ArticleArchives of microbiology1995
Involvement of transglutaminase in the formation of covalent cross-links in the cell wall of Candida albicans.
Article in Archives of microbiology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
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.
Who cites it
10 citing papers in PubMed, 52 citations in OpenAlex.
- Fractionation and Extraction of Cell Wall Proteins FromBio-protocol · 2025Article
- Promising immunotherapeutic targets for treating candidiasis.Frontiers in cellular and infection microbiology · 2024Review
- Moonlighting Proteins at the Candidal Cell Surface.Microorganisms · 2020Review
- Transglutaminases: part I-origins, sources, and biotechnological characteristics.World journal of microbiology & biotechnology · 2020Review
- The Synergism of the Small Molecule ENOblock and Fluconazole Against Fluconazole-ResistantFrontiers in microbiology · 2019Article
- TheThe Journal of biological chemistry · 2018Article
- Microbial Transglutaminase Is Immunogenic and Potentially Pathogenic in Pediatric Celiac Disease.Frontiers in pediatrics · 2018Review
- Fission yeast Cyk3p is a transglutaminase-like protein that participates in cytokinesis and cell morphogenesis.Molecular biology of the cell · 2012Article
- Cell wall and secreted proteins of Candida albicans: identification, function, and expression.Microbiology and molecular biology reviews : MMBR · 1998Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Activity of the enzyme glutaminyl-peptide--glutamylyl-transferase (EC 2.3.2.13; transglutaminase), which forms the interpeptidic cross-link N epsilon-(gamma-glutamic)-lysine, was demonstrated in cell-free extracts obtained from both the yeast like and mycelial forms of Candida albicans. Higher levels of enzymatic activity were observed in the cell wall fraction, whereas the cytosol contained only trace amounts of activity. Cystamine, a highly specific inhibitor of the enzyme, was used to analyze a possible role of transglutaminase in the organization of the cell wall structure of the fungus. Cystamine delayed protoplast regeneration and inhibited the yeast-to-mycelium transition and the incorporation of proteins into the cell wall. The incorporation of covalently bound high-molecular-weight proteins into the wall was sensitive to cystamine. Proteic epitopes recognized by two monoclonal antibodies, one of which is specific for the mycelial walls of the fungus, were also sensitive to cystamine. These data suggest that transglutaminase may be involved in the formation of covalent bonds between different cell wall proteins during the final assembly of the mature cell wall.
Indexed as
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What OpenQuestion holds
Registered trials
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.