ArticleJournal of molecular evolution2017
Evolutionary Analysis of the Mammalian Tuftelin Sequence Reveals Features of Functional Importance.
Article in Journal of molecular evolution, 2017. 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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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, 7 citations in OpenAlex.
- Oncogenic tuftelin 1 as a potential molecular-targeted for inhibiting hepatocellular carcinoma growth.World journal of gastroenterology · 2021Article
- [Expression of tuftelin protein and its clinical value in HBV-related liver cancer tissues].Zhonghua gan zang bing za zhi = Zhonghua ganzangbing zazhi = Chinese journal of hepatology · 2021Article
- Tuftelin 1 (TUFT1) Promotes the Proliferation and Migration of Renal Cell CarcinomaPathology oncology research : POR · 2021Article
- Tuftelin and HIFs expression in osteogenesis.Histochemistry and cell biology · 2019Article
- Tuftelin Is Required for NGF-Induced Differentiation of PC12 Cells.Journal of molecular neuroscience : MN · 2019Article
- Exploring the rearrangement of sensory intelligence in proteobacteria: insight of Pho regulon.World journal of microbiology & biotechnology · 2018Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tuftelin (TUFT1) is an acidic, phosphorylated glycoprotein, initially discovered in developing enamel matrix. TUFT1 is expressed in many mineralized and non-mineralized tissues. We performed an evolutionary analysis of 82 mammalian TUFT1 sequences to identify residues and motifs that were conserved during 220 million years (Ma) of evolution. We showed that 168 residues (out of the 390 residues composing the human TUFT1 sequence) are under purifying selection. Our analyses identified several, new, putatively functional domains and confirmed previously described functional domains, such as the TIP39 interaction domain, which correlates with nuclear localization of the TUFT1 protein, that was demonstrated in several tissues. We also identified several sites under positive selection, which could indicate evolutionary changes possibly related to the functional diversification of TUFT1 during evolution in some lineages. We discovered that TUFT1 and MYZAP (myocardial zonula adherens protein) share a common ancestor that was duplicated circa 500 million years ago. Taken together, these findings expand our knowledge of TUFT1 evolution and provide new information that will be useful for further investigation of TUFT1 functions.
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