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Volumn 3, Issue 2, 2009, Pages 239-241

1H, 13C, and 15N NMR assignments of StnII-R29Q, a defective lipid binding mutant of the sea anemone actinoporin Sticholysin II

Author keywords

Actinoporin; Equinatoxin; NMR resonance assignment; Sticholysin

Indexed keywords

COELENTERATE VENOM; MUTANT PROTEIN; STICHOLYSIN II;

EID: 70449533092     PISSN: 18742718     EISSN: 1874270X     Source Type: Journal    
DOI: 10.1007/s12104-009-9184-2     Document Type: Article
Times cited : (8)

References (10)
  • 1
    • 39349103788 scopus 로고    scopus 로고
    • Sea anemone actinoporins: The transition from a folded soluble state to a functionally active membrane-bound oligomeric pore
    • DOI 10.2174/138920307783018686
    • J Alegre-Cebollada M Oñaderra JG Gavilanes A Martínez del Pozo 2007 Sea anemone actinoporins: the transition from a folded soluble state to a functionally active membrane-bound oligomeric pore Curr Protein Pept Sci 8 558 572 10.2174/138920307783018686 (Pubitemid 351266989)
    • (2007) Current Protein and Peptide Science , vol.8 , Issue.6 , pp. 558-572
    • Alegre-Cebollada, J.1    Onaderra, M.2    Gavilanes, J.G.3    Martínez Del Pozo, A.4
  • 2
    • 33846197988 scopus 로고    scopus 로고
    • Silent mutations at the 5′-end of the cDNA of actinoporins from the sea anemone Stichodactyla helianthus allow their heterologous overproduction in Escherichia coli
    • DOI 10.1016/j.jbiotec.2006.07.006, PII S016816560600592X
    • J Alegre-Cebollada G Clementi M Cunietti C Porres M Oñaderra JG Gavilanes A Martínez del Pozo 2007 Silent mutations at the 5′-end of the cDNA of actinoporins from the sea anemone Stichodactyla helianthus allow their heterologous overproduction in Escherichia coli J Biotechnol 127 211 221 10.1016/j.jbiotec.2006.07.006 (Pubitemid 46107142)
    • (2007) Journal of Biotechnology , vol.127 , Issue.2 , pp. 211-221
    • Alegre-Cebollada, J.1    Clementi, G.2    Cunietti, M.3    Porres, C.4    Onaderra, M.5    Gavilanes, J.G.6    Martínez Del Pozo, A.7
  • 4
    • 0036027362 scopus 로고    scopus 로고
    • Cytolytic peptide and protein toxins from sea anemones (Anthozoa: Actiniaria)
    • DOI 10.1016/S0041-0101(01)00191-X, PII S004101010100191X
    • G Anderluh P Macek 2002 Cytolytic peptide and protein toxins from sea anemones (Anthozoa: Actiniaria) Toxicon 40 111 124 10.1016/S0041-0101(01)00191-X (Pubitemid 33016540)
    • (2002) Toxicon , vol.40 , Issue.2 , pp. 111-124
    • Anderluh, G.1    Macek, P.2
  • 5
    • 0034880806 scopus 로고    scopus 로고
    • Crystal structure of the soluble form of equinatoxin II, a pore-forming toxin from the sea anemone Actinia equina
    • DOI 10.1016/S0969-2126(01)00592-5, PII S0969212601005925
    • A Athanasiadis G Anderluh P Macek D Turk 2001 Crystal structure of the soluble form of equinatoxin II, a pore-forming toxin from the sea anemone Actinia equina Structure 9 341 346 10.1016/S0969-2126(01)00592-5 (Pubitemid 32772579)
    • (2001) Structure , vol.9 , Issue.4 , pp. 341-346
    • Athanasiadis, A.1    Anderluh, G.2    Macek, P.3    Turk, D.4
  • 7
  • 8
    • 0036304122 scopus 로고    scopus 로고
    • Solution structure of the eukaryotic pore-forming cytolysin equinatoxin II: Implications for pore formation
    • DOI 10.1006/jmbi.2001.5321
    • MG Hinds W Zhang G Anderluh PE Hansen RS Norton 2002 Solution structure of the eukaryotic pore-forming cytolysin equinatoxin II: implications for pore formation J Mol Biol 315 1219 1229 10.1006/jmbi.2001.5321 (Pubitemid 34729299)
    • (2002) Journal of Molecular Biology , vol.315 , Issue.5 , pp. 1219-1229
    • Hinds, M.G.1    Zhang, W.2    Anderluh, G.3    Hansen, P.E.4    Norton, R.S.5
  • 9
    • 0242542032 scopus 로고    scopus 로고
    • Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation
    • DOI 10.1016/j.str.2003.09.019
    • JM Mancheño J Martín-Benito M Martínez-Ripoll JG Gavilanes JA Hermoso 2003 Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation Structure 11 1319 1328 10.1016/j.str.2003.09.019 (Pubitemid 37412414)
    • (2003) Structure , vol.11 , Issue.11 , pp. 1319-1328
    • Mancheno, J.M.1    Martin-Benito, J.2    Martinez-Ripoll, M.3    Gavilanes, J.G.4    Hermoso, J.A.5
  • 10
    • 9244241054 scopus 로고    scopus 로고
    • Pore-forming protein toxins: From structure to function
    • DOI 10.1016/j.pbiomolbio.2004.01.009, PII S0079610704000033
    • MW Parker SC Feil 2005 Pore-forming protein toxins: from structure to function Prog Biophys Mol Biol 88 91 142 10.1016/j.pbiomolbio.2004.01.009 (Pubitemid 39547775)
    • (2005) Progress in Biophysics and Molecular Biology , vol.88 , Issue.1 , pp. 91-142
    • Parker, M.W.1    Feil, S.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.