Evidence map›Paper›PMID 14734808›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Complement regulation at the molecular level: the structure of decay-accelerating factor.

P Lukacik, P Roversi, J White, D Esser, G P Smith, J Billington, P A Williams, P M Rudd, M R Wormald, D J Harvey and 7 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

55 citing papers in PubMed, 128 citations in OpenAlex.

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  18. 3D analysis of CROMER (DAF) and a new antigen CRAG.Blood transfusion = Trasfusione del sangue · 2022
    Article
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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

17 authors at 1 institution in 1 country.

P LukacikLaboratory of Molecular Biophysics and Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, England.
P Roversi
J White
D Esser
G P Smith
J Billington
P A Williams
P M Rudd
M R Wormald
D J Harvey
M D M Crispin
C M Radcliffe
R A Dwek
D J Evans
B P Morgan
R A G Smith
S M Lea
University of Oxford · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

The human complement regulator CD55 is a key molecule protecting self-cells from complement-mediated lysis. X-ray diffraction and analytical ultracentrifugation data reveal a rod-like arrangement of four short consensus repeat (SCR) domains in both the crystal and solution. The stalk linking the four SCR domains to the glycosylphosphatidylinositol anchor is extended by the addition of 11 highly charged O-glycans and positions the domains an estimated 177 A above the membrane. Mutation mapping and hydrophobic potential analysis suggest that the interaction with the convertase, and thus complement regulation, depends on the burial of a hydrophobic patch centered on the linker between SCR domains 2 and 3.

Indexed as

CD55 AntigensComplement System ProteinsCrystallizationGlycosylationHumansHydrophobic and Hydrophilic InteractionsModels, MolecularRepetitive Sequences, Amino AcidSolutionsvon Willebrand FactorCD55 AntigensComplement System ProteinsSolutionsvon Willebrand Factor

Identifiers

PMID14734808
PMCPMC337044
OpenAlexW2159946497

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.