메뉴 건너뛰기




Volumn 9, Issue 7, 1999, Pages

Membrane proteins: A tale of barrels and corks

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0033535603     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(99)80157-2     Document Type: Note
Times cited : (14)

References (10)
  • 1
    • 0032414254 scopus 로고    scopus 로고
    • Transmembrane signalling across the ligand-gated FhuA receptor; Crystal structures of free and ferrichrome-bound states reveal allosteric changes
    • Lochner KP, Rees B, Koebnik R, Mitschler A, Moulinier L, Rosenbusch J, Moras D: Transmembrane signalling across the ligand-gated FhuA receptor; Crystal structures of free and ferrichrome-bound states reveal allosteric changes. Cell 1998, 95:771-778.
    • (1998) Cell , vol.95 , pp. 771-778
    • Lochner, K.P.1    Rees, B.2    Koebnik, R.3    Mitschler, A.4    Moulinier, L.5    Rosenbusch, J.6    Moras, D.7
  • 2
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • Ferguson AD, Hofmann E, Coulton JW, Diederichs K, Welte W: Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide. Science 1998, 282:2215-2220.
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5
  • 4
    • 0027328751 scopus 로고
    • Bacterial porins - Lessons from 3 high-resolution structures
    • Cowan SW: Bacterial porins - Lessons from 3 high-resolution structures. Curr Opin Struct Biol 1993, 3:501-507.
    • (1993) Curr Opin Struct Biol , vol.3 , pp. 501-507
    • Cowan, S.W.1
  • 5
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution
    • Schirmer T, Keller TA, Wang YF, Rosenbusch JP: Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution. Science 1995, 267:512-514.
    • (1995) Science , vol.267 , pp. 512-514
    • Schirmer, T.1    Keller, T.A.2    Wang, Y.F.3    Rosenbusch, J.P.4
  • 6
    • 0031985785 scopus 로고    scopus 로고
    • Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose
    • Forst D, Welte W, Wacker T, Diederichs K: Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose. Nature Struct Biol 1998, 5:37-46.
    • (1998) Nature Struct Biol , vol.5 , pp. 37-46
    • Forst, D.1    Welte, W.2    Wacker, T.3    Diederichs, K.4
  • 7
    • 0027308190 scopus 로고
    • Conversion of the FhuA-transport protein into a diffusion channel through the outer membrane of Escherichia coli
    • Killman H, Benz R, Braun V: Conversion of the FhuA-transport protein into a diffusion channel through the outer membrane of Escherichia coli. EMBO J 1993, 12:3007-3016.
    • (1993) EMBO J , vol.12 , pp. 3007-3016
    • Killman, H.1    Benz, R.2    Braun, V.3
  • 8
    • 0031860932 scopus 로고    scopus 로고
    • A molecular dynamics study of the pores formed by E. coli OmpF porin in a fully hydrated POPE bilayer
    • Tieleman DP, Berendsen HJC: A molecular dynamics study of the pores formed by E. coli OmpF porin in a fully hydrated POPE bilayer. Biophys J 1998, 74:2786-2801.
    • (1998) Biophys J , vol.74 , pp. 2786-2801
    • Tieleman, D.P.1    Berendsen, H.J.C.2
  • 9
    • 0032570779 scopus 로고    scopus 로고
    • Do transmembrane protein superfolds exist?
    • Jones DT: Do transmembrane protein superfolds exist? FEBS Lett 1998, 423:281-285.
    • (1998) FEBS Lett , vol.423 , pp. 281-285
    • Jones, D.T.1
  • 10
    • 0031733336 scopus 로고    scopus 로고
    • Structure of the outer membrane protein A transmembrane domain
    • Pautsch A, Schulz GE: Structure of the outer membrane protein A transmembrane domain. Nature Struct Biol 1998, 5:1013-1017.
    • (1998) Nature Struct Biol , vol.5 , pp. 1013-1017
    • Pautsch, A.1    Schulz, G.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.