Evidence map›Paper›PMID 15322283›Full record

ArticleProtein science : a publication of the Protein Society2004

Biological activity, membrane-targeting modification, and crystallization of soluble human decay accelerating factor expressed in E. coli.

Jennifer White, Petra Lukacik, Dirk Esser, Michael Steward, Naomi Giddings, Jeremy R Bright, Sarah J Fritchley, B Paul Morgan, Susan M Lea, Geoffrey P Smith and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.2field-weighted citation impact, top 23% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 42 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 3 institutions in 1 country.

Jennifer WhiteAdprotech Ltd., Chesterford Research Park, Little Chesterford, Saffron Walden, Essex CB10 1XL, UK.
Petra Lukacik
Dirk Esser
Michael Steward
Naomi Giddings
Jeremy R Bright
Sarah J Fritchley
B Paul Morgan
Susan M Lea
Geoffrey P Smith
Richard A G Smith
MRC Laboratory of Molecular Biology · GBUniversity of Oxford · GBUniversity of Wales · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Decay-accelerating factor (DAF, CD55) is a glycophosphatidyl inositol-anchored glycoprotein that regulates the activity of C3 and C5 convertases. In addition to understanding the mechanism of complement inhibition by DAF through structural studies, there is also an interest in the possible therapeutic potential of the molecule. In this report we describe the cloning, expression in Escherichia coli, isolation and membrane-targeting modification of the four short consensus repeat domains of soluble human DAF with an additional C-terminal cysteine residue to permit site-specific modification. The purified refolded recombinant protein was active against both classical and alternative pathway assays of complement activation and had similar biological activity to soluble human DAF expressed in Pichia pastoris. Modification with a membrane-localizing peptide restored cell binding and gave a large increase in antihemolytic potency. These data suggested that the recombinant DAF was correctly folded and suitable for structural studies as well as being the basis for a DAF-derived therapeutic. Crystals of the E. coli-derived protein were obtained and diffracted to 2.2 A, thus permitting the first detailed X-ray crystallography studies on a functionally active human complement regulator protein with direct therapeutic potential.

Indexed as

Amino Acid SequenceAnimalsCD55 AntigensCell MembraneCells, CulturedComplement ActivationComplement C3aCrystallizationEscherichia coliGuinea PigsHemolysisHumansInclusion BodiesInhibitory Concentration 50Molecular Sequence DataProtein Structure, TertiaryCD55 AntigensComplement C3aRecombinant Proteins

Identifiers

PMID15322283
PMCPMC2280017
OpenAlexW1963544181

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.