Evidence map›Paper›PMID 19672690›Full record

ArticleMycopathologia2010

Identification of a Candida parapsilosis strain producing extracellular serine peptidase with keratinolytic activity.

Alane Beatriz Vermelho, Ana Maria Mazotto, Ana Cristina Nogueira de Melo, Flávia Helena Cardoso Vieira, Thalita Rodrigues Duarte, Andrew Macrae, Marília Martins Nishikawa, Elba Pinto da Silva Bon

Abstract read
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In one paragraph

Article in Mycopathologia, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.6field-weighted citation impact, top 12% 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

8 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Secretion of serine proteases by planktonic- and biofilm-growing cells of Candida parapsilosis.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2025
    Article
  3. Article
  4. Article
  5. Extracellular peptidases from Deinococcus radiodurans.Extremophiles : life under extreme conditions · 2015
    Article
  6. Article
  7. Keratinases and sulfide from Bacillus subtilis SLC to recycle feather waste.World journal of microbiology & biotechnology · 2012
    Article
  8. 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

8 authors at 2 institutions in 1 country.

Alane Beatriz VermelhoLaboratório Protease de Microrganismos, Departamento de Microbiologia Geral, Instituto de Microbiologia Prof Paulo de Góes, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil. abvermelho@micro.ufrj.br
Ana Maria Mazotto
Ana Cristina Nogueira de Melo
Flávia Helena Cardoso Vieira
Thalita Rodrigues Duarte
Andrew Macrae
Marília Martins Nishikawa
Elba Pinto da Silva Bon
Universidade Federal do Rio de Janeiro · BRFundação Oswaldo Cruz · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A yeast strain isolated from feather waste from a chicken processing plant was identified as Candida parapsilosis by biochemical tests and morphological studies. The yeast was able to grow in phosphate-buffered saline supplemented with 1% native feather as the sole carbon and nitrogen source. A keratin substrate was obtained from the feathers by dimethylsulphoxide extraction. A 20-fold concentrated culture supernatant from Candida parapsilosis grown on feathers was analysed by SDS-PAGE electrophoresis containing either 1% gelatin or 1% keratin as copolymerised substrates. The presence of a single band with an approximate molecular mass of 60 kDa with gelatinolytic and keratinolytic activities was observed. This proteolytic activity was fully inhibited by phenylmethylsulphonyl fluoride. These results suggest that the extracellular enzyme belongs to the serine peptidase class. This is the first report of an extracellular serine peptidase produced by C. parapsilosis with keratinolytic activity. The role of this enzyme in yeast-host interactions is discussed.

Indexed as

AnimalsCandidaChickensExtracellular SpaceFeathersGelatinHost-Pathogen InteractionsHumansIndustrial WasteKeratinsMolecular WeightOnychomycosisPeptide HydrolasesPhenylmethylsulfonyl FluorideSerine ProteasesSerine Proteinase InhibitorsGelatinIndustrial WastekeratinaseKeratinsPeptide HydrolasesPhenylmethylsulfonyl FluorideSerine ProteasesSerine Proteinase Inhibitors

Identifiers

PMID19672690
OpenAlexW2093506043

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.