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Article

Bioorthogonal profiling of protein methylation (BPPM) using an azido analog of S-adenosyl-L-methionine.

Current protocols in chemical biology - 1 Jan 2013

Blum Gil, Islam Kabirul, Luo Minkui

Abstract excerpt

Protein methyltransferases (PMTs) utilize S-adenosyl-L-methionine (SAM) as a cofactor and transfer its sulfonium methyl moiety to diverse substrates. These methylation events can lead to meaningful biological outcomes, from transcriptional activation/silencing to cell cycle regulation. This article describes recently developed technology based on protein engineering in tandem with SAM analog cofactors and...

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Share to Azides
Share to Histocompatibility Antigens
Share to Histone-Lysine N-Methyltransferase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Methylation

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Share to S-Adenosylmethionine

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Source

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Identifiers

PMID: 23667794
DOI: 10.1002/9780470559277.ch120240
PMCID: PMC3647616

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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