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

Structure-guided design of a methyl donor cofactor that controls a viral histone H3 lysine 27 methyltransferase activity.

Journal of medicinal chemistry - 10 Nov 2011

Li Jiaojie, Wei Hua, Zhou Ming-Ming

Abstract excerpt

vSET (a viral SET domain protein) is an attractive polycomb repressive complex 2 (PRC2) surrogate to study the effect of histone H3 lysine 27 (H3K27) methylation on gene transcription, as both catalyze histone H3K27 trimethylation. To control the enzymatic activity of vSET in vivo with an engineered S-adenosyl-l-methionine (SAM) analogue as methyl donor cofactor, we have carried out structure-guided design,...

Read the complete abstract on PubMed

Topics

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

Share to Coenzymes
Share to Histone-Lysine N-Methyltransferase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Histones

Share to Lysine

Share to Methylation

Share to Paramecium

Share to Stereoisomerism

Share to Viral Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 21958314
DOI: 10.1021/jm201000j
PMCID: PMC3326379

Genes

SET

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure-guided design of a methyl donor cofactor that controls a viral histone H3 lysine 27 methyltransferase activity.PMID 21958314Read ↗

A computational design strategy for discovering the protein targets of histone lysine methyltransferasesSemantic proximity Read ↗

High-resolution structures of the SARS-CoV-2 N7-methyltransferase inform therapeutic developmentSemantic proximity Read ↗

Identification and Characterization of Novel Broad-Spectrum Inhibitors of the Flavivirus MethyltransferaseSemantic proximity Read ↗

Discovery of a Non-Nucleoside SETD2 Methyltransferase Inhibitor against Acute Myeloid Leukemia.Semantic proximity Read ↗

Discovery and characterisation of the automethylation properties of PRDM9.Semantic proximity Read ↗

A combinatorial domain screening platform reveals epigenetic effector interactions for transcriptional perturbationSemantic proximity Read ↗

Characterization of the histone methyltransferase PRDM9 using biochemical, biophysical and chemical biology techniques.Semantic proximity Read ↗

Structure of the PRC2 complex and application to drug discovery.Semantic proximity Read ↗

Crystal structures of the human histone H4K20 methyltransferases SUV420H1 and SUV420H2.Semantic proximity Read ↗

Attenuation of SARS‐CoV‐2 replication and associated inflammation by concomitant targeting of viral and host cap 2'‐O‐ribose methyltransferasesSemantic proximity Read ↗

Discovery and engineering of hypercompact epigenetic modulators for durable gene activationSemantic proximity Read ↗

SRA- and SET-domain-containing proteins link RNA polymerase V occupancy to DNA methylation.Semantic proximity Read ↗

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