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Volumn 3, Issue 1, 1996, Pages 31-36

Negative cooperativity exhibited by the lytic ammo-terminal domain of human perforin: Implications for perforin-mediated cell lysis

Author keywords

Cytolysis; Kinetics; Negative cooperativity; Perforin

Indexed keywords

MEMBRANE PROTEIN; PERFORIN; PORE FORMING CYTOTOXIC PROTEIN;

EID: 0029657919     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(96)90081-2     Document Type: Article
Times cited : (8)

References (13)
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  • 6
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    • Channel-forming activity of the perforin N-terminus and a putative α-helical region homologous with complement C9
    • Persechini, P.M., Ojcius, D.M., Adeodato, S.C., Notaroberto, P.C., Daniel, C.B. & Young, J.D.-E. (1992). Channel-forming activity of the perforin N-terminus and a putative α-helical region homologous with complement C9. Biochemistry 31, 5017-5021.
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  • 8
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    • Structure and function of human perforin
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  • 9
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  • 10
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    • Aspartate receptors of Escherichia coli and Salmonella typhimurium bind an aspartate ligand with negative and half-of-the-sites cooperativity
    • Biemann, H.P. & Koshland, D.E. (1994). Aspartate receptors of Escherichia coli and Salmonella typhimurium bind an aspartate ligand with negative and half-of-the-sites cooperativity. Biochemistry 33, 629-634.
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  • 11
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    • Negative cooperativity in the binding of nucleotides to Escherichia coli replicative helicase Dna B protein. Interactions with fluorescent nucleotide analogs
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    • Comparative properties and methods of preparation of lipid vesicles (liposomes)
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.