Evidence map›Paper›PMID 28206688›Full record

ArticleAngewandte Chemie (International ed. in English)2017

Palladium-Mediated Arylation of Lysine in Unprotected Peptides.

Hong Geun Lee, Guillaume Lautrette, Bradley L Pentelute, Stephen L Buchwald

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
8.1field-weighted citation impact, top 2% 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

42 citing papers in PubMed, 131 citations in OpenAlex.

  1. Functionalization of Peptides via Radical Arylation.Chembiochem : a European journal of chemical biology · 2026
    Review
  2. Article
  3. Article
  4. Photoredox-Catalyzed Lysine C(spJournal of the American Chemical Society · 2026
    Article
  5. Review
  6. Article
  7. Review
  8. Ultrafast Au(III)-Mediated Arylation of Cysteine.Journal of the American Chemical Society · 2024
    Article
  9. Recent Advances in Bioorthogonal Ligation and Bioconjugation.Topics in current chemistry (Cham) · 2023
    Review
  10. Review
  11. Selective Stepwise Arylation of Unprotected Peptides by PtAngewandte Chemie (International ed. in English) · 2022
    Article
  12. Article
  13. Pd(II)-Mediated C-H Activation for Cysteine Bioconjugation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022
    Article
  14. Peptide stapling by late-stage Suzuki-Miyaura cross-coupling.Beilstein journal of organic chemistry · 2022
    Article
  15. Organometallic AlaChem catalysis · 2021
    Article
  16. Review
  17. Article
  18. An Organometallic Strategy for Cysteine Borylation.Journal of the American Chemical Society · 2021
    Article
  19. DeaminativeChemical science · 2021
    Article
  20. Gold-Based Pharmacophore Inhibits Intracellular MYC Protein.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021
    Article
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

4 authors at 1 institution in 1 country.

Hong Geun LeeDepartment of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA, 02139, USA.
Guillaume LautretteDepartment of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA, 02139, USA.
Bradley L PenteluteDepartment of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA, 02139, USA.
Stephen L BuchwaldDepartment of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA, 02139, USA.
Massachusetts Institute of Technology · US

Funding

Cysteine ArylationR01GM110535 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI PENTELUTE, BRADLEY LETHER · 2014 to 2018
$1.5M
NIGMS NIH HHS R01 GM110535
6 · The paper itself

Abstract

A mild method for the arylation of lysine in an unprotected peptide is presented. In the presence of a preformed biarylphosphine-supported palladium(II)-aryl complex and a weak base, lysine amino groups underwent C-N bond formation at room temperature. The process generally exhibited high selectivity for lysine over other amino acids containing nucleophilic side chains and was applicable to the conjugation of a variety of organic compounds, including complex drug molecules, with an array of peptides. Finally, this method was also successfully applied to the formation of cyclic peptides by macrocyclization.

Indexed as

CyclizationLysineMolecular StructureOrganometallic CompoundsPalladiumPeptides, CyclicLysineOrganometallic CompoundsPalladiumPeptides, Cyclicbioconjugationchemoselectivitycross-couplingpeptide macrocyclizationphosphane ligands

Identifiers

PMID28206688
PMCPMC5741856
OpenAlexW2588794854

What OpenQuestion holds

Textmetadata
LicenceTDM
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.