Evidence map›Paper›PMID 12966142›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2003

Candida albicans secreted aspartyl proteinases in virulence and pathogenesis.

Julian R Naglik, Stephen J Challacombe, Bernhard Hube

Open access · greenAbstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 504 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
504citing papers in PubMed, 2 pooled it
12.1field-weighted citation impact, top 1% 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

504 citing papers in PubMed, 2 syntheses or guidelines pooled it, 1,143 citations in OpenAlex.

  1. Pooled it
  2. A systematic review on the implication of Candida in peri-implantitis.International journal of implant dentistry · 2021
    Pooled it
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444 more citing papers are in PubMed but not listed here.

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 2 institutions in 2 countries.

Julian R NaglikDepartment of Oral Medicine, Pathology & Immunology, GKT Dental Institute, Kings College London, London, United Kingdom. julian.naglik@kcl.ac.uk
Stephen J Challacombe
Bernhard Hube
King's College London · GBRobert Koch Institute · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Candida albicans is the most common fungal pathogen of humans and has developed an extensive repertoire of putative virulence mechanisms that allows successful colonization and infection of the host under suitable predisposing conditions. Extracellular proteolytic activity plays a central role in Candida pathogenicity and is produced by a family of 10 secreted aspartyl proteinases (Sap proteins). Although the consequences of proteinase secretion during human infections is not precisely known, in vitro, animal, and human studies have implicated the proteinases in C. albicans virulence in one of the following seven ways: (i) correlation between Sap production in vitro and Candida virulence, (ii) degradation of human proteins and structural analysis in determining Sap substrate specificity, (iii) association of Sap production with other virulence processes of C. albicans, (iv) Sap protein production and Sap immune responses in animal and human infections, (v) SAP gene expression during Candida infections, (vi) modulation of C. albicans virulence by aspartyl proteinase inhibitors, and (vii) the use of SAP-disrupted mutants to analyze C. albicans virulence. Sap proteins fulfill a number of specialized functions during the infective process, which include the simple role of digesting molecules for nutrient acquisition, digesting or distorting host cell membranes to facilitate adhesion and tissue invasion, and digesting cells and molecules of the host immune system to avoid or resist antimicrobial attack by the host. We have critically discussed the data relevant to each of these seven criteria, with specific emphasis on how this proteinase family could contribute to Candida virulence and pathogenesis.

Indexed as

Aspartic Acid EndopeptidasesCandida albicansCandidiasisFungal ProteinsHumansVirulenceAspartic Acid EndopeptidasesFungal Proteins

Identifiers

PMID12966142
PMCPMC193873
OpenAlexW2137959581

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.