메뉴 건너뛰기




Volumn 1808, Issue 8, 2011, Pages 2051-2058

5- and 4′-Hydroxylated flavonoids affect voltage gating of single alpha-hemolysin pore

Author keywords

Alpha hemolysin channel; Channel voltage gating; Dipole potential modifiers; Flavonoids; Planar lipid bilayers

Indexed keywords

2',4',6' TRIHYDROXY ACETOPHENONE; 4 [4 [4 (4 DIBUTYLAMINOPHENYL) 1,3 BUTADIENYL]PYRIDINIO] 1 BUTANESULFONIC ACID; 6 OXOCHOLESTANOL; ALPHA HEMOLYSIN; AMINO ACID; BIOCHANIN A; CATECHIN; DAIDZEIN; FLAVONOID; GENISTEIN; GENISTIN; MYRICETIN; PHLORETIN; PHLORIZIN; QUERCETIN; ROSE BENGAL; TAXIFOLIN; UNCLASSIFIED DRUG; BACTERIAL TOXIN; HEMOLYSIN; MEMBRANE LIPID; STAPHYLOCOCCAL ALPHA-TOXIN; STAPHYLOCOCCUS ALPHA TOXIN;

EID: 79958089942     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2011.04.005     Document Type: Article
Times cited : (20)

References (61)
  • 1
    • 0015610693 scopus 로고
    • Effects of staphylococcal-toxin on the structure of erythrocyte membranes: A biochemical and freeze-etching study
    • J.H. Freer, J.P. Arbuthnott, and B. Billcliffe Effects of staphylococcal-toxin on the structure of erythrocyte membranes: a biochemical and freeze-etching study J. Gen. Microbiol. 75 1973 321 332
    • (1973) J. Gen. Microbiol. , vol.75 , pp. 321-332
    • Freer, J.H.1    Arbuthnott, J.P.2    Billcliffe, B.3
  • 3
    • 0025787798 scopus 로고
    • Alpha-toxin of Staphylococcus aureus
    • S. Bhakdi, and J. Tranum-Jensen Alpha-toxin of Staphylococcus aureus Microbiol. Rev. 55 1991 733 751 (Pubitemid 21895174)
    • (1991) Microbiological Reviews , vol.55 , Issue.4 , pp. 733-751
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 4
    • 0029916264 scopus 로고    scopus 로고
    • Staphylococcal alpha-toxin, streptolysin-O, and Escherichia coli hemolysin: Prototypes of pore-forming bacterial cytolysins
    • DOI 10.1007/s002030050300
    • S. Bhakdi, H. Bayley, A. Valeva, I. Walev, B. Walker, M. Kehoe, and M. Palmer Staphylococcal alpha-toxin, streptolysin-O, and Escherichia coli hemolysin: prototypes of pore-forming bacterial cytolysins Arch. Microbiol. 165 1996 73 79 (Pubitemid 26081834)
    • (1996) Archives of Microbiology , vol.165 , Issue.2 , pp. 73-79
    • Bhakdi, S.1    Bayley, H.2    Valeva, A.3    Walev, I.4    Walker, B.5    Weller, U.6    Kehoe, M.7    Palmer, M.8
  • 5
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore
    • DOI 10.1126/science.274.5294.1859
    • L. Song, M.R. Hobaugh, C. Shustak, S. Cheley, H. Bayley, and J.E. Gouaux Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore Science 274 1996 1859 1866 (Pubitemid 26424757)
    • (1996) Science , vol.274 , Issue.5294 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 8
    • 0033594410 scopus 로고    scopus 로고
    • Stochastic sensing of organic analytes by a pore-forming protein containing a molecular adapter
    • DOI 10.1038/19491
    • L.Q. Gu, O. Braha, S. Conlan, S. Cheley, and H. Bayley Stochastic sensing of organic analytes by a pore-forming protein containing a molecular adapter Nature 398 1999 686 690 (Pubitemid 29197642)
    • (1999) Nature , vol.398 , Issue.6729 , pp. 686-690
    • Gu, L.-Q.1    Braha, O.2    Conlan, S.3    Cheley, S.4    Bayley, H.5
  • 9
    • 33746590221 scopus 로고    scopus 로고
    • Transport of α-helical peptides through α-hemolysin and aerolysin pores
    • DOI 10.1021/bi0604835
    • R. Stefureac, Y.T. Long, H.B. Kraatz, P. Howard, and J.S. Lee Transport of alpha-helical peptides through alpha-hemolysin and aerolysin pores Biochem. 45 2006 9172 9179 (Pubitemid 44156380)
    • (2006) Biochemistry , vol.45 , Issue.30 , pp. 9172-9179
    • Stefureac, R.1    Long, Y.-T.2    Kraatz, H.-B.3    Howard, P.4    Lee, J.S.5
  • 11
    • 33745756692 scopus 로고    scopus 로고
    • Single polymer molecules in a protein nanopore in the limit of a strong polymer-pore attraction
    • O.V. Krasilnikov, C.G. Rodrigues, and S.M. Bezrukov Single polymer molecules in a protein nanopore in the limit of a strong polymer-pore attraction Phys. Rev. Lett. 97 2006 018301
    • (2006) Phys. Rev. Lett. , vol.97 , pp. 018301
    • Krasilnikov, O.V.1    Rodrigues, C.G.2    Bezrukov, S.M.3
  • 13
    • 72549099597 scopus 로고    scopus 로고
    • Interaction of heparins and dextran sulfates with a mesoscopic protein nanopore
    • L.R. Teixeira, P.G. Merzlyak, A. Valeva, and O.V. Krasilnikov Interaction of heparins and dextran sulfates with a mesoscopic protein nanopore Biophys. J. 97 2009 2894 2903
    • (2009) Biophys. J. , vol.97 , pp. 2894-2903
    • Teixeira, L.R.1    Merzlyak, P.G.2    Valeva, A.3    Krasilnikov, O.V.4
  • 14
    • 78650688478 scopus 로고    scopus 로고
    • Investigation of single-molecule kinetics mediated by weak hydrogen bonds within a biological nanopore
    • A. Asandei, A. Apetrei, Y. Park, K.S. Hahm, and T. Luchian Investigation of single-molecule kinetics mediated by weak hydrogen bonds within a biological nanopore Langmuir 27 2011 19 24
    • (2011) Langmuir , vol.27 , pp. 19-24
    • Asandei, A.1    Apetrei, A.2    Park, Y.3    Hahm, K.S.4    Luchian, T.5
  • 17
    • 77954340928 scopus 로고    scopus 로고
    • Impact of distant charge reversals within a robust beta-barrel protein pore
    • M.M. Mohammad, and L. Movileanu Impact of distant charge reversals within a robust beta-barrel protein pore J. Phys. Chem. B 114 2010 8750 8759
    • (2010) J. Phys. Chem. B , vol.114 , pp. 8750-8759
    • Mohammad, M.M.1    Movileanu, L.2
  • 18
    • 16344384707 scopus 로고    scopus 로고
    • Polymer partitioning from nonideal solutions into protein voids
    • O.V. Krasilnikov, and S.M. Bezrukov Polymer partitioning from nonideal solutions into protein voids Macromolecules 37 2004 2650 2657
    • (2004) Macromolecules , vol.37 , pp. 2650-2657
    • Krasilnikov, O.V.1    Bezrukov, S.M.2
  • 19
    • 0022504362 scopus 로고
    • Ionic channels formed by Staphylococcus aureus alpha-toxin: Voltage-dependent inhibition by divalent and trivalent cations
    • G. Menestrina Ionic channels formed by Staphylococcus aureus alpha-toxin: voltage-dependent inhibition by divalent and trivalent cations J. Membr. Biol. 90 1986 177 190 (Pubitemid 16075063)
    • (1986) Journal of Membrane Biology , vol.90 , Issue.2 , pp. 177-190
    • Menestrina, G.1
  • 20
    • 0025282764 scopus 로고
    • Pore-forming toxins: Experiments with S. Aureus α-toxin, C. Perfringens θ-toxin and E. Coli haemolysin in lipid bilayers, liposomes and intact cells
    • DOI 10.1016/0041-0101(90)90292-F
    • G. Menestrina, C.L. Bashford, and C.A. Pasternak Pore-forming toxins: experiments with S. aureus alpha-toxin, C. perfringens theta-toxin and E. coli haemolysin in lipid bilayers, liposomes and intact cells Toxicon 28 1990 477 491 (Pubitemid 20214767)
    • (1990) Toxicon , vol.28 , Issue.5 , pp. 477-491
    • Menestrina, G.1    Bashford, C.L.2    Pasternak, C.A.3
  • 21
    • 0028980231 scopus 로고
    • Protonation dynamics of the alpha-toxin ion channel from spectral analysis of pH-dependent current fluctuations
    • J.J. Kasianowicz, and S.M. Bezrukov Protonation dynamics of the alpha-toxin ion channel from spectral analysis of pH-dependent current fluctuations Biophys. J. 69 1995 94 105
    • (1995) Biophys. J. , vol.69 , pp. 94-105
    • Kasianowicz, J.J.1    Bezrukov, S.M.2
  • 22
    • 0036400016 scopus 로고    scopus 로고
    • Dietary flavonoids: Bioavailability, metabolic effects, and safety
    • DOI 10.1146/annurev.nutr.22.111401.144957
    • J.A. Ross, and C.M. Kasum Dietary flavonoids: bioavailability, metabolic effects, and safety Annu. Rev. Nutr. 22 2002 19 34 (Pubitemid 35221452)
    • (2002) Annual Review of Nutrition , vol.22 , pp. 19-34
    • Ross, J.A.1    Kasum, C.M.2
  • 24
    • 0036401813 scopus 로고    scopus 로고
    • Flavonoids as anticancer agents: Structure-activity relationship study
    • DOI 10.2174/1568011023353714
    • M. Lopez-Lazaro Flavonoids as anticancer agents: structure-activity relationship study Curr. Med. Chem. Anticancer Agents. 2 2002 691 714 (Pubitemid 35175268)
    • (2002) Current Medicinal Chemistry - Anti-Cancer Agents , vol.2 , Issue.6 , pp. 691-714
    • Lopez-Lazaro, M.1
  • 26
    • 19544378483 scopus 로고    scopus 로고
    • Polyphenols: Dietary components with established benefits to health?
    • DOI 10.1002/jsfa.2204
    • P. Kroon, and G. Williamson Polyphenols: dietary components with established benefits to health? J. Sci. Food Agric. 85 2005 1239 1240 (Pubitemid 40728344)
    • (2005) Journal of the Science of Food and Agriculture , vol.85 , Issue.8 , pp. 1239-1240
    • Kroon, P.1    Williamson, G.2
  • 28
    • 1542605222 scopus 로고    scopus 로고
    • Flavonoids: Antioxidants or signalling molecules?
    • DOI 10.1016/j.freeradbiomed.2004.01.001, PII S0891584904000334
    • R.J. Williams, J.P. Spencer, and C. Rice-Evans Flavonoids: antioxidants or signalling molecules? Free Radic. Biol. Med. 36 2004 838 849 (Pubitemid 38352901)
    • (2004) Free Radical Biology and Medicine , vol.36 , Issue.7 , pp. 838-849
    • Williams, R.J.1    Spencer, J.P.E.2    Rice-Evans, C.3
  • 30
    • 34547300030 scopus 로고    scopus 로고
    • Effect of agents modifying the membrane dipole potential on properties of syringomycin e channels
    • DOI 10.1021/la7005452
    • O.S. Ostroumova, Y.A. Kaulin, P.A. Gurnev, and L.V. Schagina Effect of agents modifying the membrane dipole potential on properties of syringomycin E channels Langmuir 23 2007 6889 6892 (Pubitemid 47143204)
    • (2007) Langmuir , vol.23 , Issue.13 , pp. 6889-6892
    • Ostroumova, O.S.1    Kaulin, Y.A.2    Gurnev, P.A.3    Schagina, L.V.4
  • 31
    • 79952108507 scopus 로고    scopus 로고
    • Surfactin activity depends on the membrane dipole potential
    • O.S. Ostroumova, V.V. Malev, M.G. Ilin, and L.V. Schagina Surfactin activity depends on the membrane dipole potential Langmuir 26 2010 15092 15097
    • (2010) Langmuir , vol.26 , pp. 15092-15097
    • Ostroumova, O.S.1    Malev, V.V.2    Ilin, M.G.3    Schagina, L.V.4
  • 32
    • 0030851433 scopus 로고    scopus 로고
    • Effect of the dipole potential of a bilayer lipid membrane on gramicidin channel dissociation kinetics
    • T.I. Rokitskaya, Y.N. Antonenko, and E.A. Kotova Effect of the dipole potential of a bilayer lipid membrane on gramicidin channel dissociation kinetics Biophys. J. 73 1997 850 854 (Pubitemid 27337619)
    • (1997) Biophysical Journal , vol.73 , Issue.2 , pp. 850-854
    • Rokitskaya, T.I.1    Antonenko, Y.N.2    Kotova, E.A.3
  • 33
    • 0345254912 scopus 로고    scopus 로고
    • Genistein Can Modulate Channel Function by a Phosphorylation-Independent Mechanism: Importance of Hydrophobic Mismatch and Bilayer Mechanics
    • DOI 10.1021/bi034887y
    • T.C. Hwang, R.E. Koeppe, and O.S. Andersen Genistein can modulate channel function by a phosphorylation-independent mechanism: importance of hydrophobic mismatch and bilayer mechanics Biochem. 42 2003 13646 13658 (Pubitemid 37444915)
    • (2003) Biochemistry , vol.42 , Issue.46 , pp. 13646-13658
    • Hwang, T.-C.1    Koeppe II, R.E.2    Andersen, O.S.3
  • 34
    • 33749610849 scopus 로고    scopus 로고
    • Phlorizin- and 6-ketocholestanol-mediated antagonistic modulation of alamethicin activity in phospholipid planar membranes
    • DOI 10.1021/la0613777
    • T. Luchian, and L. Mereuta Phlorizin- and 6-ketocholestanol-mediated antagonistic modulation of alamethicin activity in phospholipid planar membranes Langmuir 22 2006 8452 8457 (Pubitemid 44547070)
    • (2006) Langmuir , vol.22 , Issue.20 , pp. 8452-8457
    • Luchian, T.1    Mereuta, L.2
  • 35
    • 0015459562 scopus 로고
    • Formation of bimolecular membranes from lipid monolayers and study of their electrical properties
    • M. Montal, and P. Muller Formation of bimolecular membranes from lipid monolayers and study of their electrical properties Proc. Natl. Acad. Sci. USA 65 1972 3561 3566
    • (1972) Proc. Natl. Acad. Sci. USA , vol.65 , pp. 3561-3566
    • Montal, M.1    Muller, P.2
  • 36
    • 0033832671 scopus 로고    scopus 로고
    • Interaction of phloretin with membranes: On the mode of action of phloretin at the water-lipid interface
    • R. Cseh, M. Hetzer, K. Wolf, J. Kraus, G. Bringmann, and R. Benz Interaction of phloretin with membranes: on the mode of action of phloretin at the water-lipid interface Eur. Biophys. J. 29 2000 172 183
    • (2000) Eur. Biophys. J. , vol.29 , pp. 172-183
    • Cseh, R.1    Hetzer, M.2    Wolf, K.3    Kraus, J.4    Bringmann, G.5    Benz, R.6
  • 37
    • 0020584454 scopus 로고
    • Phloretin and phloretin analogs: Mode of action in planar lipid bilayers and monolayers
    • J. Reyes, F. Greco, R. Motais, and R. Latorre Phloretin and phloretin analogs: mode of action in planar lipid bilayers and monolayers J. Membr. Biol. 72 1983 93 103 (Pubitemid 13128306)
    • (1983) Journal of Membrane Biology , vol.72 , Issue.1-2 , pp. 93-103
    • Reyes, J.1    Greco, F.2    Motais, R.3    Latorre, R.4
  • 38
    • 0017161652 scopus 로고
    • Effect of phloretin on the permeability of thin lipid membranes
    • O.S. Andersen, A. Finkelstein, I. Katz, and A. Cass Effect of phloretin on the permeability of thin lipid membranes J. Gen. Physiol. 67 1976 749 771
    • (1976) J. Gen. Physiol. , vol.67 , pp. 749-771
    • Andersen, O.S.1    Finkelstein, A.2    Katz, I.3    Cass, A.4
  • 39
    • 0036150196 scopus 로고    scopus 로고
    • Estimation of electrochrome dyes position in the bilayer through the 2nd harmonic of capacitive current
    • DOI 10.1016/S1567-5394(01)00167-0, PII S1567539401001670
    • V.I. Passechnik, and V.S. Sokolov Estimation of electrochrome dyes position in the bilayer through the 2nd harmonic of capacitive current Bioelectrochem. 55 2002 47 51 (Pubitemid 34084749)
    • (2002) Bioelectrochemistry , vol.55 , Issue.1-2 , pp. 47-51
    • Passechnik, V.I.1    Sokolov, V.S.2
  • 40
    • 0043172554 scopus 로고    scopus 로고
    • Effective gating charge of ion channels induced by toxin syringomycin E in lipid bilayers
    • DOI 10.1016/S1567-5394(03)00041-0
    • L.V. Schagina, Ph.A. Gurnev, J.Y. Takemoto, and V.V. Malev Effective gating charge of ion channels induced by toxin syringomycin E in lipid bilayers Bioelectrochem. 60 2003 21 27 (Pubitemid 36945002)
    • (2003) Bioelectrochemistry , vol.60 , Issue.1-2 , pp. 21-27
    • Schagina, L.V.1    Gurnev, P.A.2    Takemoto, J.Y.3    Malev, V.V.4
  • 41
    • 0027177939 scopus 로고
    • Internal electrostatic potentials in bilayers: Measuring and controlling dipole potentials in lipid vesicles
    • J.C. Franklin, and D.S. Cafiso Internal electrostatic potentials in bilayers: measuring and controlling dipole potentials in lipid vesicles Biophys. J. 65 1993 289 299 (Pubitemid 23206061)
    • (1993) Biophysical Journal , vol.65 , Issue.1 , pp. 289-299
    • Franklin, J.C.1    Cafiso, D.S.2
  • 42
    • 0342933118 scopus 로고
    • Transport of oppositely charged lipophilic probe ions in lipid bilayer membranes having various structures
    • A.D. Pickar, and R. Benz Transport of oppositely charged lipophilic probe ions in lipid bilayer membranes having various structures J. Membr. Biol. 44 1978 353 376 (Pubitemid 9123077)
    • (1979) Journal of Membrane Biology , vol.44 , Issue.3-4 , pp. 353-376
    • Pickar, A.D.1    Benz, R.2
  • 43
    • 0031910472 scopus 로고    scopus 로고
    • The adsorption of phloretin to lipid monolayers and bilayers cannot be explained by langmuir adsorption isotherms alone
    • R. Cseh, and R. Benz The adsorption of phloretin to lipid monolayers and bilayers cannot be explained by langmuir adsorption isotherms alone Biophys. J. 74 1998 1399 1408 (Pubitemid 28108548)
    • (1998) Biophysical Journal , vol.74 , Issue.3 , pp. 1399-1408
    • Cseh, R.1    Benz, R.2
  • 44
    • 0036671109 scopus 로고    scopus 로고
    • Origin of membrane dipole potential: Contribution of the phospholipid fatty acid chains
    • DOI 10.1016/S0009-3084(02)00013-0, PII S0009308402000130
    • U. Peterson, D.A. Mannock, R.N. Lewis, P. Pohl, R.N. McElhaney, and E.E. Pohl Origin of membrane dipole potential: contribution of the phospholipid fatty acid chains Chem. Phys. Lipids 117 2002 19 27 (Pubitemid 35007265)
    • (2002) Chemistry and Physics of Lipids , vol.117 , Issue.1-2 , pp. 19-27
    • Peterson, U.1    Mannock, D.A.2    Lewis, R.N.A.H.3    Pohl, P.4    McElhaney, R.N.5    Pohl, E.E.6
  • 45
    • 13844253232 scopus 로고    scopus 로고
    • Electric field strength of membrane lipids from vertebrate species: Membrane lipid composition and Na+-K+-ATPase molecular activity
    • T. Starke-Peterkovic, N. Turner, P.L. Else, and R.J. Clarke Electric field strength of membrane lipids from vertebrate species: membrane lipid composition and Na+-K+-ATPase molecular activity Am. J. Physiol. Regul. Integr. Comp. Physiol. 288 2005 663 670
    • (2005) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.288 , pp. 663-670
    • Starke-Peterkovic, T.1    Turner, N.2    Else, P.L.3    Clarke, R.J.4
  • 46
    • 0017494614 scopus 로고
    • Calculation of liquid-junction potentials and membrane potentials on the basis of the Planck theory
    • W.E. Morf Calculation of liquid-junction potentials and membrane potentials on the basis of the Planck theory Anal. Chem. 49 1977 810 813
    • (1977) Anal. Chem. , vol.49 , pp. 810-813
    • Morf, W.E.1
  • 47
    • 0020630499 scopus 로고
    • Electrostatic modeling of ion pores. II. Effects attributable to the membrane dipole potential
    • P.C. Jordan Electrostatic modeling of ion pores. II. Effects attributable to the membrane dipole potential Biophys. J. 41 1983 189 195 (Pubitemid 13124862)
    • (1983) Biophysical Journal , vol.41 , Issue.2 , pp. 189-195
    • Jordan, P.C.1
  • 48
    • 0030070198 scopus 로고    scopus 로고
    • Fluorescent styryl dyes of the RH series affect a potential drop on the membrane/solution boundary
    • DOI 10.1016/0005-2736(95)00197-2
    • D.Y. Malkov, and V.S. Sokolov Fluorescent styryl dyes of the RH series affect a potential drop on the membrane/solution boundary Biochim. Biophys. Acta 1278 1996 197 204 (Pubitemid 26062575)
    • (1996) Biochimica et Biophysica Acta - Biomembranes , vol.1278 , Issue.2 , pp. 197-204
    • Malkov, D.Yu.1    Sokolov, V.S.2
  • 49
    • 0024119703 scopus 로고
    • Influence of pH on the potential-dependence of staphylococcal toxin channels functioning in phosphatidylcholine bilayer
    • O.V. Krasilnikov, P.G. Merzlyak, R.Z. Sabirov, V.I. Ternovsky, and R.K. Zaripova Influence of pH on the potential-dependence of staphylococcal toxin channels functioning in phosphatidylcholine bilayer Ukr. Biokhim. Zh. 60 1988 60 66
    • (1988) Ukr. Biokhim. Zh. , vol.60 , pp. 60-66
    • Krasilnikov, O.V.1    Merzlyak, P.G.2    Sabirov, R.Z.3    Ternovsky, V.I.4    Zaripova, R.K.5
  • 50
    • 34248152648 scopus 로고    scopus 로고
    • Crystal Structures of Multidrug Binding Protein TtgR in Complex with Antibiotics and Plant Antimicrobials
    • DOI 10.1016/j.jmb.2007.03.062, PII S0022283607004287
    • Y. Alguel, C. Meng, W. Teran, T. Krell, J.L. Ramos, M.T. Gallegos, and X. Zhang Crystal structures of multidrug binding protein TtgR in complex with antibiotics and plant antimicrobials J. Mol. Biol. 369 2007 829 840 (Pubitemid 46709926)
    • (2007) Journal of Molecular Biology , vol.369 , Issue.3 , pp. 829-840
    • Alguel, Y.1    Meng, C.2    Teran, W.3    Krell, T.4    Ramos, J.L.5    Gallegos, M.-T.6    Zhang, X.7
  • 51
    • 77952671938 scopus 로고    scopus 로고
    • Conformational differences between the wild type and V30M mutant transthyretin modulate its binding to genistein: Implications to tetramer stability and ligand-binding
    • D.B. Trivella, L. Bleicher, Lde C. Palmieri, H.J. Wiggers, C.A. Montanari, J.W. Kelly, L.M. Lima, D. Foguel, and I. Polikarpov Conformational differences between the wild type and V30M mutant transthyretin modulate its binding to genistein: implications to tetramer stability and ligand-binding J. Struct. Biol. 170 2010 522 531
    • (2010) J. Struct. Biol. , vol.170 , pp. 522-531
    • Trivella, D.B.1    Bleicher, L.2    Palmieri, L.C.3    Wiggers, H.J.4    Montanari, C.A.5    Kelly, J.W.6    Lima, L.M.7    Foguel, D.8    Polikarpov, I.9
  • 52
    • 10044245924 scopus 로고    scopus 로고
    • Understanding the selectivity of genistein for human estrogen receptor-β using X-ray crystallography and computational methods
    • DOI 10.1016/j.str.2004.09.015, PII S0969212604003508
    • E.S. Manas, Z.B. Xu, R.J. Unwalla, and W.S. Somers Understanding the selectivity of genistein for human estrogen receptor-beta using X-ray crystallography and computational methods Structure 12 2004 2197 2207 (Pubitemid 39610434)
    • (2004) Structure , vol.12 , Issue.12 , pp. 2197-2207
    • Manas, E.S.1    Xu, Z.B.2    Unwalla, R.J.3    Somers, W.S.4
  • 55
    • 77950887221 scopus 로고    scopus 로고
    • Flavonol activation defines an unanticipated ligand-binding site in the kinase-RNase domain of IRE1
    • R.L. Wiseman, Y. Zhang, K.P. Lee, H.P. Harding, C.M. Haynes, J. Price, F. Sicheri, and D. Ron Flavonol activation defines an unanticipated ligand-binding site in the kinase-RNase domain of IRE1 Mol. Cell 38 2010 291 304
    • (2010) Mol. Cell , vol.38 , pp. 291-304
    • Wiseman, R.L.1    Zhang, Y.2    Lee, K.P.3    Harding, H.P.4    Haynes, C.M.5    Price, J.6    Sicheri, F.7    Ron, D.8
  • 57
    • 0036151286 scopus 로고    scopus 로고
    • Structure and mechanism of anthocyanidin synthase from Arabidopsis thaliana
    • DOI 10.1016/S0969-2126(01)00695-5, PII S0969212601006955
    • R.C. Wilmouth, J.J. Turnbull, R.W. Welford, I.J. Clifton, A.G. Prescott, and C.J. Schofield Structure and mechanism of anthocyanidin synthase from Arabidopsis thaliana Structure 10 2002 93 103 (Pubitemid 34112614)
    • (2002) Structure , vol.10 , Issue.1 , pp. 93-103
    • Wilmouth, R.C.1    Turnbull, J.J.2    Welford, R.W.D.3    Clifton, I.J.4    Prescott, A.G.5    Schofield, C.J.6
  • 58
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • DOI 10.1038/385602a0
    • F. Sicheri, I. Moarefi, and J. Kuriyan Crystal structure of the Src family tyrosine kinase Hck Nature 385 1997 602 609 (Pubitemid 27087567)
    • (1997) Nature , vol.385 , Issue.6617 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 59
    • 70149104455 scopus 로고    scopus 로고
    • Crystal structures of glycosyltransferase UGT78G1 reveal the molecular basis for glycosylation and deglycosylation of (iso)flavonoids
    • L.V. Modolo, L. Li, H. Pan, J.W. Blount, R.A. Dixon, and X. Wang Crystal structures of glycosyltransferase UGT78G1 reveal the molecular basis for glycosylation and deglycosylation of (iso)flavonoids J. Mol. Biol. 392 2009 1292 1302
    • (2009) J. Mol. Biol. , vol.392 , pp. 1292-1302
    • Modolo, L.V.1    Li, L.2    Pan, H.3    Blount, J.W.4    Dixon, R.A.5    Wang, X.6
  • 60
    • 0033634827 scopus 로고    scopus 로고
    • Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine
    • E.H. Walker, M.E. Pacold, O. Perisic, L. Stephens, P.T. Hawkins, M.P. Wymann, and R.L. Williams Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine Mol. Cell 6 2000 909 919
    • (2000) Mol. Cell , vol.6 , pp. 909-919
    • Walker, E.H.1    Pacold, M.E.2    Perisic, O.3    Stephens, L.4    Hawkins, P.T.5    Wymann, M.P.6    Williams, R.L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.