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Volumn 20, Issue 11, 2015, Pages 20777-20804

DNA catalysis: The chemical repertoire of DNAzymes

Author keywords

Biosensors; Chemically modified nucleic acids; DNAzymes; Functional nucleic acids; SELEX; Therapeutic nucleic acids

Indexed keywords

DEOXYRIBOZYME; DNA; RNA;

EID: 84949948073     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules201119730     Document Type: Review
Times cited : (128)

References (220)
  • 1
    • 52949116414 scopus 로고    scopus 로고
    • Assembling materials with DNA as the guide
    • [CrossRef] [PubMed]
    • Aldaye, F.A.; Palmer, A.L.; Sleiman, H.F. Assembling Materials with DNA as the Guide. Science 2008, 321, 1795-1799. [CrossRef] [PubMed]
    • (2008) Science , vol.321 , pp. 1795-1799
    • Aldaye, F.A.1    Palmer, A.L.2    Sleiman, H.F.3
  • 2
    • 84928143555 scopus 로고    scopus 로고
    • Programmable materials and the nature of the DNA bond
    • [CrossRef] [PubMed]
    • Jones, M.R.; Seeman, N.C.; Mirkin, C.A. Programmable materials and the nature of the DNA bond. Science 2015, 347, 840-852. [CrossRef] [PubMed]
    • (2015) Science , vol.347 , pp. 840-852
    • Jones, M.R.1    Seeman, N.C.2    Mirkin, C.A.3
  • 3
    • 77949512140 scopus 로고    scopus 로고
    • RNA targeting therapeutics: Molecular mechanisms of antisense oligonucleotides as a therapeutic platform
    • [CrossRef] [PubMed]
    • Bennett, C.F.; Swayze, E.E. RNA Targeting Therapeutics: Molecular Mechanisms of Antisense Oligonucleotides as a Therapeutic Platform. Annu. Rev. Pharmacol. Toxicol. 2010, 50, 259-293. [CrossRef] [PubMed]
    • (2010) Annu. Rev. Pharmacol. Toxicol. , vol.50 , pp. 259-293
    • Bennett, C.F.1    Swayze, E.E.2
  • 5
    • 84859131430 scopus 로고    scopus 로고
    • Fluorescent and colorimetric sensors for detection of lead, cadmium, and mercury ions
    • [CrossRef] [PubMed]
    • Kim, H.N.; Ren, W.X.; Kim, J.S.; Yoon, J. Fluorescent and colorimetric sensors for detection of lead, cadmium, and mercury ions. Chem. Soc. Rev. 2012, 41, 3210-3244. [CrossRef] [PubMed]
    • (2012) Chem. Soc. Rev. , vol.41 , pp. 3210-3244
    • Kim, H.N.1    Ren, W.X.2    Kim, J.S.3    Yoon, J.4
  • 6
    • 84878222888 scopus 로고    scopus 로고
    • Biosensors: Sense and sensibility
    • [CrossRef] [PubMed]
    • Turner, A.P.F. Biosensors: Sense and sensibility. Chem. Soc. Rev. 2013, 42, 3184-3196. [CrossRef] [PubMed]
    • (2013) Chem. Soc. Rev. , vol.42 , pp. 3184-3196
    • Turner, A.P.F.1
  • 7
    • 84899065372 scopus 로고    scopus 로고
    • Rolling circle amplification: A versatile tool for chemical biology, materials science and medicine
    • [CrossRef] [PubMed]
    • Ali, M.M.; Li, F.; Zhang, Z.; Zhang, K.; Kang, D.K.; Ankrum, J.A.; Le, X.C.; Zhao, W. Rolling circle amplification: A versatile tool for chemical biology, materials science and medicine. Chem. Soc. Rev. 2014, 43, 3324-3341. [CrossRef] [PubMed]
    • (2014) Chem. Soc. Rev. , vol.43 , pp. 3324-3341
    • Ali, M.M.1    Li, F.2    Zhang, Z.3    Zhang, K.4    Kang, D.K.5    Ankrum, J.A.6    Le, X.C.7    Zhao, W.8
  • 8
    • 44349092480 scopus 로고    scopus 로고
    • DNAzymes for sensing, nanobiotechnology and logic gate applications
    • [CrossRef] [PubMed]
    • Willner, I.; Shlyahovsky, B.; Zayats, M.; Willner, B. DNAzymes for sensing, nanobiotechnology and logic gate applications. Chem. Soc. Rev. 2008, 37, 1153-1165. [CrossRef] [PubMed]
    • (2008) Chem. Soc. Rev. , vol.37 , pp. 1153-1165
    • Willner, I.1    Shlyahovsky, B.2    Zayats, M.3    Willner, B.4
  • 9
    • 84922653837 scopus 로고    scopus 로고
    • Multiple types of logic gates based on a single G-quadruplex DNA strand
    • [CrossRef] [PubMed]
    • Guo, Y.; Zhou, L.; Xu, L.; Zhou, X.; Hu, J.; Pei, R. Multiple types of logic gates based on a single G-quadruplex DNA strand. Sci. Rep. 2014, 4, 7315. [CrossRef] [PubMed]
    • (2014) Sci. Rep. , vol.4 , pp. 7315
    • Guo, Y.1    Zhou, L.2    Xu, L.3    Zhou, X.4    Hu, J.5    Pei, R.6
  • 10
    • 84923247254 scopus 로고    scopus 로고
    • A survey of advancements in nucleic acid-based logic gates and computing for applications in biotechnology and biomedicine
    • [CrossRef] [PubMed]
    • Wu, C.; Wan, S.; Hou, W.; Zhang, L.; Xu, J.; Cui, C.; Wang, Y.; Hu, J.; Tan, W. A survey of advancements in nucleic acid-based logic gates and computing for applications in biotechnology and biomedicine. Chem. Commun. 2015, 51, 3723-3734. [CrossRef] [PubMed]
    • (2015) Chem. Commun. , vol.51 , pp. 3723-3734
    • Wu, C.1    Wan, S.2    Hou, W.3    Zhang, L.4    Xu, J.5    Cui, C.6    Wang, Y.7    Hu, J.8    Tan, W.9
  • 11
    • 84923878510 scopus 로고    scopus 로고
    • Catalytic nucleic acids (DNAzymes) as functional units for logic gates and computing circuits: From basic principles to practical applications
    • [CrossRef] [PubMed]
    • Orbach, R.;Willner, B.;Willner, I. Catalytic nucleic acids (DNAzymes) as functional units for logic gates and computing circuits: From basic principles to practical applications. Chem. Commun. 2015, 51, 4144-4160. [CrossRef] [PubMed]
    • (2015) Chem. Commun. , vol.51 , pp. 4144-4160
    • Orbach, R.1    Willner, B.2    Willner, I.3
  • 12
    • 33747164245 scopus 로고    scopus 로고
    • Aptamers come of age-at last
    • [CrossRef] [PubMed]
    • Bunka, D.H.J.; Stockley, P.G. Aptamers come of age-At last. Nat. Rev. Microbiol. 2006, 4, 588-596. [CrossRef] [PubMed]
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 588-596
    • Bunka, D.H.J.1    Stockley, P.G.2
  • 13
    • 70349786346 scopus 로고    scopus 로고
    • The chemical biology of aptamers
    • [CrossRef] [PubMed]
    • Mayer, G. The Chemical Biology of Aptamers. Angew. Chem. Int. Ed. 2009, 48, 2672-2689. [CrossRef] [PubMed]
    • (2009) Angew. Chem. Int. Ed. , vol.48 , pp. 2672-2689
    • Mayer, G.1
  • 14
    • 84874429717 scopus 로고    scopus 로고
    • Dressed for success-applying chemistry to modulate aptamer functionality
    • [CrossRef]
    • Tolle, F.; Mayer, G. Dressed for success-applying chemistry to modulate aptamer functionality. Chem. Sci. 2013, 4, 60-67. [CrossRef]
    • (2013) Chem. Sci. , vol.4 , pp. 60-67
    • Tolle, F.1    Mayer, G.2
  • 15
    • 84942746901 scopus 로고    scopus 로고
    • Generation of aptamers with an expanded chemical repertoire
    • [CrossRef] [PubMed]
    • Diafa, S.; Hollenstein, M. Generation of aptamers with an expanded chemical repertoire. Molecules 2015, 20, 16643-16671. [CrossRef] [PubMed]
    • (2015) Molecules , vol.20 , pp. 16643-16671
    • Diafa, S.1    Hollenstein, M.2
  • 16
    • 34548311711 scopus 로고    scopus 로고
    • Forty years of in vitro evolution
    • [CrossRef] [PubMed]
    • Joyce, G.F. Forty Years of in vitro Evolution. Angew. Chem. Int. Ed. 2007, 46, 6420-6436. [CrossRef] [PubMed]
    • (2007) Angew. Chem. Int. Ed. , vol.46 , pp. 6420-6436
    • Joyce, G.F.1
  • 17
    • 20344389806 scopus 로고    scopus 로고
    • DNA-based asymmetric catalysis
    • [CrossRef] [PubMed]
    • Roelfes, G.; Feringa, B.L. DNA-Based Asymmetric Catalysis. Angew. Chem. Int. Ed. 2005, 44, 3230-3232. [CrossRef] [PubMed]
    • (2005) Angew. Chem. Int. Ed. , vol.44 , pp. 3230-3232
    • Roelfes, G.1    Feringa, B.L.2
  • 18
    • 78049346344 scopus 로고    scopus 로고
    • Catalytic enantioselective syn hydration of enones in water using a DNA-based catalyst
    • [CrossRef] [PubMed]
    • Boersma, A.J.; Coquière, D.; Geerdink, D.; Rosati, F.; Feringa, B.L.; Roelfes, G. Catalytic enantioselective syn hydration of enones in water using a DNA-based catalyst. Nat. Chem. 2010, 2, 991-995. [CrossRef] [PubMed]
    • (2010) Nat. Chem. , vol.2 , pp. 991-995
    • Boersma, A.J.1    Coquière, D.2    Geerdink, D.3    Rosati, F.4    Feringa, B.L.5    Roelfes, G.6
  • 20
    • 0028675028 scopus 로고
    • A DNA enzyme that cleaves RNA
    • [CrossRef]
    • Breaker, R.R.; Joyce, G.F. A DNA enzyme that cleaves RNA. Chem. Biol. 1994, 1, 223-229. [CrossRef]
    • (1994) Chem. Biol. , vol.1 , pp. 223-229
    • Breaker, R.R.1    Joyce, G.F.2
  • 21
    • 62649161589 scopus 로고    scopus 로고
    • Biologically inspired synthetic enzymes made from DNA
    • [CrossRef] [PubMed]
    • Schlosser, K.; Li, Y. Biologically Inspired Synthetic Enzymes Made from DNA. Chem. Biol. 2009, 16, 311-322. [CrossRef] [PubMed]
    • (2009) Chem. Biol. , vol.16 , pp. 311-322
    • Schlosser, K.1    Li, Y.2
  • 22
    • 77957362844 scopus 로고    scopus 로고
    • DNA as a versatile chemical component for catalysis, encoding, and stereocontrol
    • [CrossRef] [PubMed]
    • Silverman, S.K. DNA as a Versatile Chemical Component for Catalysis, Encoding, and Stereocontrol. Angew. Chem. Int. Ed. 2010, 49, 7180-7201. [CrossRef] [PubMed]
    • (2010) Angew. Chem. Int. Ed. , vol.49 , pp. 7180-7201
    • Silverman, S.K.1
  • 23
    • 23644453112 scopus 로고    scopus 로고
    • DNA catalysis: Potential, limitations, open questions
    • [CrossRef] [PubMed]
    • Peracchi, A. DNA Catalysis: Potential, Limitations, Open Questions. ChemBioChem 2005, 6, 1316-1322. [CrossRef] [PubMed]
    • (2005) ChemBioChem , vol.6 , pp. 1316-1322
    • Peracchi, A.1
  • 24
    • 39749165700 scopus 로고    scopus 로고
    • DNAzyme technology and cancer therapy: Cleave and let die
    • [CrossRef] [PubMed]
    • Dass, C.R.; Choong, P.F.M.; Khachigian, L.M. DNAzyme technology and cancer therapy: Cleave and let die. Mol. Cancer Ther. 2008, 7, 243-251. [CrossRef] [PubMed]
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 243-251
    • Dass, C.R.1    Choong, P.F.M.2    Khachigian, L.M.3
  • 25
    • 84925465454 scopus 로고    scopus 로고
    • Tandem DNAzymes for mRNA cleavage: Choice of enzyme, metal ions and the antisense effect
    • [CrossRef] [PubMed]
    • Wang, F.; Saran, R.; Liu, J. Tandem DNAzymes for mRNA cleavage: Choice of enzyme, metal ions and the antisense effect. Bioorg. Med. Chem. Lett. 2015, 25, 1460-1463. [CrossRef] [PubMed]
    • (2015) Bioorg. Med. Chem. Lett. , vol.25 , pp. 1460-1463
    • Wang, F.1    Saran, R.2    Liu, J.3
  • 26
    • 0025194307 scopus 로고
    • Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase
    • [CrossRef] [PubMed]
    • Tuerk, C.; Gold, L. Systematic Evolution of Ligands by Exponential Enrichment: RNA Ligands to Bacteriophage T4 DNA Polymerase. Science 1990, 249, 505-510. [CrossRef] [PubMed]
    • (1990) Science , vol.249 , pp. 505-510
    • Tuerk, C.1    Gold, L.2
  • 27
    • 0025332385 scopus 로고
    • Selection in vitro of an RNA enzyme that specifically cleaves single-stranded DNA
    • [CrossRef] [PubMed]
    • Robertson, D.L.; Joyce, G.F. Selection in vitro of an RNA enzyme that specifically cleaves single-stranded DNA. Nature 1990, 344, 467-468. [CrossRef] [PubMed]
    • (1990) Nature , vol.344 , pp. 467-468
    • Robertson, D.L.1    Joyce, G.F.2
  • 28
    • 0025074907 scopus 로고
    • In vitro selection of RNA molecules that bind specific ligands
    • [CrossRef] [PubMed]
    • Ellington, A.D.; Szostak, J.W. In vitro selection of RNA molecules that bind specific ligands. Nature 1990, 346, 818-822. [CrossRef] [PubMed]
    • (1990) Nature , vol.346 , pp. 818-822
    • Ellington, A.D.1    Szostak, J.W.2
  • 29
    • 47949085051 scopus 로고    scopus 로고
    • Catalytic DNA (deoxyribozymes) for synthetic applications-current abilities and future prospects
    • [CrossRef] [PubMed]
    • Silverman, S.K. Catalytic DNA (deoxyribozymes) for synthetic applications-current abilities and future prospects. Chem. Commun. 2008, 30, 3467-3485. [CrossRef] [PubMed]
    • (2008) Chem. Commun. , vol.30 , pp. 3467-3485
    • Silverman, S.K.1
  • 30
    • 0028983570 scopus 로고
    • 2+-dependent RNA phosphoesterase activity
    • [CrossRef]
    • 2+-dependent RNA phosphoesterase activity. Chem. Biol. 1995, 2, 655-660. [CrossRef]
    • (1995) Chem. Biol. , vol.2 , pp. 655-660
    • Breaker, R.R.1    Joyce, G.F.2
  • 31
    • 0030898510 scopus 로고    scopus 로고
    • A general purpose RNA-cleaving DNA enzyme
    • [CrossRef] [PubMed]
    • Santoro, S.W.; Joyce, G.F. A general purpose RNA-cleaving DNA enzyme. Proc. Natl. Acad. Sci. USA 1997, 94, 4262-4266. [CrossRef] [PubMed]
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4262-4266
    • Santoro, S.W.1    Joyce, G.F.2
  • 33
    • 84893540958 scopus 로고    scopus 로고
    • Ultrasensitive DNAzyme beacon for lanthanides and metal speciation
    • [CrossRef] [PubMed]
    • Huang, P.-J.J.; Lin, J.; Cao, J.; Vazin, M.; Liu, J. Ultrasensitive DNAzyme Beacon for Lanthanides and Metal Speciation. Anal. Chem. 2014, 86, 1816-1821. [CrossRef] [PubMed]
    • (2014) Anal. Chem. , vol.86 , pp. 1816-1821
    • Huang, P.-J.J.1    Lin, J.2    Cao, J.3    Vazin, M.4    Liu, J.5
  • 34
    • 84907894839 scopus 로고    scopus 로고
    • In vitro selection of a new lanthanide-dependent DNAzyme for ratiometric sensing lanthanides
    • [CrossRef] [PubMed]
    • Huang, P.-J.J.; Vazin, M.; Liu, J. In vitro Selection of a New Lanthanide-Dependent DNAzyme for Ratiometric Sensing Lanthanides. Anal. Chem. 2014, 86, 9993-9999. [CrossRef] [PubMed]
    • (2014) Anal. Chem. , vol.86 , pp. 9993-9999
    • Huang, P.-J.J.1    Vazin, M.2    Liu, J.3
  • 35
    • 84941087183 scopus 로고    scopus 로고
    • A new heavy lanthanide-dependent DNAzyme displaying strong metal cooperativity and unrescuable phosphorothioate effect
    • [CrossRef] [PubMed]
    • Huang, P.-J.J.; Vazin, M.; Matuszek, Z.; Liu, J. A new heavy lanthanide-dependent DNAzyme displaying strong metal cooperativity and unrescuable phosphorothioate effect. Nucleic Acids Res. 2015, 43, 461-469. [CrossRef] [PubMed]
    • (2015) Nucleic Acids Res. , vol.43 , pp. 461-469
    • Huang, P.-J.J.1    Vazin, M.2    Matuszek, Z.3    Liu, J.4
  • 36
    • 33847779647 scopus 로고    scopus 로고
    • A catalytic beacon sensor for uranium with parts-pertrillion sensitivity and millionfold selectivity
    • [CrossRef] [PubMed]
    • Liu, J.; Brown, A.K.; Meng, X.; Cropek, D.M.; Istok, J.D.; Watson, D.B.; Lu, Y. A catalytic beacon sensor for uranium with parts-pertrillion sensitivity and millionfold selectivity. Proc. Natl. Acad. Sci. USA 2007, 104, 2056-2061. [CrossRef] [PubMed]
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2056-2061
    • Liu, J.1    Brown, A.K.2    Meng, X.3    Cropek, D.M.4    Istok, J.D.5    Watson, D.B.6    Lu, Y.7
  • 37
    • 0032568656 scopus 로고    scopus 로고
    • An amino acid as a cofactor for a catalytic polynucleotide
    • [CrossRef] [PubMed]
    • Roth, A.; Breaker, R.R. An amino acid as a cofactor for a catalytic polynucleotide. Proc. Natl. Acad. Sci. USA 1998, 95, 6027-6031. [CrossRef] [PubMed]
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6027-6031
    • Roth, A.1    Breaker, R.R.2
  • 38
    • 84929179488 scopus 로고    scopus 로고
    • In vitro selection of a sodium-specific DNAzyme and its application in intracellular sensing
    • [CrossRef] [PubMed]
    • Torabi, S.-F.; Wu, P.; McGhee, C.E.; Chen, L.; Hwang, K.; Zheng, N.; Cheng, J.; Lu, Y. In vitro selection of a sodium-specific DNAzyme and its application in intracellular sensing. Proc. Natl. Acad. Sci. USA 2015, 112, 5903-5908. [CrossRef] [PubMed]
    • (2015) Proc. Natl. Acad. Sci. USA , vol.112 , pp. 5903-5908
    • Torabi, S.-F.1    Wu, P.2    McGhee, C.E.3    Chen, L.4    Hwang, K.5    Zheng, N.6    Cheng, J.7    Lu, Y.8
  • 40
    • 67649842764 scopus 로고    scopus 로고
    • A genotype-to-phenotype map of in vitro selected RNA-cleaving DNAzymes: Implications for accessing the target phenotype
    • [CrossRef] [PubMed]
    • Schlosser, K.; Lam, J.C.F.; Li, Y. A genotype-to-phenotype map of in vitro selected RNA-cleaving DNAzymes: Implications for accessing the target phenotype. Nucleic Acids Res. 2009, 37, 3545-3557. [CrossRef] [PubMed]
    • (2009) Nucleic Acids Res. , vol.37 , pp. 3545-3557
    • Schlosser, K.1    Lam, J.C.F.2    Li, Y.3
  • 41
    • 84890042199 scopus 로고    scopus 로고
    • In-ice evolution of RNA polymerase ribozyme activity
    • [CrossRef] [PubMed]
    • Attwater, J.; Wochner, A.; Holliger, P. In-ice evolution of RNA polymerase ribozyme activity. Nat. Chem. 2013, 5, 1011-1018. [CrossRef] [PubMed]
    • (2013) Nat. Chem. , vol.5 , pp. 1011-1018
    • Attwater, J.1    Wochner, A.2    Holliger, P.3
  • 42
    • 84928673153 scopus 로고    scopus 로고
    • In vitro selection of deoxyribozymes active with Cd2+ ions resulting in variants of DNAzyme 8-17
    • [CrossRef] [PubMed]
    • Kasprowicz, A.; Stokowa-Soltys, K.; Wrzesinski, J.; Jezowska-Bojczuk, M.; Ciesiolka, J. In vitro selection of deoxyribozymes active with Cd2+ ions resulting in variants of DNAzyme 8-17. Dalton Trans. 2015, 44, 8138-8149. [CrossRef] [PubMed]
    • (2015) Dalton Trans. , vol.44 , pp. 8138-8149
    • Kasprowicz, A.1    Stokowa-Soltys, K.2    Wrzesinski, J.3    Jezowska-Bojczuk, M.4    Ciesiolka, J.5
  • 43
    • 84857807846 scopus 로고    scopus 로고
    • Establishing broad generality of DNA catalysts for site-specific hydrolysis of single-stranded DNA
    • [CrossRef] [PubMed]
    • Xiao, Y.; Wehrmann, R.J.; Ibrahim, N.A.; Silverman, S.K. Establishing broad generality of DNA catalysts for site-specific hydrolysis of single-stranded DNA. Nucleic Acids Res. 2012, 40, 1778-1786. [CrossRef] [PubMed]
    • (2012) Nucleic Acids Res. , vol.40 , pp. 1778-1786
    • Xiao, Y.1    Wehrmann, R.J.2    Ibrahim, N.A.3    Silverman, S.K.4
  • 44
    • 84870937297 scopus 로고    scopus 로고
    • Systematic evaluation of the dependence of deoxyribozyme catalysis on random region length
    • [CrossRef] [PubMed]
    • Velez, T.E.; Singh, J.; Xiao, Y.; Allen, E.C.; Wong, O.Y.; Chandra, M.; Kwon, S.C.; Silverman, S.K. Systematic Evaluation of the Dependence of Deoxyribozyme Catalysis on Random Region Length. ACS Comb. Sci. 2012, 14, 680-687. [CrossRef] [PubMed]
    • (2012) ACS Comb. Sci. , vol.14 , pp. 680-687
    • Velez, T.E.1    Singh, J.2    Xiao, Y.3    Allen, E.C.4    Wong, O.Y.5    Chandra, M.6    Kwon, S.C.7    Silverman, S.K.8
  • 45
    • 80053317845 scopus 로고    scopus 로고
    • A divalent metal-dependent self-cleaving DNAzyme with a tyrosine side chain
    • [CrossRef] [PubMed]
    • Lam, C.H.; Hipolito, C.J.; Hollenstein, M.; Perrin, D.M. A divalent metal-dependent self-cleaving DNAzyme with a tyrosine side chain. Org. Biomol. Chem. 2011, 9, 6949-6954. [CrossRef] [PubMed]
    • (2011) Org. Biomol. Chem. , vol.9 , pp. 6949-6954
    • Lam, C.H.1    Hipolito, C.J.2    Hollenstein, M.3    Perrin, D.M.4
  • 46
    • 77957307747 scopus 로고    scopus 로고
    • The structural diversity of deoxyribozymes
    • [CrossRef] [PubMed]
    • McManus, S.A.; Li, Y. The Structural Diversity of Deoxyribozymes. Molecules 2010, 15, 6269-6284. [CrossRef] [PubMed]
    • (2010) Molecules , vol.15 , pp. 6269-6284
    • McManus, S.A.1    Li, Y.2
  • 47
    • 84899550322 scopus 로고    scopus 로고
    • Nucleic acid catalysis: Metals, nucleobases, and other cofactors
    • [CrossRef] [PubMed]
    • Ward, W.L.; Plakos, K.; DeRose, V.J. Nucleic Acid Catalysis: Metals, Nucleobases, and Other Cofactors. Chem. Rev. 2014, 114, 4318-4342. [CrossRef] [PubMed]
    • (2014) Chem. Rev. , vol.114 , pp. 4318-4342
    • Ward, W.L.1    Plakos, K.2    DeRose, V.J.3
  • 48
    • 70349327390 scopus 로고    scopus 로고
    • DNA-catalyzed sequence-specific hydrolysis of DNA
    • [CrossRef] [PubMed]
    • Chandra, M.; Sachdeva, A.; Silverman, S.K. DNA-Catalyzed Sequence-Specific Hydrolysis of DNA. Nat. Chem. Biol. 2009, 5, 718-720. [CrossRef] [PubMed]
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 718-720
    • Chandra, M.1    Sachdeva, A.2    Silverman, S.K.3
  • 51
    • 0347089036 scopus 로고    scopus 로고
    • A deoxyribozyme that harnesses light to repair thymine dimers in DNA
    • [CrossRef] [PubMed]
    • Chinnapen, D.J.; Sen, D. A Deoxyribozyme That Harnesses Light to Repair Thymine Dimers in DNA. Proc. Natl. Acad. Sci. USA 2004, 101, 65-69. [CrossRef] [PubMed]
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 65-69
    • Chinnapen, D.J.1    Sen, D.2
  • 52
    • 0026669321 scopus 로고
    • A small metalloribozyme with a two-step mechanism
    • [CrossRef] [PubMed]
    • Pan, T.; Uhlenbeck, O.C. A small metalloribozyme with a two-step mechanism. Nature 1992, 358, 560-563. [CrossRef] [PubMed]
    • (1992) Nature , vol.358 , pp. 560-563
    • Pan, T.1    Uhlenbeck, O.C.2
  • 55
    • 0030498356 scopus 로고    scopus 로고
    • 2+ ion as a cofactor for a novel RNA-cleaving deoxyribozyme
    • [CrossRef]
    • 2+ Ion as a Cofactor for a Novel RNA-Cleaving Deoxyribozyme. Angew. Chem. Int. Ed. 1996, 35, 2837-2841. [CrossRef]
    • (1996) Angew. Chem. Int. Ed. , vol.35 , pp. 2837-2841
    • Faulhammer, D.1    Famulok, M.2
  • 56
    • 0032558463 scopus 로고    scopus 로고
    • Mechanism and utility of an RNA-cleaving DNA enzyme
    • [CrossRef] [PubMed]
    • Santoro, S.W.; Joyce, G.F. Mechanism and Utility of an RNA-Cleaving DNA Enzyme. Biochemistry 1998, 37, 13330-13342. [CrossRef] [PubMed]
    • (1998) Biochemistry , vol.37 , pp. 13330-13342
    • Santoro, S.W.1    Joyce, G.F.2
  • 57
    • 1142281951 scopus 로고    scopus 로고
    • Dinucleotide junction cleavage versatility of 8-17 deoxyribozyme
    • [CrossRef] [PubMed]
    • Cruz, R.P.G.; Withers, J.B.; Li, Y. Dinucleotide Junction Cleavage Versatility of 8-17 Deoxyribozyme. Chem. Biol. 2004, 11, 57-67. [CrossRef] [PubMed]
    • (2004) Chem. Biol. , vol.11 , pp. 57-67
    • Cruz, R.P.G.1    Withers, J.B.2    Li, Y.3
  • 58
    • 41149095145 scopus 로고    scopus 로고
    • Sequence-function relationships provide new insight into the cleavage site selectivity of the 8-17 RNA-cleaving deoxyribozyme
    • [CrossRef] [PubMed]
    • Schlosser, K.; Gu, J.; Sule, L.; Li, Y. Sequence-function relationships provide new insight into the cleavage site selectivity of the 8-17 RNA-cleaving deoxyribozyme. Nucleic Acids Res. 2008, 36, 1472-1481. [CrossRef] [PubMed]
    • (2008) Nucleic Acids Res. , vol.36 , pp. 1472-1481
    • Schlosser, K.1    Gu, J.2    Sule, L.3    Li, Y.4
  • 59
    • 35048868774 scopus 로고    scopus 로고
    • Rational design of "Turn-On" allosteric DNAzyme catalytic beacons for aqueous mercury ions with ultra high sensitivity and selectivity
    • [CrossRef] [PubMed]
    • Liu, J.; Lu, Y. Rational Design of "Turn-On" Allosteric DNAzyme Catalytic Beacons for Aqueous Mercury Ions with Ultra high Sensitivity and Selectivity. Angew. Chem. Int. Ed. 2007, 46, 7587-7590. [CrossRef] [PubMed]
    • (2007) Angew. Chem. Int. Ed. , vol.46 , pp. 7587-7590
    • Liu, J.1    Lu, Y.2
  • 60
    • 0034650291 scopus 로고    scopus 로고
    • In vitro selection and characterization of a highly efficient Zn(II)-dependent RNA-cleaving deoxyribozyme
    • [CrossRef] [PubMed]
    • Li, J.; Zheng, W.; Kwon, A.H.; Lu, Y. In vitro selection and characterization of a highly efficient Zn(II)-dependent RNA-cleaving deoxyribozyme. Nucleic Acids Res. 2000, 28, 481-488. [CrossRef] [PubMed]
    • (2000) Nucleic Acids Res. , vol.28 , pp. 481-488
    • Li, J.1    Zheng, W.2    Kwon, A.H.3    Lu, Y.4
  • 61
    • 77956133904 scopus 로고    scopus 로고
    • Probing the function of nucleotides in the catalytic cores of the 8-17 and 10-23 DNAzymes by abasic nucleotide and C3 spacer substitutions
    • [CrossRef] [PubMed]
    • Wang, B.; Cao, L.Q.; Chiuman, W.; Li, Y.F.; Xi, Z. Probing the Function of Nucleotides in the Catalytic Cores of the 8-17 and 10-23 DNAzymes by Abasic Nucleotide and C3 Spacer Substitutions. Biochemistry 2010, 49, 7553-7562. [CrossRef] [PubMed]
    • (2010) Biochemistry , vol.49 , pp. 7553-7562
    • Wang, B.1    Cao, L.Q.2    Chiuman, W.3    Li, Y.F.4    Xi, Z.5
  • 62
    • 0031556016 scopus 로고    scopus 로고
    • Characterization and divalent metal-ion dependence of in vitro selected deoxyribozymes which cleave DNA/RNA chimeric oligonucleotides
    • [CrossRef] [PubMed]
    • Faulhammer, D.; Famulok, M. Characterization and divalent metal-ion dependence of in vitro selected deoxyribozymes which cleave DNA/RNA chimeric oligonucleotides. J. Mol. Biol. 1997, 269, 188-202. [CrossRef] [PubMed]
    • (1997) J. Mol. Biol. , vol.269 , pp. 188-202
    • Faulhammer, D.1    Famulok, M.2
  • 63
    • 3342955521 scopus 로고    scopus 로고
    • Tracing sequence diversity change of RNA-cleaving deoxyribozymes under increasing selection pressure during in vitro selection
    • [CrossRef] [PubMed]
    • Schlosser, K.; Li, Y. Tracing Sequence Diversity Change of RNA-Cleaving Deoxyribozymes under Increasing Selection Pressure during in vitro Selection. Biochemistry 2004, 43, 9695-9707. [CrossRef] [PubMed]
    • (2004) Biochemistry , vol.43 , pp. 9695-9707
    • Schlosser, K.1    Li, Y.2
  • 64
    • 49249091384 scopus 로고    scopus 로고
    • In vitro selection of small RNA-cleaving deoxyribozymes that cleave pyrimidine-pyrimidine junctions
    • [CrossRef] [PubMed]
    • Schlosser, K.; Gu, J.; Lam, J.C.F.; Li, Y. In vitro selection of small RNA-cleaving deoxyribozymes that cleave pyrimidine-pyrimidine junctions. Nucleic Acids Res. 2008, 36, 4768-4777. [CrossRef] [PubMed]
    • (2008) Nucleic Acids Res. , vol.36 , pp. 4768-4777
    • Schlosser, K.1    Gu, J.2    Lam, J.C.F.3    Li, Y.4
  • 65
    • 79959284618 scopus 로고    scopus 로고
    • Characterization of non-8-17 sequences uncovers structurally diverse RNA-cleaving deoxyribozymes
    • [CrossRef] [PubMed]
    • Lam, J.C.F.; Kwan, S.O.; Li, Y. Characterization of non-8-17 sequences uncovers structurally diverse RNA-cleaving deoxyribozymes. Mol. BioSyst. 2011, 7, 2139-2146. [CrossRef] [PubMed]
    • (2011) Mol. BioSyst. , vol.7 , pp. 2139-2146
    • Lam, J.C.F.1    Kwan, S.O.2    Li, Y.3
  • 66
    • 3042732096 scopus 로고    scopus 로고
    • Directed evolution of nucleic acid enzymes
    • [CrossRef] [PubMed]
    • Joyce, G.F. Directed Evolution of Nucleic Acid Enzymes. Annu. Rev. Biochem. 2004, 73, 791-836. [CrossRef] [PubMed]
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 791-836
    • Joyce, G.F.1
  • 69
    • 0032952507 scopus 로고    scopus 로고
    • Crystal structure of an 82-nucleotide RNA-DNA complex formed by the 10-23 DNA enzyme
    • [PubMed]
    • Nowakowski, J.; Shim, P.J.; Prasad, G.S.; Stout, C.D.; Joyce, G.F. Crystal structure of an 82-nucleotide RNA-DNA complex formed by the 10-23 DNA enzyme. Nat. Struct. Biol. 1999, 6, 151-156. [PubMed]
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 151-156
    • Nowakowski, J.1    Shim, P.J.2    Prasad, G.S.3    Stout, C.D.4    Joyce, G.F.5
  • 70
    • 34249782553 scopus 로고    scopus 로고
    • Metal-dependent global folding and activity of the 8-17 DNAzyme studied by fluorescence resonance energy transfer
    • [CrossRef] [PubMed]
    • Kim, H.-K.; Liu, J.; Li, J.; Nagraj, N.; Li, M.; Pavot, C.M.-B.; Lu, Y. Metal-Dependent Global Folding and Activity of the 8-17 DNAzyme Studied by Fluorescence Resonance Energy Transfer. J. Am. Chem. Soc. 2007, 129, 6896-6902. [CrossRef] [PubMed]
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 6896-6902
    • Kim, H.-K.1    Liu, J.2    Li, J.3    Nagraj, N.4    Li, M.5    Pavot, C.M.-B.6    Lu, Y.7
  • 71
    • 36248936102 scopus 로고    scopus 로고
    • Dissecting metal ion-dependent folding and catalysis of a single DNAzyme
    • [CrossRef] [PubMed]
    • Kim, H.-K.; Rasnik, I.; Liu, J.; Ha, T.; Lu, Y. Dissecting metal ion-dependent folding and catalysis of a single DNAzyme. Nat. Chem. Biol. 2007, 3, 763-768. [CrossRef] [PubMed]
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 763-768
    • Kim, H.-K.1    Rasnik, I.2    Liu, J.3    Ha, T.4    Lu, Y.5
  • 72
    • 77951713609 scopus 로고    scopus 로고
    • A versatile endoribonuclease mimic made of DNA: Characteristics and applications of the 8-17 RNA-cleaving DNAzyme
    • [CrossRef] [PubMed]
    • Schlosser, K.; Li, Y. A Versatile Endoribonuclease Mimic Made of DNA: Characteristics and Applications of the 8-17 RNA-Cleaving DNAzyme. ChemBioChem 2010, 11, 866-879. [CrossRef] [PubMed]
    • (2010) ChemBioChem , vol.11 , pp. 866-879
    • Schlosser, K.1    Li, Y.2
  • 73
    • 77955627343 scopus 로고    scopus 로고
    • Influence of cleavage site on global folding of an RNA-cleaving DNAzyme
    • [CrossRef] [PubMed]
    • Lam, J.C.F.; Li, Y. Influence of Cleavage Site on Global Folding of an RNA-Cleaving DNAzyme. ChemBioChem 2010, 11, 1710-1719. [CrossRef] [PubMed]
    • (2010) ChemBioChem , vol.11 , pp. 1710-1719
    • Lam, J.C.F.1    Li, Y.2
  • 74
    • 84863274881 scopus 로고    scopus 로고
    • Effect of single-base mutation on activity and folding of 10-23 deoxyribozyme studied by three-color single-molecule ALEX FRET
    • [CrossRef] [PubMed]
    • Jung, J.; Han, K.Y.; Koh, H.R.; Lee, J.; Choi, Y.M.; Kim, C.; Kim, S.K. Effect of Single-Base Mutation on Activity and Folding of 10-23 Deoxyribozyme Studied by Three-Color Single-Molecule ALEX FRET. J. Phys. Chem. B 2012, 116, 3007-3012. [CrossRef] [PubMed]
    • (2012) J. Phys. Chem. B , vol.116 , pp. 3007-3012
    • Jung, J.1    Han, K.Y.2    Koh, H.R.3    Lee, J.4    Choi, Y.M.5    Kim, C.6    Kim, S.K.7
  • 75
    • 0037175009 scopus 로고    scopus 로고
    • Sequence requirements in the catalytic core of the "10-23" DNA enzyme
    • [CrossRef] [PubMed]
    • Zaborowska, Z.; Fürste, J.P.; Erdmann, V.A.; Kurreck, J. Sequence Requirements in the Catalytic Core of the "10-23" DNA Enzyme. J. Biol. Chem. 2002, 43, 40617-40622. [CrossRef] [PubMed]
    • (2002) J. Biol. Chem. , vol.43 , pp. 40617-40622
    • Zaborowska, Z.1    Fürste, J.P.2    Erdmann, V.A.3    Kurreck, J.4
  • 76
    • 11844276654 scopus 로고    scopus 로고
    • Deletion analysis in the catalytic region of the 10-23 DNA enzyme
    • [CrossRef] [PubMed]
    • Zaborowska, Z.; Schubert, S.; Kurreck, J.; Erdmann, V.A. Deletion analysis in the catalytic region of the 10-23 DNA enzyme. FEBS Lett. 2005, 579, 554-558. [CrossRef] [PubMed]
    • (2005) FEBS Lett. , vol.579 , pp. 554-558
    • Zaborowska, Z.1    Schubert, S.2    Kurreck, J.3    Erdmann, V.A.4
  • 77
    • 24644514250 scopus 로고    scopus 로고
    • A mutational analysis of the 8-17 deoxyribozyme core
    • [CrossRef] [PubMed]
    • Peracchi, A.; Bonaccio, M.; Clerici, M. A Mutational Analysis of the 8-17 Deoxyribozyme Core. J. Mol. Biol. 2005, 352, 783-794. [CrossRef] [PubMed]
    • (2005) J. Mol. Biol. , vol.352 , pp. 783-794
    • Peracchi, A.1    Bonaccio, M.2    Clerici, M.3
  • 78
    • 84928121217 scopus 로고    scopus 로고
    • Probing the effect of minor groove interactions on the catalytic efficiency of DNAzymes 8-17 and 10-23
    • [CrossRef] [PubMed]
    • Räz, M.; Hollenstein, M. Probing the effect of minor groove interactions on the catalytic efficiency of DNAzymes 8-17 and 10-23. Mol. BioSyst. 2015, 11, 1454-1461. [CrossRef] [PubMed]
    • (2015) Mol. BioSyst. , vol.11 , pp. 1454-1461
    • Räz, M.1    Hollenstein, M.2
  • 79
    • 2342530310 scopus 로고    scopus 로고
    • Kinetic and thermodynamic characterization of the RNA-cleaving 8-17 deoxyribozyme
    • [CrossRef] [PubMed]
    • Bonaccio, M.; Credali, A.; Peracchi, A. Kinetic and thermodynamic characterization of the RNA-cleaving 8-17 deoxyribozyme. Nucleic Acids Res. 2004, 32, 916-925. [CrossRef] [PubMed]
    • (2004) Nucleic Acids Res. , vol.32 , pp. 916-925
    • Bonaccio, M.1    Credali, A.2    Peracchi, A.3
  • 80
    • 0346850835 scopus 로고    scopus 로고
    • Structural rearrangements of the 10-23 DNAzyme to b3 integrin subunit mRNA induced by cations and their relations to the catalytic activity
    • [CrossRef] [PubMed]
    • Cieslak, M.; Szymanski, J.; Adamiak, R.W.; Cierniewski, C.S. Structural Rearrangements of the 10-23 DNAzyme to b3 Integrin Subunit mRNA Induced by Cations and Their Relations to the Catalytic Activity. J. Biol. Chem. 2003, 278, 47987-47996. [CrossRef] [PubMed]
    • (2003) J. Biol. Chem. , vol.278 , pp. 47987-47996
    • Cieslak, M.1    Szymanski, J.2    Adamiak, R.W.3    Cierniewski, C.S.4
  • 81
    • 37849026396 scopus 로고    scopus 로고
    • Folding of 8-17 deoxyribozyme studied by three-color alternating-laser excitation of single molecules
    • [CrossRef] [PubMed]
    • Lee, N.K.; Koh, H.R.; Han, K.Y.; Kim, S.K. Folding of 8-17 Deoxyribozyme Studied by Three-Color Alternating-Laser Excitation of Single Molecules. J. Am. Chem. Soc. 2007, 129, 15526-15534. [CrossRef] [PubMed]
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15526-15534
    • Lee, N.K.1    Koh, H.R.2    Han, K.Y.3    Kim, S.K.4
  • 83
    • 0038131065 scopus 로고    scopus 로고
    • A lead-dependent DNAzyme with a two-step mechanism
    • [CrossRef] [PubMed]
    • Brown, A.K.; Li, J.; Pavot, C.M.-B.; Lu, Y. A Lead-Dependent DNAzyme with a Two-Step Mechanism. Biochemistry 2003, 42, 7152-7161. [CrossRef] [PubMed]
    • (2003) Biochemistry , vol.42 , pp. 7152-7161
    • Brown, A.K.1    Li, J.2    Pavot, C.M.-B.3    Lu, Y.4
  • 84
    • 0035339966 scopus 로고    scopus 로고
    • Recent advances in the elucidation of the mechanisms of action of ribozymes
    • [CrossRef] [PubMed]
    • Takagi, Y.; Warashina, M.; Stec, W.J.; Yoshinari, K.; Taira, K. Recent advances in the elucidation of the mechanisms of action of ribozymes. Nucleic Acids Res. 2001, 29, 1815-1834. [CrossRef] [PubMed]
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1815-1834
    • Takagi, Y.1    Warashina, M.2    Stec, W.J.3    Yoshinari, K.4    Taira, K.5
  • 85
    • 0041702195 scopus 로고    scopus 로고
    • Ribozyme speed limits
    • [CrossRef] [PubMed]
    • Emilsson, G.M.; Nakamura, S.; Roth, A.; Breaker, R.R. Ribozyme speed limits. RNA 2003, 9, 907-918. [CrossRef] [PubMed]
    • (2003) RNA , vol.9 , pp. 907-918
    • Emilsson, G.M.1    Nakamura, S.2    Roth, A.3    Breaker, R.R.4
  • 86
    • 0032717640 scopus 로고    scopus 로고
    • New DNA enzyme targeting egr-1 mRNA inhibits vascular smooth muscle proliferation and regrowth after injury
    • [CrossRef] [PubMed]
    • Santiago, F.S.; Lowe, H.C.; Kavurma, M.M.; Chesterman, C.N.; Baker, A.; Atkins, D.G.; Khachigian, L.M. New DNA enzyme targeting Egr-1 mRNA inhibits vascular smooth muscle proliferation and regrowth after injury. Nat. Med. 1999, 5, 1264-1269. [CrossRef] [PubMed]
    • (1999) Nat. Med. , vol.5 , pp. 1264-1269
    • Santiago, F.S.1    Lowe, H.C.2    Kavurma, M.M.3    Chesterman, C.N.4    Baker, A.5    Atkins, D.G.6    Khachigian, L.M.7
  • 88
    • 2342459633 scopus 로고    scopus 로고
    • Locked nucleic acid modified DNA enzymes targeting early growth response-1 inhibit human vascular smooth muscle cell growth
    • [CrossRef] [PubMed]
    • Fahmy, R.G.; Khachigian, L.M. Locked nucleic acid modified DNA enzymes targeting early growth response-1 inhibit human vascular smooth muscle cell growth. Nucleic Acids Res. 2004, 32, 2281-2285. [CrossRef] [PubMed]
    • (2004) Nucleic Acids Res. , vol.32 , pp. 2281-2285
    • Fahmy, R.G.1    Khachigian, L.M.2
  • 89
    • 37249019972 scopus 로고    scopus 로고
    • The advantages of being locked-assessing the cleavage of short and long RNAs by locked nucleic acid-containing 8-17 deoxyribozymes
    • [CrossRef] [PubMed]
    • Donini, S.; Clerici, M.; Wengel, J.; Vester, B.; Peracchi, A. The advantages of being locked-Assessing the cleavage of short and long RNAs by locked nucleic acid-containing 8-17 deoxyribozymes. J. Biol. Chem. 2007, 282, 35510-35518. [CrossRef] [PubMed]
    • (2007) J. Biol. Chem. , vol.282 , pp. 35510-35518
    • Donini, S.1    Clerici, M.2    Wengel, J.3    Vester, B.4    Peracchi, A.5
  • 91
    • 84874575290 scopus 로고    scopus 로고
    • Deoxyribozymes: New therapeutics to treat central nervous system disorders
    • [CrossRef] [PubMed]
    • Grimpe, B. Deoxyribozymes: New therapeutics to treat central nervous system disorders. Front. Mol. Neurosci. 2011, 4, 25. [CrossRef] [PubMed]
    • (2011) Front. Mol. Neurosci. , vol.4 , pp. 25
    • Grimpe, B.1
  • 92
    • 84858636357 scopus 로고    scopus 로고
    • Targeting insulin-like growth factor I with 10-23 DNAzymes: 2′-O-methyl modifications in the catalytic core enhance mRNA cleavage
    • [CrossRef] [PubMed]
    • Fokina, A.A.; Meschaninova, M.I.; Durfort, T.; Venyaminova, A.G.; François, J.C. Targeting Insulin-like Growth Factor I with 10-23 DNAzymes: 2′-O-Methyl Modifications in the Catalytic Core Enhance mRNA Cleavage. Biochemistry 2012, 51, 2181-2191. [CrossRef] [PubMed]
    • (2012) Biochemistry , vol.51 , pp. 2181-2191
    • Fokina, A.A.1    Meschaninova, M.I.2    Durfort, T.3    Venyaminova, A.G.4    François, J.C.5
  • 93
    • 85027931220 scopus 로고    scopus 로고
    • Activity of core-modified 10-23 DNAzymes against HCV
    • [CrossRef] [PubMed]
    • Robaldo, L.; Berzal-Herranz, A.; Montserrat, J.M.; Iribarren, A.M. Activity of Core-Modified 10-23 DNAzymes against HCV. ChemMedChem 2014, 9, 2172-2177. [CrossRef] [PubMed]
    • (2014) ChemMedChem , vol.9 , pp. 2172-2177
    • Robaldo, L.1    Berzal-Herranz, A.2    Montserrat, J.M.3    Iribarren, A.M.4
  • 95
    • 84878110171 scopus 로고    scopus 로고
    • First-in-human trial of Dz13 for nodular basal-cell carcinoma
    • [CrossRef]
    • Grassi, G.; Grassi, M. First-in-human trial of Dz13 for nodular basal-cell carcinoma. Lancet 2013, 381, 1797-1798. [CrossRef]
    • (2013) Lancet , vol.381 , pp. 1797-1798
    • Grassi, G.1    Grassi, M.2
  • 96
    • 84878113156 scopus 로고    scopus 로고
    • Safety and tolerability of an intratumorally injected DNAzyme, Dz13, in patients with nodular basal-cell carcinoma: A phase 1 first-in-human trial (DISCOVER)
    • [CrossRef]
    • Cho, E.A.; Moloney, F.J.; Cai, H.; Au-Yeung, A.; China, C.; Scolyer, R.A.; Yosufi, B.; Raftery, M.J.; Deng, J.Z.; Morton, S.W.; et al. Safety and tolerability of an intratumorally injected DNAzyme, Dz13, in patients with nodular basal-cell carcinoma: A phase 1 first-in-human trial (DISCOVER). Lancet 2013, 381, 1835-1843. [CrossRef]
    • (2013) Lancet , vol.381 , pp. 1835-1843
    • Cho, E.A.1    Moloney, F.J.2    Cai, H.3    Au-Yeung, A.4    China, C.5    Scolyer, R.A.6    Yosufi, B.7    Raftery, M.J.8    Deng, J.Z.9    Morton, S.W.10
  • 98
    • 0037151008 scopus 로고    scopus 로고
    • C-jun regulates vascular smooth muscle cell growth and neointima formation after arterial injury
    • [CrossRef] [PubMed]
    • Khachigian, L.M.; Fahmy, R.G.; Zhang, G.; Bobryshev, Y.V.; Kaniaros, A. c-Jun Regulates Vascular Smooth Muscle Cell Growth and Neointima Formation after Arterial Injury. J. Biol. Chem. 2002, 277, 22985-22991. [CrossRef] [PubMed]
    • (2002) J. Biol. Chem. , vol.277 , pp. 22985-22991
    • Khachigian, L.M.1    Fahmy, R.G.2    Zhang, G.3    Bobryshev, Y.V.4    Kaniaros, A.5
  • 99
    • 0242691046 scopus 로고    scopus 로고
    • AP-1: A double-edged sword in tumorigenesis
    • [CrossRef] [PubMed]
    • Eferl, R.; Wagner, E.F. AP-1: A double-edged sword in tumorigenesis. Nat. Rev. Cancer 2003, 3, 859-868. [CrossRef] [PubMed]
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 859-868
    • Eferl, R.1    Wagner, E.F.2
  • 101
    • 77952313777 scopus 로고    scopus 로고
    • Differentiation of effector CD4 T cell populations
    • [CrossRef] [PubMed]
    • Zhu, J.; Yamane, H.; Paul, W.E. Differentiation of Effector CD4 T Cell Populations. Annu. Rev. Immunol. 2010, 28, 445-489. [CrossRef] [PubMed]
    • (2010) Annu. Rev. Immunol. , vol.28 , pp. 445-489
    • Zhu, J.1    Yamane, H.2    Paul, W.E.3
  • 102
    • 84929783330 scopus 로고    scopus 로고
    • Out of the orphanage and into the clinic-therapeutic targeting of GATA3
    • [CrossRef] [PubMed]
    • Bochner, B.S.; Schleimer, R.P. Out of the Orphanage and into the Clinic-Therapeutic Targeting of GATA3. N. Engl. J. Med. 2015, 372, 2060-2061. [CrossRef] [PubMed]
    • (2015) N. Engl. J. Med. , vol.372 , pp. 2060-2061
    • Bochner, B.S.1    Schleimer, R.P.2
  • 103
    • 41449090371 scopus 로고    scopus 로고
    • Effective prevention and therapy of experimental allergic asthma using a GATA-3-specific DNAzyme
    • [CrossRef] [PubMed]
    • Sel, S.; Wegmann, M.; Dicke, T.; Henke, W.; Yildirim, A.O.; Renz, H.; Garn, H. Effective prevention and therapy of experimental allergic asthma using a GATA-3-specific DNAzyme. J. Allergy Clin. Immunol. 2008, 121, 910-916. [CrossRef] [PubMed]
    • (2008) J. Allergy Clin. Immunol. , vol.121 , pp. 910-916
    • Sel, S.1    Wegmann, M.2    Dicke, T.3    Henke, W.4    Yildirim, A.O.5    Renz, H.6    Garn, H.7
  • 105
    • 33646738061 scopus 로고    scopus 로고
    • Oligonucleotide-modified gold nanoparticles for intracellular gene regulation
    • [CrossRef] [PubMed]
    • Rosi, N.L.; Giljohann, D.A.; Thaxton, C.S.; Lytton-Jean, A.K.R.; Han, M.S.; Mirkin, C.A. Oligonucleotide-Modified Gold Nanoparticles for Intracellular Gene Regulation. Science 2006, 312, 1027-1030. [CrossRef] [PubMed]
    • (2006) Science , vol.312 , pp. 1027-1030
    • Rosi, N.L.1    Giljohann, D.A.2    Thaxton, C.S.3    Lytton-Jean, A.K.R.4    Han, M.S.5    Mirkin, C.A.6
  • 106
    • 84867832933 scopus 로고    scopus 로고
    • Catalytic deoxyribozyme-modified nanoparticles for RNAi-independent gene regulation
    • [CrossRef] [PubMed]
    • Yehl, K.; Joshi, J.P.; Greene, B.L.; Dyer, R.B.; Nahta, R.; Salaita, K. Catalytic Deoxyribozyme-Modified Nanoparticles for RNAi-Independent Gene Regulation. ACS Nano 2012, 6, 9150-9157. [CrossRef] [PubMed]
    • (2012) ACS Nano , vol.6 , pp. 9150-9157
    • Yehl, K.1    Joshi, J.P.2    Greene, B.L.3    Dyer, R.B.4    Nahta, R.5    Salaita, K.6
  • 107
    • 0036792125 scopus 로고    scopus 로고
    • Angiogenic inhibition mediated by a DNAzyme that targets vascular endothelial growth factor receptor 2
    • [PubMed]
    • Zhang, L.; Gasper, W.J.; Stass, S.A.; Ioffe, O.B.; Davis, M.A.; Mixson, A.J. Angiogenic Inhibition Mediated by a DNAzyme That Targets Vascular Endothelial Growth Factor Receptor 2. Cancer Res. 2002, 62, 5463-5469. [PubMed]
    • (2002) Cancer Res. , vol.62 , pp. 5463-5469
    • Zhang, L.1    Gasper, W.J.2    Stass, S.A.3    Ioffe, O.B.4    Davis, M.A.5    Mixson, A.J.6
  • 108
    • 77951673091 scopus 로고    scopus 로고
    • Activation and deactivation of DNAzyme and antisense function with light for the photochemical regulation of gene expression in mammalian cells
    • [CrossRef] [PubMed]
    • Young, D.D.; Lively, M.O.; Deiters, A. Activation and Deactivation of DNAzyme and Antisense Function with Light for the Photochemical Regulation of Gene Expression in Mammalian Cells. J. Am. Chem. Soc. 2010, 132, 6183-6193. [CrossRef] [PubMed]
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 6183-6193
    • Young, D.D.1    Lively, M.O.2    Deiters, A.3
  • 109
    • 47749107927 scopus 로고    scopus 로고
    • Deoxyribozymes: Useful DNA catalysts in vitro and in vivo
    • [CrossRef] [PubMed]
    • Baum, D.A.; Silverman, S.K. Deoxyribozymes: Useful DNA catalysts in vitro and in vivo. Cell. Mol. Life Sci. 2008, 65, 2156-2174. [CrossRef] [PubMed]
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 2156-2174
    • Baum, D.A.1    Silverman, S.K.2
  • 110
    • 79959503058 scopus 로고    scopus 로고
    • Metal ion sensors based on DNAzymes
    • [CrossRef] [PubMed]
    • Zhang, X.-B.; Kong, R.-M.; Lu, Y. Metal Ion Sensors Based on DNAzymes. Annu. Rev. Anal. Chem. 2011, 4, 105-128. [CrossRef] [PubMed]
    • (2011) Annu. Rev. Anal. Chem. , vol.4 , pp. 105-128
    • Zhang, X.-B.1    Kong, R.-M.2    Lu, Y.3
  • 111
    • 84894353625 scopus 로고    scopus 로고
    • DNA as sensors and imaging agents for metal ions
    • [CrossRef] [PubMed]
    • Xiang, Y.; Lu, Y. DNA as Sensors and Imaging Agents for Metal Ions. Inorg. Chem. 2014, 53, 1925-1942. [CrossRef] [PubMed]
    • (2014) Inorg. Chem. , vol.53 , pp. 1925-1942
    • Xiang, Y.1    Lu, Y.2
  • 113
    • 34548204760 scopus 로고    scopus 로고
    • Zinc(II) complexes as hydrolytic catalysts of phosphate diester cleavage: From model substrates to nucleic acids
    • [CrossRef]
    • Mancin, F.; Tecilla, P. Zinc(II) complexes as hydrolytic catalysts of phosphate diester cleavage: From model substrates to nucleic acids. New J. Chem. 2007, 31, 800-817. [CrossRef]
    • (2007) New J. Chem. , vol.31 , pp. 800-817
    • Mancin, F.1    Tecilla, P.2
  • 114
    • 84933557191 scopus 로고    scopus 로고
    • Copper and zinc complexes of a diaza-crown ether as artificial nucleases for the efficient hydrolytic cleavage of DNA
    • [CrossRef]
    • Li, F.Z.; Xie, J.Q.; Feng, F.M. Copper and zinc complexes of a diaza-crown ether as artificial nucleases for the efficient hydrolytic cleavage of DNA. New J. Chem. 2015, 39, 5654-5660. [CrossRef]
    • (2015) New J. Chem. , vol.39 , pp. 5654-5660
    • Li, F.Z.1    Xie, J.Q.2    Feng, F.M.3
  • 115
    • 0026649231 scopus 로고
    • Directed evolution of an RNA enzyme
    • [CrossRef] [PubMed]
    • Beaudry, A.A.; Joyce, G.F. Directed evolution of an RNA enzyme. Science 1992, 257, 635-641. [CrossRef] [PubMed]
    • (1992) Science , vol.257 , pp. 635-641
    • Beaudry, A.A.1    Joyce, G.F.2
  • 116
    • 0028233951 scopus 로고
    • Evolutionary optimization of the catalytic properties of a DNA-cleaving ribozyme
    • [CrossRef] [PubMed]
    • Tsang, J.; Joyce, G.F. Evolutionary Optimization of the Catalytic Properties of a DNA-Cleaving Ribozyme. Biochemistry 1994, 33, 5966-5973. [CrossRef] [PubMed]
    • (1994) Biochemistry , vol.33 , pp. 5966-5973
    • Tsang, J.1    Joyce, G.F.2
  • 117
    • 0030582393 scopus 로고    scopus 로고
    • Specialization of the DNA-cleaving activity of a group I ribozyme through in vitro evolution
    • [CrossRef] [PubMed]
    • Tsang, J.; Joyce, G.F. Specialization of the DNA-cleaving activity of a group I ribozyme through in vitro evolution. J. Mol. Biol. 1996, 262, 31-42. [CrossRef] [PubMed]
    • (1996) J. Mol. Biol. , vol.262 , pp. 31-42
    • Tsang, J.1    Joyce, G.F.2
  • 118
    • 0035543093 scopus 로고    scopus 로고
    • The depth of chemical time and the power of enzymes as catalysts
    • [CrossRef] [PubMed]
    • Wolfenden, R.; Snider, M.J. The Depth of Chemical Time and the Power of Enzymes as Catalysts. Acc. Chem. Res. 2001, 34, 938-945. [CrossRef] [PubMed]
    • (2001) Acc. Chem. Res. , vol.34 , pp. 938-945
    • Wolfenden, R.1    Snider, M.J.2
  • 119
    • 33645212804 scopus 로고    scopus 로고
    • The time required for water attack at the phosphorus atom of simple phosphodiesters and of DNA
    • [CrossRef] [PubMed]
    • Schroeder, G.K.; Lad, C.;Wyman, P.;Williams, N.H.;Wolfenden, R. The time required for water attack at the phosphorus atom of simple phosphodiesters and of DNA. Proc. Natl. Acad. Sci. USA 2006, 103, 4052-4055. [CrossRef] [PubMed]
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 4052-4055
    • Schroeder, G.K.1    Lad, C.2    Wyman, P.3    Williams, N.H.4    Wolfenden, R.5
  • 120
    • 0030482173 scopus 로고    scopus 로고
    • In vitro selection of self-cleaving DNAs
    • [CrossRef]
    • Carmi, N.; Shultz, L.A.; Breaker, R.R. In vitro selection of self-cleaving DNAs. Chem. Biol. 1996, 3, 1039-1046. [CrossRef]
    • (1996) Chem. Biol. , vol.3 , pp. 1039-1046
    • Carmi, N.1    Shultz, L.A.2    Breaker, R.R.3
  • 122
    • 84906216244 scopus 로고    scopus 로고
    • In vitro selection of DNA-cleaving deoxyribozyme with site-specific thymidine excision activity
    • [CrossRef] [PubMed]
    • Wang, M.Q.; Zhang, H.F.; Zhang, W.; Zhao, Y.Y.; Yasmeen, A.; Zhou, L.; Yu, X.Q.; Tang, Z. In vitro selection of DNA-cleaving deoxyribozyme with site-specific thymidine excision activity. Nucleic Acids Res. 2014, 42, 9262-9269. [CrossRef] [PubMed]
    • (2014) Nucleic Acids Res. , vol.42 , pp. 9262-9269
    • Wang, M.Q.1    Zhang, H.F.2    Zhang, W.3    Zhao, Y.Y.4    Yasmeen, A.5    Zhou, L.6    Yu, X.Q.7    Tang, Z.8
  • 123
    • 38949209141 scopus 로고    scopus 로고
    • The chemical toxicology of 2-deoxyribose oxidation in DNA
    • [CrossRef] [PubMed]
    • Dedon, P.C. The chemical toxicology of 2-deoxyribose oxidation in DNA. Chem. Res. Toxicol. 2008, 21, 206-219. [CrossRef] [PubMed]
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 206-219
    • Dedon, P.C.1
  • 124
    • 0030037715 scopus 로고    scopus 로고
    • Rates of uncatalyzed peptide bond hydrolysis in neutral solution and the transition state affinities of proteases
    • [CrossRef]
    • Radzicka, A.; Wolfenden, R. Rates of Uncatalyzed Peptide Bond Hydrolysis in Neutral Solution and the Transition State Affinities of Proteases. J. Am. Chem. Soc. 1996, 118, 6105-6109. [CrossRef]
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 6105-6109
    • Radzicka, A.1    Wolfenden, R.2
  • 125
    • 78149332105 scopus 로고    scopus 로고
    • Functional compromises among pH tolerance, site specificity, and sequence tolerance for a DNA-hyrdolyzing deoxyribozyme
    • [CrossRef] [PubMed]
    • Xiao, Y.; Chandra, M.; Silverman, S.K. Functional Compromises among pH Tolerance, Site Specificity, and Sequence Tolerance for a DNA-Hyrdolyzing Deoxyribozyme. Biochemistry 2010, 49, 9630-9637. [CrossRef] [PubMed]
    • (2010) Biochemistry , vol.49 , pp. 9630-9637
    • Xiao, Y.1    Chandra, M.2    Silverman, S.K.3
  • 127
    • 84859361211 scopus 로고    scopus 로고
    • Lanthanide ions as required cofactors for DNA catalysts
    • [CrossRef] [PubMed]
    • Dokukin, V.; Silverman, S.K. Lanthanide ions as required cofactors for DNA catalysts. Chem. Sci. 2012, 3, 1707-1714. [CrossRef] [PubMed]
    • (2012) Chem. Sci. , vol.3 , pp. 1707-1714
    • Dokukin, V.1    Silverman, S.K.2
  • 129
    • 84942292136 scopus 로고    scopus 로고
    • Generation of long, fully modified, and serum-resistant oligonucleotides by rolling circle amplification
    • [CrossRef] [PubMed]
    • Hollenstein, M. Generation of long, fully modified, and serum-resistant oligonucleotides by rolling circle amplification. Org. Biomol. Chem. 2015, 13, 9820-9824. [CrossRef] [PubMed]
    • (2015) Org. Biomol. Chem. , vol.13 , pp. 9820-9824
    • Hollenstein, M.1
  • 130
    • 84897531334 scopus 로고    scopus 로고
    • Physicochemical mechanism of light-driven DNA repair by (6-4) photolyases
    • [CrossRef] [PubMed]
    • Faraji, S.; Dreuw, A. Physicochemical Mechanism of Light-Driven DNA Repair by (6-4) Photolyases. Annu. Rev. Phys. Chem. 2014, 65, 275-292. [CrossRef] [PubMed]
    • (2014) Annu. Rev. Phys. Chem. , vol.65 , pp. 275-292
    • Faraji, S.1    Dreuw, A.2
  • 131
    • 33846023648 scopus 로고    scopus 로고
    • Towards elucidation of the mechanism of UV1C, a deoxyribozyme with photolyase activity
    • [CrossRef] [PubMed]
    • Chinnapen, D.J.F.; Sen, D. Towards elucidation of the mechanism of UV1C, a deoxyribozyme with photolyase activity. J. Mol. Biol. 2007, 365, 1326-1336. [CrossRef] [PubMed]
    • (2007) J. Mol. Biol. , vol.365 , pp. 1326-1336
    • Chinnapen, D.J.F.1    Sen, D.2
  • 132
    • 84874082725 scopus 로고    scopus 로고
    • Catalytic DNAs that harness violet light to repair thymine dimers in a DNA substrate
    • [CrossRef] [PubMed]
    • Barlev, A.; Sen, D. Catalytic DNAs That Harness Violet Light To Repair Thymine Dimers in a DNA Substrate. J. Am. Chem. Soc. 2013, 135, 2596-2603. [CrossRef] [PubMed]
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 2596-2603
    • Barlev, A.1    Sen, D.2
  • 133
    • 0028898110 scopus 로고
    • Cleavage of an amide bond by a ribozyme
    • [CrossRef] [PubMed]
    • Dai, X.; de Mesmaeker, A.; Joyce, G.F. Cleavage of an Amide Bond by a Ribozyme. Science 1995, 267, 237-241. [CrossRef] [PubMed]
    • (1995) Science , vol.267 , pp. 237-241
    • Dai, X.1    De Mesmaeker, A.2    Joyce, G.F.3
  • 134
    • 0029985731 scopus 로고    scopus 로고
    • Amide cleavage by a ribozyme: Correction
    • [CrossRef] [PubMed]
    • Joyce, G.F.; Dai, X.; de Mesmaeker, A. Amide Cleavage by a Ribozyme: Correction. Science 1996, 272, 18-19. [CrossRef] [PubMed]
    • (1996) Science , vol.272 , pp. 18-19
    • Joyce, G.F.1    Dai, X.2    De Mesmaeker, A.3
  • 135
    • 84880588383 scopus 로고    scopus 로고
    • Deoxynucleoside triphosphates bearing histamine, carboxylic acid, and hydroxyl residues-synthesis and biochemical characterization
    • [CrossRef] [PubMed]
    • Hollenstein, M. Deoxynucleoside triphosphates bearing histamine, carboxylic acid, and hydroxyl residues-Synthesis and biochemical characterization. Org. Biomol. Chem. 2013, 11, 5162-5172. [CrossRef] [PubMed]
    • (2013) Org. Biomol. Chem. , vol.11 , pp. 5162-5172
    • Hollenstein, M.1
  • 136
    • 84929590853 scopus 로고    scopus 로고
    • Pursuing DNA catalysts for protein modification
    • [CrossRef] [PubMed]
    • Silverman, S.K. Pursuing DNA Catalysts for Protein Modification. Acc. Chem. Res. 2015, 48, 1369-1379. [CrossRef] [PubMed]
    • (2015) Acc. Chem. Res. , vol.48 , pp. 1369-1379
    • Silverman, S.K.1
  • 137
    • 84875856674 scopus 로고    scopus 로고
    • Catalytic DNA with phosphatase activity
    • [CrossRef] [PubMed]
    • Chandrasekar, J.; Silverman, S.K. Catalytic DNA with phosphatase activity. Proc. Natl. Acad. Sci. USA 2013, 110, 5315-5320. [CrossRef] [PubMed]
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 5315-5320
    • Chandrasekar, J.1    Silverman, S.K.2
  • 138
    • 79959580534 scopus 로고    scopus 로고
    • Contemporary strategies for peptide macrocyclization
    • [CrossRef] [PubMed]
    • White, C.J.; Yudin, A.K. Contemporary strategies for peptide macrocyclization. Nat. Chem. 2011, 3, 509-524. [CrossRef] [PubMed]
    • (2011) Nat. Chem. , vol.3 , pp. 509-524
    • White, C.J.1    Yudin, A.K.2
  • 139
    • 84938884335 scopus 로고    scopus 로고
    • Phosphoserine lyase deoxyribozymes: DNA-catalyzed formation of dehydroalanine residues in peptides
    • [CrossRef] [PubMed]
    • Chandrasekar, J.; Wylder, A.C.; Silverman, S.K. Phosphoserine Lyase Deoxyribozymes: DNA-Catalyzed Formation of Dehydroalanine Residues in Peptides. J. Am. Chem. Soc. 2015, 137, 9575-9578. [CrossRef] [PubMed]
    • (2015) J. Am. Chem. Soc. , vol.137 , pp. 9575-9578
    • Chandrasekar, J.1    Wylder, A.C.2    Silverman, S.K.3
  • 140
    • 0030963855 scopus 로고    scopus 로고
    • RNA-catalysed carbon-carbon bond formation
    • [CrossRef] [PubMed]
    • Tarasow, T.M.; Tarasow, S.L.; Eaton, B.E. RNA-catalysed carbon-carbon bond formation. Nature 1997, 389, 54-57. [CrossRef] [PubMed]
    • (1997) Nature , vol.389 , pp. 54-57
    • Tarasow, T.M.1    Tarasow, S.L.2    Eaton, B.E.3
  • 141
    • 0033102314 scopus 로고    scopus 로고
    • A small catalytic RNA motif with diels-alderase activity
    • [CrossRef]
    • Seelig, B.; Jäschke, A. A Small Catalytic RNA Motif with Diels-Alderase Activity. Chem. Biol. 1999, 6, 167-176. [CrossRef]
    • (1999) Chem. Biol. , vol.6 , pp. 167-176
    • Seelig, B.1    Jäschke, A.2
  • 142
    • 0028969534 scopus 로고
    • Aminoacyl-RNA synthesis catalyzed by an RNA
    • [CrossRef] [PubMed]
    • Illangasekare, M.; Sanchez, G.; Nickles, T.; Yarus, M. Aminoacyl-RNA synthesis catalyzed by an RNA. Science 1995, 267, 643-647. [CrossRef] [PubMed]
    • (1995) Science , vol.267 , pp. 643-647
    • Illangasekare, M.1    Sanchez, G.2    Nickles, T.3    Yarus, M.4
  • 143
    • 67849122619 scopus 로고    scopus 로고
    • Rapid and simple ribozymic aminoacylation using three conserved nucleotides
    • [CrossRef] [PubMed]
    • Chumachenko, N.V.; Novikov, Y.; Yarus, M. Rapid and Simple Ribozymic Aminoacylation Using Three Conserved Nucleotides. J. Am. Chem. Soc. 2009, 131, 5257-5263. [CrossRef] [PubMed]
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 5257-5263
    • Chumachenko, N.V.1    Novikov, Y.2    Yarus, M.3
  • 144
    • 84898874449 scopus 로고    scopus 로고
    • Generation and selection of ribozyme variants with potential application in protein engineering and synthetic biology
    • [CrossRef] [PubMed]
    • Balke, D.; Wichert, C.; Appel, B.; Muller, S. Generation and selection of ribozyme variants with potential application in protein engineering and synthetic biology. Appl. Microbiol. Biotechnol. 2014, 98, 3389-3399. [CrossRef] [PubMed]
    • (2014) Appl. Microbiol. Biotechnol. , vol.98 , pp. 3389-3399
    • Balke, D.1    Wichert, C.2    Appel, B.3    Muller, S.4
  • 145
    • 0029956108 scopus 로고    scopus 로고
    • Ribozyme-catalysed amino-acid transfer reactions
    • [CrossRef] [PubMed]
    • Lohse, P.A.; Szostak, J.W. Ribozyme-catalysed amino-acid transfer reactions. Nature 1996, 381, 442-444. [CrossRef] [PubMed]
    • (1996) Nature , vol.381 , pp. 442-444
    • Lohse, P.A.1    Szostak, J.W.2
  • 146
    • 0030688863 scopus 로고    scopus 로고
    • Peptide bond formation by in vitro selected ribozymes
    • [PubMed]
    • Zhang, B.L.; Cech, T.R. Peptide bond formation by in vitro selected ribozymes. Nature 1997, 390, 96-100. [PubMed]
    • (1997) Nature , vol.390 , pp. 96-100
    • Zhang, B.L.1    Cech, T.R.2
  • 147
    • 0031238806 scopus 로고    scopus 로고
    • Selection of RNA amide synthase
    • [CrossRef]
    • Wiegand, T.W.; Janssen, R.C.; Eaton, B.E. Selection of RNA amide synthase. Chem. Biol. 1997, 4, 675-683. [CrossRef]
    • (1997) Chem. Biol. , vol.4 , pp. 675-683
    • Wiegand, T.W.1    Janssen, R.C.2    Eaton, B.E.3
  • 149
    • 41449109957 scopus 로고    scopus 로고
    • DNA and RNA can Be equally efficient catalysts for carbon-carbon bond formation
    • [CrossRef] [PubMed]
    • Chandra, M.; Silverman, S.K. DNA and RNA Can Be Equally Efficient Catalysts for Carbon-Carbon Bond Formation. J. Am. Chem. Soc. 2008, 130, 2936-2937. [CrossRef] [PubMed]
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 2936-2937
    • Chandra, M.1    Silverman, S.K.2
  • 150
    • 84875022373 scopus 로고    scopus 로고
    • In vitro evolution of a friedel-crafts deoxyribozyme
    • [CrossRef] [PubMed]
    • Mohan, U.; Burai, R.; McNaughton, B.R. In vitro evolution of a Friedel-Crafts deoxyribozyme. Org. Biomol. Chem. 2013, 11, 2241-2244. [CrossRef] [PubMed]
    • (2013) Org. Biomol. Chem. , vol.11 , pp. 2241-2244
    • Mohan, U.1    Burai, R.2    McNaughton, B.R.3
  • 151
    • 77649165966 scopus 로고    scopus 로고
    • A review of new developments in the friedel-crafts alkylation-from green chemistry to asymmetric catalysis
    • [CrossRef] [PubMed]
    • Rueping, M.; Nachtsheim, B.J. A review of new developments in the Friedel-Crafts alkylation-From green chemistry to asymmetric catalysis. Beilstein J. Org. Chem. 2010, 6, 24. [CrossRef] [PubMed]
    • (2010) Beilstein J. Org. Chem. , vol.6 , pp. 24
    • Rueping, M.1    Nachtsheim, B.J.2
  • 152
    • 70349784852 scopus 로고    scopus 로고
    • Enantioselective friedel-crafts reactions in water using a DNA-based catalyst
    • [CrossRef] [PubMed]
    • Boersma, A.J.; Feringa, B.L.; Roelfes, G. Enantioselective Friedel-Crafts Reactions in Water Using a DNA-Based Catalyst. Angew. Chem. Int. Ed. 2009, 48, 3346-3348. [CrossRef] [PubMed]
    • (2009) Angew. Chem. Int. Ed. , vol.48 , pp. 3346-3348
    • Boersma, A.J.1    Feringa, B.L.2    Roelfes, G.3
  • 155
    • 11144330098 scopus 로고    scopus 로고
    • Natural and engineered nucleic acids as tools to explore biology
    • [CrossRef] [PubMed]
    • Breaker, R.R. Natural and engineered nucleic acids as tools to explore biology. Nature 2004, 432, 838-845. [CrossRef] [PubMed]
    • (2004) Nature , vol.432 , pp. 838-845
    • Breaker, R.R.1
  • 156
    • 0029037713 scopus 로고
    • A DNA metalloenzyme with DNA ligase activity
    • [CrossRef] [PubMed]
    • Cuenoud, B.; Szostak, J.W. A DNA metalloenzyme with DNA ligase activity. Nature 1995, 375, 611-614. [CrossRef] [PubMed]
    • (1995) Nature , vol.375 , pp. 611-614
    • Cuenoud, B.1    Szostak, J.W.2
  • 157
    • 0033019927 scopus 로고    scopus 로고
    • Phosphorylating DNA with DNA
    • [CrossRef] [PubMed]
    • Li, Y.F.; Breaker, R.R. Phosphorylating DNA with DNA. Proc. Natl. Acad. Sci. USA 1999, 96, 2746-2751. [CrossRef] [PubMed]
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2746-2751
    • Li, Y.F.1    Breaker, R.R.2
  • 158
    • 0036235747 scopus 로고    scopus 로고
    • Sequence diversity, metal specificity, and catalytic proficiency of metal-dependent phosphorylating DNA enzymes
    • [CrossRef]
    • Wang, W.; Billen, L.P.; Li, Y.F. Sequence diversity, metal specificity, and catalytic proficiency of metal-dependent phosphorylating DNA enzymes. Chem. Biol. 2002, 9, 507-517. [CrossRef]
    • (2002) Chem. Biol. , vol.9 , pp. 507-517
    • Wang, W.1    Billen, L.P.2    Li, Y.F.3
  • 159
    • 14844349015 scopus 로고    scopus 로고
    • Secondary-structure characterization of two proficient kinase deoxyribozymes
    • [CrossRef] [PubMed]
    • Achenbach, J.C.; Jeffries, G.A.; McManus, S.A.; Billen, L.P.; Li, Y.F. Secondary-structure characterization of two proficient kinase deoxyribozymes. Biochemistry 2005, 44, 3765-3774. [CrossRef] [PubMed]
    • (2005) Biochemistry , vol.44 , pp. 3765-3774
    • Achenbach, J.C.1    Jeffries, G.A.2    McManus, S.A.3    Billen, L.P.4    Li, Y.F.5
  • 160
    • 0034696594 scopus 로고    scopus 로고
    • Capping DNA with DNA
    • [CrossRef] [PubMed]
    • Li, Y.F.; Liu, Y.; Breaker, R.R. Capping DNA with DNA. Biochemistry 2000, 39, 3106-3114. [CrossRef] [PubMed]
    • (2000) Biochemistry , vol.39 , pp. 3106-3114
    • Li, Y.F.1    Liu, Y.2    Breaker, R.R.3
  • 161
    • 1642332434 scopus 로고    scopus 로고
    • Ligating DNA with DNA
    • [CrossRef] [PubMed]
    • Sreedhara, A.; Li, Y.F.; Breaker, R.R. Ligating DNA with DNA. J. Am. Chem. Soc. 2004, 126, 3454-3460. [CrossRef] [PubMed]
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3454-3460
    • Sreedhara, A.1    Li, Y.F.2    Breaker, R.R.3
  • 162
    • 0030794322 scopus 로고    scopus 로고
    • Cofactor-assisted self-cleavage in DNA libraries with a 3′-5′-phosphoramidate bond
    • [CrossRef]
    • Burmeister, J.; von Kiedrowski, G.; Ellington, A.D. Cofactor-assisted self-cleavage in DNA libraries with a 3′-5′-phosphoramidate bond. Angew. Chem. Int. Ed. 1997, 36, 1321-1324. [CrossRef]
    • (1997) Angew. Chem. Int. Ed. , vol.36 , pp. 1321-1324
    • Burmeister, J.1    Von Kiedrowski, G.2    Ellington, A.D.3
  • 163
    • 78651267394 scopus 로고    scopus 로고
    • Improved deoxyribozymes for synthesis of covalently branched DNA and RNA
    • [CrossRef] [PubMed]
    • Lee, C.S.; Mui, T.P.; Silverman, S.K. Improved deoxyribozymes for synthesis of covalently branched DNA and RNA. Nucleic Acids Res. 39, 269-279. [CrossRef] [PubMed]
    • Nucleic Acids Res. , vol.39 , pp. 269-279
    • Lee, C.S.1    Mui, T.P.2    Silverman, S.K.3
  • 164
    • 77951731728 scopus 로고    scopus 로고
    • Deoxyribozymes: Selection design and serendipity in the development of DNA catalysts
    • [CrossRef] [PubMed]
    • Silverman, S.K. Deoxyribozymes: Selection Design and Serendipity in the Development of DNA Catalysts. Acc. Chem. Res. 2009, 42, 1521-1531. [CrossRef] [PubMed]
    • (2009) Acc. Chem. Res. , vol.42 , pp. 1521-1531
    • Silverman, S.K.1
  • 166
    • 1442286924 scopus 로고    scopus 로고
    • A DNA enzyme that mimics the first step of RNA splicing
    • [CrossRef] [PubMed]
    • Coppins, R.L.; Silverman, S.K. A DNA enzyme that mimics the first step of RNA splicing. Nat. Struct. Mol. Biol. 2004, 11, 270-274. [CrossRef] [PubMed]
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 270-274
    • Coppins, R.L.1    Silverman, S.K.2
  • 167
    • 34250809072 scopus 로고    scopus 로고
    • Deoxyribozyme-catalyzed labeling of RNA
    • [CrossRef] [PubMed]
    • Baum, D.A.; Silverman, S.K. Deoxyribozyme-catalyzed labeling of RNA. Angew. Chem. Int. Ed. 2007, 46, 3502-3504. [CrossRef] [PubMed]
    • (2007) Angew. Chem. Int. Ed. , vol.46 , pp. 3502-3504
    • Baum, D.A.1    Silverman, S.K.2
  • 168
    • 84901952492 scopus 로고    scopus 로고
    • Site-specific labeling of RNA at internal ribose hydroxyl groups: Terbium-assisted deoxyribozymes at work
    • [CrossRef] [PubMed]
    • Büttner, L.; Javadi-Zarnaghi, F.; Höbartner, C. Site-Specific Labeling of RNA at Internal Ribose Hydroxyl Groups: Terbium-Assisted Deoxyribozymes at Work. J. Am. Chem. Soc. 2014, 136, 8131-8137. [CrossRef] [PubMed]
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 8131-8137
    • Büttner, L.1    Javadi-Zarnaghi, F.2    Höbartner, C.3
  • 169
    • 84941028473 scopus 로고    scopus 로고
    • 2+-dependent conformational changes and product release during DNA-catalyzed RNA ligation monitored by bimane fluorescence
    • [CrossRef] [PubMed]
    • 2+-dependent conformational changes and product release during DNA-catalyzed RNA ligation monitored by Bimane fluorescence. Nucleic Acids Res. 2015, 43, 40-50. [CrossRef] [PubMed]
    • (2015) Nucleic Acids Res. , vol.43 , pp. 40-50
    • Turriani, E.1    Hobartner, C.2    Jovin, T.M.3
  • 170
    • 53949112902 scopus 로고    scopus 로고
    • III luminescence spectroscopy
    • [CrossRef] [PubMed]
    • III Luminescence Spectroscopy. Chem. Eur. J. 2008, 14, 8696-8703. [CrossRef] [PubMed]
    • (2008) Chem. Eur. J. , vol.14 , pp. 8696-8703
    • Kim, H.-K.1    Li, J.2    Nagraj, N.3    Lu, Y.4
  • 171
    • 84883271155 scopus 로고    scopus 로고
    • Lanthanide cofactors accelerate DNA-catalyzed synthesis of branched RNA
    • [CrossRef] [PubMed]
    • Javadi-Zarnaghi, F.; Hoebartner, C. Lanthanide Cofactors Accelerate DNA-Catalyzed Synthesis of Branched RNA. J. Am. Chem. Soc. 2013, 135, 12839-12848. [CrossRef] [PubMed]
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 12839-12848
    • Javadi-Zarnaghi, F.1    Hoebartner, C.2
  • 173
    • 84938748741 scopus 로고    scopus 로고
    • Effects of cosolvents on the folding and catalytic activities of the hammerhead ribozyme
    • [CrossRef] [PubMed]
    • Nakano, S.; Kitagawa, Y.; Yamashita, H.; Miyoshi, D.; Sugimoto, N. Effects of Cosolvents on the Folding and Catalytic Activities of the Hammerhead Ribozyme. ChemBioChem 2015, 16, 1803-1810. [CrossRef] [PubMed]
    • (2015) ChemBioChem , vol.16 , pp. 1803-1810
    • Nakano, S.1    Kitagawa, Y.2    Yamashita, H.3    Miyoshi, D.4    Sugimoto, N.5
  • 174
  • 175
    • 84875458695 scopus 로고    scopus 로고
    • Enhanced deoxyribozyme-catalyzed RNA ligation in the presence of organic cosolvents
    • [CrossRef] [PubMed]
    • Behera, A.K.; Schlund, K.J.; Mason, A.J.; Alila, K.O.; Han, M.Y.; Grout, R.L.; Baum, D.A. Enhanced deoxyribozyme-catalyzed RNA ligation in the presence of organic cosolvents. Biopolymers 2013, 99, 382-391. [CrossRef] [PubMed]
    • (2013) Biopolymers , vol.99 , pp. 382-391
    • Behera, A.K.1    Schlund, K.J.2    Mason, A.J.3    Alila, K.O.4    Han, M.Y.5    Grout, R.L.6    Baum, D.A.7
  • 177
    • 77949583070 scopus 로고    scopus 로고
    • DNA-catalyzed serine side chain reactivity and selectivity
    • [CrossRef] [PubMed]
    • Sachdeva, A.; Silverman, S.K. DNA-catalyzed serine side chain reactivity and selectivity. Chem. Commun. 2010, 46, 2215-2217. [CrossRef] [PubMed]
    • (2010) Chem. Commun. , vol.46 , pp. 2215-2217
    • Sachdeva, A.1    Silverman, S.K.2
  • 178
    • 84858311242 scopus 로고    scopus 로고
    • Covalent tagging of phosphorylated peptides by phosphate-specific deoxyribozymes
    • [CrossRef] [PubMed]
    • Sachdeva, A.; Chandra, M.; Chandrasekar, J.; Silverman, S.K. Covalent Tagging of Phosphorylated Peptides by Phosphate-Specific Deoxyribozymes. ChemBioChem 2012, 13, 654-657. [CrossRef] [PubMed]
    • (2012) ChemBioChem , vol.13 , pp. 654-657
    • Sachdeva, A.1    Chandra, M.2    Chandrasekar, J.3    Silverman, S.K.4
  • 179
    • 84885654421 scopus 로고    scopus 로고
    • DNA catalysts with tyrosine kinase activity
    • [CrossRef] [PubMed]
    • Walsh, S.M.; Sachdeva, A.; Silverman, S.K. DNA Catalysts with Tyrosine Kinase Activity. J. Am. Chem. Soc. 2013, 135, 14928-14931. [CrossRef] [PubMed]
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 14928-14931
    • Walsh, S.M.1    Sachdeva, A.2    Silverman, S.K.3
  • 180
    • 0029746712 scopus 로고    scopus 로고
    • A catalytic DNA for porphyrin metallation
    • [CrossRef] [PubMed]
    • Li, Y.; Sen, D. A Catalytic DNA for Porphyrin Metallation. Nat. Struct. Biol. 1996, 3, 743-747. [CrossRef] [PubMed]
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 743-747
    • Li, Y.1    Sen, D.2
  • 181
    • 0029945146 scopus 로고    scopus 로고
    • Recognition of anionic porphyrins by DNA aptamers
    • [CrossRef] [PubMed]
    • Li, Y.F.; Geyer, C.R.; Sen, D. Recognition of anionic porphyrins by DNA aptamers. Biochemistry 1996, 35, 6911-6922. [CrossRef] [PubMed]
    • (1996) Biochemistry , vol.35 , pp. 6911-6922
    • Li, Y.F.1    Geyer, C.R.2    Sen, D.3
  • 182
    • 0030954291 scopus 로고    scopus 로고
    • Toward an efficient DNAzyme
    • [CrossRef] [PubMed]
    • Li, Y.F.; Sen, D. Toward an efficient DNAzyme. Biochemistry 1997, 36, 5589-5599. [CrossRef] [PubMed]
    • (1997) Biochemistry , vol.36 , pp. 5589-5599
    • Li, Y.F.1    Sen, D.2
  • 183
    • 0032169981 scopus 로고    scopus 로고
    • DNA-enhanced peroxidase activity of a DNA aptamer-hemin complex
    • [CrossRef]
    • Travascio, P.; Li, Y.F.; Sen, D. DNA-enhanced peroxidase activity of a DNA aptamer-hemin complex. Chem. Biol. 1998, 5, 505-517. [CrossRef]
    • (1998) Chem. Biol. , vol.5 , pp. 505-517
    • Travascio, P.1    Li, Y.F.2    Sen, D.3
  • 184
    • 1842528248 scopus 로고    scopus 로고
    • Amplified chemiluminescence surface detection of DNA and telomerase activity using catalytic nucleic acid labels
    • [CrossRef] [PubMed]
    • Pavlov, V.; Xiao, Y.; Gill, R.; Dishon, A.; Kotler, M.; Willner, I. Amplified chemiluminescence surface detection of DNA and telomerase activity using catalytic nucleic acid labels. Anal. Chem. 2004, 76, 2152-2156. [CrossRef] [PubMed]
    • (2004) Anal. Chem. , vol.76 , pp. 2152-2156
    • Pavlov, V.1    Xiao, Y.2    Gill, R.3    Dishon, A.4    Kotler, M.5    Willner, I.6
  • 185
    • 82455205729 scopus 로고    scopus 로고
    • A hemin/G-quadruplex acts as an NADH oxidase and NADH peroxidase mimicking DNAzyme
    • [CrossRef]
    • Golub, E.; Freeman, R.; Willner, I. A Hemin/G-Quadruplex Acts as an NADH Oxidase and NADH Peroxidase Mimicking DNAzyme. Angew. Chem. Int. Ed. 2011, 50, 11710-11714. [CrossRef]
    • (2011) Angew. Chem. Int. Ed. , vol.50 , pp. 11710-11714
    • Golub, E.1    Freeman, R.2    Willner, I.3
  • 186
    • 78449237314 scopus 로고    scopus 로고
    • DNAzyme-like activity of hemin-telomeric G-quadruplexes for the optical analysis of telomerase and its inhibitors
    • [CrossRef] [PubMed]
    • Freeman, R.; Sharon, E.; Teller, C.; Henning, A.; Tzfati, Y.; Willner, I. DNAzyme-Like Activity of Hemin-Telomeric G-Quadruplexes for the Optical Analysis of Telomerase and its Inhibitors. ChemBioChem 2010, 11, 2362-2367. [CrossRef] [PubMed]
    • (2010) ChemBioChem , vol.11 , pp. 2362-2367
    • Freeman, R.1    Sharon, E.2    Teller, C.3    Henning, A.4    Tzfati, Y.5    Willner, I.6
  • 187
    • 80055005674 scopus 로고    scopus 로고
    • Peroxidase-mimicking DNAzymes for biosensing applications: A review
    • [CrossRef] [PubMed]
    • Kosman, J.; Juskowiak, B. Peroxidase-mimicking DNAzymes for biosensing applications: A review. Anal. Chim. Acta 2011, 707, 7-17. [CrossRef] [PubMed]
    • (2011) Anal. Chim. Acta , vol.707 , pp. 7-17
    • Kosman, J.1    Juskowiak, B.2
  • 188
    • 84866948623 scopus 로고    scopus 로고
    • Insights into how nucleotide supplements enhance the peroxidase-mimicking DNAzyme activity of the G-quadruplex/hemin system
    • [CrossRef] [PubMed]
    • Stefan, L.; Denat, F.; Monchaud, D. Insights into how nucleotide supplements enhance the peroxidase-mimicking DNAzyme activity of the G-quadruplex/hemin system. Nucleic Acids Res. 2012, 40, 8759-8772. [CrossRef] [PubMed]
    • (2012) Nucleic Acids Res. , vol.40 , pp. 8759-8772
    • Stefan, L.1    Denat, F.2    Monchaud, D.3
  • 189
    • 84896383329 scopus 로고    scopus 로고
    • From cascaded catalytic nucleic acids to enzyme-DNA nanostructures: Controlling reactivity, sensing, logic operations, and assembly of complex structures
    • [CrossRef] [PubMed]
    • Wang, F.; Lu, C.H.; Willner, I. From Cascaded Catalytic Nucleic Acids to Enzyme-DNA Nanostructures: Controlling Reactivity, Sensing, Logic Operations, and Assembly of Complex Structures. Chem. Rev. 2014, 114, 2881-2941. [CrossRef] [PubMed]
    • (2014) Chem. Rev. , vol.114 , pp. 2881-2941
    • Wang, F.1    Lu, C.H.2    Willner, I.3
  • 190
    • 84927940377 scopus 로고    scopus 로고
    • DNA polymerase-catalyzed incorporation of nucleotides modified with a G-quadruplex-derived DNAzyme
    • [CrossRef] [PubMed]
    • Verga, D.; Welter, M.; Steck, A.L.; Marx, A. DNA polymerase-catalyzed incorporation of nucleotides modified with a G-quadruplex-derived DNAzyme. Chem. Commun. 2015, 51, 7379-7381. [CrossRef] [PubMed]
    • (2015) Chem. Commun. , vol.51 , pp. 7379-7381
    • Verga, D.1    Welter, M.2    Steck, A.L.3    Marx, A.4
  • 191
    • 79955600302 scopus 로고    scopus 로고
    • DNA-based peroxidation catalyst-what is the exact role of topology on catalysis and is there a special binding site for catalysis?
    • [CrossRef] [PubMed]
    • Nakayama, S.; Wang, J.X.; Sintim, H.O. DNA-Based Peroxidation Catalyst-What Is the Exact Role of Topology on Catalysis and Is There a Special Binding Site for Catalysis? Chem. Eur. J. 2011, 17, 5691-5698. [CrossRef] [PubMed]
    • (2011) Chem. Eur. J. , vol.17 , pp. 5691-5698
    • Nakayama, S.1    Wang, J.X.2    Sintim, H.O.3
  • 192
    • 83755178651 scopus 로고    scopus 로고
    • Characterization of G-quadruplex/Hemin peroxidase: Substrate specificity and inactivation kinetics
    • [CrossRef] [PubMed]
    • Yang, X.; Fang, C.; Mei, H.; Chang, T.; Cao, Z.; Shangguan, D. Characterization of G-Quadruplex/Hemin Peroxidase: Substrate Specificity and Inactivation Kinetics. Chem. Eur. J. 2011, 17, 14475-14484. [CrossRef] [PubMed]
    • (2011) Chem. Eur. J. , vol.17 , pp. 14475-14484
    • Yang, X.1    Fang, C.2    Mei, H.3    Chang, T.4    Cao, Z.5    Shangguan, D.6
  • 193
    • 66249097058 scopus 로고    scopus 로고
    • Functional nucleic acid sensors
    • [CrossRef] [PubMed]
    • Liu, J.; Cao, Z.; Lu, Y. Functional Nucleic Acid Sensors. Chem. Rev. 2009, 109, 1948-1998. [CrossRef] [PubMed]
    • (2009) Chem. Rev. , vol.109 , pp. 1948-1998
    • Liu, J.1    Cao, Z.2    Lu, Y.3
  • 194
    • 84876716571 scopus 로고    scopus 로고
    • An RNA catalyst that reacts with a mechanistic inhibitor of serine protease
    • [CrossRef]
    • Ameta, S.; Jäschke, A. An RNA catalyst that reacts with a mechanistic inhibitor of serine protease. Chem. Sci. 2013, 4, 957-964. [CrossRef]
    • (2013) Chem. Sci. , vol.4 , pp. 957-964
    • Ameta, S.1    Jäschke, A.2
  • 195
    • 77950819888 scopus 로고    scopus 로고
    • Expanding the catalytic repertoire of ribozymes and deoxyribozymes beyond RNA substrates
    • [PubMed]
    • Franzen, S. Expanding the catalytic repertoire of ribozymes and deoxyribozymes beyond RNA substrates. Curr. Opin. Mol. Ther. 2010, 12, 223-232. [PubMed]
    • (2010) Curr. Opin. Mol. Ther. , vol.12 , pp. 223-232
    • Franzen, S.1
  • 196
    • 77956107133 scopus 로고    scopus 로고
    • Molecular evolution of functional nucleic acids with chemical modifications
    • [CrossRef] [PubMed]
    • Kuwahara, M.; Sugimoto, N. Molecular Evolution of Functional Nucleic Acids with Chemical Modifications. Molecules 2010, 15, 5423-5444. [CrossRef] [PubMed]
    • (2010) Molecules , vol.15 , pp. 5423-5444
    • Kuwahara, M.1    Sugimoto, N.2
  • 197
    • 84870226002 scopus 로고    scopus 로고
    • Nucleoside triphosphates-building blocks for the modification of nucleic acids
    • [CrossRef] [PubMed]
    • Hollenstein, M. Nucleoside Triphosphates-Building Blocks for the Modification of Nucleic Acids. Molecules 2012, 17, 13569-13591. [CrossRef] [PubMed]
    • (2012) Molecules , vol.17 , pp. 13569-13591
    • Hollenstein, M.1
  • 198
    • 84910002245 scopus 로고    scopus 로고
    • Synthesis of base-modified 2′-deoxyribonucleoside triphosphates and their use in enzymatic synthesis of modified DNA for applications in bioanalysis and chemical biology
    • [CrossRef] [PubMed]
    • Hocek, M. Synthesis of Base-Modified 2′-Deoxyribonucleoside Triphosphates and Their Use in Enzymatic Synthesis of Modified DNA for Applications in Bioanalysis and Chemical Biology. J. Org. Chem. 2014, 79, 9914-9921. [CrossRef] [PubMed]
    • (2014) J. Org. Chem. , vol.79 , pp. 9914-9921
    • Hocek, M.1
  • 199
    • 0034701302 scopus 로고    scopus 로고
    • RNA cleavage by a DNA enzyme with extended chemical functionality
    • [CrossRef] [PubMed]
    • Santoro, S.W.; Joyce, G.F.; Sakthivel, K.; Gramatikova, S.; Barbas, C.F. RNA cleavage by a DNA enzyme with extended chemical functionality. J. Am. Chem. Soc. 2000, 122, 2433-2439. [CrossRef] [PubMed]
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 2433-2439
    • Santoro, S.W.1    Joyce, G.F.2    Sakthivel, K.3    Gramatikova, S.4    Barbas, C.F.5
  • 200
    • 0035961485 scopus 로고    scopus 로고
    • Bridging the gap between proteins and nucleic acids: A metal-independent RNAseA mimic with two protein-like functionalities
    • [CrossRef] [PubMed]
    • Perrin, D.M.; Garestier, T.; Hélène, C. Bridging the gap between proteins and nucleic acids: A metal-independent RNAseA mimic with two protein-like functionalities. J. Am. Chem. Soc. 2001, 123, 1556-1563. [CrossRef] [PubMed]
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1556-1563
    • Perrin, D.M.1    Garestier, T.2    Hélène, C.3
  • 201
    • 1842618467 scopus 로고    scopus 로고
    • Sequence-specific cleavage of RNA in the absence of divalent metal ions by a DNAzyme incorporating imidazolyl and amino functionalities
    • [CrossRef] [PubMed]
    • Sidorov, A.V.; Grasby, J.A.; Williams, D.M. Sequence-specific cleavage of RNA in the absence of divalent metal ions by a DNAzyme incorporating imidazolyl and amino functionalities. Nucleic Acids Res. 2004, 32, 1591-1601. [CrossRef] [PubMed]
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1591-1601
    • Sidorov, A.V.1    Grasby, J.A.2    Williams, D.M.3
  • 203
    • 79952757472 scopus 로고    scopus 로고
    • Protein-inspired modified DNAzymes: Dramatic effects of shortening side-chain length of 8-imidazolyl modified deoxyadenosines in selecting RNaseA mimicking DNAzymes
    • [CrossRef] [PubMed]
    • Hipolito, C.J.; Hollenstein, M.; Lam, C.H.; Perrin, D.M. Protein-inspired modified DNAzymes: Dramatic effects of shortening side-chain length of 8-imidazolyl modified deoxyadenosines in selecting RNaseA mimicking DNAzymes. Org. Biomol. Chem. 2011, 9, 2266-2273. [CrossRef] [PubMed]
    • (2011) Org. Biomol. Chem. , vol.9 , pp. 2266-2273
    • Hipolito, C.J.1    Hollenstein, M.2    Lam, C.H.3    Perrin, D.M.4
  • 204
    • 84875987824 scopus 로고    scopus 로고
    • Toward the combinatorial selection of chemically modified DNAzyme RNase A mimics active against all-RNA substrates
    • [CrossRef] [PubMed]
    • Hollenstein, M.; Hipolito, C.J.; Lam, C.H.; Perrin, D.M. Toward the Combinatorial Selection of Chemically Modified DNAzyme RNase A Mimics Active Against all-RNA Substrates. ACS Comb. Sci. 2013, 15, 174-182. [CrossRef] [PubMed]
    • (2013) ACS Comb. Sci. , vol.15 , pp. 174-182
    • Hollenstein, M.1    Hipolito, C.J.2    Lam, C.H.3    Perrin, D.M.4
  • 205
    • 0037189886 scopus 로고    scopus 로고
    • Toward an RNaseA mimic: A DNAzyme with imidazoles and cationic amines
    • [CrossRef] [PubMed]
    • Lermer, L.; Roupioz, Y.; Ting, R.; Perrin, D.M. Toward an RNaseA mimic: A DNAzyme with imidazoles and cationic amines. J. Am. Chem. Soc. 2002, 124, 9960-9961. [CrossRef] [PubMed]
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9960-9961
    • Lermer, L.1    Roupioz, Y.2    Ting, R.3    Perrin, D.M.4
  • 206
    • 13544253729 scopus 로고    scopus 로고
    • Substrate specificity and kinetic framework of a DNAzyme with an expanded chemical repertoire: A putative RNaseA mimic that catalyzes RNA hydrolysis independent of a divalent metal cation
    • [CrossRef] [PubMed]
    • Ting, R.; Thomas, J.M.; Lermer, L.; Perrin, D.M. Substrate specificity and kinetic framework of a DNAzyme with an expanded chemical repertoire: A putative RNaseA mimic that catalyzes RNA hydrolysis independent of a divalent metal cation. Nucleic Acids Res. 2004, 32, 6660-6672. [CrossRef] [PubMed]
    • (2004) Nucleic Acids Res. , vol.32 , pp. 6660-6672
    • Ting, R.1    Thomas, J.M.2    Lermer, L.3    Perrin, D.M.4
  • 209
    • 84942520548 scopus 로고    scopus 로고
    • Directed evolution of artificial enzymes (XNAzymes) from diverse repertoires of synthetic genetic polymers
    • [CrossRef] [PubMed]
    • Taylor, A.I.; Holliger, P. Directed evolution of artificial enzymes (XNAzymes) from diverse repertoires of synthetic genetic polymers. Nat. Protoc. 2015, 10, 1625-1642. [CrossRef] [PubMed]
    • (2015) Nat. Protoc. , vol.10 , pp. 1625-1642
    • Taylor, A.I.1    Holliger, P.2
  • 211
    • 0032476840 scopus 로고    scopus 로고
    • Expanding the potential of DNA for binding and catalysis: Highly functionalized dUTP derivatives that are substrates for thermostable DNA polymerases
    • [CrossRef]
    • Sakthivel, K.; Barbas, C.F. Expanding the Potential of DNA for Binding and Catalysis: Highly Functionalized dUTP Derivatives That Are Substrates for Thermostable DNA Polymerases. Angew. Chem. Int. Ed. 1998, 37, 2872-2875. [CrossRef]
    • (1998) Angew. Chem. Int. Ed. , vol.37 , pp. 2872-2875
    • Sakthivel, K.1    Barbas, C.F.2
  • 212
    • 27544486140 scopus 로고    scopus 로고
    • A versatile toolbox for variable DNA functionalization at high density
    • [CrossRef] [PubMed]
    • Jäger, S.; Rasched, G.; Kornreich-Leshem, H.; Engeser, M.; Thum, O.; Famulok, M. A versatile toolbox for variable DNA functionalization at high density. J. Am. Chem. Soc. 2005, 127, 15071-15082. [CrossRef] [PubMed]
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 15071-15082
    • Jäger, S.1    Rasched, G.2    Kornreich-Leshem, H.3    Engeser, M.4    Thum, O.5    Famulok, M.6
  • 214
    • 84867210412 scopus 로고    scopus 로고
    • Synthesis of deoxynucleoside triphosphates that include proline, urea, or sulfamide groups and their polymerase incorporation into DNA
    • [CrossRef] [PubMed]
    • Hollenstein, M. Synthesis of deoxynucleoside triphosphates that include proline, urea, or sulfamide groups and their polymerase incorporation into DNA. Chem. Eur. J. 2012, 18, 13320-13330. [CrossRef] [PubMed]
    • (2012) Chem. Eur. J. , vol.18 , pp. 13320-13330
    • Hollenstein, M.1
  • 215
    • 84894096983 scopus 로고    scopus 로고
    • Recent advances in the syntheses of nucleoside triphosphates
    • [CrossRef]
    • Kore, A.R.; Srinivasan, B. Recent Advances in the Syntheses of Nucleoside Triphosphates. Curr. Org. Synth. 2013, 10, 903-934. [CrossRef]
    • (2013) Curr. Org. Synth. , vol.10 , pp. 903-934
    • Kore, A.R.1    Srinivasan, B.2
  • 216
    • 84941242120 scopus 로고    scopus 로고
    • Synthesis and enzymatic incorporation of modified deoxyuridine triphosphates
    • [CrossRef] [PubMed]
    • Liu, E.; Lam, C.H.; Perrin, D.M. Synthesis and Enzymatic Incorporation of Modified Deoxyuridine Triphosphates. Molecules 2015, 20, 13591-13602. [CrossRef] [PubMed]
    • (2015) Molecules , vol.20 , pp. 13591-13602
    • Liu, E.1    Lam, C.H.2    Perrin, D.M.3
  • 217
    • 84909580167 scopus 로고    scopus 로고
    • The expanding view of RNA and DNA function
    • [CrossRef] [PubMed]
    • Breaker, R.R.; Joyce, G.F. The Expanding View of RNA and DNA Function. Chem. Biol. 2014, 21, 1059-1065. [CrossRef] [PubMed]
    • (2014) Chem. Biol. , vol.21 , pp. 1059-1065
    • Breaker, R.R.1    Joyce, G.F.2
  • 218
    • 84923103998 scopus 로고    scopus 로고
    • Analyzing free zinc(II) ion concentrations in cell biology with fluorescent chelating molecules
    • [CrossRef] [PubMed]
    • Maret, W. Analyzing free zinc(II) ion concentrations in cell biology with fluorescent chelating molecules. Metallomics 2015, 7, 202-211. [CrossRef] [PubMed]
    • (2015) Metallomics , vol.7 , pp. 202-211
    • Maret, W.1
  • 220
    • 84919808110 scopus 로고    scopus 로고
    • A method for selecting modified DNAzymes without the use of modified DNA as a template in PCR
    • [CrossRef] [PubMed]
    • Renders, M.; Miller, E.; Hollenstein, M.; Perrin, D.M. A Method for Selecting Modified DNAzymes without the Use of Modified DNA as a Template in PCR. Chem. Commun. 2015, 51, 1360-1362. [CrossRef] [PubMed]
    • (2015) Chem. Commun. , vol.51 , pp. 1360-1362
    • Renders, M.1    Miller, E.2    Hollenstein, M.3    Perrin, D.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.