ReviewNature reviews. Chemistry2020
Deciphering protein post-translational modifications using chemical biology tools.
Review in Nature reviews. Chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers.
What it found
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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
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Who cites it
116 citing papers in PubMed.
- Site-Specific and Programmable Editing of Serine and Threonine in Unprotected Peptides.Journal of the American Chemical Society · 2026Article
- Single-Molecule Fingerprinting of Unlabeled Full-Length Proteins Using an Aerolysin Nanopore.Journal of the American Chemical Society · 2026Article
- Site-specific post-translational modification detection by polar charged engineered MspA nanopores.Chemical science · 2026Article
- Article
- Detection of Diagnostic Antibodies in Immune-Mediated Diseases: A Focus on Antigens and Technologies.Chembiochem : a European journal of chemical biology · 2026Review
- Advancing protein engineering via organic chemistry.Communications chemistry · 2026Review
- Proteoform medicine: characterizing and targeting protein forms in human disease.Nature reviews. Genetics · 2026Review
- Generating Ultra-Fast Protein trans-Splicing of a Cysteine-Less and Semisynthetic Split Intein for Chemical Protein Labeling.Chembiochem : a European journal of chemical biology · 2026Article
- Article
- Non-hydrolyzable acetyllysine analogs to study protein acetylation in vitro and in cells.Nature communications · 2026Article
- Mining lysine post-translational modification sites by integrating protein language model representations with structural context.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Development of Dimethylsulfonium Probes for Broad Profiling of Methyllysine Reader Proteins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Lactylation in cancer: molecular mechanisms and advances in clinical study.Molecular cancer · 2026Review
- Integration of high-throughput proteomic data and complementary omics layers with PriOmics.Genome research · 2026Article
- Modular FRET sensor for site-specific detection of protein arginine methylation in living cells.American journal of translational research · 2026Article
- Cofilin/RhoA and CREB synergistically promote invasion and migration of polyploid giant cancer cells in colorectal cancer.Journal of Cancer · 2026Article
- Induced Proximity Approach Enables the Recombinant Production of Polyphosphorylated Silk Proteins with Improved Adhesiveness.Biomacromolecules · 2025Article
- Selected Post-Translational Modifications-Phosphorylation and Glutathionylation-As Factors Involved in the Regulation During the Pregnancy Course and Foetal Membrane Release in Cows.International journal of molecular sciences · 2025Article
- Histone probes for reader and eraser investigations.Chemical science · 2025Review
- Tandem Allosteric Effects of Reactant and Product that Promote Deacetylation Cycles in Sir2.Journal of chemical information and modeling · 2025Article
56 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins carry out a wide variety of catalytic, regulatory, signalling and structural functions in living systems. Following their assembly on ribosomes and throughout their lifetimes, most eukaryotic proteins are modified by post-translational modifications; small functional groups and complex biomolecules are conjugated to amino acid side chains or termini, and the protein backbone is cleaved, spliced or cyclized, to name just a few examples. These modifications modulate protein activity, structure, location and interactions, and, thereby, control many core biological processes. Aberrant post-translational modifications are markers of cellular stress or malfunction and are implicated in several diseases. Therefore, gaining an understanding of which proteins are modified, at which sites and the resulting biological consequences is an important but complex challenge requiring interdisciplinary approaches. One of the key challenges is accessing precisely modified proteins to assign functional consequences to specific modifications. Chemical biologists have developed a versatile set of tools for accessing specifically modified proteins by applying robust chemistries to biological molecules and developing strategies for synthesizing and ligating proteins. This Review provides an overview of these tools, with selected recent examples of how they have been applied to decipher the roles of a variety of protein post-translational modifications. Relative advantages and disadvantages of each of the techniques are discussed, highlighting examples where they are used in combination and have the potential to address new frontiers in understanding complex biological processes.
Identifiers
37127974What 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.