메뉴 건너뛰기




Volumn 108, Issue , 2015, Pages 226-231

Structural basis for pore-forming mechanism of staphylococcal α-hemolysin

Author keywords

Crystal structure; Pore forming toxin; Staphylococcal hemolysin

Indexed keywords

ALPHA HEMOLYSIN; BACTERIAL TOXIN; HEMOLYSIN; STAPHYLOCOCCAL ALPHA-TOXIN;

EID: 84946547746     PISSN: 00410101     EISSN: 18793150     Source Type: Journal    
DOI: 10.1016/j.toxicon.2015.09.033     Document Type: Article
Times cited : (43)

References (15)
  • 3
    • 33644859965 scopus 로고    scopus 로고
    • Role of the amino latch of staphylococcal alpha-hemolysin in pore formation: A co-operative interaction between the N terminus and position 217
    • L. Jayasinghe, G. Miles, and H. Bayley Role of the amino latch of staphylococcal alpha-hemolysin in pore formation: a co-operative interaction between the N terminus and position 217 J. Biol. Chem. 281 2006 2195 2204
    • (2006) J. Biol. Chem. , vol.281 , pp. 2195-2204
    • Jayasinghe, L.1    Miles, G.2    Bayley, H.3
  • 5
    • 4544341370 scopus 로고    scopus 로고
    • Bacterial two-component and hetero-heptameric pore-forming cytolytic toxins: Structures, pore-forming mechanism, and organization of the genes
    • J. Kaneko, and Y. Kamio Bacterial two-component and hetero-heptameric pore-forming cytolytic toxins: structures, pore-forming mechanism, and organization of the genes Biosci. Biotechnol. Biochem. 68 2004 981 1003
    • (2004) Biosci. Biotechnol. Biochem. , vol.68 , pp. 981-1003
    • Kaneko, J.1    Kamio, Y.2
  • 6
    • 0031148369 scopus 로고    scopus 로고
    • Sequential binding of Staphylococcal gamma-hemolysin to human erythrocytes and complex formation of the hemolysin on the cell surface
    • J. Kaneko, T. Ozawa, T. Tomita, and Y. Kamio Sequential binding of Staphylococcal gamma-hemolysin to human erythrocytes and complex formation of the hemolysin on the cell surface Biosci. Biotechnol. Biochem. 61 1997 846 851
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 846-851
    • Kaneko, J.1    Ozawa, T.2    Tomita, T.3    Kamio, Y.4
  • 7
    • 0037407011 scopus 로고    scopus 로고
    • Arresting and releasing Staphylococcal alpha-hemolysin at intermediate stages of pore formation by engineered disulfide bonds
    • T. Kawate, and E. Gouaux Arresting and releasing Staphylococcal alpha-hemolysin at intermediate stages of pore formation by engineered disulfide bonds Protein Sci. 12 2003 997 1006
    • (2003) Protein Sci. , vol.12 , pp. 997-1006
    • Kawate, T.1    Gouaux, E.2
  • 9
    • 0036033671 scopus 로고    scopus 로고
    • Controlling pore assembly of staphylococcal gamma-haemolysin by low temperature and by disulphide bond formation in double-cysteine LukF mutants
    • V.T. Nguyen, H. Higuchi, and Y. Kamio Controlling pore assembly of staphylococcal gamma-haemolysin by low temperature and by disulphide bond formation in double-cysteine LukF mutants Mol. Microbiol. 45 2002 1485 1498
    • (2002) Mol. Microbiol. , vol.45 , pp. 1485-1498
    • Nguyen, V.T.1    Higuchi, H.2    Kamio, Y.3
  • 11
    • 79251549159 scopus 로고    scopus 로고
    • 2-Methyl-2,4-pentanediol induces spontaneous assembly of staphylococcal α-hemolysin into heptameric pore structure
    • Y. Tanaka, N. Hirano, J. Kaneko, Y. Kamio, M. Yao, and I. Tanaka 2-Methyl-2,4-pentanediol induces spontaneous assembly of staphylococcal α-hemolysin into heptameric pore structure Protein Sci. 20 2011 448 456
    • (2011) Protein Sci. , vol.20 , pp. 448-456
    • Tanaka, Y.1    Hirano, N.2    Kaneko, J.3    Kamio, Y.4    Yao, M.5    Tanaka, I.6
  • 12
    • 0029125825 scopus 로고
    • Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal alpha-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification
    • B. Walker, and H. Bayley Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal alpha-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification J. Biol. Chem. 270 1995 23065 23071
    • (1995) J. Biol. Chem. , vol.270 , pp. 23065-23071
    • Walker, B.1    Bayley, H.2
  • 13
    • 0029240394 scopus 로고
    • An intermediate in the assembly of a pore-forming protein trapped with a genetically-engineered switch
    • B. Walker, O. Braha, S. Cheley, and H. Bayley An intermediate in the assembly of a pore-forming protein trapped with a genetically-engineered switch Chem. Biol. 2 1995 99 105
    • (1995) Chem. Biol. , vol.2 , pp. 99-105
    • Walker, B.1    Braha, O.2    Cheley, S.3    Bayley, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.