Structural Basis for Recognition of the Pore-Forming Toxin Intermedilysin by Human Complement Receptor CD59 (Q27678091)

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Susan M. Lea

object named as

Susan M Lea

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author name string

Richard A G Smith

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Doryen Bubeck

Assembly and regulation of the membrane attack complex based on structures of C5b6 and sC5b9.

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publication date

30 May 2013

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published in

Cell Reports

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volume

3

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issue

5

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page(s)

1369-77

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cites work

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Mapping the intermedilysin-human CD59 receptor interface reveals a deep correspondence with the binding site on CD59 for complement binding proteins C8alpha and C9

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Specific protein-membrane contacts are required for prepore and pore assembly by a cholesterol-dependent cytolysin

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2 June 2018

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2 June 2018

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27 November 2018

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12 December 2020

The Glycosylation of the Complement Regulatory Protein, Human Erythrocyte CD59

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12 December 2020

Synthesis and utilization of reversible and irreversible light-activated nanovalves derived from the channel protein MscL

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12 December 2020

Human protectin (CD59), an 18,000-20,000 MW complement lysis restricting factor, inhibits C5b-8 catalysed insertion of C9 into lipid bilayers

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12 December 2020