ArticleNature protocols2017
Nonradioactive quantification of autophagic protein degradation with L-azidohomoalanine labeling.
Article in Nature protocols, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers, 1 of them a synthesis that pooled it.
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Who cites it
32 citing papers in PubMed, 1 synthesis or guideline pooled it.
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- Exploiting the Therapeutic Interaction of WNT Pathway Activation and Asparaginase for Colorectal Cancer Therapy.Cancer discovery · 2020Article
- 3D visualization of macromolecule synthesis.eLife · 2020Article
- Quantitative analysis of global protein stability rates in tissues.Scientific reports · 2020Article
- Pharmacological clearance of misfolded rhodopsin for the treatment of RHO-associated retinitis pigmentosa.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Trichoplein binds PCM1 and controls endothelial cell function by regulating autophagy.EMBO reports · 2020Article
- Inhibition of transcription by dactinomycin reveals a new characteristic of immunogenic cell stress.EMBO molecular medicine · 2020Article
- Comprehensive autophagy evaluation in cardiac disease models.Cardiovascular research · 2020Review
- DAPK1 Promotes Extrasynaptic GluN2B Phosphorylation and Striatal Spine Instability in the YAC128 Mouse Model of Huntington Disease.Frontiers in cellular neuroscience · 2020Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
At present, several assays that use radioisotope labeling to quantify the degradation of long-lived proteins have been developed to measure autophagic flux. Here, we describe a nonradioactive pulse-chase protocol using L-azidohomoalanine (AHA) labeling to quantify long-lived protein degradation during autophagy. AHA is used as a surrogate for L-methionine, and, when added to cultured cells grown in methionine-free medium, AHA is incorporated into proteins during de novo protein synthesis. After a chase period to remove short-lived proteins, autophagy is induced by starvation or other stimuli. Cells then undergo a 'click' reaction between the azide group of AHA and a fluorescently tagged alkyne probe. The AHA-containing proteins can then be detected by flow cytometry. This protocol is nonradioactive, sensitive and quantitative, and it is easy to perform. It is also applicable to various cell culture systems. The whole protocol is estimated to take 4-5 d to complete.
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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.