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Volumn 53, Issue 16, 2010, Pages 6018-6027

Strategies for recognition of stem-loop RNA structures by synthetic ligands: Application to the HIV-1 frameshift stimulatory sequence

Author keywords

[No Author keywords available]

Indexed keywords

2 ETHYL 3 CARBOXYQUINOLINE DERIVATIVE; 2 ETHYLQUINOLINE 3 CARBOXAMIDE; 2 ETHYLQUINOLINE 3 CARBOXYLIC ACID; ALKENE; AMIDE; CARBOXYLIC ACID DERIVATIVE; DISULFIDE; GAG PROTEIN; MITOMYCIN C; NEOMYCIN; POL PROTEIN; QUINOLINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 77955904335     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm100231t     Document Type: Article
Times cited : (30)

References (71)
  • 1
    • 0142011647 scopus 로고    scopus 로고
    • Targeting RNA with small molecules
    • For reviews, see
    • For reviews, see: Tor, Y. Targeting RNA with small molecules ChemBioChem 2003, 4, 998-1007
    • (2003) ChemBioChem , vol.4 , pp. 998-1007
    • Tor, Y.1
  • 2
    • 43149103943 scopus 로고    scopus 로고
    • Targeting RNA with small molecules
    • Thomas, J. R.; Hergenrother, P. J. Targeting RNA with small molecules Chem. Rev. 2008, 108, 1171-1224
    • (2008) Chem. Rev. , vol.108 , pp. 1171-1224
    • Thomas, J.R.1    Hergenrother, P.J.2
  • 3
    • 0344641913 scopus 로고    scopus 로고
    • Sequence-specific DNA recognition by polyamides
    • Dervan, P. B.; Bürli, R. W. Sequence-specific DNA recognition by polyamides Curr. Opin. Chem. Biol. 1999, 3, 688-693
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 688-693
    • Dervan, P.B.1    Bürli, R.W.2
  • 4
    • 67650527061 scopus 로고    scopus 로고
    • Synthesis at the molecular frontier
    • Wender, P. A.; Miller, B. L. Synthesis at the molecular frontier Nature 2009, 460, 197-201
    • (2009) Nature , vol.460 , pp. 197-201
    • Wender, P.A.1    Miller, B.L.2
  • 5
    • 36749088862 scopus 로고    scopus 로고
    • HIV drug development: The next 25 years
    • Flexner, C. HIV drug development: the next 25 years Nat. Rev. Drug Discovery 2007, 6, 959-966
    • (2007) Nat. Rev. Drug Discovery , vol.6 , pp. 959-966
    • Flexner, C.1
  • 6
    • 35348992176 scopus 로고    scopus 로고
    • Protease inhibitor resistance in HIV-infected patients: Molecular and clinical perspectives
    • Martinez-Cajas, J. L.; Wainberg, M. A. Protease inhibitor resistance in HIV-infected patients: molecular and clinical perspectives Antiviral Res. 2007, 76, 203-221
    • (2007) Antiviral Res. , vol.76 , pp. 203-221
    • Martinez-Cajas, J.L.1    Wainberg, M.A.2
  • 7
    • 0028120730 scopus 로고
    • HIV resistance to reverse transcriptase inhibitors
    • De Clercq, E. HIV resistance to reverse transcriptase inhibitors Biochem. Pharmacol. 1994, 47, 155-169
    • (1994) Biochem. Pharmacol. , vol.47 , pp. 155-169
    • De Clercq, E.1
  • 8
    • 20644469472 scopus 로고    scopus 로고
    • Antiretroviral therapies for treatment-experienced patients: Current status and research challenges
    • Struble, K.; Murray, J.; Cheng, B.; Gegeny, T.; Miller, V.; Gulick, R. Antiretroviral therapies for treatment-experienced patients: current status and research challenges AIDS 2005, 19, 747-756
    • (2005) AIDS , vol.19 , pp. 747-756
    • Struble, K.1    Murray, J.2    Cheng, B.3    Gegeny, T.4    Miller, V.5    Gulick, R.6
  • 9
    • 0027370433 scopus 로고
    • Small molecules that selectively block RNA binding of HIV-1 Rev protein inhibit Rev function and viral production
    • Zapp, M. L.; Stern, S.; Green, M. R. Small molecules that selectively block RNA binding of HIV-1 Rev protein inhibit Rev function and viral production Cell 1993, 74, 969-978
    • (1993) Cell , vol.74 , pp. 969-978
    • Zapp, M.L.1    Stern, S.2    Green, M.R.3
  • 11
    • 0034624435 scopus 로고    scopus 로고
    • Neomycin-acridine conjugate: A potent inhibitor of Rev-RRE binding
    • Kirk, S. R.; Luedtke, N. W.; Tor, Y. Neomycin-acridine conjugate: a potent inhibitor of Rev-RRE binding J. Am. Chem. Soc. 2000, 122, 980-981
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 980-981
    • Kirk, S.R.1    Luedtke, N.W.2    Tor, Y.3
  • 12
    • 0030985913 scopus 로고    scopus 로고
    • Direct observation of aminoglycoside-RNA interactions by surface plasmon resonance
    • Hendrix, M.; Priestley, E. S.; Joyce, G. F.; Wong, C. H. Direct observation of aminoglycoside-RNA interactions by surface plasmon resonance J. Am. Chem. Soc. 1997, 119, 3641-3648
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 3641-3648
    • Hendrix, M.1    Priestley, E.S.2    Joyce, G.F.3    Wong, C.H.4
  • 13
    • 0032491152 scopus 로고    scopus 로고
    • Inhibitors of protein-RNA complexation that target the RNA: Specific recognition of human immunodeficiency virus type 1 TAR RNA by small organic molecules
    • Mei, H. Y.; Cui, M.; Heldsinger, A.; Lemrow, S. M.; Loo, J. A.; Sannes-Lowery, K. A.; Sharmeen, L.; Czarnik, A. W. Inhibitors of protein-RNA complexation that target the RNA: specific recognition of human immunodeficiency virus type 1 TAR RNA by small organic molecules Biochemistry 1998, 37, 14204-14212
    • (1998) Biochemistry , vol.37 , pp. 14204-14212
    • Mei, H.Y.1    Cui, M.2    Heldsinger, A.3    Lemrow, S.M.4    Loo, J.A.5    Sannes-Lowery, K.A.6    Sharmeen, L.7    Czarnik, A.W.8
  • 15
  • 18
    • 0023870815 scopus 로고
    • Characterization of ribosomal frameshifting in HIV-1 gag-pol expression
    • Jacks, T.; Power, M. D.; Masiarz, F. R.; Luciw, P. A.; Barr, P. J.; Varmus, H. E. Characterization of ribosomal frameshifting in HIV-1 gag-pol expression Nature 1988, 331, 280-283
    • (1988) Nature , vol.331 , pp. 280-283
    • Jacks, T.1    Power, M.D.2    Masiarz, F.R.3    Luciw, P.A.4    Barr, P.J.5    Varmus, H.E.6
  • 19
    • 0026717107 scopus 로고
    • Human immunodeficiency virus type 1 gag-pol frameshifting is dependent on downstream mRNA secondary structure: Demonstration by expression in vivo
    • Parkin, N. T.; Chamorro, M; Varmus, H. E. Human immunodeficiency virus type 1 gag-pol frameshifting is dependent on downstream mRNA secondary structure: demonstration by expression in vivo J. Virol. 1992, 66, 5147-5151
    • (1992) J. Virol. , vol.66 , pp. 5147-5151
    • Parkin, N.T.1    Chamorro, M.2    Varmus, H.E.3
  • 20
    • 0026018243 scopus 로고
    • Overexpression of the gag-pol precursor from human immunodeficiency virus type 1 proviral genomes results in efficient proteolytic processing in the absence of virion production
    • Park, J.; Morrow, C. D. Overexpression of the gag-pol precursor from human immunodeficiency virus type 1 proviral genomes results in efficient proteolytic processing in the absence of virion production J. Virol. 1991, 65, 5111-5117
    • (1991) J. Virol. , vol.65 , pp. 5111-5117
    • Park, J.1    Morrow, C.D.2
  • 21
    • 0027214941 scopus 로고
    • Overexpression of the HIV-1 gag-pol polyprotein results in intracellular activation of HIV-1 protease and inhibition of assembly and budding of virus-like particles
    • Karacostas, V.; Wolffe, E. J.; Nagashima, K.; Gonda, M. A.; Moss, B. Overexpression of the HIV-1 gag-pol polyprotein results in intracellular activation of HIV-1 protease and inhibition of assembly and budding of virus-like particles Virology 1993, 193, 661-671
    • (1993) Virology , vol.193 , pp. 661-671
    • Karacostas, V.1    Wolffe, E.J.2    Nagashima, K.3    Gonda, M.A.4    Moss, B.5
  • 22
    • 0031901133 scopus 로고    scopus 로고
    • Importance of ribosomal frameshifting for human immunodeficiency virus type 1 particle assembly and replication
    • Hung, M.; Patel, P.; Davis, S.; Green, S. R. Importance of ribosomal frameshifting for human immunodeficiency virus type 1 particle assembly and replication J. Virol. 1998, 72, 4819-4824
    • (1998) J. Virol. , vol.72 , pp. 4819-4824
    • Hung, M.1    Patel, P.2    Davis, S.3    Green, S.R.4
  • 23
    • 0035138477 scopus 로고    scopus 로고
    • Maintenance of the Gag/Gag-Pol ratio is important for human immunodeficiency virus type 1 RNA dimerization and viral infectivity
    • Shehu-Xhilaga, M.; Crowe, S. M.; Mak, J. Maintenance of the Gag/Gag-Pol ratio is important for human immunodeficiency virus type 1 RNA dimerization and viral infectivity J. Virol. 2001, 75, 1834-1841
    • (2001) J. Virol. , vol.75 , pp. 1834-1841
    • Shehu-Xhilaga, M.1    Crowe, S.M.2    Mak, J.3
  • 24
    • 30844443739 scopus 로고    scopus 로고
    • Decreasing the frameshift efficiency translates into an equivalent reduction of the replication of the human immunodeficiency virus type 1
    • Dulude, D.; Berchiche, Y. A.; Gendron, K.; Brakier-Gingras, L.; Heveker, N. Decreasing the frameshift efficiency translates into an equivalent reduction of the replication of the human immunodeficiency virus type 1 Virology 2006, 345, 127-136
    • (2006) Virology , vol.345 , pp. 127-136
    • Dulude, D.1    Berchiche, Y.A.2    Gendron, K.3    Brakier-Gingras, L.4    Heveker, N.5
  • 25
    • 0036924931 scopus 로고    scopus 로고
    • Characterization of the frameshift stimulatory signal controlling a programmed -1 ribosomal frameshift in the human immunodeficiency virus type 1
    • Dulude, D.; Baril, M.; Brakier-Gingras, L. Characterization of the frameshift stimulatory signal controlling a programmed -1 ribosomal frameshift in the human immunodeficiency virus type 1 Nucleic Acids Res. 2002, 30, 5094-5102
    • (2002) Nucleic Acids Res. , vol.30 , pp. 5094-5102
    • Dulude, D.1    Baril, M.2    Brakier-Gingras, L.3
  • 26
    • 0036314316 scopus 로고    scopus 로고
    • Analysis of natural variants of the human immunodeficiency virus type 1 gag-pol frameshift stem-loop structure
    • Telenti, A.; Martinez, R.; Munoz, M.; Bleiber, G.; Greub, G.; Sanglard, D.; Peters, S. Analysis of natural variants of the human immunodeficiency virus type 1 gag-pol frameshift stem-loop structure J. Virol. 2002, 76, 7868-7873
    • (2002) J. Virol. , vol.76 , pp. 7868-7873
    • Telenti, A.1    Martinez, R.2    Munoz, M.3    Bleiber, G.4    Greub, G.5    Sanglard, D.6    Peters, S.7
  • 27
    • 0141631892 scopus 로고    scopus 로고
    • Efficiency of a programmed -1 ribosomal frameshift in the different subtypes of the human immunodeficiency virus type 1 group M
    • Baril, M.; Dulude, D.; Gendron, K.; Lemay, G.; Brakier-Gingras, L. Efficiency of a programmed -1 ribosomal frameshift in the different subtypes of the human immunodeficiency virus type 1 group M RNA 2003, 9, 1246-1253
    • (2003) RNA , vol.9 , pp. 1246-1253
    • Baril, M.1    Dulude, D.2    Gendron, K.3    Lemay, G.4    Brakier-Gingras, L.5
  • 28
    • 0031901133 scopus 로고    scopus 로고
    • Importance of ribosomal frameshifting for human immunodeficiency virus type 1 particle assembly and replication
    • Hung, M.; Patel, P.; Davis, S.; Green, S. R. Importance of ribosomal frameshifting for human immunodeficiency virus type 1 particle assembly and replication J. Virol. 1998, 72, 4819-4824
    • (1998) J. Virol. , vol.72 , pp. 4819-4824
    • Hung, M.1    Patel, P.2    Davis, S.3    Green, S.R.4
  • 29
    • 62249145571 scopus 로고    scopus 로고
    • Ribosomal frameshifting: An emerging target in HIV
    • Gareiss, P. C.; Miller, B. L. Ribosomal frameshifting: an emerging target in HIV Curr. Opin. Invest. Drugs 2009, 10, 121-128
    • (2009) Curr. Opin. Invest. Drugs , vol.10 , pp. 121-128
    • Gareiss, P.C.1    Miller, B.L.2
  • 30
    • 0041660967 scopus 로고    scopus 로고
    • Solution structure of the HIV-1 frameshift inducing stem-loop RNA
    • Staple, D. W.; Butcher, S. E. Solution structure of the HIV-1 frameshift inducing stem-loop RNA Nucleic Acids Res. 2003, 31, 4326-4331
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4326-4331
    • Staple, D.W.1    Butcher, S.E.2
  • 31
    • 20344397919 scopus 로고    scopus 로고
    • Solution structure and thermodynamic investigation of the HIV-1 frameshift inducing element
    • Staple, D. W.; Butcher, S. E. Solution structure and thermodynamic investigation of the HIV-1 frameshift inducing element J. Mol. Biol. 2005, 349, 1011
    • (2005) J. Mol. Biol. , vol.349 , pp. 1011
    • Staple, D.W.1    Butcher, S.E.2
  • 33
    • 36749056800 scopus 로고    scopus 로고
    • Characterization of the mechanical unfolding of RNA pseudoknots
    • Green, L.; Kim, C.-H.; Bustamante, C.; Tinoco, I. Characterization of the mechanical unfolding of RNA pseudoknots J. Mol. Biol. 2008, 375, 511-528
    • (2008) J. Mol. Biol. , vol.375 , pp. 511-528
    • Green, L.1    Kim, C.-H.2    Bustamante, C.3    Tinoco, I.4
  • 34
    • 69149104281 scopus 로고    scopus 로고
    • Triplex structures in an RNA pseudoknot enhance mechanical stability and increase efficiency of -1 ribosomal frameshifting
    • Chen, G.; Chang, K.; Chou, M.; Bustamante, C.; Tinoco, I. Triplex structures in an RNA pseudoknot enhance mechanical stability and increase efficiency of -1 ribosomal frameshifting Proc. Natl. Acad. Sci. U.S.A. 2009, 106, 12706-12711
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 12706-12711
    • Chen, G.1    Chang, K.2    Chou, M.3    Bustamante, C.4    Tinoco, I.5
  • 36
    • 35048828472 scopus 로고    scopus 로고
    • Identification of a selective small-molecule ligand for HIV-1 frameshift-inducing stem-loop RNA from an 11,325 member resin bound dynamic combinatorial library
    • McNaughton, B. R.; Gareiss, P. C.; Miller, B. L. Identification of a selective small-molecule ligand for HIV-1 frameshift-inducing stem-loop RNA from an 11,325 member resin bound dynamic combinatorial library J. Am. Chem. Soc. 2007, 129, 11306-11307
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 11306-11307
    • McNaughton, B.R.1    Gareiss, P.C.2    Miller, B.L.3
  • 37
    • 0027523654 scopus 로고
    • Solution structure of a complex between [N-MeCys3,N-MeCys7]TANDEM and [d(GATATC)]2
    • Addess, K. J.; Sinsheimer, J. S.; Feigon, J. Solution structure of a complex between [N-MeCys3,N-MeCys7]TANDEM and [d(GATATC)]2 Biochemistry 1993, 32, 2498-2508
    • (1993) Biochemistry , vol.32 , pp. 2498-2508
    • Addess, K.J.1    Sinsheimer, J.S.2    Feigon, J.3
  • 38
    • 0028092080 scopus 로고
    • Sequence specificity of quinoxaline antibiotics. 1. Solution structure of a 1:1 complex between triostin A and [d(GACGTC)]2 and comparison with the solution structure of the [N-MeCys3,N-MeCys7]TANDEM-[d(GATATC)]2 complex
    • Addess, K. J.; Feigon, J. Sequence specificity of quinoxaline antibiotics. 1. Solution structure of a 1:1 complex between triostin A and [d(GACGTC)]2 and comparison with the solution structure of the [N-MeCys3,N-MeCys7]TANDEM-[d(GATATC)]2 complex Biochemistry 1994, 33, 12386-12397
    • (1994) Biochemistry , vol.33 , pp. 12386-12397
    • Addess, K.J.1    Feigon, J.2
  • 40
    • 70350167221 scopus 로고    scopus 로고
    • Selection and characterization of small molecules that bind the HIV-1 frameshift site RNA
    • Marcheschi, R. J.; Mouzakis, K. D.; Butcher, S. E. Selection and characterization of small molecules that bind the HIV-1 frameshift site RNA ACS Chem. Biol. 2009, 4, 844-854
    • (2009) ACS Chem. Biol. , vol.4 , pp. 844-854
    • Marcheschi, R.J.1    Mouzakis, K.D.2    Butcher, S.E.3
  • 41
    • 42449084551 scopus 로고    scopus 로고
    • Selection of peptides interfering with a ribosomal frameshift in the human immunodeficiency virus type 1
    • Dulude, D.; Théberge-Julien, G.; Brakier-Gringras, L.; Heveker, N. Selection of peptides interfering with a ribosomal frameshift in the human immunodeficiency virus type 1 RNA 2008, 14, 981-991
    • (2008) RNA , vol.14 , pp. 981-991
    • Dulude, D.1    Théberge-Julien, G.2    Brakier-Gringras, L.3    Heveker, N.4
  • 42
    • 0033773876 scopus 로고    scopus 로고
    • Understanding the genetic diversity of HIV-1
    • McCutchan, F. E. Understanding the genetic diversity of HIV-1 AIDS 2000, 14, S31-S44
    • (2000) AIDS , vol.14
    • McCutchan, F.E.1
  • 44
    • 3342967467 scopus 로고    scopus 로고
    • Deoxystreptamine dimers bind to RNA hairpin loops
    • Liu, X.; Thomas, J. R.; Hergenrother, P. J. Deoxystreptamine dimers bind to RNA hairpin loops J. Am. Chem. Soc. 2004, 126, 9196-9197
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 9196-9197
    • Liu, X.1    Thomas, J.R.2    Hergenrother, P.J.3
  • 45
    • 0033579844 scopus 로고    scopus 로고
    • RNA-aminoglycoside antibiotic interactions: Fluorescence detection of binding and conformational change
    • Llano-Sotelo, B.; Chow, C. S. RNA-aminoglycoside antibiotic interactions: Fluorescence detection of binding and conformational change Bioorg. Med. Chem. Lett. 1999, 9, 213-216
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 213-216
    • Llano-Sotelo, B.1    Chow, C.S.2
  • 46
    • 0141483331 scopus 로고    scopus 로고
    • RNA-ligand interactions: Affinity and specificity of aminoglycoside dimers and acridine conjugates to the HIV-1 Rev response element
    • Luedtke, N. W.; Liu, Q.; Tor, Y. RNA-ligand interactions: affinity and specificity of aminoglycoside dimers and acridine conjugates to the HIV-1 Rev response element Biochemistry 2003, 42, 11391-11403
    • (2003) Biochemistry , vol.42 , pp. 11391-11403
    • Luedtke, N.W.1    Liu, Q.2    Tor, Y.3
  • 47
    • 0034829399 scopus 로고    scopus 로고
    • RNA-selective coordination complexes identified via dynamic combinatorial chemistry
    • Sequence 10
    • Sequence 10: Karan, C.; Miller, B. L. RNA-selective coordination complexes identified via dynamic combinatorial chemistry J. Am. Chem. Soc. 2001, 123, 7455-7456
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 7455-7456
    • Karan, C.1    Miller, B.L.2
  • 48
    • 57149094863 scopus 로고    scopus 로고
    • Dynamic combinatorial selection of small molecules capable of inhibiting the (CUG) repeat RNA-MBNL1 interaction in vitro: Discovery of lead compounds targeting myotonic dystrophy (DM1)
    • Sequence 11
    • Sequence 11: Gareiss, P. C.; Sobczak, K.; McNaughton, B. R.; Palde, P. B.; Thornton, C. A.; Miller, B. L. Dynamic combinatorial selection of small molecules capable of inhibiting the (CUG) repeat RNA-MBNL1 interaction in vitro: discovery of lead compounds targeting myotonic dystrophy (DM1) J. Am. Chem. Soc. 2008, 130, 16254-16261
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 16254-16261
    • Gareiss, P.C.1    Sobczak, K.2    McNaughton, B.R.3    Palde, P.B.4    Thornton, C.A.5    Miller, B.L.6
  • 49
    • 33847087446 scopus 로고
    • Rate constants and equilibrium constants for thiol-disulfide interchange reactions involving oxidized glutathione
    • Szajewski, R. P.; Whitesides, G. M. Rate constants and equilibrium constants for thiol-disulfide interchange reactions involving oxidized glutathione J. Am. Chem. Soc. 1980, 102, 2011-2026
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 2011-2026
    • Szajewski, R.P.1    Whitesides, G.M.2
  • 50
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang, C.; Sinskey, A. J.; Lodish, H. F. Oxidized redox state of glutathione in the endoplasmic reticulum Science 1992, 257, 1496-1502
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 52
    • 0037900064 scopus 로고    scopus 로고
    • Synthesis of biologically active dicarba analogues of the peptide hormone oxytocin using ring-closing metathesis
    • Stymiest, J. L.; Mitchell, B. F.; Wong, S.; Vederas, J. C. Synthesis of biologically active dicarba analogues of the peptide hormone oxytocin using ring-closing metathesis Org. Lett. 2003, 5, 47-49
    • (2003) Org. Lett. , vol.5 , pp. 47-49
    • Stymiest, J.L.1    Mitchell, B.F.2    Wong, S.3    Vederas, J.C.4
  • 53
    • 33947651297 scopus 로고    scopus 로고
    • Dicarba analogues of the cyclic enkephalin peptides H-Tyr-c[D-Cys-Gly- Phe-D(or L)-Cys]NH(2) retain high opioid activity
    • Berezowska, I.; Chung, N. N.; Lemieux, C.; Wilkes, B. C.; Schiller, P. W. Dicarba analogues of the cyclic enkephalin peptides H-Tyr-c[D-Cys-Gly-Phe-D(or L)-Cys]NH(2) retain high opioid activity J. Med. Chem. 2007, 50, 1414-1417
    • (2007) J. Med. Chem. , vol.50 , pp. 1414-1417
    • Berezowska, I.1    Chung, N.N.2    Lemieux, C.3    Wilkes, B.C.4    Schiller, P.W.5
  • 54
    • 34347270982 scopus 로고    scopus 로고
    • Synthesis of stable and potent delta/mu opioid peptides: Analogues of H-Tyr-c[D-Cys-Gly-Phe-D-Cys]-OH by ring-closing metathesis
    • Mollica, A.; Guardiani, G.; Davis, P.; Ma, S.; Porreca, F.; Lai, J.; Mannina, L.; Sobolev, A. P.; Hruby, V. J. Synthesis of stable and potent delta/mu opioid peptides: analogues of H-Tyr-c[D-Cys-Gly-Phe-D-Cys]-OH by ring-closing metathesis J. Med. Chem. 2007, 50, 3138-3142
    • (2007) J. Med. Chem. , vol.50 , pp. 3138-3142
    • Mollica, A.1    Guardiani, G.2    Davis, P.3    Ma, S.4    Porreca, F.5    Lai, J.6    Mannina, L.7    Sobolev, A.P.8    Hruby, V.J.9
  • 55
    • 0034602053 scopus 로고    scopus 로고
    • Target-accelerated combinatorial synthesis and discovery of highly potent antibiotics effective against vancomycin-resistant bacteria
    • Nicolaou, K. C.; Hughes, R.; Cho, S. Y.; Winssinger, N.; Smethurst, C.; Labischinski, H.; Endermann, R. Target-accelerated combinatorial synthesis and discovery of highly potent antibiotics effective against vancomycin-resistant bacteria Angew. Chem., Int. Ed. 2000, 39, 3823-3828
    • (2000) Angew. Chem., Int. Ed. , vol.39 , pp. 3823-3828
    • Nicolaou, K.C.1    Hughes, R.2    Cho, S.Y.3    Winssinger, N.4    Smethurst, C.5    Labischinski, H.6    Endermann, R.7
  • 56
    • 36049015757 scopus 로고    scopus 로고
    • The remarkable metal-catalysed olefin metathesis reaction
    • Hoveyda, A. H.; Zhugralin, A. R. The remarkable metal-catalysed olefin metathesis reaction Nature 2007, 250, 243-251
    • (2007) Nature , vol.250 , pp. 243-251
    • Hoveyda, A.H.1    Zhugralin, A.R.2
  • 58
    • 25444514293 scopus 로고    scopus 로고
    • Synthesis of oxytocin analogues with replacement of sulfur by carbon gives potent antagonists with increased stability
    • Stymiest, J. L.; Mitchell, B. F.; Wong, S.; Vederas, J. C. Synthesis of oxytocin analogues with replacement of sulfur by carbon gives potent antagonists with increased stability J. Org. Chem. 2005, 70, 7799-7809
    • (2005) J. Org. Chem. , vol.70 , pp. 7799-7809
    • Stymiest, J.L.1    Mitchell, B.F.2    Wong, S.3    Vederas, J.C.4
  • 59
    • 14844362056 scopus 로고    scopus 로고
    • Self-selection in olefin cross metathesis: The effect of remote functionality
    • McNaughton, B. R.; Bucholtz, K. M.; Camaano-Moure, A.; Miller, B. L. Self-selection in olefin cross metathesis: the effect of remote functionality Org. Lett. 2005, 7, 733-736
    • (2005) Org. Lett. , vol.7 , pp. 733-736
    • McNaughton, B.R.1    Bucholtz, K.M.2    Camaano-Moure, A.3    Miller, B.L.4
  • 60
    • 0033617465 scopus 로고    scopus 로고
    • Greatly simplified procedures for the synthesis of alpha-amino acids by the direct alkylation of pseudoephedrine glycinamide hydrate
    • Myers, A. G.; Schnider, P.; Kwon, S.; Kung, D. W. Greatly simplified procedures for the synthesis of alpha-amino acids by the direct alkylation of pseudoephedrine glycinamide hydrate J. Org. Chem. 1999, 64, 3322-3327
    • (1999) J. Org. Chem. , vol.64 , pp. 3322-3327
    • Myers, A.G.1    Schnider, P.2    Kwon, S.3    Kung, D.W.4
  • 61
    • 27144462310 scopus 로고    scopus 로고
    • Convenient access to glutamic acid side chain homologues compatible with solid phase peptide synthesis
    • Ryan, S. J.; Zhang, Y.; Kennan, A. J. Convenient access to glutamic acid side chain homologues compatible with solid phase peptide synthesis Org. Lett. 2005, 7, 4765-4767
    • (2005) Org. Lett. , vol.7 , pp. 4765-4767
    • Ryan, S.J.1    Zhang, Y.2    Kennan, A.J.3
  • 63
    • 4544381198 scopus 로고    scopus 로고
    • Biochemical mechanisms of drug action: What does it take for success?
    • Swinney, D. C. Biochemical mechanisms of drug action: what does it take for success? Nat. Rev. Drug Discovery 2004, 3, 801-808
    • (2004) Nat. Rev. Drug Discovery , vol.3 , pp. 801-808
    • Swinney, D.C.1
  • 64
    • 33748325882 scopus 로고    scopus 로고
    • Drug-target residence time and its implications for lead optimization
    • Copeland, R. A.; Pompliano, D. L.; Meek, T. D. Drug-target residence time and its implications for lead optimization Nat. Rev. Drug Discovery 2006, 5, 730-739
    • (2006) Nat. Rev. Drug Discovery , vol.5 , pp. 730-739
    • Copeland, R.A.1    Pompliano, D.L.2    Meek, T.D.3
  • 65
    • 37049036372 scopus 로고    scopus 로고
    • Binding kinetics of darunavir to human immunodeficiency virus type 1 protease explain the potent antiviral activity and high genetic barrier
    • Dierynck, I.; De Wit, M.; Gustin, E.; Keuleers, I.; Vandersmissen, J.; Hallenberger, S.; Hertogs, K. Binding kinetics of darunavir to human immunodeficiency virus type 1 protease explain the potent antiviral activity and high genetic barrier J. Virol. 2007, 81, 13845-13851
    • (2007) J. Virol. , vol.81 , pp. 13845-13851
    • Dierynck, I.1    De Wit, M.2    Gustin, E.3    Keuleers, I.4    Vandersmissen, J.5    Hallenberger, S.6    Hertogs, K.7
  • 66
    • 0030985913 scopus 로고    scopus 로고
    • Direct observation of aminoglycoside-RNA interactions by surface plasmon resonance
    • Hendrix, M.; Priestley, E. S.; Joyce, G. F.; Wong, C. H. Direct observation of aminoglycoside-RNA interactions by surface plasmon resonance J. Am. Chem. Soc. 1997, 119, 3641-3648
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 3641-3648
    • Hendrix, M.1    Priestley, E.S.2    Joyce, G.F.3    Wong, C.H.4
  • 68
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann, T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays J. Immunol. Methods 1983, 65, 55-63
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 71
    • 0035799891 scopus 로고    scopus 로고
    • A convenient method for the efficient removal of ruthenium byproducts generated during olefin metathesis reactions
    • Ahn, Y. M.; Yang, K.; Georg, G. I. A convenient method for the efficient removal of ruthenium byproducts generated during olefin metathesis reactions Org. Lett. 2001, 3, 1411-1413
    • (2001) Org. Lett. , vol.3 , pp. 1411-1413
    • Ahn, Y.M.1    Yang, K.2    Georg, G.I.3


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