skip to main content
Ngôn ngữ:
Giới hạn tìm kiếm: Giới hạn tìm kiếm: Dạng tài nguyên Hiển thị kết quả với: Hiển thị kết quả với: Chỉ mục

Identification of lysine acetyltransferase p300 substrates using 4-pentynoyl-coenzyme A and bioorthogonal proteomics

Yu-Ying, Yang ; Markus, Grammel ; Howard, Hang C

Bioorganic & Medicinal Chemistry Letters, 01 September 2011, Vol.21(17), pp.4976-4979 [Tạp chí có phản biện]

ISSN: 0960-894X ; E-ISSN: 1464-3405 ; DOI: 10.1016/j.bmcl.2011.05.060

Toàn văn sẵn có

Trích dẫn Trích dẫn bởi
  • Nhan đề:
    Identification of lysine acetyltransferase p300 substrates using 4-pentynoyl-coenzyme A and bioorthogonal proteomics
  • Tác giả: Yu-Ying, Yang ; Markus, Grammel ; Howard, Hang C
  • Chủ đề: Acetylation ; Chemical Reporter ; Bioorthogonal Ligation ; Proteomics ; Medicine ; Chemistry ; Anatomy & Physiology
  • Là 1 phần của: Bioorganic & Medicinal Chemistry Letters, 01 September 2011, Vol.21(17), pp.4976-4979
  • Mô tả: Proteomic studies have identified a plethora of lysine acetylated proteins in eukaryotes and bacteria. Determining the individual lysine acetyltransferases responsible for each protein acetylation mark is crucial for elucidating the underlying regulatory mechanisms, but has been challenging due to limited biochemical methods. Here, we describe the application of a bioorthogonal chemical proteomics method to profile and identify substrates of individual lysine acetyltransferases. Addition of 4-pentynoyl-coenzyme A, an alkynyl chemical reporter for protein acetylation, to cell extracts, together with purified lysine acetyltransferase p300, enabled the fluorescent profiling and identification of protein substrates via Cu(I)-catalyzed alkyne–azide cycloaddition. We identified several known protein substrates of the acetyltransferase p300 as well as the lysine residues that were modified. Interestingly, several new candidate p300 substrates and their sites of acetylation were also...
  • Ngôn ngữ: English
  • Số nhận dạng: ISSN: 0960-894X ; E-ISSN: 1464-3405 ; DOI: 10.1016/j.bmcl.2011.05.060

Đang tìm Cơ sở dữ liệu bên ngoài...