Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

PHF1 Tudor and N-terminal domains synergistically target partially unwrapped nucleosomes to increase DNA accessibility

21 Dec 2016

Abstract excerpt

The Tudor domain of human PHF1 recognizes trimethylated lysine 36 on histone H3 (H3K36me3). PHF1 relies on this interaction to regulate PRC2 methyltransferase activity, localize to DNA double strand breaks and mediate nucleosome accessibility. Here, we investigate the impact of the PHF1 N-terminal domain (NTD) on the Tudor domain interaction with the nucleosome. We show that the NTD is partially ordered when it...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cancer Mechanisms and Therapy
Share to Nuclear Receptors and Signaling
Share to Signaling Pathways in Disease

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 28082396
DOI: 10.1093/nar/gkw1320

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

PHF1 Tudor and N-terminal domains synergistically target partially unwrapped nucleosomes to increase DNA accessibilityPMID 28082396Read ↗

The Tudor domain of the PHD finger protein 1 is a dual reader of lysine trimethylation at lysine 36 of histone H3 and lysine 27 of histone variant H3t.Semantic proximity Read ↗

Structural and histone binding ability characterizations of human PWWP domains.Semantic proximity Read ↗

The N-terminal region of DNMT3A combines multiple chromatin reading motifs to guide recruitmentSemantic proximity Read ↗

Refined read-out: The hUHRF1 Tandem-Tudor domain prefers binding to histone H3 tails containing K4me1 in the context of H3K9me2/3Semantic proximity Read ↗

The Human Telomeric Protein TRF1 Specifically Recognizes Nucleosomal Binding Sites and Alters Nucleosome StructureSemantic proximity Read ↗

Structural basis for PRC2 decoding of active histone methylation marks H3K36me2/3.Semantic proximity Read ↗

Binding of regulatory proteins to nucleosomes is modulated by dynamic histone tailsSemantic proximity Read ↗

PHF20 Readers Link Methylation of Histone H3K4 and p53 with H4K16 Acetylation.Semantic proximity Read ↗

The fork restart factor PHF6 interacts with RRM2 and binds to H3K56ac marked nascent DNASemantic proximity Read ↗

Comprehensive nucleosome interactome screen establishes fundamental principles of nucleosome binding.Semantic proximity Read ↗

Histone methylation by PRC2 is inhibited by active chromatin marks.Semantic proximity Read ↗

Histone H3 N-terminal recognition by the PHD finger of PHRF1 is required for proper DNA damage responseSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.