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.

30

Publications

1.6K

Citations

120

Authors

40

Institutions

Publications per year

2017–2026

9

Publications

30

Authors

120

  1. CT
    Christopher T. Walsh

    Harvard University, United States

    9 publications · 641 citations

    9

    h-index

  2. MA
    Mohamed A. Marahiel

    Philipps University of Marburg, Germany

    4 publications · 417 citations

    4

    h-index

  3. SG
    Sylvie Garneau‐Tsodikova

    University of Kentucky, United States

    3 publications · 54 citations

    3

    h-index

  4. DS
    Dirk Schwarzer

    University of Tübingen, Germany

    2 publications · 197 citations

    2

    h-index

  5. SM
    Shogo Mori

    University of Kentucky, United States

    2 publications · 27 citations

    2

    h-index

1–5 of 120

Venues

  1. Biochemistry

    4 publications · 182 citations

    5

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  2. Journal of the American Chemical Society

    JACS · 4 publications · 297 citations

    4

    h-index

  3. ChemBioChem

    3 publications · 150 citations

    3

    h-index

  4. Chemistry & Biology

    3 publications · 230 citations

    3

    h-index

  5. Nature Communications

    2 publications · 132 citations

    2

    h-index

1–5