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Current Chemical Biology Approaches to Interrogate Protein Methyltransferases

期刊

ACS CHEMICAL BIOLOGY
卷 7, 期 3, 页码 443-463

出版社

AMER CHEMICAL SOC
DOI: 10.1021/cb200519y

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资金

  1. V Foundation for Cancer Research through 2009 V Foundation
  2. March of Dimes Birth Defects Foundation
  3. Alfred W. Bressler Scholars Endowment Fund Alfred
  4. NIH through NINDS [1R21NS071520-01]
  5. NIGMS [1R01GM096056-01]
  6. NIH [1-DP2-OD007335-01]
  7. Starr Foundation
  8. W. H. Goodwin and A. Goodwin the Commonwealth Foundation for Cancer Research
  9. Experimental Therapeutics Center of Memorial Sloan-Kettering Cancer Center

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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.

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