Evidence map›Paper›PMID 14766843›Full record

ArticleJournal of clinical microbiology2004

Purification and characterization of a 43-kilodalton extracellular serine proteinase from Cryptococcus neoformans.

Jae il Yoo Ji, Yeong Seon Lee, Chul-Yong Song, Bong Su Kim

Open access · greenAbstract read
In one paragraph

Article in Journal of clinical microbiology, 2004. 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
0.7field-weighted citation impact, top 32% 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, 26 citations in OpenAlex.

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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

4 authors at 2 institutions in 2 countries.

Jae il Yoo JiLaboratory of Antimicrobial Resistant Pathogens, Department of Bacteriology, National Institute of Health, Chung-Ang University, Seoul, Korea.
Yeong Seon Lee
Chul-Yong Song
Bong Su Kim
National Institute of Health · AMChung-Ang University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An extracellular proteinase was purified from culture filtrates of Cryptococcus neoformans NHPY24 by DEAE ion-exchange chromatography and gelatin affinity column chromatography with azoalbumin as the substrate. The molecular mass of the purified enzyme was 43 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, its pH optimum was 7.0 to 8.0, and maximal activity was obtained at pH 7.5 and 37 degrees C. By isoelectric focusing, the purified enzyme had a pI of 4.77. Enzyme activity was inhibited by serine proteinase inhibitors such as phenylmethylsulfonyl fluoride and diisopropylfluorophosphate. The purified enzyme was thus a serine proteinase. It hydrolyzed natural substrates including hemoglobin, beta-casein, and gamma globulin.

Indexed as

Cryptococcus neoformansElectrophoresis, Polyacrylamide GelHydrogen-Ion ConcentrationKineticsSerine EndopeptidasesSerine Proteinase InhibitorsSubstrate SpecificityThermodynamicsSerine EndopeptidasesSerine Proteinase Inhibitors

Identifiers

PMID14766843
PMCPMC344434
OpenAlexW2071317464

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.