메뉴 건너뛰기




Volumn 7, Issue 12, 2013, Pages 10863-10869

Thermodynamic basis for engineering high-affinity, high-specificity binding-induced DNA Clamp Nanoswitches

Author keywords

biomolecular switch; clamp mechanism; DNA nanomachines; ligand induced fit; molecular beacons; specificity; triplex

Indexed keywords

BIO-MOLECULAR; LIGAND-INDUCED FIT; MOLECULAR BEACON; NANOMACHINES; SPECIFICITY; TRIPLEX;

EID: 84891365461     PISSN: 19360851     EISSN: 1936086X     Source Type: Journal    
DOI: 10.1021/nn404305e     Document Type: Article
Times cited : (58)

References (62)
  • 1
    • 0029670262 scopus 로고    scopus 로고
    • Molecular Beacons: Probes That Fluoresce Upon Hybridization
    • Tyagi, S.; Kramer, F. R. Molecular Beacons: Probes That Fluoresce Upon Hybridization Nat. Biotechnol. 1996, 14, 303-308
    • (1996) Nat. Biotechnol. , vol.14 , pp. 303-308
    • Tyagi, S.1    Kramer, F.R.2
  • 3
    • 0042736856 scopus 로고    scopus 로고
    • Allosteric Switching by Mutually Exclusive Folding of Protein Domains
    • Radley, T. L.; Markowska, A. I.; Bettinger, B. T.; Ha, J. H.; Loh, S. N. Allosteric Switching by Mutually Exclusive Folding of Protein Domains J. Mol. Biol. 2003, 332, 529-536
    • (2003) J. Mol. Biol. , vol.332 , pp. 529-536
    • Radley, T.L.1    Markowska, A.I.2    Bettinger, B.T.3    Ha, J.H.4    Loh, S.N.5
  • 4
    • 58149164666 scopus 로고    scopus 로고
    • 2+-Sensing Molecular Switch Based on Alternate Frame Protein Folding
    • 2+-Sensing Molecular Switch Based on Alternate Frame Protein Folding ACS Chem. Biol. 2008, 3, 723-732
    • (2008) ACS Chem. Biol. , vol.3 , pp. 723-732
    • Stratton, M.M.1    Mitrea, D.M.2    Loh, S.N.3
  • 5
    • 78650796409 scopus 로고    scopus 로고
    • Converting a Protein into a Switch for Biosensing and Functional Regulation
    • Stratton, M. M.; Loh, S. N. Converting a Protein Into a Switch for Biosensing and Functional Regulation Protein Sc. 2011, 20, 19-29
    • (2011) Protein Sc. , vol.20 , pp. 19-29
    • Stratton, M.M.1    Loh, S.N.2
  • 7
  • 8
    • 70349770900 scopus 로고    scopus 로고
    • Generation of New Protein Functions by Nonhomologous Combinations and Rearrangements of Domains and Modules
    • Koide, S. Generation Of New Protein Functions by Nonhomologous Combinations and Rearrangements of Domains and Modules Curr. Opin. Biotech. 2009, 20, 398-404
    • (2009) Curr. Opin. Biotech. , vol.20 , pp. 398-404
    • Koide, S.1
  • 9
    • 33645798851 scopus 로고    scopus 로고
    • The Fluorescent Toolbox for Assessing Protein Location and Function
    • Giepmans, B. N.; Adams, S. R.; Ellisman, M. H.; Tsien, R. Y. The Fluorescent Toolbox for Assessing Protein Location and Function Science 2006, 312, 217-224
    • (2006) Science , vol.312 , pp. 217-224
    • Giepmans, B.N.1    Adams, S.R.2    Ellisman, M.H.3    Tsien, R.Y.4
  • 11
    • 34247465989 scopus 로고    scopus 로고
    • Engineering Modular Protein Interaction Switches by Sequence Overlap
    • Sallee, N. A.; Yeh, B. J.; Lim, W. A. Engineering Modular Protein Interaction Switches by Sequence Overlap J. Am. Chem. Soc. 2007, 129, 4606-4611
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 4606-4611
    • Sallee, N.A.1    Yeh, B.J.2    Lim, W.A.3
  • 12
    • 0032824805 scopus 로고    scopus 로고
    • Folding Funnels and Binding Mechanisms
    • Ma, B.; Kumar, S.; Tsai, C.; Nussinov, R. Folding Funnels and Binding Mechanisms Protein Eng. 1999, 12 (9) 713-720
    • (1999) Protein Eng. , vol.12 , Issue.9 , pp. 713-720
    • Ma, B.1    Kumar, S.2    Tsai, C.3    Nussinov, R.4
  • 13
    • 0033621104 scopus 로고    scopus 로고
    • Folding and Binding Cascades: Shifts in Energy Landscapes
    • Tsai, C. J.; Ma, B.; Nussinov, R. Folding and Binding Cascades: Shifts in Energy Landscapes Proc. Natl. Acad. Sci. U.S.A. 1999, 96, 9970-9972
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 9970-9972
    • Tsai, C.J.1    Ma, B.2    Nussinov, R.3
  • 14
    • 0033970020 scopus 로고    scopus 로고
    • Folding and Binding Cascades: Dynamic Landscapes and Population Shifts
    • Kumar, S.; Ma, B.; Tsai, C.; Sinha, N.; Nussinov, R. Folding and Binding Cascades: Dynamic Landscapes and Population Shifts Protein Sc. 2000, 9, 10-19
    • (2000) Protein Sc. , vol.9 , pp. 10-19
    • Kumar, S.1    Ma, B.2    Tsai, C.3    Sinha, N.4    Nussinov, R.5
  • 15
    • 0036147568 scopus 로고    scopus 로고
    • Multiple Diverse Ligands Binding at a Single Protein Site: A Matter of Pre-Existing Populations
    • Ma, B.; Shatsky, M.; Wolfson, H. J.; Nussinov, R. Multiple Diverse Ligands Binding at a Single Protein Site: a Matter of Pre-Existing Populations Protein Sc. 2002, 11, 184-197
    • (2002) Protein Sc. , vol.11 , pp. 184-197
    • Ma, B.1    Shatsky, M.2    Wolfson, H.J.3    Nussinov, R.4
  • 16
    • 78650419952 scopus 로고    scopus 로고
    • Switch Based Biosensors: A New Approach Towards Real-Time, in Vivo Molecular Detection
    • Plaxco, K. W.; Soh, H. T. Switch Based Biosensors: a New Approach Towards Real-Time, in Vivo Molecular Detection Trends Biotechnol. 2011, 29, 1-5
    • (2011) Trends Biotechnol. , vol.29 , pp. 1-5
    • Plaxco, K.W.1    Soh, H.T.2
  • 17
    • 0002724139 scopus 로고
    • The Role of Induced Fit and Conformational Changes of Enzymes in Specificity and Catalysis
    • Herschlag, D. The Role of Induced Fit and Conformational Changes of Enzymes in Specificity and Catalysis Bioorg. Chem. 1988, 16, 62-96
    • (1988) Bioorg. Chem. , vol.16 , pp. 62-96
    • Herschlag, D.1
  • 19
    • 55549109430 scopus 로고    scopus 로고
    • Role of Induced Fit in Enzyme Specificity: A Molecular Forward/Reverse Switch
    • Johnson, K. A. Role of Induced Fit in Enzyme Specificity: A Molecular Forward/Reverse Switch J. Biol. Chem. 2008, 283, 26297-26301
    • (2008) J. Biol. Chem. , vol.283 , pp. 26297-26301
    • Johnson, K.A.1
  • 20
    • 44349104094 scopus 로고    scopus 로고
    • Design of Protein Function Leaps by Directed Domain Interface Evolution
    • Huang, J.; Koide, A.; Makabe, K.; Koide, S. Design of Protein Function Leaps by Directed Domain Interface Evolution Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 6578-6583
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 6578-6583
    • Huang, J.1    Koide, A.2    Makabe, K.3    Koide, S.4
  • 21
    • 70149092506 scopus 로고    scopus 로고
    • Structural Basis for Exquisite Specificity of Affinity Clamps, Synthetic Binding Proteins Generated Through Directed Domain-Interface Evolution
    • Huang, J.; Makabe, K.; Biancalana, M.; Koide, A.; Koide, S. Structural Basis for Exquisite Specificity of Affinity Clamps, Synthetic Binding Proteins Generated Through Directed Domain-Interface Evolution J. Mol. Biol. 2009, 392, 1221-1231
    • (2009) J. Mol. Biol. , vol.392 , pp. 1221-1231
    • Huang, J.1    Makabe, K.2    Biancalana, M.3    Koide, A.4    Koide, S.5
  • 22
    • 69549120468 scopus 로고    scopus 로고
    • Thermodynamic Basis for the Optimization of Binding-Induced Biomolecular Switches and Structure-Switching Biosensors
    • Vallée-Bélisle, A.; Ricci, F.; Plaxco, K. W. Thermodynamic Basis for the Optimization of Binding-Induced Biomolecular Switches and Structure-Switching Biosensors Proc. Natl. Acad. Sci. U.S.A. 2009, 106, 13802-13807
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 13802-13807
    • Vallée-Bélisle, A.1    Ricci, F.2    Plaxco, K.W.3
  • 23
    • 80055106927 scopus 로고    scopus 로고
    • High-Precision, in Vitro Validation of the Sequestration Mechanism for Generating Ultrasensitive Dose-Response Curves in Regulatory Networks
    • Ricci, F.; Vallée-Bélisle, A.; Plaxco, K. W. High-Precision, in Vitro Validation of the Sequestration Mechanism for Generating Ultrasensitive Dose-Response Curves in Regulatory Networks PLoS Comp. Biol. 2011, 7, e1002171
    • (2011) PLoS Comp. Biol. , vol.7 , pp. 1002171
    • Ricci, F.1    Vallée-Bélisle, A.2    Plaxco, K.W.3
  • 24
    • 84866521002 scopus 로고    scopus 로고
    • Rational Design of Allosteric Inhibitors and Activators Using the Population-Shift Model: In Vitro Validation and Application to an Artificial Biosensor
    • Ricci, F.; Vallée-Bélisle, A.; Porchetta, A.; Plaxco, K. W. Rational Design of Allosteric Inhibitors and Activators Using the Population-Shift Model: in Vitro Validation and Application to an Artificial Biosensor J. Am. Chem. Soc. 2012, 134, 15177-15180
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 15177-15180
    • Ricci, F.1    Vallée-Bélisle, A.2    Porchetta, A.3    Plaxco, K.W.4
  • 25
    • 84856834769 scopus 로고    scopus 로고
    • Engineering Biosensors with Extended, Narrowed, or Arbitrarily Edited Dynamic Range
    • Vallée-Bélisle, A.; Ricci, F.; Plaxco, K. W. Engineering Biosensors With Extended, Narrowed, or Arbitrarily Edited Dynamic Range J. Am. Chem. Soc. 2012, 134, 2876-2879
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 2876-2879
    • Vallée-Bélisle, A.1    Ricci, F.2    Plaxco, K.W.3
  • 26
    • 84871546095 scopus 로고    scopus 로고
    • Using Distal-Site Mutations and Allosteric Inhibition to Tune, Extend, and Narrow the Useful Dynamic Range of Aptamer-Based Sensors
    • Porchetta, A.; Vallée-Bélisle, A.; Plaxco, K. W.; Ricci, F. Using Distal-Site Mutations and Allosteric Inhibition to Tune, Extend, and Narrow the Useful Dynamic Range of Aptamer-Based Sensors J. Am. Chem. Soc. 2012, 134, 20601-20604
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 20601-20604
    • Porchetta, A.1    Vallée-Bélisle, A.2    Plaxco, K.W.3    Ricci, F.4
  • 27
    • 0028091661 scopus 로고
    • Single-Strand-Targeted Triplex Formation: Stability, Specificity and Rnase H Activation Properties
    • Kandimalla, E. R.; Agrawal, S. Single-Strand-Targeted Triplex Formation: Stability, Specificity and Rnase H Activation Properties Gene 1994, 149, 115-121
    • (1994) Gene , vol.149 , pp. 115-121
    • Kandimalla, E.R.1    Agrawal, S.2
  • 28
    • 0029658622 scopus 로고    scopus 로고
    • Single Strand Targeted Triplex Formation: Physicochemical and Biochemical Properties of Foldback Triplexes
    • Kandimalla, E. R.; Manning, A.; Agrawal, S. Single Strand Targeted Triplex Formation: Physicochemical and Biochemical Properties of Foldback Triplexes J. Biomol. Str. Dyn. 1996, 14, 79-90
    • (1996) J. Biomol. Str. Dyn. , vol.14 , pp. 79-90
    • Kandimalla, E.R.1    Manning, A.2    Agrawal, S.3
  • 29
    • 0001120760 scopus 로고    scopus 로고
    • Preorganization of DNA: Design Principles for Improving Nucleic Acid Recognition by Synthetic Oligonucleotides
    • Kool, E. T. Preorganization of DNA: Design Principles for Improving Nucleic Acid Recognition by Synthetic Oligonucleotides Chem. Rev. 1997, 97, 1473-1487
    • (1997) Chem. Rev. , vol.97 , pp. 1473-1487
    • Kool, E.T.1
  • 30
    • 0025369611 scopus 로고
    • Spectroscopic and Calorimetric Investigation on the DNA Triplex Formed by D(CTCTTCTTTCTTTTCTTTCTTCTC) and D(GAGAAGAAAGA) at Acidic pH
    • Xodo, L. E.; Manzini, G.; Quadrifoglio, F. Spectroscopic and Calorimetric Investigation on the DNA Triplex Formed by D(CTCTTCTTTCTTTTCTTTCTTCTC) and D(GAGAAGAAAGA) at Acidic pH Nucleic Acids Res. 1990, 18, 3557-3564
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3557-3564
    • Xodo, L.E.1    Manzini, G.2    Quadrifoglio, F.3
  • 32
    • 0000378838 scopus 로고
    • The Structure of Crystals Containing a Hydrogen Bonded Complex of 1-Methylthymine and 9-Methyladenine
    • Hoogsteen, K. The Structure of Crystals Containing a Hydrogen Bonded Complex of 1-Methylthymine and 9-Methyladenine Acta Crystallogr. 1959, 12, 822-823
    • (1959) Acta Crystallogr. , vol.12 , pp. 822-823
    • Hoogsteen, K.1
  • 33
    • 0000403995 scopus 로고
    • The Crystal and Molecular Structure of a Hydrogen-Bonded Complex between 1-Methylthymine and 9-Methyladenine
    • Hoogsteen, K. The Crystal and Molecular Structure of a Hydrogen-Bonded Complex Between 1-Methylthymine and 9-Methyladenine Acta Crystallogr. 1963, 16, 907-916
    • (1963) Acta Crystallogr. , vol.16 , pp. 907-916
    • Hoogsteen, K.1
  • 34
    • 0027425105 scopus 로고
    • Oligonucleotide Clamps Arrest DNA Synthesis on a Single-Stranded DNA Target
    • Giovannangeli, C.; Thuong, N. T.; Helene, C. Oligonucleotide Clamps Arrest DNA Synthesis on a Single-Stranded DNA Target Proc. Natl. Acad. Sci. U.S.A. 1993, 90, 10013-10017
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 10013-10017
    • Giovannangeli, C.1    Thuong, N.T.2    Helene, C.3
  • 35
    • 33846292246 scopus 로고    scopus 로고
    • A Molecular Probe for the Detection of Homopurine Sequences
    • Trkulja, I.; Biner, S. M.; Langenegger, S. M.; Häner, R. A Molecular Probe for the Detection of Homopurine Sequences ChemBioChem 2007, 8, 25-27
    • (2007) ChemBioChem , vol.8 , pp. 25-27
    • Trkulja, I.1    Biner, S.M.2    Langenegger, S.M.3    Häner, R.4
  • 36
    • 84866392385 scopus 로고    scopus 로고
    • Improved DNA Clamps by Stacking to Adjacent Nucleobases
    • Fatthalla, M. I.; Pedersen, E. B. Improved DNA Clamps by Stacking to Adjacent Nucleobases Helv. Chim. Acta 2012, 95, 1538-1547
    • (2012) Helv. Chim. Acta , vol.95 , pp. 1538-1547
    • Fatthalla, M.I.1    Pedersen, E.B.2
  • 38
    • 0032539693 scopus 로고    scopus 로고
    • A Unified View of Polymer, Dumbbell, and Oligonucleotide DNA Nearest-Neighbor Thermodynamics
    • Santalucia, J., Jr. A Unified View of Polymer, Dumbbell, and Oligonucleotide DNA Nearest-Neighbor Thermodynamics Proc. Natl. Acad. Sci. U.S.A. 1998, 95, 1460-1465
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 1460-1465
    • Santalucia Jr., J.1
  • 40
  • 41
    • 0028089696 scopus 로고
    • Electrostatic Effect in DNA Triple Helices
    • Volker, J.; Klump, H. H. Electrostatic Effect in DNA Triple Helices Biochemistry 1994, 33, 13502-13508
    • (1994) Biochemistry , vol.33 , pp. 13502-13508
    • Volker, J.1    Klump, H.H.2
  • 42
    • 11944253600 scopus 로고
    • Energetics of Formation of Sixteen Triple Helical Complexes Which Vary at a Single Position Within a Pyrimidine Motif
    • Best, G. C.; Dervan, P. B. Energetics of Formation of Sixteen Triple Helical Complexes Which Vary at a Single Position Within a Pyrimidine Motif J. Am. Chem. Soc. 1195, 117, 1187-1193
    • (1195) J. Am. Chem. Soc. , vol.117 , pp. 1187-1193
    • Best, G.C.1    Dervan, P.B.2
  • 43
    • 28544438039 scopus 로고    scopus 로고
    • Real-Time Assays with Molecular Beacons and Other Fluorescent Nucleic Acid Hybridization Probes
    • Marras, S. A. E.; Tyagi, S.; Kramer, F. R. Real-Time Assays With Molecular Beacons and Other Fluorescent Nucleic Acid Hybridization Probes Clin. Chim. Acta 2006, 363, 48-60
    • (2006) Clin. Chim. Acta , vol.363 , pp. 48-60
    • Marras, S.A.E.1    Tyagi, S.2    Kramer, F.R.3
  • 44
    • 55149090099 scopus 로고    scopus 로고
    • E-DNA Sensors for Convenient, Label-Free Electrochemical Detection of Hybridization
    • Ricci, F.; Plaxco, K. W. E-DNA Sensors for Convenient, Label-Free Electrochemical Detection of Hybridization Microchim. Acta 2008, 163, 149-155
    • (2008) Microchim. Acta , vol.163 , pp. 149-155
    • Ricci, F.1    Plaxco, K.W.2
  • 45
    • 0031983834 scopus 로고    scopus 로고
    • Multicolor molecular beacons for allele discrimination
    • Tyagi, S.; Bratu, D. P.; Kramer, F. R. Multicolor molecular beacons for allele discrimination Nat. Biotechnol. 1998, 16, 49-53
    • (1998) Nat. Biotechnol. , vol.16 , pp. 49-53
    • Tyagi, S.1    Bratu, D.P.2    Kramer, F.R.3
  • 46
    • 84863116178 scopus 로고    scopus 로고
    • Optimizing the Specificity of Nucleic Acid Hybridization
    • Zhang, D. Y.; Chen, S. X.; Yin, P. Optimizing the Specificity of Nucleic Acid Hybridization Nature Chem. 2012, 4, 208-214
    • (2012) Nature Chem. , vol.4 , pp. 208-214
    • Zhang, D.Y.1    Chen, S.X.2    Yin, P.3
  • 47
    • 0022555885 scopus 로고
    • Determination and Analysis of Urea and Guanidine Hydrochloride Denaturation Curves
    • Pace, C. N. Determination and Analysis of Urea and Guanidine Hydrochloride Denaturation Curves Meth. Enzymol. 1986, 131, 266-280
    • (1986) Meth. Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 48
    • 0033592945 scopus 로고    scopus 로고
    • Applicability of Urea in the Thermodynamic Analysis of Secondary and Tertiary RNA Folding
    • Shelton, V. M.; Sosnick, T. R.; Pan, T. Applicability of Urea in the Thermodynamic Analysis of Secondary and Tertiary RNA Folding Biochemistry 1999, 38, 16831-16839
    • (1999) Biochemistry , vol.38 , pp. 16831-16839
    • Shelton, V.M.1    Sosnick, T.R.2    Pan, T.3
  • 49
    • 0023697408 scopus 로고
    • Unfolding Free Energy Changes Determined by the Linear Extrapolation Method. 1. Unfolding of Phenylmethanesulfonyl α-Chymotrypsin Using Different Denaturants
    • Santoro, M. M.; Bolen, D. W. Unfolding Free Energy Changes Determined by the Linear Extrapolation Method. 1. Unfolding of Phenylmethanesulfonyl α-Chymotrypsin Using Different Denaturants Biochemistry 1988, 27, 8063-8068
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 50
    • 0016345760 scopus 로고
    • Chemical and Biological Evolution of Nucleotide Binding Protein
    • Rossmann, M. G.; Moras, D.; Olsen, K. W. Chemical and Biological Evolution of Nucleotide Binding Protein Nature 1974, 250, 194-199
    • (1974) Nature , vol.250 , pp. 194-199
    • Rossmann, M.G.1    Moras, D.2    Olsen, K.W.3
  • 51
    • 0001126390 scopus 로고
    • Do Genes-In-Pieces Imply Proteins-In-Pieces?
    • Blake, C. C. F. Do Genes-In-Pieces Imply Proteins-In-Pieces? Nature 1978, 273, 267-268
    • (1978) Nature , vol.273 , pp. 267-268
    • Blake, C.C.F.1
  • 52
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of Cell Regulatory Systems Through Protein Interaction Domains
    • Pawson, T.; Nash, P. Assembly of Cell Regulatory Systems Through Protein Interaction Domains Science 2003, 300, 445-452
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 53
    • 1242320280 scopus 로고    scopus 로고
    • Triplex-Forming Oligonucleotide Target Sequences in the Human Genome
    • Goñi, J. R.; de la Cruz, X.; Orozco, M. Triplex-Forming Oligonucleotide Target Sequences in the Human Genome Nucleic Acids Res. 2004, 32, 354-360
    • (2004) Nucleic Acids Res. , vol.32 , pp. 354-360
    • Goñi, J.R.1    De La Cruz, X.2    Orozco, M.3
  • 55
    • 38849122813 scopus 로고    scopus 로고
    • Multidomain Targeting Generates a High-Affinity Thrombin-Inhibiting Bivalent Aptamer
    • Muller, J.; Wulffen, B.; Potzsch, B.; Mayer, G. Multidomain Targeting Generates a High-Affinity Thrombin-Inhibiting Bivalent Aptamer ChemBioChem. 2007, 8, 2223-2226
    • (2007) ChemBioChem. , vol.8 , pp. 2223-2226
    • Muller, J.1    Wulffen, B.2    Potzsch, B.3    Mayer, G.4
  • 59
    • 38349121586 scopus 로고    scopus 로고
    • Programming Biomolecular Self-Assembly Pathways
    • Yin, P.; Choi, H. M. T.; Calvert, C. R.; Pierce, N. A. Programming Biomolecular Self-Assembly Pathways Nature 2008, 451, 318-322
    • (2008) Nature , vol.451 , pp. 318-322
    • Yin, P.1    Choi, H.M.T.2    Calvert, C.R.3    Pierce, N.A.4
  • 62
    • 79952998426 scopus 로고    scopus 로고
    • Nucleic Acid Based Molecular Devices
    • Krishnan, Y.; Simmel, F. C. Nucleic Acid Based Molecular Devices Angew. Chem., Int. Ed. 2011, 50, 3124-3156
    • (2011) Angew. Chem., Int. Ed. , vol.50 , pp. 3124-3156
    • Krishnan, Y.1    Simmel, F.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.