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Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor.
Nat Struct Mol Biol. 2008 Jan;15(1):109-11. doi: 10.1038/nsmb1326. Epub 2007 Dec 16.
3
Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A.
Science. 2006 May 5;312(5774):748-51. doi: 10.1126/science.1125162. Epub 2006 Apr 6.
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Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase.
Nat Struct Mol Biol. 2007 Aug;14(8):689-95. doi: 10.1038/nsmb1273. Epub 2007 Jun 24.
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Targeting the JMJD2A histone lysine demethylase.
Nat Struct Mol Biol. 2007 Aug;14(8):682-4. doi: 10.1038/nsmb0807-682.
6
Structural basis of the recognition of a methylated histone tail by JMJD2A.
Proc Natl Acad Sci U S A. 2007 Jun 26;104(26):10818-23. doi: 10.1073/pnas.0704525104. Epub 2007 Jun 13.
7
Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity.
Nature. 2007 Jul 5;448(7149):87-91. doi: 10.1038/nature05971. Epub 2007 Jun 24.
8
Engineering human JMJD2A tudor domains for an improved understanding of histone peptide recognition.
Proteins. 2023 Jan;91(1):32-46. doi: 10.1002/prot.26408. Epub 2022 Aug 16.
9
The X-linked mental retardation gene SMCX/JARID1C defines a family of histone H3 lysine 4 demethylases.
Cell. 2007 Mar 23;128(6):1077-88. doi: 10.1016/j.cell.2007.02.017. Epub 2007 Feb 22.
10
Tudor domain of histone demethylase KDM4B is a reader of H4K20me3.
Acta Biochim Biophys Sin (Shanghai). 2020 Aug 5;52(8):901-906. doi: 10.1093/abbs/gmaa064.

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R-2-hydroxyglutarate-mediated inhibition of KDM4A compromises telomere integrity.
Nucleic Acids Res. 2025 Jun 6;53(11). doi: 10.1093/nar/gkaf512.
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KDM4B mutations in human cancers.
Mutat Res. 2024 Jul-Dec;829:111866. doi: 10.1016/j.mrfmmm.2024.111866. Epub 2024 Jun 11.
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Histone Readers and Their Roles in Cancer.
Cancer Treat Res. 2023;190:245-272. doi: 10.1007/978-3-031-45654-1_8.
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KDM4 Demethylases: Structure, Function, and Inhibitors.
Adv Exp Med Biol. 2023;1433:87-111. doi: 10.1007/978-3-031-38176-8_5.
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Lysine Demethylation in Pathogenesis.
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Histone 4 lysine 20 tri-methylation: a key epigenetic regulator in chromatin structure and disease.
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Shaping eukaryotic epigenetic systems by horizontal gene transfer.
Bioessays. 2023 Jul;45(7):e2200232. doi: 10.1002/bies.202200232.

本文引用的文献

1
Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase.
Nat Struct Mol Biol. 2007 Aug;14(8):689-95. doi: 10.1038/nsmb1273. Epub 2007 Jun 24.
2
Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity.
Nature. 2007 Jul 5;448(7149):87-91. doi: 10.1038/nature05971. Epub 2007 Jun 24.
3
Structural basis of the recognition of a methylated histone tail by JMJD2A.
Proc Natl Acad Sci U S A. 2007 Jun 26;104(26):10818-23. doi: 10.1073/pnas.0704525104. Epub 2007 Jun 13.
4
Chromatin modifications and their function.
Cell. 2007 Feb 23;128(4):693-705. doi: 10.1016/j.cell.2007.02.005.
5
Diversity within the JMJD2 histone demethylase family.
Biochem Biophys Res Commun. 2007 Feb 23;353(4):973-7. doi: 10.1016/j.bbrc.2006.12.147. Epub 2006 Dec 27.
7
The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36.
Nature. 2006 Jul 20;442(7100):312-6. doi: 10.1038/nature04853. Epub 2006 May 28.
8
Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF.
Nature. 2006 Jul 6;442(7098):91-5. doi: 10.1038/nature04802. Epub 2006 May 21.
9
Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2.
Nature. 2006 Jul 6;442(7098):100-3. doi: 10.1038/nature04814. Epub 2006 May 21.
10
Structural insights into histone demethylation by JMJD2 family members.
Cell. 2006 May 19;125(4):691-702. doi: 10.1016/j.cell.2006.04.024. Epub 2006 May 4.

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