1994) Structural studies of metal binding by inositol monophosphatase: Evidence for two-metal ion catalysis. Biochemistry 33(32): 9468-9476.
    • (1994) Biochemistry , vol.33 , Issue.32 , pp. 9468-9476
    • Bone, R.1    Frank, L.2    Springer, J.P.3    Atack, J.R.4
  • 32
    • 0034713880 scopus 로고    scopus 로고
    • Crystal structures of fructose 1, 6-bisphosphatase: Mechanism of catalysis and allosteric inhibition revealed in product complexes
    • Choe J-Y, Fromm HJ, Honzatko RB (2000) Crystal structures of fructose 1, 6-bisphosphatase: mechanism of catalysis and allosteric inhibition revealed in product complexes. Biochemistry 39(29):8565-8574.
    • (2000) Biochemistry , vol.39 , Issue.29 , pp. 8565-8574
    • Choe, J.-Y.1    Fromm, H.J.2    Honzatko, R.B.3
  • 33
    • 34250773963 scopus 로고    scopus 로고
    • The role of metal ions in phosphate ester hydrolysis
    • Kamerlin SCL, Wilkie J (2007) The role of metal ions in phosphate ester hydrolysis. Org Biomol Chem 5(13):2098-2108.
    • (2007) Org Biomol Chem , vol.5 , Issue.13 , pp. 2098-2108
    • Scl, K.1    Wilkie, J.2
  • 34
    • 40149088986 scopus 로고    scopus 로고
    • Prodrugs: Design and clinical applications
    • Rautio J, et al. (2008) Prodrugs: Design and clinical applications. Nat Rev Drug Discov 7(3):255-270.
    • (2008) Nat Rev Drug Discov , vol.7 , Issue.3 , pp. 255-270
    • Rautio, J.1
  • 35
    • 0023651444 scopus 로고
    • Oligoribonucleotide synthesis using T7 RNA polymerase and synthetic DNA templates
    • Milligan JF, Groebe DR, Witherell GW, Uhlenbeck OC (1987) Oligoribonucleotide synthesis using T7 RNA polymerase and synthetic DNA templates. Nucleic Acids Res 15(21):8783-8798.
    • (1987) Nucleic Acids Res , vol.15 , Issue.21 , pp. 8783-8798
    • Milligan, J.F.1    Groebe, D.R.2    Witherell, G.W.3    Uhlenbeck, O.C.4
  • 36
    • 0037420377 scopus 로고    scopus 로고
    • Deoxyribozymes with 2'-5' RNA ligase activity
    • Flynn-Charlebois A, et al. (2003) Deoxyribozymes with 2'-5' RNA ligase activity. J Am Chem Soc 125(9):2444-2454.
    • (2003) J Am Chem Soc , vol.125 , Issue.9 , pp. 2444-2454
    • Flynn-Charlebois, A.1
  • 37
    • 0347594188 scopus 로고    scopus 로고
    • Characterization of deoxyribozymes that synthesize branched RNA
    • Wang Y, Silverman SK (2003) Characterization of deoxyribozymes that synthesize branched RNA. Biochemistry 42(51):15252-15263.
    • (2003) Biochemistry , vol.42 , Issue.51 , pp. 15252-15263
    • Wang, Y.1    Silverman, S.K.2
  • 39
    • 77951081423 scopus 로고    scopus 로고
    • Chemistry and biology of deoxynyboquinone, a potent inducer of cancer cell death
    • Bair JS, Palchaudhuri R, Hergenrother PJ (2010) Chemistry and biology of deoxynyboquinone, a potent inducer of cancer cell death. J Am Chem Soc 132(15): 5469-5478.
    • (2010) J Am Chem Soc , vol.132 , Issue.15 , pp. 5469-5478
    • Bair, J.S.1    Palchaudhuri, R.2    Hergenrother, P.J.3
  • 40
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko A, Tomas H, Havlis J, Olsen JV, Mann M (2006) In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat Protoc 1(6): 2856-2860.
    • (2006) Nat Protoc , vol.1 , Issue.6 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5


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