다음과 같은 기능을 한번의 로그인으로 사용 할 수 있습니다.
NTIS 바로가기
International journal of medical microbiology : IJMM, v.290 no.4/5, 2000년, pp.389 - 394
Gilbert, Robert J.C. (Division of Structural Biology, Wellcome Trust Centre for Human Genetics, Old Road, Headington, Oxford, OX3 7BN, UK) , Jiménez, José (Department of Crystallography, Birkbeck College, Malet Street, London, WC1E 7HX, UK) , L. (Department of Crystallography, Birkbeck College, Malet Street, London, WC1E 7HX, UK) , Chen, Shaoxia (Department of Microbiology and Immunology, University of Leicester, Leicester, LE1 8AH, UK) , Andrew, S. Peter W. (Department of Crystallography, Birkbeck College, Malet Street, London, WC1E 7HX, UK) , Saibil, Helen R.
AI-Helper
AbstractIn this paper we describe reconstructions by electron cryo-microscopy of two oligomeric states of the pore-forming toxin pneumolysin. The results are interpreted by the fitting of atomic models of separated domains to the 3-dimensional electron density maps, revealing two steps in the mechan...
Microb. Pathog. Alexander 24 167 1998 10.1006/mpat.1997.0185 Amino acid changes affecting the activity of pneumolysin alter the behaviour of pneumococci in pneumonia
Biol. Bayley 7 R763 1997 Toxin structure: part of a hole? Curr
J. Mol. Biol. Czajkowsky 276 325 1998 10.1006/jmbi.1997.1535 Staphylococcal α-hemolysin can form hexamers in phospholipid bilayers
J. Mol. Graphics Esnouf 15 132 1997 10.1016/S1093-3263(97)00021-1 An extensively modified version of Molscript that includes greatly enhanced coloring capabilities
J. Mol. Biol. Gilbert 284 1223 1998 10.1006/jmbi.1998.2258 Self-interaction of pneumolysin, the pore-forming protein toxin of Streptococcus pneumoniae
Cell Gilbert 97 647 1999 10.1016/S0092-8674(00)80775-8 Two structural transitions in membrane pore formation by pneumolysin, the pore-forming toxin of Streptococcus pneumoniae
J. Mol. Biol. Gilbert 293 1145 1999 10.1006/jmbi.1999.3210 Studies on the structure and mechanism of a bacterial protein toxin by analytical ultracentrifugation and small-angle neutron scattering
J. Biol. Chem. Harris 266 6936 1991 10.1016/S0021-9258(20)89592-1 Kinetic aspects of the aggregation of Clostridium perfringens θ-toxin on erythrocyte membranes
Biophys. J. Harroun 76 937 1999 10.1016/S0006-3495(99)77257-7 Experimental evidence for hydrophobic matching and membrane-mediated interactions in lipid bilayers containing gramicidin
Biochemistry Killian 35 1037 1996 10.1021/bi9519258 Induction of non-bilayer structures in diacylphosphatidylcholine model membranes by transmembrane α-helical peptides: Importance of hydrophobic mismatch and proposed role of tryptophans
J. Appl. Crystallogr. Kraulis 24 946 1991 10.1107/S0021889891004399 Molscript - a program to produce both detailed and schematic plots of protein structures
Acta Crystallogr. D Merritt 50 869 1994 10.1107/S0907444994006396 Raster3d version-2.0 - a program for photorealistic molecular graphics
FEBS Lett. Morgan 371 77 1995 10.1016/0014-5793(95)00887-F Subunit organisation and symmetry of pore-forming oligomeric pneumolysin
Rev. Med. Microbiol. Morgan 7 221 1996 10.1097/00013542-199610000-00004 Thiol-activated cytolysins
J. Biochem. Nakamura 123 1145 1998 10.1093/oxfordjournals.jbchem.a022054 Contribution of tryptophan residues to the structural changes in perfringolysin O during interaction with liposomal membranes
FEBS Lett. Olofsson 319 125 1993 10.1016/0014-5793(93)80050-5 The projection structure of perfringolysin O (Clostridium perfringens θ-toxin)
Nature Struct. Biol. Olson 6 134 1999 10.1038/5821 Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel
J. Biol. Chem. Palmer 271 26664 1996 10.1074/jbc.271.43.26664 Membrane-penetrating domain of streptolysin O identified by cysteine scanning mutagenesis
EMBO J. Palmer 17 1598 1998 10.1093/emboj/17.6.1598 Assembly mechanism of the oligomeric streptolysin O pore: the early membrane lesion is lined by a free edge of the lipid membrane and is extended gradually during oligomerization
Structure Pedelacq 7 277 1999 10.1016/S0969-2126(99)80038-0 The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins
Nature Petosa 385 833 1997 10.1038/385833a0 Crystal structure of the anthrax toxin protective antigen
Cell Rossjohn 89 685 1997 10.1016/S0092-8674(00)80251-2 Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
J. Mol. Biol. Rossjohn 284 449 1998 10.1006/jmbi.1998.2167 The molecular mechanism of pneumolysin, a virulence factor from Streptococcus pneumoniae
Cell Shatursky 99 293 1999 10.1016/S0092-8674(00)81660-8 The mechanism of membrane insertion for a cholesterol-dependent cytolysin: A novel paradigm for pore-forming toxins
Biochemistry Shepard 37 14563 1998 10.1021/bi981452f Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin: An α-helical to β-sheet transition identified by fluorescence spectroscopy
Faraday Discuss Smart 111 185 1998 10.1039/a806771f Structure-based prediction of the conductance properties of ion channels
Science Song 274 1859 1996 10.1126/science.274.5294.1859 Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore
해당 논문의 주제분야에서 활용도가 높은 상위 5개 콘텐츠를 보여줍니다.
더보기 버튼을 클릭하시면 더 많은 관련자료를 살펴볼 수 있습니다.
*원문 PDF 파일 및 링크정보가 존재하지 않을 경우 KISTI DDS 시스템에서 제공하는 원문복사서비스를 사용할 수 있습니다.
Copyright KISTI. All Rights Reserved.
※ AI-Helper는 부적절한 답변을 할 수 있습니다.