ArticleProceedings of the National Academy of Sciences of the United States of America1992
Cloning and expression of chicken erythrocyte transglutaminase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 34 citations in OpenAlex.
- Substrate specificity of microbial transglutaminase as revealed by three-dimensional docking simulation and mutagenesis.Protein engineering, design & selection : PEDS · 2009Article
- Tissue transglutaminase, protein cross-linking and Alzheimer's disease: review and views.International journal of clinical and experimental pathology · 2008Article
- Nucleotide binding by the erythrocyte transglutaminase/Gh protein, probed with fluorescent analogs of GTP and GDP.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Interactions of G(h)/transglutaminase with phospholipase Cdelta1 and with GTP.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- A superfamily of archaeal, bacterial, and eukaryotic proteins homologous to animal transglutaminases.Protein science : a publication of the Protein Society · 1999Article
- Association of a transglutaminase-related antigen with intermediate filaments.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Nonsteroidal antiinflammatory drugs cause apoptosis and induce cyclooxygenases in chicken embryo fibroblasts.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
We report the sequences of cDNAs encoding chicken erythrocyte transglutaminase (EC 2.3.2.13). The complete mRNA consists of 3345/3349 nucleotides and predicts a single open reading frame. Nine peptide sequences derived from partial digests of the isolated protein agreed with the corresponding translation of the open reading frame. Approximately 60% identities between the avian protein and three related mammalian enzymes were found. Chicken erythrocyte transglutaminase mRNA is most abundant in red blood cells and kidney, and it accumulates during erythroid cell differentiation.
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Registered trials
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