메뉴 건너뛰기




Volumn 60, Issue 13, 2017, Pages 5646-5662

Urinary Tract Infection: Which Conformation of the Bacterial Lectin FimH Is Therapeutically Relevant?

Author keywords

[No Author keywords available]

Indexed keywords

2 CHLORO 4 IODO PHENYL 2,3,4,6 TETRA O ACETYL ALPHA DEXTRO MANNOPYRANOSIDE; 2',3 DICHLORO BIPHENYL 4 YL ALPHA DEXTRO MANNOPYRANOSIDE; 2',3,4' TRICHLORO BIPHENYL 4 YL ALPHA DEXTRO MANNOPYRANOSIDE; 2,'3',4' TRICHLORO BIPHENYL 4 YL 2,3,4,6 TETRA O ACETYL ALPHA DEXTRO MANNOPYRANOSIDE; 3 CHLORO 2' METHOXY BIPHENYL 4 YL ALPHA DEXTRO MANNOPYRANOSIDE; 3 CHLORO 2' METHYL BIPHENYL 4 YL ALPHA DEXTRO MANNOPYRANOSIDE; 3 CHLORO 3' (TRIFLUOROMETHYL)BIPHENYL 4 YL ALPHA DEXTRO MANNOPYRANOSIDE; 3 CHLORO 3' METHYL BIPHENYL 4 YL ALPHA DEXTRO MANNOPYRANOSIDE; 3 CHLORO 3' NITRO BIPHENYL 4 YL ALPHA DEXTRO MANNOPYRANOSIDE; 3 CHLORO 4' (TRIFLUOROMETHYL)BIPHENYL 4 YL 2,3,4,6 TETRA O ACETYL ALPHA DEXTRO MANNOPYRANOSIDE; 3 CHLORO 4' (TRIFLUOROMETHYL)BIPHENYL 4 YL ALPHA DEXTRO MANNOPYRANOSIDE; 3 CHLORO 4' METHOXY BIPHENYL 4 YL ALPHA DEXTRO MANNOPYRANOSIDE; 3 CHLORO 4' METHYL BIPHENYL 4 YL ALPHA DEXTRO MANNOPYRANOSIDE; 3 CHLORO 4' NITRO BIPHENYL 4 YL ALPHA DEXTRO MANNOPYRANOSIDE; 3 CHLORO BIPHENYL 4 YL 2,3,4,6 TETRA O ACETYL ALPHA DEXTRO MANNOPYRANOSIDE; 3 CHLORO BIPHENYL 4 YL ALPHA DEXTRO MANNOPYRANOSIDE; 3' CHLORO 4' (ALPHA DEXTRO MANNOPYRANOSYLOXY)BIPHENYL 3 CARBONITRIL; 3' CHLORO 4' (ALPHA DEXTRO MANNOPYRANOSYLOXY)BIPHENYL 4 CARBONITRIL; 3,3' DICHLORO BIPHENYL 4 YL ALPHA DEXTRO MANNOPYRANOSIDE; 3,3',4' TRICHLORO BIPHENYL 4 YL 2,3,4,6 TETRA O ACETYL ALPHA DEXTRO MANNOPYRANOSIDE; 3,3',4' TRICHLORO BIPHENYL 4 YL ALPHA DEXTRO MANNOPYRANOSIDE; 3,4' DICHLORO 3' (TRIFLUOROMETHYL)BIPHENYL 4 YL ALPHA DEXTRO MANNOPYRANOSIDE; 3,4' DICHLORO BIPHENYL 4 YL 2,3,4,6 TETRA O ACETYL ALPHA DEXTRO MANNOPYRANOSIDE; 3,4' DICHLORO BIPHENYL 4 YL ALPHA DEXTRO MANNOPYRANOSIDE; 4' ACETYL 3 CHLORO BIPHENYL 4 YL ALPHA DEXTRO MANNOPYRANOSIDE; BACTERIAL LECTIN FIMH; BIPHENYL DERIVATIVE; LECTIN; PROTEIN INHIBITOR; UNCLASSIFIED DRUG; UNINDEXED DRUG; ADHESIN; ANTIINFECTIVE AGENT; ARTIFICIAL MEMBRANE; FIMBRIA PROTEIN; FIMH PROTEIN, E COLI;

EID: 85023752836     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/acs.jmedchem.7b00342     Document Type: Article
Times cited : (27)

References (104)
  • 1
    • 0033665053 scopus 로고    scopus 로고
    • Urinary Tract Infection: Self-Reported Incidence and Associated Costs
    • Foxman, B.; Barlow, R.; D'Arcy, H.; Gillespie, B.; Sobel, J. D. Urinary Tract Infection: Self-Reported Incidence and Associated Costs Ann. Epidemiol. 2000, 10, 509-515 10.1016/S1047-2797(00)00072-7
    • (2000) Ann. Epidemiol. , vol.10 , pp. 509-515
    • Foxman, B.1    Barlow, R.2    D'Arcy, H.3    Gillespie, B.4    Sobel, J.D.5
  • 2
    • 0038270674 scopus 로고    scopus 로고
    • Epidemiology of Urinary Tract Infections
    • Foxman, B.; Brown, P. Epidemiology of Urinary Tract Infections Infect. Dis. Clin. North Am. 2003, 17, 227-241 10.1016/S0891-5520(03)00005-9
    • (2003) Infect. Dis. Clin. North Am. , vol.17 , pp. 227-241
    • Foxman, B.1    Brown, P.2
  • 3
    • 0037300154 scopus 로고    scopus 로고
    • The Etiology of Urinary Tract Infection: Traditional and Emerging Pathogens
    • Ronald, A. The Etiology of Urinary Tract Infection: Traditional and Emerging Pathogens DM, Dis.-Mon. 2003, 49, 71-82 10.1067/mda.2003.8
    • (2003) DM, Dis.-Mon. , vol.49 , pp. 71-82
    • Ronald, A.1
  • 4
    • 46749131414 scopus 로고    scopus 로고
    • Origins and Virulence Mechanisms of Uropathogenic Escherichia coli
    • Wiles, T. J.; Kulesus, R. R.; Mulvey, M. A. Origins and Virulence Mechanisms of Uropathogenic Escherichia Coli Exp. Mol. Pathol. 2008, 85, 11-19 10.1016/j.yexmp.2008.03.007
    • (2008) Exp. Mol. Pathol. , vol.85 , pp. 11-19
    • Wiles, T.J.1    Kulesus, R.R.2    Mulvey, M.A.3
  • 5
    • 0038825532 scopus 로고    scopus 로고
    • Acute Uncomplicated Urinary Tract Infection in Women
    • Fihn, S. D. Acute Uncomplicated Urinary Tract Infection in Women N. Engl. J. Med. 2003, 349, 259-266 10.1056/NEJMcp030027
    • (2003) N. Engl. J. Med. , vol.349 , pp. 259-266
    • Fihn, S.D.1
  • 6
    • 3042793159 scopus 로고    scopus 로고
    • Acute Uncomplicated Cystitis in an Era of Increasing Antibiotic Resistance: A Proposed Approach to Empirical Therapy
    • Hooton, T. M.; Besser, R.; Foxman, B.; Fritsche, T. R.; Nicolle, L. E. Acute Uncomplicated Cystitis in an Era of Increasing Antibiotic Resistance: A Proposed Approach to Empirical Therapy Clin. Infect. Dis. 2004, 39, 75-80 10.1086/422145
    • (2004) Clin. Infect. Dis. , vol.39 , pp. 75-80
    • Hooton, T.M.1    Besser, R.2    Foxman, B.3    Fritsche, T.R.4    Nicolle, L.E.5
  • 7
    • 84858650295 scopus 로고    scopus 로고
    • In Vitro Antimicrobial Resistance of Urinary Escherichia coli Isolates among U.S. Outpatients from 2000 to 2010
    • Sanchez, G. V.; Master, R. N.; Karlowsky, J. A.; Bordon, J. M. In Vitro Antimicrobial Resistance of Urinary Escherichia Coli Isolates among U.S. Outpatients from 2000 to 2010 Antimicrob. Agents Chemother. 2012, 56, 2181-2183 10.1128/AAC.06060-11
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 2181-2183
    • Sanchez, G.V.1    Master, R.N.2    Karlowsky, J.A.3    Bordon, J.M.4
  • 8
    • 69949132847 scopus 로고    scopus 로고
    • The ARESC Study: An International Survey on the Antimicrobial Resistance of Pathogens Involved in Uncomplicated Urinary Tract Infections
    • Schito, G. C.; Naber, K. G.; Botto, H.; Palou, J.; Mazzei, T.; Gualco, L.; Marchese, A. The ARESC Study: An International Survey on the Antimicrobial Resistance of Pathogens Involved in Uncomplicated Urinary Tract Infections Int. J. Antimicrob. Agents 2009, 34, 407-413 10.1016/j.ijantimicag.2009.04.012
    • (2009) Int. J. Antimicrob. Agents , vol.34 , pp. 407-413
    • Schito, G.C.1    Naber, K.G.2    Botto, H.3    Palou, J.4    Mazzei, T.5    Gualco, L.6    Marchese, A.7
  • 9
    • 33747325623 scopus 로고    scopus 로고
    • Antibiotic Resistance in Escherichia coli Outpatient Urinary Isolates: Final Results from the North American Urinary Tract Infection Collaborative Alliance (NAUTICA)
    • NAUTICA Group
    • Zhanel, G. G.; Hisanaga, T. L.; Laing, N. M.; DeCorby, M. R.; Nichol, K. A.; Weshnoweski, B.; Johnson, J.; Noreddin, A.; Low, D. E.; Karlowsky, J. A.; Hoban, D. J.; NAUTICA Group Antibiotic Resistance in Escherichia Coli Outpatient Urinary Isolates: Final Results from the North American Urinary Tract Infection Collaborative Alliance (NAUTICA) Int. J. Antimicrob. Agents 2006, 27, 468-475 10.1016/j.ijantimicag.2006.02.009
    • (2006) Int. J. Antimicrob. Agents , vol.27 , pp. 468-475
    • Zhanel, G.G.1    Hisanaga, T.L.2    Laing, N.M.3    DeCorby, M.R.4    Nichol, K.A.5    Weshnoweski, B.6    Johnson, J.7    Noreddin, A.8    Low, D.E.9    Karlowsky, J.A.10    Hoban, D.J.11
  • 10
    • 34548108138 scopus 로고    scopus 로고
    • Targeting Virulence: A New Paradigm for Antimicrobial Therapy
    • Clatworthy, A. E.; Pierson, E.; Hung, D. T. Targeting Virulence: A New Paradigm for Antimicrobial Therapy Nat. Chem. Biol. 2007, 3, 541-548 10.1038/nchembio.2007.24
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 541-548
    • Clatworthy, A.E.1    Pierson, E.2    Hung, D.T.3
  • 11
    • 0034255341 scopus 로고    scopus 로고
    • Bad Bugs and Beleaguered Bladders: Interplay between Uropathogenic Escherichia coli and Innate Host Defenses
    • Mulvey, M. A.; Schilling, J. D.; Martinez, J. J.; Hultgren, S. J. Bad Bugs and Beleaguered Bladders: Interplay between Uropathogenic Escherichia Coli and Innate Host Defenses Proc. Natl. Acad. Sci. U. S. A. 2000, 97, 8829-8835 10.1073/pnas.97.16.8829
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 8829-8835
    • Mulvey, M.A.1    Schilling, J.D.2    Martinez, J.J.3    Hultgren, S.J.4
  • 12
    • 0035283006 scopus 로고    scopus 로고
    • Structure and Function of Escherichia coli Type 1 Pili: New Insight into the Pathogenesis of Urinary Tract Infections
    • Schilling, J. D.; Mulvey, M. a; Hultgren, S. J. Structure and Function of Escherichia Coli Type 1 Pili: New Insight into the Pathogenesis of Urinary Tract Infections J. Infect. Dis. 2001, 183 (Suppl) S36-40 10.1086/318855
    • (2001) J. Infect. Dis. , vol.183 , pp. S36-40
    • Schilling, J.D.1    Mulvey, M.A.2    Hultgren, S.J.3
  • 15
    • 0030859026 scopus 로고    scopus 로고
    • Diversity of the Escherichia coli Type 1 Fimbrial Lectin: Differential Binding to Mannosides and Uroepithelial Cells
    • Sokurenko, E. V.; Chesnokova, V.; Doyle, R. J.; Hasty, D. L. Diversity of the Escherichia Coli Type 1 Fimbrial Lectin: Differential Binding to Mannosides and Uroepithelial Cells J. Biol. Chem. 1997, 272, 17880-17886 10.1074/jbc.272.28.17880
    • (1997) J. Biol. Chem. , vol.272 , pp. 17880-17886
    • Sokurenko, E.V.1    Chesnokova, V.2    Doyle, R.J.3    Hasty, D.L.4
  • 16
    • 0023191455 scopus 로고
    • Bacterial Lectins, Cell-Cell Recognition and Infectious Disease
    • Sharon, N. Bacterial Lectins, Cell-Cell Recognition and Infectious Disease FEBS Lett. 1987, 217, 145-157 10.1016/0014-5793(87)80654-3
    • (1987) FEBS Lett. , vol.217 , pp. 145-157
    • Sharon, N.1
  • 17
    • 33748145105 scopus 로고    scopus 로고
    • Structural and Functional Insights into the Assembly of Type 1 Pili from Escherichia coli
    • Capitani, G.; Eidam, O.; Glockshuber, R.; Grütter, M. G. Structural and Functional Insights into the Assembly of Type 1 Pili from Escherichia Coli Microbes Infect. 2006, 8, 2284-2290 10.1016/j.micinf.2006.03.013
    • (2006) Microbes Infect. , vol.8 , pp. 2284-2290
    • Capitani, G.1    Eidam, O.2    Glockshuber, R.3    Grütter, M.G.4
  • 18
    • 0142042801 scopus 로고    scopus 로고
    • Anti-Adhesion Therapy of Bacterial Diseases: Prospects and Problems
    • Ofek, I.; Hasty, D. L.; Sharon, N. Anti-Adhesion Therapy of Bacterial Diseases: Prospects and Problems FEMS Immunol. Med. Microbiol. 2003, 38, 181-191 10.1016/S0928-8244(03)00228-1
    • (2003) FEMS Immunol. Med. Microbiol. , vol.38 , pp. 181-191
    • Ofek, I.1    Hasty, D.L.2    Sharon, N.3
  • 19
    • 33646103431 scopus 로고    scopus 로고
    • Carbohydrates as Future Anti-Adhesion Drugs for Infectious Diseases
    • Sharon, N. Carbohydrates as Future Anti-Adhesion Drugs for Infectious Diseases Biochim. Biophys. Acta, Gen. Subj. 2006, 1760, 527-537 10.1016/j.bbagen.2005.12.008
    • (2006) Biochim. Biophys. Acta, Gen. Subj. , vol.1760 , pp. 527-537
    • Sharon, N.1
  • 20
    • 0034747254 scopus 로고    scopus 로고
    • Uroplakin Ia Is the Urothelial Receptor for Uropathogenic Escherichia coli: Evidence from in Vitro FimH Binding
    • Zhou, G.; Mo, W.-J.; Sebbel, P.; Min, G.; Neubert, T. A.; Glockshuber, R.; Wu, X.-R.; Sun, T.-T.; Kong, X.-P. Uroplakin Ia Is the Urothelial Receptor for Uropathogenic Escherichia Coli: Evidence from in Vitro FimH Binding J. Cell Sci. 2001, 114, 4095-4103
    • (2001) J. Cell Sci. , vol.114 , pp. 4095-4103
    • Zhou, G.1    Mo, W.-J.2    Sebbel, P.3    Min, G.4    Neubert, T.A.5    Glockshuber, R.6    Wu, X.-R.7    Sun, T.-T.8    Kong, X.-P.9
  • 21
    • 35649003866 scopus 로고    scopus 로고
    • Intervention with Bacterial Adhesion by Multivalent Carbohydrates
    • Pieters, R. J. Intervention with Bacterial Adhesion by Multivalent Carbohydrates Med. Res. Rev. 2007, 27, 796-816 10.1002/med.20089
    • (2007) Med. Res. Rev. , vol.27 , pp. 796-816
    • Pieters, R.J.1
  • 23
    • 70350211420 scopus 로고    scopus 로고
    • Structural Biology of the Chaperone-Usher Pathway of Pilus Biogenesis
    • Waksman, G.; Hultgren, S. J. Structural Biology of the Chaperone-Usher Pathway of Pilus Biogenesis Nat. Rev. Microbiol. 2009, 7, 765-774 10.1038/nrmicro2220
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 765-774
    • Waksman, G.1    Hultgren, S.J.2
  • 28
    • 36749065533 scopus 로고    scopus 로고
    • Expression of Flagella Is Coincident with Uropathogenic Escherichia coli Ascension to the Upper Urinary Tract
    • Lane, M. C.; Alteri, C. J.; Smith, S. N.; Mobley, H. L. T. Expression of Flagella Is Coincident with Uropathogenic Escherichia Coli Ascension to the Upper Urinary Tract Proc. Natl. Acad. Sci. U. S. A. 2007, 104, 16669-16674 10.1073/pnas.0607898104
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 16669-16674
    • Lane, M.C.1    Alteri, C.J.2    Smith, S.N.3    Mobley, H.L.T.4
  • 29
    • 0037188917 scopus 로고    scopus 로고
    • Bacterial Adhesion to Target Cells Enhanced by Shear Force
    • Thomas, W. E.; Trintchina, E.; Forero, M.; Vogel, V.; Sokurenko, E. V. Bacterial Adhesion to Target Cells Enhanced by Shear Force Cell 2002, 109, 913-923 10.1016/S0092-8674(02)00796-1
    • (2002) Cell , vol.109 , pp. 913-923
    • Thomas, W.E.1    Trintchina, E.2    Forero, M.3    Vogel, V.4    Sokurenko, E.V.5
  • 30
    • 4444247401 scopus 로고    scopus 로고
    • Shear-Dependent "stick-and-Roll" Adhesion of Type 1 Fimbriated Escherichia coli
    • Thomas, W. E.; Nilsson, L. M.; Forero, M.; Sokurenko, E. V.; Vogel, V. Shear-Dependent "Stick-and-Roll" Adhesion of Type 1 Fimbriated Escherichia Coli Mol. Microbiol. 2004, 53, 1545-1557 10.1111/j.1365-2958.2004.04226.x
    • (2004) Mol. Microbiol. , vol.53 , pp. 1545-1557
    • Thomas, W.E.1    Nilsson, L.M.2    Forero, M.3    Sokurenko, E.V.4    Vogel, V.5
  • 34
    • 0018412567 scopus 로고
    • Prevention of Colonization of the Urinary Tract of Mice with Escherichia coli by Blocking of Bacterial Adherence with Methyl Alpha-D-Mannopyranoside
    • Aronson, M.; Medalia, O.; Schori, L.; Mirelman, D.; Sharon, N.; Ofek, I. Prevention of Colonization of the Urinary Tract of Mice with Escherichia Coli by Blocking of Bacterial Adherence with Methyl Alpha-D-Mannopyranoside J. Infect. Dis. 1979, 139, 329-332 10.1093/infdis/139.3.329
    • (1979) J. Infect. Dis. , vol.139 , pp. 329-332
    • Aronson, M.1    Medalia, O.2    Schori, L.3    Mirelman, D.4    Sharon, N.5    Ofek, I.6
  • 35
    • 0023095282 scopus 로고
    • Aromatic α-Glycosides of Mannose Are Powerful Inhibitors of the Adherence of Type 1 Fimbritated Escherichia coli to Teast and Intestinal Epithelial Cells
    • Firon, N.; Ashkenazi, S.; Mirelman, D.; Ofek, I.; Sharon, N. Aromatic α-Glycosides of Mannose Are Powerful Inhibitors of the Adherence of Type 1 Fimbritated Escherichia Coli to Teast and Intestinal Epithelial Cells Infect. Immun. 1987, 55, 472-476
    • (1987) Infect. Immun. , vol.55 , pp. 472-476
    • Firon, N.1    Ashkenazi, S.2    Mirelman, D.3    Ofek, I.4    Sharon, N.5
  • 36
    • 79955037995 scopus 로고    scopus 로고
    • Squaric Acid Monoamide Mannosides as Ligands for the Bacterial Lectin FimH: Covalent Inhibition or Not?
    • Grabosch, C.; Hartmann, M.; Schmidt-Lassen, J.; Lindhorst, T. K. Squaric Acid Monoamide Mannosides as Ligands for the Bacterial Lectin FimH: Covalent Inhibition or Not? ChemBioChem 2011, 12, 1066-1074 10.1002/cbic.201000774
    • (2011) ChemBioChem , vol.12 , pp. 1066-1074
    • Grabosch, C.1    Hartmann, M.2    Schmidt-Lassen, J.3    Lindhorst, T.K.4
  • 42
    • 84864409295 scopus 로고    scopus 로고
    • FimH Antagonists: Structure-Activity and Structure-Property Relationships for Biphenyl α-D-Mannopyranosides
    • Pang, L.; Kleeb, S.; Lemme, K.; Rabbani, S.; Scharenberg, M.; Zalewski, A.; Schädler, F.; Schwardt, O.; Ernst, B. FimH Antagonists: Structure-Activity and Structure-Property Relationships for Biphenyl α-D-Mannopyranosides ChemMedChem 2012, 7, 1404-1422 10.1002/cmdc.201200125
    • (2012) ChemMedChem , vol.7 , pp. 1404-1422
    • Pang, L.1    Kleeb, S.2    Lemme, K.3    Rabbani, S.4    Scharenberg, M.5    Zalewski, A.6    Schädler, F.7    Schwardt, O.8    Ernst, B.9
  • 46
    • 0031824605 scopus 로고    scopus 로고
    • Inhibition of the Type-1 Fimbriae-Mediated Adhesion of Escherichia coli to Erythrocytes by Multiantennary Alpha-Mannosyl Clusters - The Effect of Multivalency
    • Lindhorst, T. K.; Kieburg, C.; Krallmann-Wenzel, U. Inhibition of the Type-1 Fimbriae-Mediated Adhesion of Escherichia Coli to Erythrocytes by Multiantennary Alpha-Mannosyl Clusters-The Effect of Multivalency Glycoconjugate J. 1998, 15, 605-613 10.1023/A:1006920027641
    • (1998) Glycoconjugate J. , vol.15 , pp. 605-613
    • Lindhorst, T.K.1    Kieburg, C.2    Krallmann-Wenzel, U.3
  • 47
    • 12244292949 scopus 로고    scopus 로고
    • Inhibition of Adhesion of Type 1 Fimbriated Escherichia coli to Highly Mannosylated Ligands
    • Nagahori, N.; Lee, R. T.; Nishimura, S. I.; Pagé, D.; Roy, R.; Lee, Y. C. Inhibition of Adhesion of Type 1 Fimbriated Escherichia Coli to Highly Mannosylated Ligands ChemBioChem 2002, 3, 836-844 10.1002/1439-7633(20020902)3:9<836::AID-CBIC836>3.0.CO;2-2
    • (2002) ChemBioChem , vol.3 , pp. 836-844
    • Nagahori, N.1    Lee, R.T.2    Nishimura, S.I.3    Pagé, D.4    Roy, R.5    Lee, Y.C.6
  • 49
    • 0035917347 scopus 로고    scopus 로고
    • A Modular Approach for the Synthesis of Oligosaccharide Mimetics
    • Patel, A.; Lindhorst, T. K. A Modular Approach for the Synthesis of Oligosaccharide Mimetics J. Org. Chem. 2001, 66, 2674-2680 10.1021/jo005671u
    • (2001) J. Org. Chem. , vol.66 , pp. 2674-2680
    • Patel, A.1    Lindhorst, T.K.2
  • 50
    • 37549038807 scopus 로고    scopus 로고
    • Mannosylated G(0) Dendrimers with Nanomolar Affinities to Escherichia coli FimH
    • Touaibia, M.; Wellens, A.; Shiao, T. C.; Wang, Q.; Sirois, S.; Bouckaert, J.; Roy, R. Mannosylated G(0) Dendrimers with Nanomolar Affinities to Escherichia Coli FimH ChemMedChem 2007, 2, 1190-1201 10.1002/cmdc.200700063
    • (2007) ChemMedChem , vol.2 , pp. 1190-1201
    • Touaibia, M.1    Wellens, A.2    Shiao, T.C.3    Wang, Q.4    Sirois, S.5    Bouckaert, J.6    Roy, R.7
  • 51
    • 78651268228 scopus 로고    scopus 로고
    • The Functional Valency of Dodecamannosylated Fullerenes with Escherichia coli FimH - Towards Novel Bacterial Antiadhesives
    • Durka, M.; Buffet, K.; Iehl, J.; Holler, M.; Nierengarten, J.-F.; Taganna, J.; Bouckaert, J.; Vincent, S. P. The Functional Valency of Dodecamannosylated Fullerenes with Escherichia Coli FimH-Towards Novel Bacterial Antiadhesives Chem. Commun. 2011, 47, 1321-1323 10.1039/C0CC04468G
    • (2011) Chem. Commun. , vol.47 , pp. 1321-1323
    • Durka, M.1    Buffet, K.2    Iehl, J.3    Holler, M.4    Nierengarten, J.-F.5    Taganna, J.6    Bouckaert, J.7    Vincent, S.P.8
  • 52
    • 84878590386 scopus 로고    scopus 로고
    • Heptyl α-D-Mannosides Grafted on a β-Cyclodextrin Core to Interfere with Escherichia coli Adhesion: An in Vivo Multivalent Effect
    • Bouckaert, J.; Li, Z.; Xavier, C.; Almant, M.; Caveliers, V.; Lahoutte, T.; Weeks, S. D.; Kovensky, J.; Gouin, S. G. Heptyl α-D-Mannosides Grafted on a β-Cyclodextrin Core to Interfere with Escherichia Coli Adhesion: An in Vivo Multivalent Effect Chem.-Eur. J. 2013, 19, 7847-7855 10.1002/chem.201204015
    • (2013) Chem. - Eur. J. , vol.19 , pp. 7847-7855
    • Bouckaert, J.1    Li, Z.2    Xavier, C.3    Almant, M.4    Caveliers, V.5    Lahoutte, T.6    Weeks, S.D.7    Kovensky, J.8    Gouin, S.G.9
  • 53
    • 77957238759 scopus 로고    scopus 로고
    • Expression of the Carbohydrate Recognition Domain of FimH and Development of a Competitive Binding Assay
    • Rabbani, S.; Jiang, X.; Schwardt, O.; Ernst, B. Expression of the Carbohydrate Recognition Domain of FimH and Development of a Competitive Binding Assay Anal. Biochem. 2010, 407, 188-195 10.1016/j.ab.2010.08.007
    • (2010) Anal. Biochem. , vol.407 , pp. 188-195
    • Rabbani, S.1    Jiang, X.2    Schwardt, O.3    Ernst, B.4
  • 54
    • 84862564470 scopus 로고    scopus 로고
    • The Tyrosine Gate as a Potential Entropic Lever in the Receptor-Binding Site of the Bacterial Adhesin FimH
    • Wellens, A.; Lahmann, M.; Touaibia, M.; Vaucher, J.; Oscarson, S.; Roy, R.; Remaut, H.; Bouckaert, J. The Tyrosine Gate as a Potential Entropic Lever in the Receptor-Binding Site of the Bacterial Adhesin FimH Biochemistry 2012, 51, 4790-4799 10.1021/bi300251r
    • (2012) Biochemistry , vol.51 , pp. 4790-4799
    • Wellens, A.1    Lahmann, M.2    Touaibia, M.3    Vaucher, J.4    Oscarson, S.5    Roy, R.6    Remaut, H.7    Bouckaert, J.8
  • 56
    • 0033551911 scopus 로고    scopus 로고
    • X-Ray Structure of the FimC-FimH Chaperone-Adhesin Complex from Uropathogenic
    • Choudhury, D. X-Ray Structure of the FimC-FimH Chaperone-Adhesin Complex from Uropathogenic Science 1999, 285, 1061-1066 10.1126/science.285.5430.1061
    • (1999) Science , vol.285 , pp. 1061-1066
    • Choudhury, D.1
  • 59
    • 0036392235 scopus 로고    scopus 로고
    • Chaperone-Independent Folding of Type 1 Pilus Domains
    • Vetsch, M.; Sebbel, P.; Glockshuber, R. Chaperone-Independent Folding of Type 1 Pilus Domains J. Mol. Biol. 2002, 322, 827-840 10.1016/S0022-2836(02)00845-8
    • (2002) J. Mol. Biol. , vol.322 , pp. 827-840
    • Vetsch, M.1    Sebbel, P.2    Glockshuber, R.3
  • 67
    • 0015417053 scopus 로고
    • Utilization of Operational Schemes for Analog Synthesis in Drug Design
    • Topliss, J. G. Utilization of Operational Schemes for Analog Synthesis in Drug Design J. Med. Chem. 1972, 15, 1006-1011 10.1021/jm00280a002
    • (1972) J. Med. Chem. , vol.15 , pp. 1006-1011
    • Topliss, J.G.1
  • 68
    • 0017344045 scopus 로고
    • A Manual Method for Applying the Hansch Approach to Drug Design
    • Topliss, J. G. A Manual Method for Applying the Hansch Approach to Drug Design J. Med. Chem. 1977, 20, 463-469 10.1021/jm00214a001
    • (1977) J. Med. Chem. , vol.20 , pp. 463-469
    • Topliss, J.G.1
  • 69
    • 0040914011 scopus 로고
    • Analysis. A Method for the Correlation of Biological Activity and Chemical Structure
    • Hansch, C.; Fujita, T. Analysis. A Method for the Correlation of Biological Activity and Chemical Structure J. Am. Chem. Soc. 1964, 86, 1616-1626 10.1021/ja01062a035
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 1616-1626
    • Hansch, C.1    Fujita, T.2
  • 70
    • 0001454089 scopus 로고
    • Quantitative Structure-Activity Relationships in Drug Design
    • Hansch, C. Quantitative Structure-Activity Relationships in Drug Design Sect. Title Pharmacodyn. 1971, 11, 271-342
    • (1971) Sect. Title Pharmacodyn. , vol.11 , pp. 271-342
    • Hansch, C.1
  • 71
    • 0028936571 scopus 로고
    • An Exact Mathematical Expression for Describing Competitive Binding of Two Different Ligands to a Protein Molecule
    • Wang, Z.-X. An Exact Mathematical Expression for Describing Competitive Binding of Two Different Ligands to a Protein Molecule FEBS Lett. 1995, 360, 111-114 10.1016/0014-5793(95)00062-E
    • (1995) FEBS Lett. , vol.360 , pp. 111-114
    • Wang, Z.-X.1
  • 72
    • 0002311366 scopus 로고    scopus 로고
    • High-Throughput Measurements of Solubility Profiles
    • Testa, B. van de Waterbeemd, H. Folkers, G. Guy, R. Verlag Helvetica Chimica Acta: Zürich
    • Avdeef, A. High-Throughput Measurements of Solubility Profiles. In Pharmacokinetic Optimization in Drug Research; Testa, B.; van de Waterbeemd, H.; Folkers, G.; Guy, R., Eds.; Verlag Helvetica Chimica Acta: Zürich, 2001; pp 305-325.
    • (2001) Pharmacokinetic Optimization in Drug Research , pp. 305-325
    • Avdeef, A.1
  • 73
    • 0023790173 scopus 로고
    • The Measurement of Partition Coefficients
    • Dearden, J.; Bresnen, G. The Measurement of Partition Coefficients Quant. Struct.-Act. Relat. 1988, 7, 133-144 10.1002/qsar.19880070304
    • (1988) Quant. Struct.-Act. Relat. , vol.7 , pp. 133-144
    • Dearden, J.1    Bresnen, G.2
  • 74
    • 0032568397 scopus 로고    scopus 로고
    • Physicochemical High Throughput Screening: Parallel Artificial Membrane Permeation Assay in the Description of Passive Absorption Processes
    • Kansy, M.; Senner, F.; Gubernator, K. Physicochemical High Throughput Screening: Parallel Artificial Membrane Permeation Assay in the Description of Passive Absorption Processes J. Med. Chem. 1998, 41, 1007-1010 10.1021/jm970530e
    • (1998) J. Med. Chem. , vol.41 , pp. 1007-1010
    • Kansy, M.1    Senner, F.2    Gubernator, K.3
  • 75
    • 84929316918 scopus 로고    scopus 로고
    • The Tyrosine Gate of the Bacterial Lectin FimH: A Conformational Analysis by NMR Spectroscopy and X-Ray Crystallography
    • Fiege, B.; Rabbani, S.; Preston, R. C.; Jakob, R. P.; Zihlmann, P.; Schwardt, O.; Jiang, X.; Maier, T.; Ernst, B. The Tyrosine Gate of the Bacterial Lectin FimH: A Conformational Analysis by NMR Spectroscopy and X-Ray Crystallography ChemBioChem 2015, 16, 1235-1246 10.1002/cbic.201402714
    • (2015) ChemBioChem , vol.16 , pp. 1235-1246
    • Fiege, B.1    Rabbani, S.2    Preston, R.C.3    Jakob, R.P.4    Zihlmann, P.5    Schwardt, O.6    Jiang, X.7    Maier, T.8    Ernst, B.9
  • 77
    • 0028153922 scopus 로고
    • FimH Family of Type 1 Fimbrial Adhesins: Functional Heterogeneity due to Minor Sequence Variations among fimH Genes
    • Sokurenko, E. V.; Courtney, H. S.; Ohman, D. E.; Klemm, P.; Hasty, D. L. FimH Family of Type 1 Fimbrial Adhesins: Functional Heterogeneity due to Minor Sequence Variations among fimH Genes J. Bacteriol. 1994, 176, 748-755 10.1128/jb.176.3.748-755.1994
    • (1994) J. Bacteriol. , vol.176 , pp. 748-755
    • Sokurenko, E.V.1    Courtney, H.S.2    Ohman, D.E.3    Klemm, P.4    Hasty, D.L.5
  • 78
    • 0029063295 scopus 로고
    • Quantitative Differences in Adhesiveness of Type 1 Fimbriated Escherichia coli due to Structural Differences in fimH Genes
    • Sokurenko, E. V.; Courtney, H. S.; Maslow, J.; Siitonen, A.; Hasty, D. L. Quantitative Differences in Adhesiveness of Type 1 Fimbriated Escherichia Coli due to Structural Differences in fimH Genes J. Bacteriol. 1995, 177, 3680-3686 10.1128/jb.177.13.3680-3686.1995
    • (1995) J. Bacteriol. , vol.177 , pp. 3680-3686
    • Sokurenko, E.V.1    Courtney, H.S.2    Maslow, J.3    Siitonen, A.4    Hasty, D.L.5
  • 79
    • 0034978222 scopus 로고    scopus 로고
    • Establishment of a Persistent Escherichia coli Reservoir during the Acute Phase of a Bladder Infection
    • Mulvey, M. A.; Schilling, J. D.; Hultgren, S. J. Establishment of a Persistent Escherichia Coli Reservoir during the Acute Phase of a Bladder Infection Infect. Immun. 2001, 69, 4572-4579 10.1128/IAI.69.7.4572-4579.2001
    • (2001) Infect. Immun. , vol.69 , pp. 4572-4579
    • Mulvey, M.A.1    Schilling, J.D.2    Hultgren, S.J.3
  • 83
    • 0030444550 scopus 로고    scopus 로고
    • Guidance in the Setting of Drug Particle Size Specifications to Minimize Variability in Absorption
    • Johnson, K. C.; Swindell, A. C. Guidance in the Setting of Drug Particle Size Specifications to Minimize Variability in Absorption Pharm. Res. 1996, 13, 1795-1798 10.1023/A:1016068705255
    • (1996) Pharm. Res. , vol.13 , pp. 1795-1798
    • Johnson, K.C.1    Swindell, A.C.2
  • 84
    • 0034461768 scopus 로고    scopus 로고
    • Drug-like Properties and the Causes of Poor Solubility and Poor Permeability
    • Lipinski, C. A. Drug-like Properties and the Causes of Poor Solubility and Poor Permeability J. Pharmacol. Toxicol. Methods 2000, 44, 235-249 10.1016/S1056-8719(00)00107-6
    • (2000) J. Pharmacol. Toxicol. Methods , vol.44 , pp. 235-249
    • Lipinski, C.A.1
  • 85
    • 0029865450 scopus 로고    scopus 로고
    • Design of Drugs Involving the Concepts and Theories of Drug Metabolism and Pharmacokinetics
    • Smith, D. A.; Jones, B. C.; Walker, D. K. Design of Drugs Involving the Concepts and Theories of Drug Metabolism and Pharmacokinetics Med. Res. Rev. 1996, 16, 243-266 10.1002/(SICI)1098-1128(199605)16:3<243::AID-MED2>3.3.CO;2-R
    • (1996) Med. Res. Rev. , vol.16 , pp. 243-266
    • Smith, D.A.1    Jones, B.C.2    Walker, D.K.3
  • 86
    • 0035953319 scopus 로고    scopus 로고
    • Property-Based Design: Optimization of Drug Absorption and Pharmacokinetics
    • van de Waterbeemd, H.; Smith, D. A.; Beaumont, K.; Walker, D. K. Property-Based Design: Optimization of Drug Absorption and Pharmacokinetics J. Med. Chem. 2001, 44, 1313-1333 10.1021/jm000407e
    • (2001) J. Med. Chem. , vol.44 , pp. 1313-1333
    • Van De Waterbeemd, H.1    Smith, D.A.2    Beaumont, K.3    Walker, D.K.4
  • 89
    • 0028143313 scopus 로고
    • Construction and Characterization of a Set of E. Coli Strains Deficient in All Known Loci Affecting the Proteolytic Stability of Secreted Recombinant Proteins
    • Meerman, H. J.; Georgiou, G. Construction and Characterization of a Set of E. Coli Strains Deficient in All Known Loci Affecting the Proteolytic Stability of Secreted Recombinant Proteins Bio/Technology 1994, 12, 1107-1110 10.1038/nbt1194-1107
    • (1994) Bio/Technology , vol.12 , pp. 1107-1110
    • Meerman, H.J.1    Georgiou, G.2
  • 91
    • 69049089340 scopus 로고    scopus 로고
    • 2 nd ed. RSC Publishing: Cambridge, UK
    • Cooper, A. Biophysical Chemistry, 2 nd ed.; RSC Publishing: Cambridge, UK, 2011.
    • (2011) Biophysical Chemistry
    • Cooper, A.1
  • 92
    • 84861840835 scopus 로고    scopus 로고
    • High-Precision Isothermal Titration Calorimetry with Automated Peak-Shape Analysis
    • Keller, S.; Vargas, C.; Zhao, H.; Piszczek, G.; Brautigam, C. A.; Schuck, P. High-Precision Isothermal Titration Calorimetry with Automated Peak-Shape Analysis Anal. Chem. 2012, 84, 5066-5073 10.1021/ac3007522
    • (2012) Anal. Chem. , vol.84 , pp. 5066-5073
    • Keller, S.1    Vargas, C.2    Zhao, H.3    Piszczek, G.4    Brautigam, C.A.5    Schuck, P.6
  • 93
    • 33845937672 scopus 로고    scopus 로고
    • Studying Multisite Binary and Ternary Protein Interactions by Global Analysis of Isothermal Titration Calorimetry Data in SEDPHAT: Application to Adaptor Protein Complexes in Cell Signaling
    • Houtman, J. C. D.; Brown, P. H.; Bowden, B.; Yamaguchi, H.; Appella, E.; Samelson, L. E.; Schuck, P. Studying Multisite Binary and Ternary Protein Interactions by Global Analysis of Isothermal Titration Calorimetry Data in SEDPHAT: Application to Adaptor Protein Complexes in Cell Signaling Protein Sci. 2007, 16, 30-42 10.1110/ps.062558507
    • (2007) Protein Sci. , vol.16 , pp. 30-42
    • Houtman, J.C.D.1    Brown, P.H.2    Bowden, B.3    Yamaguchi, H.4    Appella, E.5    Samelson, L.E.6    Schuck, P.7
  • 94
    • 84880529288 scopus 로고    scopus 로고
    • Protein and Ligand Preparation: Parameters, Protocols, and Influence on Virtual Screening Enrichments
    • Madhavi Sastry, G.; Adzhigirey, M.; Day, T.; Annabhimoju, R.; Sherman, W. Protein and Ligand Preparation: Parameters, Protocols, and Influence on Virtual Screening Enrichments J. Comput.-Aided Mol. Des. 2013, 27, 221-234 10.1007/s10822-013-9644-8
    • (2013) J. Comput.-Aided Mol. Des. , vol.27 , pp. 221-234
    • Madhavi Sastry, G.1    Adzhigirey, M.2    Day, T.3    Annabhimoju, R.4    Sherman, W.5
  • 95
    • 85023781871 scopus 로고    scopus 로고
    • Protein Preparation Wizard. version 3.4. Schrödinger Release 2015-4, Schrödinger, LLC: New York, NY
    • Protein Preparation Wizard. Epik, version 3.4., Schrödinger Release 2015-4, Schrödinger, LLC: New York, NY, 2015.
    • (2015) Epik
  • 96
    • 85023764364 scopus 로고    scopus 로고
    • version 6.9; Schrödinger, LLC: New York, NY
    • Impact, version 6.9; Schrödinger, LLC: New York, NY, 2015.
    • (2015) Impact
  • 98
    • 0036310711 scopus 로고    scopus 로고
    • On the Role of the Crystal Environment in Determining Protein Side-Chain Conformations
    • Jacobson, M. P.; Friesner, R. A.; Xiang, Z.; Honig, B. On the Role of the Crystal Environment in Determining Protein Side-Chain Conformations J. Mol. Biol. 2002, 320, 597-608 10.1016/S0022-2836(02)00470-9
    • (2002) J. Mol. Biol. , vol.320 , pp. 597-608
    • Jacobson, M.P.1    Friesner, R.A.2    Xiang, Z.3    Honig, B.4
  • 99
    • 85023773399 scopus 로고    scopus 로고
    • version 4.2, Schrödinger Release 2015-4; Schrödinger, LLC: New York, NY
    • Prime, version 4.2, Schrödinger Release 2015-4; Schrödinger, LLC: New York, NY, 2015.
    • (2015) Prime
  • 100
    • 79952580651 scopus 로고    scopus 로고
    • Parameterization of a B3LYP Specific Correction for Noncovalent Interactions and Basis Set Superposition Error on a Gigantic Data Set of CCSD(T) Quality Noncovalent Interaction Energies
    • Schneebeli, S. T.; Bochevarov, A. D.; Friesner, R. A. Parameterization of a B3LYP Specific Correction for Noncovalent Interactions and Basis Set Superposition Error on a Gigantic Data Set of CCSD(T) Quality Noncovalent Interaction Energies J. Chem. Theory Comput. 2011, 7, 658-668 10.1021/ct100651f
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 658-668
    • Schneebeli, S.T.1    Bochevarov, A.D.2    Friesner, R.A.3
  • 102
    • 85023772002 scopus 로고    scopus 로고
    • version 9.0, Schrödinger Release 2015-4; Schrödinger, LLC: New York, NY
    • Jaguar, version 9.0, Schrödinger Release 2015-4; Schrödinger, LLC: New York, NY, 2015.
    • (2015) Jaguar
  • 104
    • 77950571108 scopus 로고    scopus 로고
    • New Substructure Filters for Removal of Pan Assay Interference Compounds (PAINS) from Screening Libraries and for Their Exclusion in Bioassays
    • Baell, J. B.; Holloway, G. A. New Substructure Filters for Removal of Pan Assay Interference Compounds (PAINS) from Screening Libraries and for Their Exclusion in Bioassays J. Med. Chem. 2010, 53, 2719-2740 10.1021/jm901137j
    • (2010) J. Med. Chem. , vol.53 , pp. 2719-2740
    • Baell, J.B.1    Holloway, G.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.