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Recognition of Histone H3K14 Acylation by MORF.
Structure. 2017 Apr 4;25(4):650-654.e2. doi: 10.1016/j.str.2017.02.003. Epub 2017 Mar 9.
2
Histone H3K23-specific acetylation by MORF is coupled to H3K14 acylation.
Nat Commun. 2019 Oct 17;10(1):4724. doi: 10.1038/s41467-019-12551-5.
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Expanding the Reader Landscape of Histone Acylation.
Structure. 2017 Apr 4;25(4):571-573. doi: 10.1016/j.str.2017.03.010.
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Selective recognition of histone crotonylation by double PHD fingers of MOZ and DPF2.
Nat Chem Biol. 2016 Dec;12(12):1111-1118. doi: 10.1038/nchembio.2218. Epub 2016 Oct 24.
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A Subset of Human Bromodomains Recognizes Butyryllysine and Crotonyllysine Histone Peptide Modifications.
Structure. 2015 Oct 6;23(10):1801-1814. doi: 10.1016/j.str.2015.08.004. Epub 2015 Sep 10.

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H3K14: A histone site closely related to diseases.
J Cancer. 2025 Jul 28;16(11):3537-3550. doi: 10.7150/jca.118273. eCollection 2025.
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Modulation of the substrate preference of a MYST acetyltransferase by a scaffold protein.
J Biol Chem. 2025 Mar;301(3):108262. doi: 10.1016/j.jbc.2025.108262. Epub 2025 Feb 3.
3
A multivalent engagement of ENL with MOZ.
Nat Struct Mol Biol. 2025 Apr;32(4):709-718. doi: 10.1038/s41594-024-01455-8. Epub 2025 Jan 10.
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KAT2A and KAT2B prevent double-stranded RNA accumulation and interferon signaling to maintain intestinal stem cell renewal.
Sci Adv. 2024 Aug 9;10(32):eadl1584. doi: 10.1126/sciadv.adl1584. Epub 2024 Aug 7.
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Substrate and Functional Diversity of Protein Lysine Post-translational Modifications.
Genomics Proteomics Bioinformatics. 2024 May 9;22(1). doi: 10.1093/gpbjnl/qzae019.
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HBO1, a MYSTerious KAT and its links to cancer.
Biochim Biophys Acta Gene Regul Mech. 2024 Sep;1867(3):195045. doi: 10.1016/j.bbagrm.2024.195045. Epub 2024 Jun 6.
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The winged helix domain of MORF binds CpG islands and the TAZ2 domain of p300.
iScience. 2024 Feb 29;27(4):109367. doi: 10.1016/j.isci.2024.109367. eCollection 2024 Apr 19.
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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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The MOZ-BRPF1 acetyltransferase complex in epigenetic crosstalk linked to gene regulation, development, and human diseases.
Front Cell Dev Biol. 2023 Jan 11;10:1115903. doi: 10.3389/fcell.2022.1115903. eCollection 2022.
10
Engaging with benzoyllysine through a π-π-π mechanism.
Curr Opin Chem Biol. 2023 Feb;72:102252. doi: 10.1016/j.cbpa.2022.102252. Epub 2022 Dec 23.

本文引用的文献

1
Selective recognition of histone crotonylation by double PHD fingers of MOZ and DPF2.
Nat Chem Biol. 2016 Dec;12(12):1111-1118. doi: 10.1038/nchembio.2218. Epub 2016 Oct 24.
2
Structural Insights into Histone Crotonyl-Lysine Recognition by the AF9 YEATS Domain.
Structure. 2016 Sep 6;24(9):1606-12. doi: 10.1016/j.str.2016.05.023. Epub 2016 Aug 18.
3
Diverse Activities of Histone Acylations Connect Metabolism to Chromatin Function.
Mol Cell. 2016 Aug 18;63(4):547-552. doi: 10.1016/j.molcel.2016.06.038.
4
Insights into newly discovered marks and readers of epigenetic information.
Nat Chem Biol. 2016 Aug 18;12(9):662-8. doi: 10.1038/nchembio.2149.
6
Regulation of KAT6 Acetyltransferases and Their Roles in Cell Cycle Progression, Stem Cell Maintenance, and Human Disease.
Mol Cell Biol. 2016 Jun 29;36(14):1900-7. doi: 10.1128/MCB.00055-16. Print 2016 Jul 15.
7
Molecular Coupling of Histone Crotonylation and Active Transcription by AF9 YEATS Domain.
Mol Cell. 2016 Apr 21;62(2):181-193. doi: 10.1016/j.molcel.2016.03.028.
9
YEATS2 is a selective histone crotonylation reader.
Cell Res. 2016 May;26(5):629-32. doi: 10.1038/cr.2016.49. Epub 2016 Apr 22.
10
The Taf14 YEATS domain is a reader of histone crotonylation.
Nat Chem Biol. 2016 Jun;12(6):396-8. doi: 10.1038/nchembio.2065. Epub 2016 Apr 18.

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