ArticleFrontiers in cell and developmental biology2021
SPAAC Pulse-Chase: A Novel Click Chemistry-Based Method to Determine the Half-Life of Cellular Proteins.
Article in Frontiers in cell and developmental biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Advancements and applications of click chemistry in protein labeling and bioconjugation.RSC advances · 2026Review
- Mitochondrial respiration modulates Hsf1 activation and the heat shock response.bioRxiv : the preprint server for biology · 2026Article
- Optimizing bio-orthogonal non-canonical amino acid tagging (BONCAT) for low-disruption labeling of Arabidopsis proteins in vivo.Plant physiology · 2026Article
- Deep Learning-Based Protein Half-Life Prediction for Identifying Rate-Limiting Enzymes in Metabolic Pathways to Alleviate Bottleneck Reactions.Journal of microbiology and biotechnology · 2026Article
- Can plitidepsin be used as an antiviral against RSV?mSphere · 2025Article
- An Enigma of N-termini dependent protein degradation.Biochemistry and biophysics reports · 2025Article
- Residue-Specific Incorporation of Noncanonical Amino Acids in Auxotrophic Hosts:Chemical reviews · 2025Review
- Specific branches of the proteostasis network regulate the toxicity associated with mistranslation.Nucleic acids research · 2025Article
- Intracellular protein editing enables incorporation of noncanonical residues in endogenous proteins.Science (New York, N.Y.) · 2025Article
- The FBXO45-GEF-H1 Axis Controls Germinal Center Formation and B-cell Lymphomagenesis.Cancer discovery · 2025Article
- Engineered Proteins and Materials Utilizing Residue-Specific Noncanonical Amino Acid Incorporation.Chemical reviews · 2024Review
- Cellular turnover and degradation of the most common missense cystathionine beta-synthase variants causing homocystinuria.Protein science : a publication of the Protein Society · 2024Article
- Generation of site-specifically labelled fluorescent human XPA to investigate DNA binding dynamics during nucleotide excision repair.Methods (San Diego, Calif.) · 2024Article
- IL-2Rα KO mice exhibit maternal microchimerism and reveal nuclear localization of IL-2Rα in lymphoid and non-lymphoid cells.Frontiers in immunology · 2024Article
- Labeling strategies to track protozoan parasite proteome dynamics.Current opinion in chemical biology · 2023Review
- TNF-α-Driven Changes in Polarized EGF Receptor Trafficking Facilitate Phosphatidylinositol 3-Kinase/Protein Kinase B Signaling From the Apical Surface of MDCK Epithelial Cells.Traffic (Copenhagen, Denmark)Article
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4 authors.
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Abstract
Assessing the stability and degradation of proteins is central to the study of cellular biological processes. Here, we describe a novel pulse-chase method to determine the half-life of cellular proteins that overcomes the limitations of other commonly used approaches. This method takes advantage of pulse-labeling of nascent proteins in living cells with the bioorthogonal amino acid L-azidohomoalanine (AHA) that is compatible with click chemistry-based modifications. We validate this method in both mammalian and yeast cells by assessing both over-expressed and endogenous proteins using various fluorescent and chemiluminescent click chemistry-compatible probes. Importantly, while cellular stress responses are induced to a limited extent following live-cell AHA pulse-labeling, we also show that this response does not result in changes in cell viability and growth. Moreover, this method is not compromised by the cytotoxicity evident in other commonly used protein half-life measurement methods and it does not require the use of radioactive amino acids. This new method thus presents a versatile, customizable, and valuable addition to the toolbox available to cell biologists to determine the stability of cellular proteins.
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