ReviewAnnual review of biochemistry2015
Application of the protein semisynthesis strategy to the generation of modified chromatin.
Review in Annual review of biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 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
35 citing papers in PubMed, 73 citations in OpenAlex.
- Site-specific protein functionalization by late-stage reversible cysteine masking.Nature communications · 2026Article
- Histone modification cross-talk: analytical tools and molecular mechanisms.The Biochemical journal · 2026Review
- Advancing protein engineering via organic chemistry.Communications chemistry · 2026Review
- Histone probes for reader and eraser investigations.Chemical science · 2025Review
- Nucleosome context regulates chromatin reader preference.Nucleic acids research · 2025Article
- A Versatile Method for Site-Specific Chemical Installation of Aromatic Posttranslational Modification Analogs into Proteins.Journal of the American Chemical Society · 2024Article
- Site-Specific Acetylation of the Transcription Factor Protein Max Modulates Its DNA Binding Activity.ACS central science · 2024Article
- Interrogating epigenetic mechanisms with chemically customized chromatin.Nature reviews. Genetics · 2024Review
- Beyond the tail: the consequence of context in histone post-translational modification and chromatin research.The Biochemical journal · 2024Article
- Post-translational activation of the C-terminus of polypeptides for the synthesis of peptide thioesters and peptide thioester surrogates.Frontiers in chemistry · 2024Review
- Synthesis of ubiquitinated proteins for biochemical and functional analysis.Chemical science · 2023Review
- Chemical probes and methods for the study of protein arginine methylation.RSC chemical biology · 2023Review
- Limited choice of natural amino acids as mimetics restricts design of protein lysine methylation studies.Nature communications · 2023Article
- Posttranslational Chemical Mutagenesis Methods to Insert Posttranslational Modifications into Recombinant Proteins.Molecules (Basel, Switzerland) · 2022Review
- Molecular probes for cellular imaging of post-translational proteoforms.RSC chemical biology · 2022Review
- The interplay between DNA and histone methylation: molecular mechanisms and disease implications.EMBO reports · 2021Review
- Chemoenzymatic Semisynthesis of Proteins.Chemical reviews · 2020Review
- Interactions With Histone H3 & Tools to Study Them.Frontiers in cell and developmental biology · 2020Review
- Chemical Biology of Autophagy-Related Proteins With Posttranslational Modifications: From Chemical Synthesis to Biological Applications.Frontiers in chemistry · 2020Review
- Strategies for Generating Modified Nucleosomes: Applications within Structural Biology Studies.ACS chemical biology · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Histone proteins are subject to a host of posttranslational modifications (PTMs) that modulate chromatin structure and function. Such control is achieved by the direct alteration of the intrinsic physical properties of the chromatin fiber or by regulating the recruitment and activity of a host of trans-acting nuclear factors. The sheer number of histone PTMs presents a formidable barrier to understanding the molecular mechanisms at the heart of epigenetic regulation of eukaryotic genomes. One aspect of this multifarious problem, namely how to access homogeneously modified chromatin for biochemical studies, is well suited to the sensibilities of the organic chemist. Indeed, recent years have witnessed a critical role for synthetic protein chemistry methods in generating the raw materials needed for studying how histone PTMs regulate chromatin biochemistry. This review focuses on what is arguably the most powerful, and widely employed, of these chemical strategies, namely histone semisynthesis via the chemical ligation of peptide fragments.
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.