Current chemical biology approaches to interrogate protein methyltransferases Journal Article
| Author: | Luo, M. |
| Article Title: | Current chemical biology approaches to interrogate protein methyltransferases |
| Abstract: | Protein methyltransferases (PMTs) play various physiological and pathological roles through methylating histone and nonhistone targets. However, most PMTs including more than 60 human PMTs remain to be fully characterized. The current approaches to elucidate the functions of PMTs have been diversified by many emerging chemical biology technologies. This review focuses on progress in these aspects and is organized into four discussion modules (assays, substrates, cofactors, and inhibitors) that are important to elucidate biological functions of PMTs. These modules are expected to provide general guidance and present emerging methods for researchers to select and combine suitable PMT-activity assays, well-defined substrates, novel SAM surrogates, and PMT inhibitors to interrogate PMTs. © 2012 American Chemical Society. |
| Keywords: | protein phosphorylation; unclassified drug; sequence analysis; drug activity; review; mass spectrometry; protein analysis; animals; protein; in vivo study; high throughput screening; in vitro study; enzyme activity; assay; enzyme linked immunosorbent assay; methyltransferase; methyltransferases; models, molecular; radiometry; antibody detection; ic 50; biochemistry; protein microarray; antibody; protein methylation; conjugation; s adenosylhomocysteine; chemical mutagenesis; methyltransferase inhibitor; 5' aziridine s adenosylhomocysteine; 5' n iodoethyl s adenosylhomocysteine; allantodapsone; c 7280948; epz004777; n6 benzyl s adenosylhomocysteine; rm65; stilbamidine; sulfonium alkyl s adenosylhomocysteine; unc0638 |
| Journal Title: | ACS Chemical Biology |
| Volume: | 7 |
| Issue: | 3 |
| ISSN: | 1554-8929 |
| Publisher: | American Chemical Society |
| Date Published: | 2012-03-16 |
| Start Page: | 443 |
| End Page: | 463 |
| Language: | English |
| DOI: | 10.1021/cb200519y |
| PROVIDER: | scopus |
| PMCID: | PMC3306480 |
| PUBMED: | 22220966 |
| DOI/URL: | |
| Notes: | --- - "Export Date: 2 April 2012" - "CODEN: ACBCC" - "Source: Scopus" |
