Thiolation Domain Function
Thiolation Domain Function is a biochemical mechanism within nonribosomal peptide synthetase (NRPS) systems that serves to covalently bind activated amino acid or peptidyl intermediates via a thioester linkage to a phosphopantetheine arm, thereby enabling their translocation between catalytic domains during peptide assembly.
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David E. Ehmann, Cathryn A. Shaw-Reid, Heather C. Losey et al. · Proceedings of the National Academy of Sciences · 2000 · 110 citations
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Harvard University
Cambridge, United States
9 h-index
30 publications
2.1K citations
Philipps University of Marburg
Marburg, Germany
5 h-index
14 publications
1.4K citations
University of Kentucky
Lexington, United States
3 h-index
12 publications
235 citations
University of Illinois Urbana-Champaign
Urbana, United States
2 h-index
6 publications
398 citations
Maurice Wilkins Centre
Auckland, New Zealand
2 h-index
4 publications
339 citations
Max Planck Institute for Terrestrial Microbiology
Marburg, Germany
2 h-index
10 publications
808 citations

Victoria University of Wellington
Wellington, New Zealand
2 h-index
5 publications
366 citations
Stanford University
Stanford, United States
2 h-index
6 publications
258 citations
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JACS · 4 publications · 297 citations
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