Evidence map›Paper›PMID 7507156›Full record

ReviewImmunologic research1993

Membrane defence against complement lysis: the structure and biological properties of CD59.

A Davies, P J Lachmann

Open access · bronzeAbstract readReview
PubMed Publisher
In one paragraph

Review in Immunologic research, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

59 citing papers in PubMed, 161 citations in OpenAlex.

  1. Trial
  2. Trial
  3. Review
  4. Article
  5. Comparison of Fucoidans fromInternational journal of molecular sciences · 2023
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. The Immunogenetics of Autoimmune Blistering Diseases.Advances in experimental medicine and biology · 2022
    Review
  11. Review
  12. Dihydro-stilbene gigantol relieves CClActa pharmacologica Sinica · 2020
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Frontiers in microbiology · 2017
    Review
  20. Article
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

2 authors at 1 institution in 1 country.

A DaviesMolecular Immunopathology Unit, MRC Centre, Cambridge, England.
P J Lachmann
MRC Epidemiology Unit · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The complement system is an important branch of the innate immune response, constituting a first line of defence against invading microorganisms which activate complement via both antibody-dependent and -independent mechanisms. Activation of complement leads to (a) a direct attack upon the activating cell surface by assembly of the pore-forming membrane attack complex (MAC), and (b) the generation of inflammatory mediators which target and recruit other branches of the immune system. However, uncontrolled complement activation can lead to widespread tissue damage in the host, since certain of the activation products, notably the fragment C3b and the C5b-7 complex, can bind nonspecifically to any nearby cell membranes. Therefore it is important that complement activation is tightly regulated. Our own cells express a number of membrane-bound control proteins which limit complement activation at the cell surface and prevent accidental complement-mediated damage. These include decay-accelerating factor, complement receptor 1 and membrane cofactor protein, all of which are active at the level of C3/C5 convertase formation. Until recently, cell surface control of MAC assembly had been attributed to a single 65-kD membrane protein called homologous restriction factor (alternatively named C8-binding protein and MAC-inhibiting protein). However a second MAC-inhibiting protein has since been discovered and it is now clear that this protein plays a major role in the control of membrane attack. This review charts the rapid progress made in elucidating the protein and gene structure, and the mechanism of action of this most recently discovered complement inhibitor, CD59.

Indexed as

AnimalsAntigens, CDCD59 AntigensComplement ActivationComplement Inactivator ProteinsComplement Membrane Attack ComplexHumansImmune System DiseasesMembrane GlycoproteinsTissue DistributionT-LymphocytesAntigens, CDCD59 AntigensComplement Inactivator ProteinsComplement Membrane Attack ComplexMembrane Glycoproteins

Identifiers

PMID7507156
OpenAlexW2013771339

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.