ArticleMycopathologia1999
Isolation and identification of a 92-kDa stress induced protein from Candida albicans.
Article in Mycopathologia, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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.
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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.
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Who cites it
6 citing papers in PubMed, 20 citations in OpenAlex.
- Moonlighting Proteins at the Candidal Cell Surface.Microorganisms · 2020Review
- Potential molecular mechanisms for fruiting body formation of Cordyceps illustrated in the case ofMycology · 2017Article
- Prediction of the clinical outcome in invasive candidiasis patients based on molecular fingerprints of five anti-Candida antibodies in serum.Molecular & cellular proteomics : MCP · 2011Article
- Oxidative stress inactivates cobalamin-independent methionine synthase (MetE) in Escherichia coli.PLoS biology · 2004Article
- Transcriptional regulation of methionine synthase by homocysteine and choline in Aspergillus nidulans.The Biochemical journal · 2003Article
- Preclinical assessment of the efficacy of mycograb, a human recombinant antibody against fungal HSP90.Antimicrobial agents and chemotherapy · 2003Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It was previously shown that the presence of estrogen enhances survival of Candida albicans under heat and oxidative stresses. A 92-kDa protein is inducible by heat shock and estrogen in C. albicans. Previous studies have described this protein as hsp90 because of its molecular size and heat inducibility as seen on electrophoretic gels and Western blots. In this study, ion exchange, hydroxyapatite and size exclusion chromatography were used to isolate a 92-kDa-protein band. The N-terminal sequence of isolated protein blotted onto a PVDF membrane was determined to be V-Q-S-?-V-L-G-F-P-R. This sequence is homologous to the N-terminal sequence of the MET6 gene product, cobalamin-independent methionine synthase, from Saccharomyces cerevisiae. The results of this study suggest that a cobalamin-independent methionine synthase homolog is inducible by heat and estrogen in C. albicans. This study also suggests that Candida hsp90 is more likely to exist as an 82-kDa protein as predicted by a previously described cDNA and not as a 92-kDa protein as reported in the literature.
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Registered trials
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