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Volumn 109, Issue 28, 2012, Pages 11156-11159

Polyene antibiotic that inhibits membrane transport proteins

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CARRIER PROTEIN; ERGOSTEROL; NATAMYCIN; STEROL;

EID: 84863929700     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1203375109     Document Type: Article
Times cited : (92)

References (34)
  • 1
    • 55649119761 scopus 로고    scopus 로고
    • Update on the epidemiology and diagnosis of invasive fungal infection
    • Cuenca-Estrella M, et al. (2008) Update on the epidemiology and diagnosis of invasive fungal infection. Int J Antimicrob Agents 32(Suppl 2):S143-S147.
    • (2008) Int J Antimicrob Agents , vol.32 , Issue.SUPPL. 2
    • Cuenca-Estrella, M.1
  • 2
    • 0037451929 scopus 로고    scopus 로고
    • The epidemiology of sepsis in the United States from 1979 through 2000
    • DOI 10.1056/NEJMoa022139
    • Martin GS, Mannino DM, Eaton S, Moss M (2003) The epidemiology of sepsis in the United States from 1979 through 2000. N Engl J Med 348:1546-1554. (Pubitemid 36437931)
    • (2003) New England Journal of Medicine , vol.348 , Issue.16 , pp. 1546-1554
    • Martin, G.S.1    Mannino, D.M.2    Eaton, S.3    Moss, M.4
  • 3
    • 34248189223 scopus 로고    scopus 로고
    • Tracking the microbes in sepsis: Advancements in treatment bring challenges for microbial epidemiology
    • DOI 10.1086/515403
    • Llewelyn MJ, Cohen J (2007) Tracking the microbes in sepsis: Advancements in treatment bring challenges for microbial epidemiology. Clin Infect Dis 44:1343-1348. (Pubitemid 46717297)
    • (2007) Clinical Infectious Diseases , vol.44 , Issue.10 , pp. 1343-1348
    • Llewelyn, M.J.1    Cohen, J.2
  • 4
    • 47849102650 scopus 로고    scopus 로고
    • Outwitting multidrug resistance to antifungals
    • DOI 10.1126/science.1159746
    • Monk BC, Goffeau A (2008) Outwitting multidrug resistance to antifungals. Science 321:367-369. (Pubitemid 352035829)
    • (2008) Science , vol.321 , Issue.5887 , pp. 367-369
    • Monk, B.C.1    Goffeau, A.2
  • 5
    • 39349086422 scopus 로고    scopus 로고
    • Resistance to antifungal agents: Mechanisms and clinical impact
    • DOI 10.1086/524071
    • Kanafani ZA, Perfect JR (2008) Antimicrobial resistance: Resistance to antifungal agents: Mechanisms and clinical impact. Clin Infect Dis 46:120-128. (Pubitemid 351263573)
    • (2008) Clinical Infectious Diseases , vol.46 , Issue.1 , pp. 120-128
    • Kanafani, Z.A.1    Perfect, J.R.2
  • 6
    • 0022862167 scopus 로고
    • How do the polyene macrolide antibiotics affect the cellular membrane properties?
    • Bolard J (1986) How do the polyene macrolide antibiotics affect the cellular membrane properties? Biochim Biophys Acta 864:257-304.
    • (1986) Biochim Biophys Acta , vol.864 , pp. 257-304
    • Bolard, J.1
  • 7
    • 44449087557 scopus 로고    scopus 로고
    • Natamycin blocks fungal growth by binding specifically to ergosterol without permeabilizing the membrane
    • te Welscher YM, et al. (2008) Natamycin blocks fungal growth by binding specifically to ergosterol without permeabilizing the membrane. J Biol Chem 283:6393-6401.
    • (2008) J Biol Chem , vol.283 , pp. 6393-6401
    • Te Welscher, Y.M.1
  • 8
    • 0027231368 scopus 로고
    • Sterol composition of yeast organelle membranes and subcellular distribution of enzymes involved in sterol metabolism
    • Zinser E, Paltauf F, Daum G (1993) Sterol composition of yeast organelle membranes and subcellular distribution of enzymes involved in sterol metabolism. J Bacteriol 175:2853-2858. (Pubitemid 23148716)
    • (1993) Journal of Bacteriology , vol.175 , Issue.10 , pp. 2853-2858
    • Zinser, E.1    Paltauf, F.2    Daum, G.3
  • 10
    • 0035114940 scopus 로고    scopus 로고
    • Construction of phosphatidylethanolamine-less strain of Saccharomyces cerevisiae. Effect on amino acid transport
    • Robl I, Grassl R, Tanner W, Opekarová M (2001) Construction of phosphatidylethanolamine-less strain of Saccharomyces cerevisiae. Effect on amino acid transport. Yeast 18:251-260.
    • (2001) Yeast , vol.18 , pp. 251-260
    • Robl, I.1    Grassl, R.2    Tanner, W.3    Opekarová, M.4
  • 11
    • 0033396550 scopus 로고    scopus 로고
    • Substrate specificity and gene expression of the amino acid permeases in Saccharomyces cerevisiae
    • Regenberg B, Düring-Olsen L, Kielland-Brandt MC, Holmberg S (1999) Substrate specificity and gene expression of the amino-acid permeases in Saccharomyces cerevisiae. Curr Genet 36:317-328. (Pubitemid 30021324)
    • (1999) Current Genetics , vol.36 , Issue.6 , pp. 317-328
    • Regenberg, B.1    During-Olsen, L.2    Kielland-Brandt, M.C.3    Holmberg, S.4
  • 13
    • 1342333128 scopus 로고    scopus 로고
    • Four permeases import proline and the toxic proline analogue azetidine-2-carboxylate into yeast
    • DOI 10.1002/yea.1052
    • Andréasson C, Neve EP, Ljungdahl PO (2004) Four permeases import proline and the toxic proline analogue azetidine-2-carboxylate into yeast. Yeast 21:193-199. (Pubitemid 38256419)
    • (2004) Yeast , vol.21 , Issue.3 , pp. 193-199
    • Andreasson, C.1    Neve, E.P.A.2    Ljungdahl, P.O.3
  • 15
    • 0028798082 scopus 로고
    • Amino acid transporters of lower eukaryotes: Regulation, structure and topogenesis
    • Sophianopoulou V, Diallinas G (1995) Amino acid transporters of lower eukaryotes: Regulation, structure and topogenesis. FEMS Microbiol Rev 16:53-75.
    • (1995) FEMS Microbiol Rev , vol.16 , pp. 53-75
    • Sophianopoulou, V.1    Diallinas, G.2
  • 16
    • 0031567123 scopus 로고    scopus 로고
    • Yeast nutrient transporters
    • Horák J (1997) Yeast nutrient transporters. Biochim Biophys Acta 1331:41-79.
    • (1997) Biochim Biophys Acta , vol.1331 , pp. 41-79
    • Horák, J.1
  • 17
    • 7044231515 scopus 로고    scopus 로고
    • Amphotericin B as a potential probe of the physical state of vesicle membranes
    • DOI 10.1021/ol0487276
    • Zumbuehl A, Stano P, Heer D, Walde P, Carreira EM (2004) Amphotericin B as a potential probe of the physical state of vesicle membranes. Org Lett 6:3683-3686. (Pubitemid 39421922)
    • (2004) Organic Letters , vol.6 , Issue.21 , pp. 3683-3686
    • Zumbuehl, A.1    Stano, P.2    Heer, D.3    Walde, P.4    Carreira, E.M.5
  • 19
    • 65249154315 scopus 로고    scopus 로고
    • Functional interactions between sphingolipids and sterols in biological membranes regulating cell physiology
    • Guan XL, et al. (2009) Functional interactions between sphingolipids and sterols in biological membranes regulating cell physiology. Mol Biol Cell 20:2083-2095.
    • (2009) Mol Biol Cell , vol.20 , pp. 2083-2095
    • Guan, X.L.1
  • 20
    • 0028107843 scopus 로고
    • Nystatin changes the properties of transporters for arginine and sugars. An in vitro study
    • Opekarová M, Tanner W (1994) Nystatin changes the properties of transporters for arginine and sugars. An in vitro study. FEBS Lett 350:46-50.
    • (1994) FEBS Lett , vol.350 , pp. 46-50
    • Opekarová, M.1    Tanner, W.2
  • 21
    • 52649145364 scopus 로고    scopus 로고
    • Inhibition of human immunodeficiency virus type 1 assembly and release by the cholesterol-binding compound amphotericin B methyl ester: Evidence for Vpu dependence
    • Waheed AA, et al. (2008) Inhibition of human immunodeficiency virus type 1 assembly and release by the cholesterol-binding compound amphotericin B methyl ester: Evidence for Vpu dependence. J Virol 82:9776-9781.
    • (2008) J Virol , vol.82 , pp. 9776-9781
    • Waheed, A.A.1
  • 22
    • 0035992124 scopus 로고    scopus 로고
    • Response of gene expression in Saccharomyces cerevisiae to amphotericin B and nystatin measured by microarrays
    • Zhang L, et al. (2002) Response of gene expression in Saccharomyces cerevisiae to amphotericin B and nystatin measured by microarrays. J Antimicrob Chemother 49:905-915. (Pubitemid 34692884)
    • (2002) Journal of Antimicrobial Chemotherapy , vol.49 , Issue.6 , pp. 905-915
    • Zhang, L.1    Zhang, Y.2    Zhou, Y.3    An, S.4    Zhou, Y.5    Cheng, J.6
  • 24
    • 84857134391 scopus 로고    scopus 로고
    • Amphotericin primarily kills yeast by simply binding ergosterol
    • Gray KC, et al. (2012) Amphotericin primarily kills yeast by simply binding ergosterol. Proc Natl Acad Sci USA 109:2234-2239.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 2234-2239
    • Gray, K.C.1
  • 26
    • 46749087921 scopus 로고    scopus 로고
    • Synthesis and biological studies of 35-deoxy amphotericin B methyl ester
    • Szpilman AM, Manthorpe JM, Carreira EM (2008) Synthesis and biological studies of 35-deoxy amphotericin B methyl ester. Angew Chem Int Ed Engl 47:4339-4342.
    • (2008) Angew Chem Int Ed Engl , vol.47 , pp. 4339-4342
    • Szpilman, A.M.1    Manthorpe, J.M.2    Carreira, E.M.3
  • 28
    • 33748766086 scopus 로고    scopus 로고
    • An alternative bactericidal mechanism of action for lantibiotic peptides that target lipid II
    • Hasper HE, et al. (2006) An alternative bactericidal mechanism of action for lantibiotic peptides that target lipid II. Science 313:1636-1637.
    • (2006) Science , vol.313 , pp. 1636-1637
    • Hasper, H.E.1
  • 29
    • 68449090734 scopus 로고    scopus 로고
    • Effects of antibiotics and a protooncogene homolog on destruction of protein translocator SecY
    • van Stelten J, Silva F, Belin D, Silhavy TJ (2009) Effects of antibiotics and a protooncogene homolog on destruction of protein translocator SecY. Science 325:753-756.
    • (2009) Science , vol.325 , pp. 753-756
    • Van Stelten, J.1    Silva, F.2    Belin, D.3    Silhavy, T.J.4
  • 34
    • 0345255797 scopus 로고    scopus 로고
    • Visualization of Protein Compartmentation within the Plasma Membrane of Living Yeast Cells
    • DOI 10.1091/mbc.E03-04-0221
    • Malínská K, Malínský J, Opekarová M, Tanner W (2003) Visualization of protein compartmentation within the plasma membrane of living yeast cells. Mol Biol Cell 14:4427-4436. (Pubitemid 37444645)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.11 , pp. 4427-4436
    • Malinska, K.1    Malinsky, J.2    Opekarova, M.3    Tanner, W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.