Getting a chemical handle on protein post-translational modification

被引:39
作者
Heal, William P.
Tate, Edward W. [1 ]
机构
[1] Univ London Imperial Coll Sci Technol & Med, Dept Chem, London SW7 2AZ, England
基金
英国生物技术与生命科学研究理事会;
关键词
GLCNAC-MODIFIED PROTEINS; N-MYRISTOYL-TRANSFERASE; ACTIVITY-BASED PROTEOMICS; O-LINKED GLYCOSYLATION; ACTIVITY-BASED PROBES; CLICK CHEMISTRY; IN-VIVO; SIGNALING PATHWAYS; MASS-SPECTROMETRY; RAB GTPASES;
D O I
10.1039/b917894e
中图分类号
O62 [有机化学];
学科分类号
070303 ; 081704 ;
摘要
This article highlights the emerging field of chemical proteomics, a powerful technology for the study of post-and co-translational modification of proteins. Genome mapping and the study of protein post-translational modifications have revealed the astounding chemical complexity present in the proteome of even the simplest organisms. The identification and characterisation of the modifications present on specific proteins in such complex mixtures has become a central challenge for post-genomic functional studies in cell and systems biology. In the chemical proteomic approach to this problem, protein-modifying enzymes and bioorthogonal chemoselective elaboration are exploited to deliver chemical tags to specific modified residues, enabling new advances in our understanding of protein modification.
引用
收藏
页码:731 / 738
页数:8
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