Evidence map›Paper›PMID 25862418›Full record

ReviewMolecular immunology2015

MBL-associated serine proteases (MASPs) and infectious diseases.

Marcia H Beltrame, Angelica B W Boldt, Sandra J Catarino, Hellen C Mendes, Stefanie E Boschmann, Isabela Goeldner, Iara Messias-Reason

Abstract readReview
In one paragraph

Review in Molecular immunology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed, 63 citations in OpenAlex.

  1. Trial
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  8. Contact Lens Wear Alters Transcriptional Responses tobioRxiv : the preprint server for biology · 2024
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  15. An immunogenetic view of COVID-19.Genetics and molecular biology · 2021
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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

7 authors at 2 institutions in 1 country.

Marcia H BeltrameDepartment of Clinical Pathology, Hospital de Clínicas, Universidade Federal do Paraná (UFPR), Curitiba, PR, Brazil.
Angelica B W BoldtDepartment of Genetics, Universidade Federal do Paraná, Curitiba, PR, Brazil.
Sandra J CatarinoDepartment of Clinical Pathology, Hospital de Clínicas, Universidade Federal do Paraná (UFPR), Curitiba, PR, Brazil.
Hellen C MendesDepartment of Clinical Pathology, Hospital de Clínicas, Universidade Federal do Paraná (UFPR), Curitiba, PR, Brazil.
Stefanie E BoschmannDepartment of Clinical Pathology, Hospital de Clínicas, Universidade Federal do Paraná (UFPR), Curitiba, PR, Brazil.
Isabela GoeldnerDepartment of Clinical Pathology, Hospital de Clínicas, Universidade Federal do Paraná (UFPR), Curitiba, PR, Brazil.
Iara Messias-ReasonDepartment of Clinical Pathology, Hospital de Clínicas, Universidade Federal do Paraná (UFPR), Curitiba, PR, Brazil. Electronic address: iaramessias@yahoo.com.br.
Hospital de Clínicas Universidade Federal do Paraná · BRUniversidade Federal do Paraná · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The lectin pathway of the complement system has a pivotal role in the defense against infectious organisms. After binding of mannan-binding lectin (MBL), ficolins or collectin 11 to carbohydrates or acetylated residues on pathogen surfaces, dimers of MBL-associated serine proteases 1 and 2 (MASP-1 and MASP-2) activate a proteolytic cascade, which culminates in the formation of the membrane attack complex and pathogen lysis. Alternative splicing of the pre-mRNA encoding MASP-1 results in two other products, MASP-3 and MAp44, which regulate activation of the cascade. A similar mechanism allows the gene encoding MASP-2 to produce the truncated MAp19 protein. Polymorphisms in MASP1 and MASP2 genes are associated with protein serum levels and functional activity. Since the first report of a MASP deficiency in 2003, deficiencies in lectin pathway proteins have been associated with recurrent infections and several polymorphisms were associated with the susceptibility or protection to infectious diseases. In this review, we summarize the findings on the role of MASP polymorphisms and serum levels in bacterial, viral and protozoan infectious diseases.

Indexed as

Bacterial InfectionsComplement Pathway, Mannose-Binding LectinComplement System ProteinsGene Expression RegulationHumansMannose-Binding LectinMannose-Binding Protein-Associated Serine ProteasesPolymorphism, GeneticProtozoan InfectionsSignal TransductionVirus DiseasesComplement System ProteinsMannose-Binding LectinMannose-Binding Protein-Associated Serine ProteasesMASP1 protein, humanMASP2 protein, humanComplement systemMAp19MAp44MASP-1MASP-2MASP-3

Identifiers

PMID25862418
PMCPMC7112674
OpenAlexW1975734905

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.