Evidence map›Paper›PMID 29760386›Full record

ArticleNature communications2018

Rapid labelling and covalent inhibition of intracellular native proteins using ligand-directed N-acyl-N-alkyl sulfonamide.

Tomonori Tamura, Tsuyoshi Ueda, Taiki Goto, Taku Tsukidate, Yonatan Shapira, Yuki Nishikawa, Alma Fujisawa, Itaru Hamachi

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
9.1field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

87 citing papers in PubMed, 239 citations in OpenAlex.

  1. Article
  2. Toward Ideal Proximity-Driven Reactions in Chemical Biology.Chembiochem : a European journal of chemical biology · 2026
    Review
  3. Review
  4. Review
  5. Review
  6. Precision Chemistry for Protein Lysine Modification.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Review
  7. Targeting Adaptive and Innate Immune Responses with Covalent Aptamers.Journal of the American Chemical Society · 2026
    Article
  8. Review
  9. RSC chemical biology · 2026
    Article
  10. Expediated synthesis ofOrganic & biomolecular chemistry · 2026
    Article
  11. Article
  12. Lysine Targeting Group-Transfer Chimeras for Proximity Induction.Angewandte Chemie (International ed. in English) · 2026
    Article
  13. Review
  14. A Scalable Design for Proximity-Inducing Molecules.bioRxiv : the preprint server for biology · 2026
    Article
  15. Review
  16. Article
  17. Review
  18. N-Acyl-N-Alkyl Sulfonamide Mediated Bioconjugation ofHis-Tag Fused Proteins.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  19. Article
  20. Article

27 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Tomonori TamuraDepartment of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto, 615-8510, Japan.ORCID http://orcid.org/0000-0003-1648-9296
Tsuyoshi UedaDepartment of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto, 615-8510, Japan.
Taiki GotoDepartment of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto, 615-8510, Japan.
Taku TsukidateDepartment of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto, 615-8510, Japan.
Yonatan ShapiraFeinberg Graduate School, Weizmann Institute of Science, Rehovot, 7610001, Israel.
Yuki NishikawaDepartment of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto, 615-8510, Japan.
Alma FujisawaDepartment of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto, 615-8510, Japan.
Itaru HamachiDepartment of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto, 615-8510, Japan. ihamachi@sbchem.kyoto-u.ac.jp.
Kyoto University · JPWeizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Selective modification of native proteins in live cells is one of the central challenges in recent chemical biology. As a unique bioorthogonal approach, ligand-directed chemistry recently emerged, but the slow kinetics limits its scope. Here we successfully overcome this obstacle using N-acyl-N-alkyl sulfonamide as a reactive group. Quantitative kinetic analyses reveal that ligand-directed N-acyl-N-alkyl sulfonamide chemistry allows for rapid modification of a lysine residue proximal to the ligand binding site of a target protein, with a rate constant of ~10

Indexed as

Chemistry Techniques, AnalyticalAnimalsCell Line, TumorHeLa CellsHeterocyclic Compounds, 1-RingHSP90 Heat-Shock ProteinsHumansKineticsLysineMiceMyoblastsStaining and LabelingSulfanilamidesTetrahydrofolate DehydrogenaseTOR Serine-Threonine KinasesHeterocyclic Compounds, 1-RingHSP90 Heat-Shock ProteinsLysineSulfanilamidesTetrahydrofolate DehydrogenaseTOR Serine-Threonine Kinases

Identifiers

PMID29760386
PMCPMC5951806
OpenAlexW2806557186

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.