Mapping CD55 function. The structure of two pathogen-binding domains at 1.7 A (Q27640215)

2

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Ian Goodfellow

3

Ian G Goodfellow

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Susan M. Lea

Susan Lea

8

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David J Evans

David J Evans

7

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O Brad Spiller

6

O Brad Spiller

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author name string

Pamela Williams

1

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Jason Billington

4

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Robert Powell

Journal of Biological Chemistry

5

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language of work or name

English

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publication date

21 March 2003

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published in

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volume

278

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issue

12

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page(s)

10691-6

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cites work

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Decay accelerating factor of complement is anchored to cells by a C-terminal glycolipid

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Binding of Escherichia coli adhesin AfaE to CD55 triggers cell-surface expression of the MHC class I-related molecule MICA

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The seven-span transmembrane receptor CD97 has a cellular ligand (CD55, DAF)

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Human complement regulators: a major target for pathogenic microorganisms

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Human and rodent decay-accelerating factors (CD55) are not species restricted in their complement-inhibiting activities

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Characterization of the active sites in decay-accelerating factor

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Characterization of echoviruses that bind decay accelerating factor (CD55): evidence that some haemagglutinating strains use more than one cellular receptor

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Determination of the affinity and kinetic constants for the interaction between the human virus echovirus 11 and its cellular receptor, CD55.

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Determination of the structure of a decay accelerating factor-binding clinical isolate of echovirus 11 allows mapping of mutants with altered receptor requirements for infection

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Short consensus repeat-3 domain of recombinant decay-accelerating factor is recognized by Escherichia coli recombinant Dr adhesin in a model of a cell-cell interaction

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Interaction with decay-accelerating factor facilitates coxsackievirus B infection of polarized epithelial cells

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Mapping the binding domains on decay accelerating factor (DAF) for haemagglutinating enteroviruses: implications for the evolution of a DAF-binding phenotype

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Crystallization and preliminary X-ray diffraction analysis of a biologically active fragment of CD55

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Secondary structure of a complement control protein module by two-dimensional 1H NMR

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Identifiers

DOI

10.1074/JBC.M212561200

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

12499389

1 reference

Consolidated OpenCitations Corpus – April 2017