The DOI matches its Crossref record; 73 of the 73 references it cites were found in a registry or an index.
TET2 in Normal and Malignant Hematopoiesis
Abstract
The ten-eleven translocation (TET) family of enzymes were originally cloned from the translocation breakpoint of t(10;11) in infant acute myeloid leukemia (AML) with subsequent genomic analyses revealing somatic mutations and suppressed expression of TET family members across a range of malignancies, particularly enriched in hematological neoplasms. The TET family of enzymes is responsible for the hydroxylation of 5-methylcytosines (5-mC) to 5-hydroxymethylcytosine (5-hmC), followed by active and passive mechanisms leading to DNA demethylation. Given the complexity and importance of DNA methylation events in cellular proliferation and differentiation, it comes as no surprise that the TET family of enzymes is intricately regulated by both small molecules and regulatory cooperating proteins. Here, we review the structure and function of TET2, its interactions with cooperating mutations and small molecules, and its role in aberrant hematopoiesis.
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“Mechanistically, DNMT3A catalyzes de novo DNA methylation whereas TET2 oxidizes methylated CpG to 5-hydroxymethyl cytosine (5-hmC) facilitating further modification to unmodified cysteine; mutations thus cause dysregulated DNA methylation and demethylation, respectively, altering the expression of genes involved in proliferation, differentiation and inflammation via chromatin-level changes 209,210”
From Clonal haematopoiesis and dysregulation of the immune system (2023) · cites this paper as [209]
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Conversion of 5-Methylcytosine to 5-Hydroxymethylcytosine in Mammalian DNA by MLL Partner TET1
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Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine
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Tumor hypoxia: From basic knowledge to therapeutic implications
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Clonal haematopoiesis and dysregulation of the immune system
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Metadata
- Authors
- Bowman, R. L., & Levine, R. L.
- Venue
- Cold Spring Harbor Perspectives in Medicine
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2017-02-27
- Volume
- 7
- Issue
- 8
- Pages
- a026518
- ISSN
- 2157-1422
- Cited by
- 94
- References
- 73
- Language
- en
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