4.6 Review

Chemical approaches to mapping the function of post-translational modifications

Journal

FEBS JOURNAL
Volume 275, Issue 9, Pages 1949-1959

Publisher

WILEY
DOI: 10.1111/j.1742-4658.2008.06347.x

Keywords

chemoselective ligation; post-translational modification; protein glycosylation; protein modification; synthetic proteins

Funding

  1. Biotechnology and Biological Sciences Research Council [BB/D005949/1, BB/C510824/1, EGA17763, BB/E004350/1] Funding Source: researchfish
  2. Engineering and Physical Sciences Research Council [EP/E000614/1, EP/D023335/1, GR/T26542/01, EP/D023343/1] Funding Source: researchfish
  3. Biotechnology and Biological Sciences Research Council [BB/E004350/1, BB/D005949/1, EGA17763] Funding Source: Medline
  4. BBSRC [BB/D005949/1, BB/E004350/1] Funding Source: UKRI
  5. EPSRC [EP/E000614/1] Funding Source: UKRI

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Strategies for the chemical construction of synthetic proteins with precisely positioned post-translational modifications or their mimics offer a powerful method for dissecting the complexity of functional protein alteration and the associated complexity of proteomes.

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