메뉴 건너뛰기




Volumn 45, Issue 9, 1999, Pages 1628-1650

Aptamers: An emerging class of molecules that rival antibodies in diagnostics

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; APTAMER; OLIGONUCLEOTIDE; UNCLASSIFIED DRUG;

EID: 0032860385     PISSN: 00099147     EISSN: None     Source Type: Journal    
DOI: 10.1093/clinchem/45.9.1628     Document Type: Article
Times cited : (1867)

References (181)
  • 2
    • 0025194307 scopus 로고
    • Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase
    • Tuerk C, Gold L. Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase. Science 1990;249:505-10.
    • (1990) Science , vol.249 , pp. 505-510
    • Tuerk, C.1    Gold, L.2
  • 3
    • 0025074907 scopus 로고
    • In vitro selection of RNA molecules that bind specific ligands
    • Ellington AD, Szostak J. In vitro selection of RNA molecules that bind specific ligands. Nature 1990;346:818-22.
    • (1990) Nature , vol.346 , pp. 818-822
    • Ellington, A.D.1    Szostak, J.2
  • 4
    • 0031279943 scopus 로고    scopus 로고
    • In vivo imaging of inflammation using an aptamer inhibitor of human neutrophil elastase
    • Charlton J, Sennello J, Smith D. In vivo imaging of inflammation using an aptamer inhibitor of human neutrophil elastase. Chem Biol 1997;4:809-16.
    • (1997) Chem Biol , vol.4 , pp. 809-816
    • Charlton, J.1    Sennello, J.2    Smith, D.3
  • 5
    • 36949065559 scopus 로고
    • Assay of plasma insulin in human subjects by immunological methods
    • Yallow RS, Berson SA. Assay of plasma insulin in human subjects by immunological methods. Nature 1959;185:1648-9.
    • (1959) Nature , vol.185 , pp. 1648-1649
    • Yallow, R.S.1    Berson, S.A.2
  • 6
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Kohler G, Milstein C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 1975;256:496-7.
    • (1975) Nature , vol.256 , pp. 496-497
    • Kohler, G.1    Milstein, C.2
  • 7
    • 0023626927 scopus 로고
    • Removal of interference by immunoglobulins in an enzyme-amplified immunoassay for thyrotropin in serum
    • Clark PM, Price CP. Removal of interference by immunoglobulins in an enzyme-amplified immunoassay for thyrotropin in serum. Clin Chem 1987;33:414.
    • (1987) Clin Chem , vol.33 , pp. 414
    • Clark, P.M.1    Price, C.P.2
  • 8
    • 0009691384 scopus 로고
    • Monoclonal antibodies in diagnostic immunoassays
    • Ritter MA, Ladyman HM, eds. Cambridge, UK: Cambridge University Press
    • Cook DB, Self CH. Monoclonal antibodies in diagnostic immunoassays. In: Ritter MA, Ladyman HM, eds. Monoclonal antibodies. Cambridge, UK: Cambridge University Press, 1995:180-208.
    • (1995) Monoclonal Antibodies , pp. 180-208
    • Cook, D.B.1    Self, C.H.2
  • 9
    • 0021713342 scopus 로고
    • Production of functional chimeric mouse/human antibody
    • Boulianne GL, Hozumi N, Shulman MJ, Production of functional chimeric mouse/human antibody. Nature 1984;312:643-6.
    • (1984) Nature , vol.312 , pp. 643-646
    • Boulianne, G.L.1    Hozumi, N.2    Shulman, M.J.3
  • 11
    • 0025112794 scopus 로고
    • Searching for peptide ligands with an epitope library
    • Scott JK, Smith GP. Searching for peptide ligands with an epitope library. Science 1990;249:386-90.
    • (1990) Science , vol.249 , pp. 386-390
    • Scott, J.K.1    Smith, G.P.2
  • 13
    • 0031574037 scopus 로고    scopus 로고
    • Antibody-ribosome-mRNA (ARM) complexes as efficient selection particles for in vitro display and evolution of antibody combining sites
    • He M, Taussig MJ. Antibody-ribosome-mRNA (ARM) complexes as efficient selection particles for in vitro display and evolution of antibody combining sites. Nucleic Acids Res 1997;25:5132-4.
    • (1997) Nucleic Acids Res , vol.25 , pp. 5132-5134
    • He, M.1    Taussig, M.J.2
  • 14
    • 0032564346 scopus 로고    scopus 로고
    • Ribosome display efficiently selects and evolves high-affinity antibodies in vitro from immune libraries
    • Hanes J, Jermutus L, Weber-Bornhauser S, Bosshard HR, Pluckthun A. Ribosome display efficiently selects and evolves high-affinity antibodies in vitro from immune libraries. Proc Natl Acad Sci U S A 1998;95:14130-5.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 14130-14135
    • Hanes, J.1    Jermutus, L.2    Weber-Bornhauser, S.3    Bosshard, H.R.4    Pluckthun, A.5
  • 15
    • 0030817279 scopus 로고    scopus 로고
    • RNA-peptide fusions for the in vitro selection of peptides and proteins
    • Roberts RW, Szostak JW. RNA-peptide fusions for the in vitro selection of peptides and proteins. Proc Natl Acad Sci U S A 1997;94:12297-302.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 12297-12302
    • Roberts, R.W.1    Szostak, J.W.2
  • 16
    • 0033593238 scopus 로고    scopus 로고
    • Towards the design of an antibody that recognizes a given protein epitope
    • Kirkham PM, Neri D, Winter G. Towards the design of an antibody that recognizes a given protein epitope. J Mol Biol 1999;285:909-15.
    • (1999) J Mol Biol , vol.285 , pp. 909-915
    • Kirkham, P.M.1    Neri, D.2    Winter, G.3
  • 17
    • 0021712715 scopus 로고
    • Immunization in vitro and production of monoclonal antibodies specific to insoluble and weakly immunogenic proteins
    • Van Ness J. Laemmli UK, Pettijohn DE. Immunization in vitro and production of monoclonal antibodies specific to insoluble and weakly immunogenic proteins. Proc Natl Acad Sci U S A 1984; 81:7897-901.
    • (1984) Proc Natl Acad Sci U S A , vol.81 , pp. 7897-7901
    • Van Ness, J.1    Laemmli, U.K.2    Pettijohn, D.E.3
  • 18
    • 0025372284 scopus 로고
    • Autogenous translational operator recognized by bacteriophage T4 DNA polymerase
    • Tuerk C, Eddy S, Parma D, Gold L. Autogenous translational operator recognized by bacteriophage T4 DNA polymerase. J Mol Biol 1990;213:749-61.
    • (1990) J Mol Biol , vol.213 , pp. 749-761
    • Tuerk, C.1    Eddy, S.2    Parma, D.3    Gold, L.4
  • 19
    • 0029114788 scopus 로고
    • Potent 2′-amino-2′deoxypyrimidine RNA inhibitors of basic fibro-blast growth factor
    • Jellinek D, Green LS, Bell C, Lynott CK, Gill N, Vargeese C, et al. Potent 2′-amino-2′deoxypyrimidine RNA inhibitors of basic fibro-blast growth factor. Biochemistry 1995;34:11363-72.
    • (1995) Biochemistry , vol.34 , pp. 11363-11372
    • Jellinek, D.1    Green, L.S.2    Bell, C.3    Lynott, C.K.4    Gill, N.5    Vargeese, C.6
  • 20
    • 0031563773 scopus 로고    scopus 로고
    • Oligonucleotide inhibitors of human thrombin that bind distinct epitopes
    • Tasset DM, Kubik MF, Steiner W. Oligonucleotide inhibitors of human thrombin that bind distinct epitopes. J Mol Biol 1997; 272:688-98.
    • (1997) J Mol Biol , vol.272 , pp. 688-698
    • Tasset, D.M.1    Kubik, M.F.2    Steiner, W.3
  • 23
    • 0028826936 scopus 로고
    • Peptide conjugation to an in vitro-selected DNA ligand improves enzyme inhibition
    • Lin Y, Padmapriya A, Morden KM. Jayasena SD. Peptide conjugation to an in vitro-selected DNA ligand improves enzyme inhibition. Proc Natl Acad Sci U S A 1995;92:11044-8.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 11044-11048
    • Lin, Y.1    Padmapriya, A.2    Morden, K.M.3    Jayasena, S.D.4
  • 25
    • 0028224199 scopus 로고
    • High-resolution molecular discrimination by RNA
    • Jenison RD, Gill SC, Pardi A, Polisky B. High-resolution molecular discrimination by RNA. Science 1994;263:1425-9.
    • (1994) Science , vol.263 , pp. 1425-1429
    • Jenison, R.D.1    Gill, S.C.2    Pardi, A.3    Polisky, B.4
  • 26
    • 0030832285 scopus 로고    scopus 로고
    • In vitro selection of a 7-methyl-guanosine binding RNA that inhibits translation of capped mRNA molecules
    • Haller AA, Sarnow P. In vitro selection of a 7-methyl-guanosine binding RNA that inhibits translation of capped mRNA molecules. Proc Natl Acad Sci U S A 1997;94:8521-6.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 8521-8526
    • Haller, A.A.1    Sarnow, P.2
  • 27
    • 0027180473 scopus 로고
    • An RNA motif that binds ATP
    • Sassanfar M, Szostak JW. An RNA motif that binds ATP. Nature 1993:364:550-3.
    • (1993) Nature , vol.364 , pp. 550-553
    • Sassanfar, M.1    Szostak, J.W.2
  • 29
    • 0029924638 scopus 로고    scopus 로고
    • RNA aptamers that bind L-arginine with sub-micromolar dissociation constants and high enantioselectivity
    • Geiger A, Burgstaller P, von der Eltz H, Roeder A, Famulok M. RNA aptamers that bind L-arginine with sub-micromolar dissociation constants and high enantioselectivity. Nucleic Acids Res 1996; 24:1029-36.
    • (1996) Nucleic Acids Res , vol.24 , pp. 1029-1036
    • Geiger, A.1    Burgstaller, P.2    Von der Eltz, H.3    Roeder, A.4    Famulok, M.5
  • 30
    • 11944267365 scopus 로고
    • Antisense oligonucleotides: A new therapeutic principle
    • Uhlmann E, Peyman A. Antisense oligonucleotides: a new therapeutic principle. Chem Rev 1990;90:543-84.
    • (1990) Chem Rev , vol.90 , pp. 543-584
    • Uhlmann, E.1    Peyman, A.2
  • 31
    • 0030271959 scopus 로고    scopus 로고
    • Antisense oligonucleotides: Towards clinical trials
    • Agrawal S. Antisense oligonucleotides: towards clinical trials. Trends Biotechnol 1996:14:376-87.
    • (1996) Trends Biotechnol , vol.14 , pp. 376-387
    • Agrawal, S.1
  • 32
    • 0030132985 scopus 로고    scopus 로고
    • Exploiting the potential of antisense: Beyond phosphorothioate oligodeoxynucleotides
    • Stein CA. Exploiting the potential of antisense: beyond phosphorothioate oligodeoxynucleotides. Chem Biol 1996;3:319-23.
    • (1996) Chem Biol , vol.3 , pp. 319-323
    • Stein, C.A.1
  • 33
    • 0029943679 scopus 로고    scopus 로고
    • Phosphorothioate antisense: Question of specificity
    • Stein CA. Phosphorothioate antisense: question of specificity. Trends Biotechnol 1996;14:147-9.
    • (1996) Trends Biotechnol , vol.14 , pp. 147-149
    • Stein, C.A.1
  • 34
    • 0015807624 scopus 로고
    • Polynucleotides containing 2′-amino-2′-deoxyribose and 2′-axido-2′-deoxyribose
    • Hobbs J, Sternbach H, Sprinzl M, Eckstein F. Polynucleotides containing 2′-amino-2′-deoxyribose and 2′-axido-2′-deoxyribose. Biochemistry 1973;12:5138-45.
    • (1973) Biochemistry , vol.12 , pp. 5138-5145
    • Hobbs, J.1    Sternbach, H.2    Sprinzl, M.3    Eckstein, F.4
  • 35
    • 0026337408 scopus 로고
    • Kinetic characterization of ribonuclease-resistant 2'-modified hammerhead ribozymes
    • Pieken WA, Olsen DB, Benseler F, Aurup H, Eckstein F. Kinetic characterization of ribonuclease-resistant 2'-modified hammerhead ribozymes. Science 1991;253:314-7.
    • (1991) Science , vol.253 , pp. 314-317
    • Pieken, W.A.1    Olsen, D.B.2    Benseler, F.3    Aurup, H.4    Eckstein, F.5
  • 36
    • 0026542605 scopus 로고
    • Hammerhead ribozyme-mediated cleavage of the long terminal repeat RNA of human immunodeficiency virus type 1
    • Heidenreich O, Eckstein F. Hammerhead ribozyme-mediated cleavage of the long terminal repeat RNA of human immunodeficiency virus type 1. J Biol Chem 1992;267:1904-9.
    • (1992) J Biol Chem , vol.267 , pp. 1904-1909
    • Heidenreich, O.1    Eckstein, F.2
  • 37
  • 39
    • 0031012128 scopus 로고    scopus 로고
    • Potent 2′-amino-, and 2′-fluoro-2′-deoxyribonucleotide RNA inhibitors of keratinocyte growth factor
    • Pagratis NC, Bell C, Chang Y-F, Jennings S. Fitzwater T, Jellinek D, et al. Potent 2′-amino-, and 2′-fluoro-2′-deoxyribonucleotide RNA inhibitors of keratinocyte growth factor. Nat Biotechnol 1997;15:68-73.
    • (1997) Nat Biotechnol , vol.15 , pp. 68-73
    • Pagratis, N.C.1    Bell, C.2    Chang, Y.-F.3    Jennings, S.4    Fitzwater, T.5    Jellinek, D.6
  • 40
    • 0032167704 scopus 로고    scopus 로고
    • Staining of cell surface human CD4 with 2′-F-pyrimidine-containing RNA aptamers for flow cytometry
    • Davis KA. Lin Y, Abrams B, Jayasena SD. Staining of cell surface human CD4 with 2′-F-pyrimidine-containing RNA aptamers for flow cytometry. Nucleic Acids Res 1998;26:3915-24.
    • (1998) Nucleic Acids Res , vol.26 , pp. 3915-3924
    • Davis, K.A.1    Lin, Y.2    Abrams, B.3    Jayasena, S.D.4
  • 41
    • 0025008851 scopus 로고
    • Enzymatic incorporation of a new base pair into DNA and RNA extends the genetic alphabet
    • Piccirilli JA, Krauch T, Moroney SE, Benner SA. Enzymatic incorporation of a new base pair into DNA and RNA extends the genetic alphabet. Nature 1990;343:33-7.
    • (1990) Nature , vol.343 , pp. 33-37
    • Piccirilli, J.A.1    Krauch, T.2    Moroney, S.E.3    Benner, S.A.4
  • 42
    • 0026523058 scopus 로고
    • Ribosome-mediated incorporation of a non-standard amino acid into a peptide through expansion of the genetic code
    • Bain DJ, Switzer C, Chamberlin AR, Benner SA. Ribosome-mediated incorporation of a non-standard amino acid into a peptide through expansion of the genetic code. Nature 1992; 356:537-9.
    • (1992) Nature , vol.356 , pp. 537-539
    • Bain, D.J.1    Switzer, C.2    Chamberlin, A.R.3    Benner, S.A.4
  • 43
    • 0000615415 scopus 로고
    • 6-(6-aminohexyl)isoguanosine, into RNA
    • 6-(6-aminohexyl)isoguanosine, into RNA. J Am Chem Sec 1993;115:4461-7.
    • (1993) J Am Chem Sec , vol.115 , pp. 4461-4467
    • Tor, Y.1    Dervan, P.B.2
  • 44
    • 11944258509 scopus 로고
    • Hydrophobic, non-hydrogen-bonding bases and base pairs in DNA
    • Schweitzer BA, Fool ET. Hydrophobic, non-hydrogen-bonding bases and base pairs in DNA. J Am Chem Sec 1995;117:1863-72.
    • (1995) J Am Chem Sec , vol.117 , pp. 1863-1872
    • Schweitzer, B.A.1    Fool, E.T.2
  • 45
    • 0031792598 scopus 로고    scopus 로고
    • Efficient replication between non-hydrogen-bonded nucleotide shape analogues
    • Guckian KM, Krugh TR, Kool ET. Efficient replication between non-hydrogen-bonded nucleotide shape analogues. Nat Struct Biol 1998;5:950-9.
    • (1998) Nat Struct Biol , vol.5 , pp. 950-959
    • Guckian, K.M.1    Krugh, T.R.2    Kool, E.T.3
  • 46
    • 0028136665 scopus 로고
    • The application of a modified nucleotide in aptamer selection: Novel thrombin aptamers containing 5-(1-pentynyl)-2′-deoxyuridine
    • Latham JA, Johnson R, Toole JJ. The application of a modified nucleotide in aptamer selection: novel thrombin aptamers containing 5-(1-pentynyl)-2′-deoxyuridine. Nucleic Acids Res 1994; 22:2817-22.
    • (1994) Nucleic Acids Res , vol.22 , pp. 2817-2822
    • Latham, J.A.1    Johnson, R.2    Toole, J.J.3
  • 47
    • 0026575221 scopus 로고
    • Selection of single-stranded DNA molecules that bind and inhibit human thrombin
    • Bock LC, Griffin LC, Latham JA, Vermaas EH, Toole JJ. Selection of single-stranded DNA molecules that bind and inhibit human thrombin. Nature 1992;355:564-6.
    • (1992) Nature , vol.355 , pp. 564-566
    • Bock, L.C.1    Griffin, L.C.2    Latham, J.A.3    Vermaas, E.H.4    Toole, J.J.5
  • 48
    • 0029161984 scopus 로고
    • New uridine derivatives for systematic evolution of RNA ligands by exponential enrichment
    • Dewey TM, Mundt AA, Crouch GJ, Zyzniewski MC, Eaton BE. New uridine derivatives for systematic evolution of RNA ligands by exponential enrichment. J Am Chem Sec 1995;117:8474-5.
    • (1995) J Am Chem Sec , vol.117 , pp. 8474-8475
    • Dewey, T.M.1    Mundt, A.A.2    Crouch, G.J.3    Zyzniewski, M.C.4    Eaton, B.E.5
  • 49
    • 0031151974 scopus 로고    scopus 로고
    • The joys of in vitro selection: Chemically dressing oligonucleotides to satiate protein targets
    • Eaton BE. The joys of in vitro selection: chemically dressing oligonucleotides to satiate protein targets. Curr Opin Chem Biol 1997;1:10-6.
    • (1997) Curr Opin Chem Biol , vol.1 , pp. 10-16
    • Eaton, B.E.1
  • 50
    • 0028179384 scopus 로고
    • Evidence for a non-α-helical DNA-binding motif in the Rel homology region
    • Liu J, Sodeoka M, Lane WS, Verdine GL. Evidence for a non-α-helical DNA-binding motif in the Rel homology region. Proc Natl Acad Sci U S A 1994;91:908-12.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 908-912
    • Liu, J.1    Sodeoka, M.2    Lane, W.S.3    Verdine, G.L.4
  • 51
    • 0026782249 scopus 로고
    • Identification of an amino acid-base contact in the GCN4-DNA complex by bromouracil-mediated photocrosslinking
    • Blatter EE, Ebright YW, Ebright RH. Identification of an amino acid-base contact in the GCN4-DNA complex by bromouracil-mediated photocrosslinking. Nature 1992;359:650-2.
    • (1992) Nature , vol.359 , pp. 650-652
    • Blatter, E.E.1    Ebright, Y.W.2    Ebright, R.H.3
  • 52
    • 0028323417 scopus 로고
    • Telomeric protein-DNA point contacts identified by photo-cross-linking using 5-bromode-oxyuridine
    • Hicke BJ, Willis MC, Koch TH, Cech TR. Telomeric protein-DNA point contacts identified by photo-cross-linking using 5-bromode-oxyuridine. Biochemistry 1994;33:3364-73.
    • (1994) Biochemistry , vol.33 , pp. 3364-3373
    • Hicke, B.J.1    Willis, M.C.2    Koch, T.H.3    Cech, T.R.4
  • 53
    • 0027717964 scopus 로고
    • Photocrosslinking of 5-iodouracil-substituted RNA and DNA to proteins
    • Willis MC, Hicke BJ, Uhlenbeck OC, Cech TR, Koch TH. Photocrosslinking of 5-iodouracil-substituted RNA and DNA to proteins. Science 1993;262:1255-7.
    • (1993) Science , vol.262 , pp. 1255-1257
    • Willis, M.C.1    Hicke, B.J.2    Uhlenbeck, O.C.3    Cech, T.R.4    Koch, T.H.5
  • 54
    • 0029912468 scopus 로고    scopus 로고
    • High yield photocrosslinking of a 5-iodocytidine (IC) substituted RNA to its associated protein
    • Meisenheimer KM, Meisenheimer PL, Willis MC, Koch TH. High yield photocrosslinking of a 5-iodocytidine (IC) substituted RNA to its associated protein. Nucleic Acids Res 1996;24:981-2.
    • (1996) Nucleic Acids Res , vol.24 , pp. 981-982
    • Meisenheimer, K.M.1    Meisenheimer, P.L.2    Willis, M.C.3    Koch, T.H.4
  • 55
    • 0029557118 scopus 로고
    • Using in vitro selection to direct the covalent attachment of human immunodeficiency virus type i Rev protein to high-affinity RNA ligands
    • Jensen KB, Atkinson BL, Willis MC, Koch TH, Gold L Using in vitro selection to direct the covalent attachment of human immunodeficiency virus type i Rev protein to high-affinity RNA ligands. Proc Natl Acad Sci U S A 1995;92;12220-4.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 12220-12224
    • Jensen, K.B.1    Atkinson, B.L.2    Willis, M.C.3    Koch, T.H.4    Gold, L.5
  • 56
    • 0028606714 scopus 로고
    • An RNA-protein contact determined by 5-bromouridine substitution, photocrosslinking and sequencing
    • Willis MC, LeCuyer KA, Meisenheimer KM, Uhlenbeck OC, Koch TH. An RNA-protein contact determined by 5-bromouridine substitution, photocrosslinking and sequencing. Nucleic Acids Res 1994;22:4947-52.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4947-4952
    • Willis, M.C.1    LeCuyer, K.A.2    Meisenheimer, K.M.3    Uhlenbeck, O.C.4    Koch, T.H.5
  • 58
    • 0003103710 scopus 로고
    • RNA: The shape of things to come
    • Gesteland R, Atkins J, eds. Plainview, NY: Cold Spring Harbor Laboratory Press
    • Gold L, Allen P, Binkley J, Brown D, Schneider B, Yasset D, et al. RNA: the shape of things to come. In: Gesteland R, Atkins J, eds. The RNA world. Plainview, NY: Cold Spring Harbor Laboratory Press, 1993:497-509.
    • (1993) The RNA World , pp. 497-509
    • Gold, L.1    Allen, P.2    Binkley, J.3    Brown, D.4    Schneider, B.5    Yasset, D.6
  • 60
    • 0029902343 scopus 로고    scopus 로고
    • Small RNA-divalent domains
    • Ciesiolka J, Yarus M. Small RNA-divalent domains. RNA 1996; 2:785-93.
    • (1996) RNA , vol.2 , pp. 785-793
    • Ciesiolka, J.1    Yarus, M.2
  • 61
    • 0030608959 scopus 로고    scopus 로고
    • 2+-binding RNA motifs with an asymmetric purine-rich internal loop and a G-A base pair
    • 2+3-binding RNA motifs with an asymmetric purine-rich internal loop and a G-A base pair. RNA 1997;3:1289-300.
    • (1997) RNA , vol.3 , pp. 1289-1300
    • Hofmann, H.-P.1    Limmer, S.2    Hornung, V.3    Sprinzl, M.4
  • 62
    • 0026599465 scopus 로고
    • Selection in vitro of single-stranded DNA molecules that fold into specific ligand-binding structures
    • Ellington AD, Szostak JW. Selection in vitro of single-stranded DNA molecules that fold into specific ligand-binding structures. Nature 1992;355:850-2.
    • (1992) Nature , vol.355 , pp. 850-852
    • Ellington, A.D.1    Szostak, J.W.2
  • 63
    • 0027173323 scopus 로고
    • Three small ribooligo-nucleotides with specific arginine sites
    • Connell GJ, Illangesekare M, Yarus M. Three small ribooligo-nucleotides with specific arginine sites. Biochemistry 1993;32:5497-502.
    • (1993) Biochemistry , vol.32 , pp. 5497-5502
    • Connell, G.J.1    Illangesekare, M.2    Yarus, M.3
  • 64
    • 0028011717 scopus 로고
    • Molecular recognition of amino acids by RNA-aptamers: An L-citrulline binding RNA motif and its evolution into an L-arginine binder
    • Famulok M. Molecular recognition of amino acids by RNA-aptamers: an L-citrulline binding RNA motif and its evolution into an L-arginine binder. J Am Chem Sec 1994;116:1698-706.
    • (1994) J Am Chem Sec , vol.116 , pp. 1698-1706
    • Famulok, M.1
  • 65
    • 0028823341 scopus 로고
    • Identification of two novel arginine binding DNAs
    • Harada K, Frankel AD. Identification of two novel arginine binding DNAs. EMBO J 1995;14:5798-811.
    • (1995) EMBO J , vol.14 , pp. 5798-5811
    • Harada, K.1    Frankel, A.D.2
  • 66
    • 0029138009 scopus 로고
    • RNA aptamers that bind flavin and nicotinamide redox cofactors
    • Lauhon CT, Szostak JW. RNA aptamers that bind flavin and nicotinamide redox cofactors. J Am Chem Sec 1995:117:1246-57.
    • (1995) J Am Chem Sec , vol.117 , pp. 1246-1257
    • Lauhon, C.T.1    Szostak, J.W.2
  • 67
    • 0027995790 scopus 로고
    • Isolation of RNA aptamers for biological cofactors by in vitro selection
    • Burgstaller P, Famulok M. Isolation of RNA aptamers for biological cofactors by in vitro selection. Angew Chem 1994;33:1084-7.
    • (1994) Angew Chem , vol.33 , pp. 1084-1087
    • Burgstaller, P.1    Famulok, M.2
  • 68
    • 0028058105 scopus 로고
    • In vitro selection of RNA aptamers specific for cyanocobalamin
    • Lorsch JR, Szostak JW. In vitro selection of RNA aptamers specific for cyanocobalamin. Biochemistry 1994;33:973-82.
    • (1994) Biochemistry , vol.33 , pp. 973-982
    • Lorsch, J.R.1    Szostak, J.W.2
  • 69
    • 0030833542 scopus 로고    scopus 로고
    • RNA aptamers to the adenosine moiety of S-adenosyl methionine: Structural inferences from variations on a theme and the reproducibility of SELEX
    • Burke DH, Gold L. RNA aptamers to the adenosine moiety of S-adenosyl methionine: structural inferences from variations on a theme and the reproducibility of SELEX. Nucleic Acids Res 1997;25:2020-4.
    • (1997) Nucleic Acids Res , vol.25 , pp. 2020-2024
    • Burke, D.H.1    Gold, L.2
  • 70
    • 0032514717 scopus 로고    scopus 로고
    • Functional requirements for specific ligand recognition by a biotin-binding RNA pseudoknot
    • Wilson C, Nix J, Szostak J. Functional requirements for specific ligand recognition by a biotin-binding RNA pseudoknot. Biochemistry 1998;37:14410-9.
    • (1998) Biochemistry , vol.37 , pp. 14410-14419
    • Wilson, C.1    Nix, J.2    Szostak, J.3
  • 71
    • 0029294539 scopus 로고
    • Specific binding of aminoglycoside antibiotics to RNA
    • Wang Y, Rando RR. Specific binding of aminoglycoside antibiotics to RNA. Chem Biol 1995;2:281-90.
    • (1995) Chem Biol , vol.2 , pp. 281-290
    • Wang, Y.1    Rando, R.R.2
  • 73
    • 0029294685 scopus 로고
    • In vitro selection of RNA lectins: Using combinatorial chemistry to interpret ribozyme evolution
    • Lato SM, Boles AR, Ellington AD. In vitro selection of RNA lectins: using combinatorial chemistry to interpret ribozyme evolution. Chem Biol 1995;2:291-303.
    • (1995) Chem Biol , vol.2 , pp. 291-303
    • Lato, S.M.1    Boles, A.R.2    Ellington, A.D.3
  • 74
    • 0029766901 scopus 로고    scopus 로고
    • RNA molecules that specifically and stoichiometrically bind aminoglycoside antibiotics with high affinities
    • Wang Y, Killian J, Hamasaki K, Rando RR. RNA molecules that specifically and stoichiometrically bind aminoglycoside antibiotics with high affinities. Biochemistry 1996;35:12338-46.
    • (1996) Biochemistry , vol.35 , pp. 12338-12346
    • Wang, Y.1    Killian, J.2    Hamasaki, K.3    Rando, R.R.4
  • 76
    • 0031965013 scopus 로고    scopus 로고
    • In vitro selection and characterization of streptomycin-binding RNAs: Recognition discrimination between antibiotics
    • Wallace ST, Schroeder R. In vitro selection and characterization of streptomycin-binding RNAs: recognition discrimination between antibiotics. RNA 1998;4:112-23.
    • (1998) RNA , vol.4 , pp. 112-123
    • Wallace, S.T.1    Schroeder, R.2
  • 77
    • 0032052277 scopus 로고    scopus 로고
    • An RNA aptamer to the xanthine/guanine base with a distinctive mode of purine recognition
    • Kiga D, Futamura Y, Sakamoto K, Yokoyama S. An RNA aptamer to the xanthine/guanine base with a distinctive mode of purine recognition. Nucleic Acids Res 1998;26:1755-60.
    • (1998) Nucleic Acids Res , vol.26 , pp. 1755-1760
    • Kiga, D.1    Futamura, Y.2    Sakamoto, K.3    Yokoyama, S.4
  • 78
    • 0028965943 scopus 로고
    • A DNA aptamer that binds adenosine and ATP
    • Huizenga DE, Szostak JW. A DNA aptamer that binds adenosine and ATP. Biochemistry 1995;34:656-65.
    • (1995) Biochemistry , vol.34 , pp. 656-665
    • Huizenga, D.E.1    Szostak, J.W.2
  • 79
    • 0029062420 scopus 로고
    • In vitro selection of RNA ligands to substance P
    • Nieuwlandt D, Wecker M, Gold L. In vitro selection of RNA ligands to substance P. Biochemistry 1995;34:5651-9.
    • (1995) Biochemistry , vol.34 , pp. 5651-5659
    • Nieuwlandt, D.1    Wecker, M.2    Gold, L.3
  • 81
    • 0026651981 scopus 로고
    • RNA pseudoknots that inhibit HIV-1 reverse transcriptase
    • Tuerk C, MacDougal S, Gold L. RNA pseudoknots that inhibit HIV-1 reverse transcriptase. Proc Natl Acad Sci U S A 1992;89:6988-92.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 6988-6992
    • Tuerk, C.1    Macdougal, S.2    Gold, L.3
  • 82
    • 0029945147 scopus 로고    scopus 로고
    • Inhibitory RNA ligands to reverse transcriptase from feline immunodeficiency virus
    • Chen H, McBroom DG, Zhu Y-Q, Gold L, North TW. Inhibitory RNA ligands to reverse transcriptase from feline immunodeficiency virus. Biochemistry 1996;35:6923-30.
    • (1996) Biochemistry , vol.35 , pp. 6923-6930
    • Chen, H.1    McBroom, D.G.2    Zhu, Y.-Q.3    Gold, L.4    North, T.W.5
  • 83
    • 0028065203 scopus 로고
    • Selection of high-affinity RNA ligands to reverse transcriptase: Inhibition of cDNA synthesis and RNase H activity
    • Chen H, Gold L. Selection of high-affinity RNA ligands to reverse transcriptase: inhibition of cDNA synthesis and RNase H activity. Biochemistry 1994;33:8746-56.
    • (1994) Biochemistry , vol.33 , pp. 8746-8756
    • Chen, H.1    Gold, L.2
  • 84
    • 0030606308 scopus 로고    scopus 로고
    • Oligonucleotide inhibitors of Taq DNA polymerase facilitate detection of low copy number targets by PCR
    • Dang C, Jayasena SD. Oligonucleotide inhibitors of Taq DNA polymerase facilitate detection of low copy number targets by PCR. J Mol Biol 1996;264:268-78.
    • (1996) J Mol Biol , vol.264 , pp. 268-278
    • Dang, C.1    Jayasena, S.D.2
  • 86
    • 0027361841 scopus 로고
    • High-affinity RNA ligands to basic fibroblast growth factor inhibit receptor binding
    • Jellinek D, Lynott CK, Rifkin DB, Janjic N. High-affinity RNA ligands to basic fibroblast growth factor inhibit receptor binding. Proc Natl Acad Sci U S A 1993;90:11227-31.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 11227-12231
    • Jellinek, D.1    Lynott, C.K.2    Rifkin, D.B.3    Janjic, N.4
  • 88
    • 0028011142 scopus 로고
    • Characterization of an in vitro-selected RNA ligand to the HIV-1 Rev protein
    • Jensen KB, Green L, MacDougal-Waugh S, Tuerk C. Characterization of an in vitro-selected RNA ligand to the HIV-1 Rev protein. J Mol Blol 1994;235:237-47.
    • (1994) J Mol Blol , vol.235 , pp. 237-247
    • Jensen, K.B.1    Green, L.2    MacDougal-Waugh, S.3    Tuerk, C.4
  • 89
    • 0027434310 scopus 로고
    • Selective enrichment of RNA species for tight binding to Escherichia coli rho factor
    • Schneider D, Gold L, Platt T. Selective enrichment of RNA species for tight binding to Escherichia coli rho factor. FASEB J 1993;7:201-7.
    • (1993) FASEB J , vol.7 , pp. 201-207
    • Schneider, D.1    Gold, L.2    Platt, T.3
  • 90
    • 0028966003 scopus 로고
    • Defining a smaller RNA substrate for elongation factor Tu
    • Nazarenko IA, Uhlenbeck OC. Defining a smaller RNA substrate for elongation factor Tu. Biochemistry 1995;34:2545-52.
    • (1995) Biochemistry , vol.34 , pp. 2545-2552
    • Nazarenko, I.A.1    Uhlenbeck, O.C.2
  • 92
    • 0029395440 scopus 로고
    • In vitro selection of RNA-based irreversible inhibitors of human neutrophil elastase
    • Smith D, Kirschenheuter GP, Charlton J, Guidot DM, Repine JE. In vitro selection of RNA-based irreversible inhibitors of human neutrophil elastase. Chem Biol 1995;2:741-50.
    • (1995) Chem Biol , vol.2 , pp. 741-750
    • Smith, D.1    Kirschenheuter, G.P.2    Charlton, J.3    Guidot, D.M.4    Repine, J.E.5
  • 97
    • 0029031094 scopus 로고
    • Oligonucleotides as research, diagnostic, and therapeutic agents
    • Gold L. Oligonucleotides as research, diagnostic, and therapeutic agents. J Biol Chem 1995;270:13581-4.
    • (1995) J Biol Chem , vol.270 , pp. 13581-13584
    • Gold, L.1
  • 98
    • 33748215639 scopus 로고
    • In vitro selection of specific ligand-binding nucleic acids
    • Famulok M, Szostak JW. In vitro selection of specific ligand-binding nucleic acids. Angew Chem Int Ed Engl 1992;31:979-88.
    • (1992) Angew Chem Int Ed Engl , vol.31 , pp. 979-988
    • Famulok, M.1    Szostak, J.W.2
  • 99
    • 0031102380 scopus 로고    scopus 로고
    • Nucleic acid selection and the challenge of Combinatorial chemistry
    • Osborne SE, Ellington AD. Nucleic acid selection and the challenge of Combinatorial chemistry. Chem Rev 1997;97:349-70.
    • (1997) Chem Rev , vol.97 , pp. 349-370
    • Osborne, S.E.1    Ellington, A.D.2
  • 100
    • 0029379551 scopus 로고
    • Let's get specific: The relationship between specificity and affinity
    • Eaton BE, Gold L, Zichi DA. Let's get specific: the relationship between specificity and affinity. Chem Biol 1995;2:633-8.
    • (1995) Chem Biol , vol.2 , pp. 633-638
    • Eaton, B.E.1    Gold, L.2    Zichi, D.A.3
  • 101
    • 0027759585 scopus 로고
    • The discovery and characterization of a novel nucleotide-based thrombin inhibitor
    • Griffin LC, Toole JJ, Leung LLK. The discovery and characterization of a novel nucleotide-based thrombin inhibitor. Gene 1993; 137:25-31.
    • (1993) Gene , vol.137 , pp. 25-31
    • Griffin, L.C.1    Toole, J.J.2    Leung, L.L.K.3
  • 103
    • 0027488624 scopus 로고
    • Isolation of new ribozymes from a large pool of random sequences
    • Bartel DP, Szostak JW, Isolation of new ribozymes from a large pool of random sequences. Science 1993;261:1411-8.
    • (1993) Science , vol.261 , pp. 1411-1418
    • Bartel, D.P.1    Szostak, J.W.2
  • 104
    • 0028124128 scopus 로고
    • In vitro evolution of new ribozymes with polynucleotide kinase activity
    • Lorsch JR, Szostak JW. In vitro evolution of new ribozymes with polynucleotide kinase activity. Science 1994;371:31-6.
    • (1994) Science , vol.371 , pp. 31-36
    • Lorsch, J.R.1    Szostak, J.W.2
  • 105
    • 0029956108 scopus 로고    scopus 로고
    • Ribozyme-catalysed amino-acid transfer reactions
    • Lohse PA, Szostak JW. Ribozyme-catalysed amino-acid transfer reactions. Nature 1996;381:442-4.
    • (1996) Nature , vol.381 , pp. 442-444
    • Lohse, P.A.1    Szostak, J.W.2
  • 106
    • 0028911845 scopus 로고
    • In vitro evolution of a self-alkylating ribozyme
    • Wilson C, Szostak JW. In vitro evolution of a self-alkylating ribozyme. Nature 1995;374:777-82.
    • (1995) Nature , vol.374 , pp. 777-782
    • Wilson, C.1    Szostak, J.W.2
  • 109
    • 0032480010 scopus 로고    scopus 로고
    • The structure of HIV-1 reverse transcriptase complexed with RNA pseudoknot inhibitor
    • Jaeger J, Restle T, Steitz TA. The structure of HIV-1 reverse transcriptase complexed with RNA pseudoknot inhibitor. EMBO J 1998;17:4535-42.
    • (1998) EMBO J , vol.17 , pp. 4535-4542
    • Jaeger, J.1    Restle, T.2    Steitz, T.A.3
  • 111
    • 0031563817 scopus 로고    scopus 로고
    • Structure, recognition and adaptive binding in RNA aptamer complexes
    • Patel DJ, Suri AK, Jiang F, Jiang L, Fan P, Kumar RA, et al. Structure, recognition and adaptive binding in RNA aptamer complexes. J Mol Biol 1997;272:645-64.
    • (1997) J Mol Biol , vol.272 , pp. 645-664
    • Patel, D.J.1    Suri, A.K.2    Jiang, F.3    Jiang, L.4    Fan, P.5    Kumar, R.A.6
  • 112
  • 113
    • 0009683628 scopus 로고    scopus 로고
    • Encapsulating an amino acid in a DNA fold
    • Hsiung C, Patel DJ. Encapsulating an amino acid in a DNA fold. Nat Struct Biol 1996;3:1046-50.
    • (1996) Nat Struct Biol , vol.3 , pp. 1046-1050
    • Hsiung, C.1    Patel, D.J.2
  • 114
    • 0029972909 scopus 로고    scopus 로고
    • Structural basis of ligand discrimination by two related RNA aptamers resolved by NMR spectroscopy
    • Yang Y, Kochoyan M, Burgstaller P, Westhof E, Famulok M. Structural basis of ligand discrimination by two related RNA aptamers resolved by NMR spectroscopy. Science 1996;272:1343-7.
    • (1996) Science , vol.272 , pp. 1343-1347
    • Yang, Y.1    Kochoyan, M.2    Burgstaller, P.3    Westhof, E.4    Famulok, M.5
  • 115
    • 0029946537 scopus 로고    scopus 로고
    • Structural basis of RNA folding and recognition in an AMP-RNA aptamer complex
    • Jiang F, Kumar RA, Jones RA, Patel DJ. Structural basis of RNA folding and recognition in an AMP-RNA aptamer complex. Nature 1996;382:183-6.
    • (1996) Nature , vol.382 , pp. 183-186
    • Jiang, F.1    Kumar, R.A.2    Jones, R.A.3    Patel, D.J.4
  • 116
    • 0029864853 scopus 로고    scopus 로고
    • Molecular recognition in the FMN-RNA aptamer complex
    • Fan P, Suri AK, Fiala R, Live D, Patel DJ. Molecular recognition in the FMN-RNA aptamer complex. J Mol Biol 1996;258:480-500.
    • (1996) J Mol Biol , vol.258 , pp. 480-500
    • Fan, P.1    Suri, A.K.2    Fiala, R.3    Live, D.4    Patel, D.J.5
  • 117
    • 0028072814 scopus 로고
    • High-performance assays of small molecules: Enhanced sensitivity, rapidity, and convenience demonstrated with a noncompetitive immunometric anti-immune complex assay system for digoxin
    • Self CH, Dessi JL, Winger LA. High-performance assays of small molecules: enhanced sensitivity, rapidity, and convenience demonstrated with a noncompetitive immunometric anti-immune complex assay system for digoxin. Clin Chem 1994;40:2035-41.
    • (1994) Clin Chem , vol.40 , pp. 2035-2041
    • Self, C.H.1    Dessi, J.L.2    Winger, L.A.3
  • 118
    • 0026598003 scopus 로고
    • Production of a monoclonal antibody to cortisol: Application to a direct enzyme-linked immunosorbent assay of plasma
    • Lewis JG, Manley L, Whitlow JC, Elder PA. Production of a monoclonal antibody to cortisol: application to a direct enzyme-linked immunosorbent assay of plasma. Steroids 1992;57:82-5.
    • (1992) Steroids , vol.57 , pp. 82-85
    • Lewis, J.G.1    Manley, L.2    Whitlow, J.C.3    Elder, P.A.4
  • 119
    • 0024236301 scopus 로고
    • Production of monoclonal antibodies to estriol and their application in the development of a sensitive nonisotopic immunoassay
    • Ghosh SK. Production of monoclonal antibodies to estriol and their application in the development of a sensitive nonisotopic immunoassay. Steroids 1988;52:1-14.
    • (1988) Steroids , vol.52 , pp. 1-14
    • Ghosh, S.K.1
  • 120
    • 0024843310 scopus 로고
    • Improvement of estradiol enzymoimmunoassay, using a monoclonal antibody and an avidin/biotin amplification system
    • De Lauzon S, El Jarbi J, Desfosses B, Cittanova N. Improvement of estradiol enzymoimmunoassay, using a monoclonal antibody and an avidin/biotin amplification system. J Immunoassay 1989;10:339-57.
    • (1989) J Immunoassay , vol.10 , pp. 339-357
    • De Lauzon, S.1    El Jarbi, J.2    Desfosses, B.3    Cittanova, N.4
  • 121
    • 0024367931 scopus 로고
    • Evaluation and performance characteristics of a novel ELISA using monoclonal antibody to glycated albumin
    • Hud E, Cohen MP. Evaluation and performance characteristics of a novel ELISA using monoclonal antibody to glycated albumin. Clin Chim Acta 1989;185:157-64.
    • (1989) Clin Chim Acta , vol.185 , pp. 157-164
    • Hud, E.1    Cohen, M.P.2
  • 122
    • 0025165065 scopus 로고
    • The preparation of monoclonal antibodies which react preferentially with human bone alkaline phosphatase and not liver alkaline phosphatase
    • Hill CS, Wolfert RL. The preparation of monoclonal antibodies which react preferentially with human bone alkaline phosphatase and not liver alkaline phosphatase. Clin Chim Acta 1989; 186:315-29.
    • (1989) Clin Chim Acta , vol.186 , pp. 315-329
    • Hill, C.S.1    Wolfert, R.L.2
  • 123
    • 0026009595 scopus 로고
    • Monoclonal antibody based discrepancies between two-site immunometric tests for lutropin
    • Pettersson K, Ding Y-Q, Huhtaniemi I. Monoclonal antibody based discrepancies between two-site immunometric tests for lutropin. Clin Chem 1991;37:1745-8.
    • (1991) Clin Chem , vol.37 , pp. 1745-1748
    • Pettersson, K.1    Ding, Y.-Q.2    Huhtaniemi, I.3
  • 124
    • 0025829726 scopus 로고
    • Individual differences in lutropin immunoreactivity revealed by monoclonal antibodies
    • Pettersson KSI, Soderholm JR-M. Individual differences in lutropin immunoreactivity revealed by monoclonal antibodies. Clin Chem 1991;37:333-40.
    • (1991) Clin Chem , vol.37 , pp. 333-340
    • Pettersson, K.S.I.1    Soderholm, J.R.-M.2
  • 125
    • 0027144516 scopus 로고
    • Human chorionic gonadotropin: Molecular forms, detection and clinical implications
    • Bidart J-M, Bellet D. Human chorionic gonadotropin: molecular forms, detection and clinical implications. Trends Med 1993;4:285-90.
    • (1993) Trends Med , vol.4 , pp. 285-290
    • Bidart, J.-M.1    Bellet, D.2
  • 126
    • 85069123059 scopus 로고
    • Structure-function relationships of pituitary hormones HFSH, HLH, and HTSH
    • Abraham GE, ed. New York: Marcel Dekker
    • Rathnam P. Structure-function relationships of pituitary hormones HFSH, HLH, and HTSH. In: Abraham GE, ed. Radioassay systems in clinical endocrinology. New York: Marcel Dekker, 1981:21-34.
    • (1981) Radioassay Systems in Clinical Endocrinology , pp. 21-34
    • Rathnam, P.1
  • 127
    • 0032213173 scopus 로고    scopus 로고
    • Isolation of a fluorophore-specific DNA aptamer with weak radox activity
    • Wilson C, Szostak JW. Isolation of a fluorophore-specific DNA aptamer with weak radox activity. Chem Biol 1998;5:609-17.
    • (1998) Chem Biol , vol.5 , pp. 609-617
    • Wilson, C.1    Szostak, J.W.2
  • 130
    • 0032400827 scopus 로고    scopus 로고
    • Anti-L-Selectin oligonucleotide ligands recognize CD62L-positive Leukocytes: Binding affinity and specificity of univalent and bivalent ligands
    • Ringquist S, Parma D. Anti-L-Selectin oligonucleotide ligands recognize CD62L-positive Leukocytes: binding affinity and specificity of univalent and bivalent ligands. Cytometry 1998;33:394-405.
    • (1998) Cytometry , vol.33 , pp. 394-405
    • Ringquist, S.1    Parma, D.2
  • 132
    • 0030020793 scopus 로고    scopus 로고
    • Immunosensors: Technology and opportunities in laboratory medicine
    • Morgan CL, Newman DJ, Price CP. Immunosensors: technology and opportunities in laboratory medicine. Clin Chem 1996;42:193-209.
    • (1996) Clin Chem , vol.42 , pp. 193-209
    • Morgan, C.L.1    Newman, D.J.2    Price, C.P.3
  • 133
  • 134
    • 0026612858 scopus 로고
    • Oligonucleotide hybridisations on glass supports: A novel linker for oligonucleotide synthesis and hybridisation properties of oligonucleotides synthesised in situ
    • Maskos U, Southern EM. Oligonucleotide hybridisations on glass supports: a novel linker for oligonucleotide synthesis and hybridisation properties of oligonucleotides synthesised in situ. Nucleic Acids Res 1992;20:1679-84.
    • (1992) Nucleic Acids Res , vol.20 , pp. 1679-1784
    • Maskos, U.1    Southern, E.M.2
  • 136
    • 0028618275 scopus 로고
    • Direct fluorescence analysis of genetic polymorphisms by hybridization with oligonucleotide arrays on glass supports
    • Guo Z, Guilfoyle RA, Thiel AJ, Wang R, Smith LM Direct fluorescence analysis of genetic polymorphisms by hybridization with oligonucleotide arrays on glass supports. Nucleic Acids Res 1994;22:5456-65.
    • (1994) Nucleic Acids Res , vol.22 , pp. 5456-5465
    • Guo, Z.1    Guilfoyle, R.A.2    Thiel, A.J.3    Wang, R.4    Smith, L.M.5
  • 139
    • 0030825711 scopus 로고    scopus 로고
    • Characterization of DNA probes immobilized on gold surfaces
    • Herne TM, Tarlov MJ. Characterization of DNA probes immobilized on gold surfaces. J Am Chem Soc 1997;119:8916-20.
    • (1997) J Am Chem Soc , vol.119 , pp. 8916-8920
    • Herne, T.M.1    Tarlov, M.J.2
  • 143
    • 0033555454 scopus 로고    scopus 로고
    • Electron transfer between bases in double helical DNA
    • Kelly SO, Barton JK. Electron transfer between bases in double helical DNA. Science 1999;283:375-81.
    • (1999) Science , vol.283 , pp. 375-381
    • Kelly, S.O.1    Barton, J.K.2
  • 144
  • 145
    • 0032492720 scopus 로고    scopus 로고
    • The binding site of a specific aminoglycoside binding RNA molecule
    • Cho J, Hamasaki K, Rando R. The binding site of a specific aminoglycoside binding RNA molecule. Biochemistry 1998;37:4985-92.
    • (1998) Biochemistry , vol.37 , pp. 4985-4992
    • Cho, J.1    Hamasaki, K.2    Rando, R.3
  • 146
    • 0029670262 scopus 로고    scopus 로고
    • Molecular beacons: Probes that fluoresce upon hybridization
    • Tyagi S, Kramer FR. Molecular beacons: probes that fluoresce upon hybridization. Nat Biotechnol 1996;14:303-8.
    • (1996) Nat Biotechnol , vol.14 , pp. 303-308
    • Tyagi, S.1    Kramer, F.R.2
  • 147
    • 0031983834 scopus 로고    scopus 로고
    • Multicolor molecular beacons for allele discrimination
    • Tyagi S, Bratu DP, Kramer FR. 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
  • 148
    • 0031969531 scopus 로고    scopus 로고
    • Molecular beacon sequence analysis for detecting drug resistance in Mycobacterium tuberculosis
    • Piatek AS, Tyagi S, Pol AC, Telenti A, Miller LP, Kramer FR, et al. Molecular beacon sequence analysis for detecting drug resistance in Mycobacterium tuberculosis. Nat Biotechnol 1998;16:359-63.
    • (1998) Nat Biotechnol , vol.16 , pp. 359-363
    • Piatek, A.S.1    Tyagi, S.2    Pol, A.C.3    Telenti, A.4    Miller, L.P.5    Kramer, F.R.6
  • 149
    • 0029692711 scopus 로고    scopus 로고
    • Microchip electrophoretic immunoassay for serum cortisol
    • Koutny LB, Schmalzing D, Taylor TA, Fuchs M. Microchip electrophoretic immunoassay for serum cortisol. Anal Chem 1996;68:18-22.
    • (1996) Anal Chem , vol.68 , pp. 18-22
    • Koutny, L.B.1    Schmalzing, D.2    Taylor, T.A.3    Fuchs, M.4
  • 150
    • 0027958617 scopus 로고
    • Affinity probe capillary electrophoresis: Analysis of recombinant human growth hormone with a fluorescent labeled antibody fragment
    • Shimura K, Karger BL. Affinity probe capillary electrophoresis: analysis of recombinant human growth hormone with a fluorescent labeled antibody fragment. Anal Chem 1994;66:9-15.
    • (1994) Anal Chem , vol.66 , pp. 9-15
    • Shimura, K.1    Karger, B.L.2
  • 151
    • 0002221165 scopus 로고    scopus 로고
    • The avidin-biotin system
    • Diamandis, EP, Christopoulos TK, eds. San Diego, CA: Academic Press
    • Bayer EA, Wilchek M. The avidin-biotin system. In: Diamandis, EP, Christopoulos TK, eds. Immunoassay. San Diego, CA: Academic Press, 1996:237-67.
    • (1996) Immunoassay , pp. 237-267
    • Bayer, E.A.1    Wilchek, M.2
  • 152
    • 0032214640 scopus 로고    scopus 로고
    • Aptamers as ligands in affinity probe capillary electrophoresis
    • German I, Buchanan DD, Kennedy RT. Aptamers as ligands in affinity probe capillary electrophoresis. Anal Chem 1998;70:4540-5.
    • (1998) Anal Chem , vol.70 , pp. 4540-4545
    • German, I.1    Buchanan, D.D.2    Kennedy, R.T.3
  • 153
    • 0031559579 scopus 로고    scopus 로고
    • Inhibition of multiple thermostable DNA polymerases by a heterodimeric aptamer
    • Lin Y, Jayasena SD. Inhibition of multiple thermostable DNA polymerases by a heterodimeric aptamer. J Mol Biol 1997;271:100-11.
    • (1997) J Mol Biol , vol.271 , pp. 100-111
    • Lin, Y.1    Jayasena, S.D.2
  • 154
    • 0019304419 scopus 로고
    • A monoclonal antibody for large-scale purification of human leukocyte interferon
    • Secher DS, Burke DC. A monoclonal antibody for large-scale purification of human leukocyte interferon. Nature 1980;285:446-8.
    • (1980) Nature , vol.285 , pp. 446-448
    • Secher, D.S.1    Burke, D.C.2
  • 155
    • 0023707607 scopus 로고
    • Recombinant fragment assay for gene targetting based on the polymerase chain reaction
    • Kim HS, Smithies O. Recombinant fragment assay for gene targetting based on the polymerase chain reaction. Nucleic Acids Res 1988;16:8887-903.
    • (1988) Nucleic Acids Res , vol.16 , pp. 8887-8903
    • Kim, H.S.1    Smithies, O.2
  • 156
    • 0024637354 scopus 로고
    • A non-radioactive diagnostic test for the detection of HBV DNA sequences in serum at the single molecule level
    • Larzul D, Chevrier D, Guesdon JL. A non-radioactive diagnostic test for the detection of HBV DNA sequences in serum at the single molecule level. Mol Cell Probes 1989;3:45-57.
    • (1989) Mol Cell Probes , vol.3 , pp. 45-57
    • Larzul, D.1    Chevrier, D.2    Guesdon, J.L.3
  • 157
    • 0026603267 scopus 로고
    • Prevention of pre-PCR mis-priming and primer dimerization improves low-copy-number amplifications
    • Chou Q, Russel M, Birch DE, Raymond J, Bloch W. Prevention of pre-PCR mis-priming and primer dimerization improves low-copy-number amplifications. Nucleic Acids Res 1992;20:1717-23.
    • (1992) Nucleic Acids Res , vol.20 , pp. 1717-1723
    • Chou, Q.1    Russel, M.2    Birch, D.E.3    Raymond, J.4    Bloch, W.5
  • 159
    • 0027306157 scopus 로고
    • Increased PCR sensitivity by using paraffin wax as a reaction mix overlay
    • Herbert B, Bergeron J, Potworowski EF, Tijssen P. Increased PCR sensitivity by using paraffin wax as a reaction mix overlay. Mol Cell Probes 1993;7:249-52.
    • (1993) Mol Cell Probes , vol.7 , pp. 249-252
    • Herbert, B.1    Bergeron, J.2    Potworowski, E.F.3    Tijssen, P.4
  • 161
    • 0025297178 scopus 로고
    • Direct electrophoretic detection of the allelic state of single DNA molecules in human sperm by using the polymerase chain reaction
    • Li H, Cui X, Arnheim N. Direct electrophoretic detection of the allelic state of single DNA molecules in human sperm by using the polymerase chain reaction. Proc Natl Acad Sci U S A 1990;87:4580-4.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 4580-4584
    • Li, H.1    Cui, X.2    Arnheim, N.3
  • 162
    • 0028182432 scopus 로고
    • Taq Start antibody: "hot start" PCR facilitated by a neutralizing monoclonal antibody directed against Taq polymerase
    • Kellogg DE, Rabalkin I, Chen S, Mukhamedova N, Vlasik T, Siebert PD, et al. Taq Start antibody: "hot start" PCR facilitated by a neutralizing monoclonal antibody directed against Taq polymerase. Biotechniques 1994;16:1134-7.
    • (1994) Biotechniques , vol.16 , pp. 1134-1137
    • Kellogg, D.E.1    Rabalkin, I.2    Chen, S.3    Mukhamedova, N.4    Vlasik, T.5    Siebert, P.D.6
  • 164
    • 0025988479 scopus 로고
    • Reverse transcription and DNA amplification by a Thermus thermophilus DNA polymerase
    • Myers TW, Gelfand DH. Reverse transcription and DNA amplification by a Thermus thermophilus DNA polymerase. Biochemistry 1991;30:7661-6.
    • (1991) Biochemistry , vol.30 , pp. 7661-7766
    • Myers, T.W.1    Gelfand, D.H.2
  • 165
    • 0027232296 scopus 로고
    • Detection of res gene mutations in pancreatic juice and peripheral blood of patients with pancreatic adenocarcinoma
    • Tada M, Omata M, Kawai S, Saisho H, Ohto M, Saiki RK, et al. Detection of res gene mutations in pancreatic juice and peripheral blood of patients with pancreatic adenocarcinoma. Cancer Res 1993;53:2472-4.
    • (1993) Cancer Res , vol.53 , pp. 2472-2474
    • Tada, M.1    Omata, M.2    Kawai, S.3    Saisho, H.4    Ohto, M.5    Saiki, R.K.6
  • 166
    • 0001462757 scopus 로고
    • High output genetic mapping of polyploids using PCR generated markers
    • Sobral BW, Honeycutt RJ. High output genetic mapping of polyploids using PCR generated markers. Theor Appl Genet 1993;86:105-12.
    • (1993) Theor Appl Genet , vol.86 , pp. 105-112
    • Sobral, B.W.1    Honeycutt, R.J.2
  • 167
    • 0032212020 scopus 로고    scopus 로고
    • Bispecific antibodies as novel bioconjugates
    • Ceo Y, Suresh MR. Bispecific antibodies as novel bioconjugates. Bioconjug Chem 1998;9:635-44.
    • (1998) Bioconjug Chem , vol.9 , pp. 635-644
    • Ceo, Y.1    Suresh, M.R.2
  • 168
    • 0027423672 scopus 로고
    • Synthesis and interaction of oligodeoxyribonucleotides containing 2′-amino-2′-deoxyuridine
    • Miller PS, Bham P, Kan L-S. Synthesis and interaction of oligodeoxyribonucleotides containing 2′-amino-2′-deoxyuridine. Nucleosides Nucleotides 1993;12:785-92.
    • (1993) Nucleosides Nucleotides , vol.12 , pp. 785-792
    • Miller, P.S.1    Bham, P.2    Kan, L.-S.3
  • 169
    • 0029814604 scopus 로고    scopus 로고
    • High-affinity and specific recognition of human thyroid stimulating hormone (hTSH) Dy in vitro selected 2′-amino-modified RNA
    • Lin Y, Nieuwlandt D, Magallanez A, Feistner B, Jayasena SD. High-affinity and specific recognition of human thyroid stimulating hormone (hTSH) Dy in vitro selected 2'-amino-modified RNA. Nucleic Acids Res 1996;24:3407-14.
    • (1996) Nucleic Acids Res , vol.24 , pp. 3407-3414
    • Lin, Y.1    Nieuwlandt, D.2    Magallanez, A.3    Feistner, B.4    Jayasena, S.D.5
  • 172
    • 0027216959 scopus 로고
    • Monoclonal antibodies to human chorionic gonadotropin (HCG) and their use in two-site binding enzyme immunoassays
    • Bottger V, Micheel B, Scharte G, Kaiser G, Wolf G, Schmechta H. Monoclonal antibodies to human chorionic gonadotropin (HCG) and their use in two-site binding enzyme immunoassays. Hybridoma 1993;12:81-91.
    • (1993) Hybridoma , vol.12 , pp. 81-91
    • Bottger, V.1    Micheel, B.2    Scharte, G.3    Kaiser, G.4    Wolf, G.5    Schmechta, H.6
  • 173
    • 0023231282 scopus 로고
    • Ultrasensitive immunoradiometric assay for chorionic gonadotropin which does not cross-react with luteinizing hormone nor free β chain of hCG and which detects hCG in blood of non-pregnant humans
    • Griffin J, Odell WD. Ultrasensitive immunoradiometric assay for chorionic gonadotropin which does not cross-react with luteinizing hormone nor free β chain of hCG and which detects hCG in blood of non-pregnant humans. J Immunol Methods 1987;103:275-83.
    • (1987) J Immunol Methods , vol.103 , pp. 275-283
    • Griffin, J.1    Odell, W.D.2
  • 174
    • 0027064888 scopus 로고
    • Dual regulation of vascular endothelial growth factor bioavailability by genetic and proteolytic mechanisms
    • Houck KA, Leung DW, Rowland AM, Winer J, Ferrara N. Dual regulation of vascular endothelial growth factor bioavailability by genetic and proteolytic mechanisms. J Biol Chem 1992;267:26031-7.
    • (1992) J Biol Chem , vol.267 , pp. 26031-26037
    • Houck, K.A.1    Leung, D.W.2    Rowland, A.M.3    Winer, J.4    Ferrara, N.5
  • 175
    • 0030669030 scopus 로고    scopus 로고
    • Exploring the metabolic and genetic control of gene expression on a genomic scale
    • DeRisi JL, Iyer VR, Brown PO. Exploring the metabolic and genetic control of gene expression on a genomic scale. Science 1997;278:680-6.
    • (1997) Science , vol.278 , pp. 680-686
    • DeRisi, J.L.1    Iyer, V.R.2    Brown, P.O.3
  • 176
    • 0033040986 scopus 로고    scopus 로고
    • Proteomics: Translating genomics into products?
    • Dove A. Proteomics: translating genomics into products? Nat Biotechnol 1999;17:233-6.
    • (1999) Nat Biotechnol , vol.17 , pp. 233-236
    • Dove, A.1
  • 177
    • 0023651444 scopus 로고
    • Oligoribo-nucleotide synthesis using T7 RNA polymerase and synthetic DNA templates
    • Milligan JF, Groebe DR, Witherell GW, Uhlenbeck OC. Oligoribo-nucleotide synthesis using T7 RNA polymerase and synthetic DNA templates. Nucleic Acids Res 1987;15:8783-98.
    • (1987) Nucleic Acids Res , vol.15 , pp. 8783-8798
    • Milligan, J.F.1    Groebe, D.R.2    Witherell, G.W.3    Uhlenbeck, O.C.4
  • 178
    • 85045502002 scopus 로고
    • Randomization of genes by PCR mutagenesis
    • Cadwell RC, Joyce GF. Randomization of genes by PCR mutagenesis. PCR Methods Appl 1992;2:28-33.
    • (1992) PCR Methods Appl , vol.2 , pp. 28-33
    • Cadwell, R.C.1    Joyce, G.F.2
  • 179
    • 0029869449 scopus 로고    scopus 로고
    • An approach to random mutagenesis of DNA using mixtures of triphosphate derivatives of nucleoside analogues
    • Zaccolo M, Williams DM, Brown DM, Gherardi E. An approach to random mutagenesis of DNA using mixtures of triphosphate derivatives of nucleoside analogues. J Mol Biol 1996;255:589-603.
    • (1996) J Mol Biol , vol.255 , pp. 589-603
    • Zaccolo, M.1    Williams, D.M.2    Brown, D.M.3    Gherardi, E.4
  • 180
    • 0029999325 scopus 로고    scopus 로고
    • Hypermutagenic PCR involving all four transitions and a sizable proportion of transversions
    • Vartanian J-P, Henry M, Wain-Hobson S. Hypermutagenic PCR involving all four transitions and a sizable proportion of transversions. Nucleic Acids Res 1996;24:2627-31.
    • (1996) Nucleic Acids Res , vol.24 , pp. 2627-2631
    • Vartanian, J.-P.1    Henry, M.2    Wain-Hobson, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.