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Volumn 55, Issue 11, 2012, Pages 5632-5636

Probing the interactions of macrolide antibiotics with membrane-mimetics by NMR spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

AZAHOMOERYTHROMYCIN; AZITHROMYCIN; AZITHROMYCIN AGLYCONE; CLARITHROMYCIN; DECLADINOSYL AZITHROMYCIN; ERYTHROMYCIN; MACROLIDE; PHOSPHOLIPASE A1; UNCLASSIFIED DRUG;

EID: 84862272695     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm300647f     Document Type: Article
Times cited : (31)

References (30)
  • 2
    • 0035840852 scopus 로고    scopus 로고
    • Anti-inflammatory effects of macrolide antibiotics
    • Culic, O.; Erakovic, V.; Parnham, M. J. Anti-inflammatory effects of macrolide antibiotics Eur. J. Pharmacol. 2001, 429, 209-229
    • (2001) Eur. J. Pharmacol. , vol.429 , pp. 209-229
    • Culic, O.1    Erakovic, V.2    Parnham, M.J.3
  • 3
    • 39549115019 scopus 로고    scopus 로고
    • Macrolide antibiotics as immunomodulatory medications: Proposed mechanisms of action
    • Shinkai, M.; Henke, M. O.; Rubin, B. K. Macrolide antibiotics as immunomodulatory medications: proposed mechanisms of action Pharmacol. Ther. 2008, 117, 393-405
    • (2008) Pharmacol. Ther. , vol.117 , pp. 393-405
    • Shinkai, M.1    Henke, M.O.2    Rubin, B.K.3
  • 6
    • 40849146982 scopus 로고    scopus 로고
    • Role of gemifloxacin in the management of community-acquired lower respiratory tract infections
    • Blondeau, J. M.; Tillotson, G. Role of gemifloxacin in the management of community-acquired lower respiratory tract infections Int. J. Antimicrob. Agents 2008, 31, 299-306
    • (2008) Int. J. Antimicrob. Agents , vol.31 , pp. 299-306
    • Blondeau, J.M.1    Tillotson, G.2
  • 7
    • 44149096519 scopus 로고    scopus 로고
    • Bacterial pneumonia
    • Loebinger, M. R.; Woilson, R. Bacterial pneumonia Medicine 2008, 36, 285-290
    • (2008) Medicine , vol.36 , pp. 285-290
    • Loebinger, M.R.1    Woilson, R.2
  • 8
    • 29044437704 scopus 로고    scopus 로고
    • Macrolide Antibiotics: Binding Site, Mechanism of Action, Resistance
    • Gaynor, M.; Mankin, A. S. Macrolide Antibiotics: Binding Site, Mechanism of Action, Resistance Front. Med. Chem. 2005, 2, 21-35
    • (2005) Front. Med. Chem. , vol.2 , pp. 21-35
    • Gaynor, M.1    Mankin, A.S.2
  • 9
    • 68149131329 scopus 로고    scopus 로고
    • Free and bound state structures of 6- O -methyl homoerythromycins and epitope mapping of their interactions with ribosomes
    • Novak, P.; Barber, J.; Cikos, A.; Arsic, B.; Plavec, J.; Lazarevski, G.; Tepes, P.; Kosutic-Hulita, N. Free and bound state structures of 6- O -methyl homoerythromycins and epitope mapping of their interactions with ribosomes Bioorg. Med. Chem. 2009, 17, 5857-5867
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 5857-5867
    • Novak, P.1    Barber, J.2    Cikos, A.3    Arsic, B.4    Plavec, J.5    Lazarevski, G.6    Tepes, P.7    Kosutic-Hulita, N.8
  • 10
    • 31544436607 scopus 로고    scopus 로고
    • Systematic approach to understanding macrolide-ribosome interactions: NMR and modeling studies of oleandomycin and its derivatives
    • Novak, P.; Tatic, I.; Tepes, P.; Kostrun, S.; Barber, J. Systematic approach to understanding macrolide-ribosome interactions: NMR and modeling studies of oleandomycin and its derivatives J. Phys. Chem. A 2006, 110, 572-579
    • (2006) J. Phys. Chem. A , vol.110 , pp. 572-579
    • Novak, P.1    Tatic, I.2    Tepes, P.3    Kostrun, S.4    Barber, J.5
  • 11
    • 11844302801 scopus 로고    scopus 로고
    • Conformational analysis of oleandomycin and its 8-methylene-9-oxime derivative by NMR and molecular modelling
    • Novak, P.; Tomisic, Z. B.; Tepes, P.; Lazarevski, G.; Plavec, J.; Turkalj, G. Conformational analysis of oleandomycin and its 8-methylene-9-oxime derivative by NMR and molecular modelling Org. Biomol. Chem. 2005, 3, 39-47
    • (2005) Org. Biomol. Chem. , vol.3 , pp. 39-47
    • Novak, P.1    Tomisic, Z.B.2    Tepes, P.3    Lazarevski, G.4    Plavec, J.5    Turkalj, G.6
  • 13
    • 0033047391 scopus 로고    scopus 로고
    • Interactions of macrolide antibiotics (Erythromycin A, roxithromycin, erythromycylamine [Dirithromycin], and azithromycin) with phospholipids: Computer-aided conformational analysis and studies on acellular and cell culture models
    • Montenez, J. P.; Van Bambeke, F.; Piret, J.; Brasseur, R.; Tulkens, P. M.; Mingeot-Leclercq, M. P. Interactions of macrolide antibiotics (Erythromycin A, roxithromycin, erythromycylamine [Dirithromycin], and azithromycin) with phospholipids: computer-aided conformational analysis and studies on acellular and cell culture models Toxicol. Appl. Pharmacol. 1999, 156, 129-140
    • (1999) Toxicol. Appl. Pharmacol. , vol.156 , pp. 129-140
    • Montenez, J.P.1    Van Bambeke, F.2    Piret, J.3    Brasseur, R.4    Tulkens, P.M.5    Mingeot-Leclercq, M.P.6
  • 14
    • 0035687129 scopus 로고    scopus 로고
    • Drug-induced phospholipidosis: Are there functional consequences?
    • Reasor, M. J.; Kacew, S. Drug-induced phospholipidosis: are there functional consequences? Exp. Biol. Med. (Maywood, NJ, U.S.) 2001, 226, 825-830
    • (2001) Exp. Biol. Med. (Maywood, NJ, U.S.) , vol.226 , pp. 825-830
    • Reasor, M.J.1    Kacew, S.2
  • 15
    • 33749042117 scopus 로고    scopus 로고
    • Drug-induced phospholipidosis
    • Anderson, N.; Borlak, J. Drug-induced phospholipidosis FEBS Lett. 2006, 580, 5533-5540
    • (2006) FEBS Lett. , vol.580 , pp. 5533-5540
    • Anderson, N.1    Borlak, J.2
  • 17
    • 77955417391 scopus 로고    scopus 로고
    • The peptide hormone ghrelin binds to membrane-mimetics via its octanoyl chain and an adjacent phenylalanine
    • Grossauer, J.; Kosol, S.; Schrank, E.; Zangger, K. The peptide hormone ghrelin binds to membrane-mimetics via its octanoyl chain and an adjacent phenylalanine Bioorg. Med. Chem. 2010, 18, 5483-5488
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 5483-5488
    • Grossauer, J.1    Kosol, S.2    Schrank, E.3    Zangger, K.4
  • 18
    • 77950519481 scopus 로고    scopus 로고
    • Dynamics and orientation of a cationic antimicrobial peptide in two membrane-mimetic systems
    • Kosol, S.; Zangger, K. Dynamics and orientation of a cationic antimicrobial peptide in two membrane-mimetic systems J. Struct. Biol. 2010, 170, 172-179
    • (2010) J. Struct. Biol. , vol.170 , pp. 172-179
    • Kosol, S.1    Zangger, K.2
  • 19
    • 34247536274 scopus 로고    scopus 로고
    • Mapping the orientation of helices in micelle-bound peptides by paramagnetic relaxation waves
    • Respondek, M.; Madl, T.; Göbl, C.; Golser, R.; Zangger, K. Mapping the orientation of helices in micelle-bound peptides by paramagnetic relaxation waves J. Am. Chem. Soc. 2007, 129, 5228-5234
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5228-5234
    • Respondek, M.1    Madl, T.2    Göbl, C.3    Golser, R.4    Zangger, K.5
  • 21
    • 77950576779 scopus 로고    scopus 로고
    • Influence of phosphocholine alkyl chain length on peptide-micelle interactions and micellar size and shape
    • Göbl, C.; Dulle, M.; Hohlweg, W.; Grossauer, J.; Falsone, S. F.; Glatter, O.; Zangger, K. Influence of phosphocholine alkyl chain length on peptide-micelle interactions and micellar size and shape J. Phys. Chem. 2010, 114, 4717-4724
    • (2010) J. Phys. Chem. , vol.114 , pp. 4717-4724
    • Göbl, C.1    Dulle, M.2    Hohlweg, W.3    Grossauer, J.4    Falsone, S.F.5    Glatter, O.6    Zangger, K.7
  • 22
  • 23
    • 70350536779 scopus 로고    scopus 로고
    • Quantitative use of paramagnetic relaxation enhancements for determining orientations and insertion depths of peptides in micelles
    • Franzmann, M.; Otzen, D.; Wimmer, R. Quantitative use of paramagnetic relaxation enhancements for determining orientations and insertion depths of peptides in micelles ChemBioChem 2009, 10, 2339-2347
    • (2009) ChemBioChem , vol.10 , pp. 2339-2347
    • Franzmann, M.1    Otzen, D.2    Wimmer, R.3
  • 24
    • 0037160426 scopus 로고    scopus 로고
    • Identification of protein surfaces by NMR measurements with a paramagnetic Gd(III) chelate
    • Pintacuda, G.; Otting, G. Identification of protein surfaces by NMR measurements with a paramagnetic Gd(III) chelate J. Am. Chem. Soc. 2002, 124, 372-373
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 372-373
    • Pintacuda, G.1    Otting, G.2
  • 25
    • 33745143943 scopus 로고    scopus 로고
    • Detailed description of the conformation and location of membrane-bound erythromycin a using isotropic bicelles
    • Matsumori, N.; Morooka, A.; Murata, M. Detailed description of the conformation and location of membrane-bound erythromycin a using isotropic bicelles J. Med. Chem. 2006, 49, 3501-3508
    • (2006) J. Med. Chem. , vol.49 , pp. 3501-3508
    • Matsumori, N.1    Morooka, A.2    Murata, M.3
  • 26
    • 0042978476 scopus 로고    scopus 로고
    • The macrolide antibiotic azithromycin interacts with lipids and affects membrane organization and fluidity: Studies on Langmuir-Blodgett monolayers, liposomes and J774 macrophages
    • Tyteca, D.; Schanck, A.; Dufrene, Y. F.; Deleu, M.; Courtoy, P. J.; Tulkens, P. M.; Mingeot-Leclercq, M. P. The macrolide antibiotic azithromycin interacts with lipids and affects membrane organization and fluidity: studies on Langmuir-Blodgett monolayers, liposomes and J774 macrophages J. Membr. Biol. 2003, 192, 203-215
    • (2003) J. Membr. Biol. , vol.192 , pp. 203-215
    • Tyteca, D.1    Schanck, A.2    Dufrene, Y.F.3    Deleu, M.4    Courtoy, P.J.5    Tulkens, P.M.6    Mingeot-Leclercq, M.P.7
  • 27
    • 0022353095 scopus 로고
    • Mechanism of cationic amphiphilic drug inhibition of purified lysosomal phospholipase A1
    • Kubo, M.; Hostetler, K. Y. Mechanism of cationic amphiphilic drug inhibition of purified lysosomal phospholipase A1 Biochemistry 1985, 24, 6515-6520
    • (1985) Biochemistry , vol.24 , pp. 6515-6520
    • Kubo, M.1    Hostetler, K.Y.2
  • 28
    • 0017075334 scopus 로고
    • Lysosomal alterations in cultured macrophages exposed to anorexigenic and psychotropic drugs
    • Drenckhahn, D.; Kleine, L.; Lullmann-Rauch, R. Lysosomal alterations in cultured macrophages exposed to anorexigenic and psychotropic drugs Lab. Invest. 1976, 35, 116-123
    • (1976) Lab. Invest. , vol.35 , pp. 116-123
    • Drenckhahn, D.1    Kleine, L.2    Lullmann-Rauch, R.3
  • 30
    • 0021959563 scopus 로고
    • Chloroquine-induced phospholipid fatty liver. Measurement of drug and lipid concentrations in rat liver lysosomes
    • Hostetler, K. Y.; Reasor, M.; Yazaki, P. J. Chloroquine-induced phospholipid fatty liver. Measurement of drug and lipid concentrations in rat liver lysosomes J. Biol. Chem. 1985, 260, 215-219
    • (1985) J. Biol. Chem. , vol.260 , pp. 215-219
    • Hostetler, K.Y.1    Reasor, M.2    Yazaki, P.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.