ArticleNature2015
Organometallic palladium reagents for cysteine bioconjugation.
Article in Nature, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 187 papers.
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.
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.
Who cites it
187 citing papers in PubMed, 505 citations in OpenAlex.
- Functionalization of Peptides via Radical Arylation.Chembiochem : a European journal of chemical biology · 2026Review
- Modular Assembly of Bioconjugates Enabled by a Pyridine-Based Chemoselective Sequential Conjugation Platform.Angewandte Chemie (International ed. in English) · 2026Article
- Site-specific protein functionalization by late-stage reversible cysteine masking.Nature communications · 2026Article
- Organometallic Chemistry Approach to Peptide Tricycles.Bioconjugate chemistry · 2026Article
- Palladacarboxamide Capping Reagents for Carbon Isotope Labeling and Pharmaceutical Diversification.Angewandte Chemie (International ed. in English) · 2026Article
- TagC-RED: An Infrared-Triggered Retro-Ene Reaction for Deep-Tissue Bioconjugation.Journal of the American Chemical Society · 2026Article
- Advancing protein engineering via organic chemistry.Communications chemistry · 2026Review
- Unlocking the Silent Proteome: Chemoselective Asn/Gln Activation for Multidimensional Protein Diversification.Journal of the American Chemical Society · 2026Article
- Biocompatible organometallics for in-cell protein arylation.Nature chemistry · 2026Article
- Biocompatible ligand balancing in transition metal coordination enables benign in-cell protein arylation.Nature chemistry · 2026Article
- Ligand-enabled next-generation glycosyl Stille cross-coupling for the stereospecific synthesis of sterically hindered aryl C-glycosides.Nature communications · 2026Article
- Engineering Light-Responsive Transcription Factors via Strategic Masking of Post-translational Modification Residues.Bioconjugate chemistry · 2026Article
- Conditionally Activatable Antibody Platforms: Mechanisms, Modalities, and Clinical Translation Potential.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026Review
- Chemoselective Histidine Bioconjugation Using Thiophosphorodichloridate Reagents.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Site-Selective Peptide and Protein Functionalization with Cyclopropenium Cations.Angewandte Chemie (International ed. in English) · 2025Article
- Achieving cysteine-selective peptide/protein bioconjugation via tunable triazine-pyridine chemistry.Science advances · 2025Article
- Pd(0)-Mediated Deallylation Chemistry: A Reassessment of Its Application in Sensing CO.The Journal of organic chemistry · 2025Article
- Cys-Lys stapling for unprotected peptides via tunable linkers.National science review · 2025Article
- Electro-induced C-H/S-H cross-coupling for the functionalization/macrocyclization of cysteine-containing peptides.Nature communications · 2025Article
- Ruthenium-MediatedJournal of the American Chemical Society · 2025Article
127 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Reactions based on transition metals have found wide use in organic synthesis, in particular for the functionalization of small molecules. However, there are very few reports of using transition-metal-based reactions to modify complex biomolecules, which is due to the need for stringent reaction conditions (for example, aqueous media, low temperature and mild pH) and the existence of multiple reactive functional groups found in biomolecules. Here we report that palladium(II) complexes can be used for efficient and highly selective cysteine conjugation (bioconjugation) reactions that are rapid and robust under a range of bio-compatible reaction conditions. The straightforward synthesis of the palladium reagents from diverse and easily accessible aryl halide and trifluoromethanesulfonate precursors makes the method highly practical, providing access to a large structural space for protein modification. The resulting aryl bioconjugates are stable towards acids, bases, oxidants and external thiol nucleophiles. The broad utility of the bioconjugation platform was further corroborated by the synthesis of new classes of stapled peptides and antibody-drug conjugates. These palladium complexes show potential as benchtop reagents for diverse bioconjugation applications.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.