View in EDS

Chemoselective Azidation of Cysteine Coupled with Traceless Staudinger Ligation Enables Site-Specific Acylation of Recombinant Proteins.

Saved in:
Bibliographic Details
Title: Chemoselective Azidation of Cysteine Coupled with Traceless Staudinger Ligation Enables Site-Specific Acylation of Recombinant Proteins.
Authors: Cui T; School of Food and Biological Engineering, Engineering Research Center of Bio-process, Ministry of Education, Key Laboratory of Animal Source of Anhui Province, Hefei University of Technology, Hefei 230009, China., Sun J; School of Food and Biological Engineering, Engineering Research Center of Bio-process, Ministry of Education, Key Laboratory of Animal Source of Anhui Province, Hefei University of Technology, Hefei 230009, China., Liu N; School of Food and Biological Engineering, Engineering Research Center of Bio-process, Ministry of Education, Key Laboratory of Animal Source of Anhui Province, Hefei University of Technology, Hefei 230009, China., Yu B; School of Food and Biological Engineering, Engineering Research Center of Bio-process, Ministry of Education, Key Laboratory of Animal Source of Anhui Province, Hefei University of Technology, Hefei 230009, China., Li YM; School of Food and Biological Engineering, Engineering Research Center of Bio-process, Ministry of Education, Key Laboratory of Animal Source of Anhui Province, Hefei University of Technology, Hefei 230009, China., Chu GC; School of Food and Biological Engineering, Engineering Research Center of Bio-process, Ministry of Education, Key Laboratory of Animal Source of Anhui Province, Hefei University of Technology, Hefei 230009, China.
Source: Organic letters [Org Lett] 2026 May 29; Vol. 28 (21), pp. 6625-6630. Date of Electronic Publication: 2026 May 14.
Publication Type: Journal Article
Journal Info: Publisher: American Chemical Society Country of Publication: United States NLM ID: 100890393 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1523-7052 (Electronic) Linking ISSN: 15237052 NLM ISO Abbreviation: Org Lett Subsets: MEDLINE
Database: MEDLINE Ultimate
Description
ISSN:1523-7052
DOI:10.1021/acs.orglett.6c01442