Evidence map›Paper›PMID 16189649›Full record

ReviewSpringer seminars in immunopathology2005

Mannan-binding-lectin-associated serine proteases, characteristics and disease associations.

Rikke Sørensen, Steffen Thiel, Jens C Jensenius

Abstract readReview
PubMed Publisher
In one paragraph

Review in Springer seminars in immunopathology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.7field-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

34 citing papers in PubMed, 132 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Review
  5. Activity of Mannose-Binding Lectin on Bacterial-Infected Chickens-A Review.Animals : an open access journal from MDPI · 2021
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Fine mapping of type 1 diabetes regions Idd9.1 and Idd9.2 reveals genetic complexity.Mammalian genome : official journal of the International Mammalian Genome Society · 2013
    Article
  15. Article
  16. Review
  17. Article
  18. Humoral innate immune response and disease.Clinical immunology (Orlando, Fla.) · 2012
    Review
  19. Article
  20. Microglia, Alzheimer's disease, and complement.International journal of Alzheimer's disease · 2012
    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

3 authors at 1 institution in 1 country.

Rikke SørensenDepartment of Medical Microbiology and Immunology, Wilhelm Meyers Allé, University of Aarhus, 8000 Aarhus, Denmark. rs@microbiology.au.dk
Steffen Thiel
Jens C Jensenius
Aarhus University · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mannan-binding lectin (MBL)-associated serine proteases (MASPs) circulate in plasma as zymogens in complexes with MBL and with L- and H-ficolin. Upon binding of MBL or ficolin to pathogen-associated molecular patterns, the MASPs are activated. MASP-2 can now cleave C4 and C2 to generate the C3 convertase, C4bC2b. The functions of the other two MASPs, MASP-1 and MASP-3 have not been elucidated. MASP-1 can cleave C2, and with low efficiency also C3, and may serve a function through direct C3 activation. No natural substrate for MASP-3 has been identified. MBL deficiency, occurring at a frequency of about 10%, is the most common congenital immunodeficiency and is associated with susceptibility to infections and autoimmune disorders. Inherited MASP-2 deficiency has been described as the result of a mutation causing the exchange of aspartic acid with a glycine at position 105, a position in the first domain, CUB1, involved in calcium binding. This mutation abolishes the binding to MBL and ficolins, and deprives MASP-2 of functional activity. The index case suffered from recurrent severe infections and autoimmune reactions. The gene frequency of the mutation among Caucasians is 3.6%. It is not found in Chinese, who present a different mutation also associated with MASP-2 deficiency.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionBase SequenceComplement Pathway, Mannose-Binding LectinDimerizationFicolinsHumansImmunologic Deficiency SyndromesLectinsMannose-Binding LectinMannose-Binding Protein-Associated Serine ProteasesModels, MolecularMultiprotein ComplexesMutationProtein Structure, QuaternarySubstrate SpecificityFicolinsLectinsMannose-Binding LectinMannose-Binding Protein-Associated Serine ProteasesMASP2 protein, humanMultiprotein Complexes

Identifiers

PMID16189649
OpenAlexW1970344276

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.