ArticleProceedings of the National Academy of Sciences of the United States of America2013
Proteome-wide profiling of activated transcription factors with a concatenated tandem array of transcription factor response elements.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 115 citations in OpenAlex.
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- Quantitative proteomics of HFD-induced fatty liver uncovers novel transcription factors of lipid metabolism.International journal of biological sciences · 2022Article
- Proteome-wide profiling of transcriptional machinery on accessible chromatin with biotinylated transposons.Science advances · 2021Article
- HSPA13 facilitates NF-κB-mediated transcription and attenuates cell death responses in TNFα signaling.Science advances · 2021Article
- Proteome-Wide Profiling of Readers for DNA Modification.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021Article
- Proteome-scale profiling reveals MAFF and MAFG as two novel key transcription factors involved in palmitic acid-induced umbilical vein endothelial cell apoptosis.BMC cardiovascular disorders · 2021Article
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Authors and funding
13 authors at 4 institutions in 2 countries.
Funding
Abstract
Transcription factors (TFs) are families of proteins that bind to specific DNA sequences, or TF response elements (TFREs), and function as regulators of many cellular processes. Because of the low abundance of TFs, direct quantitative measurement of TFs on a proteome scale remains a challenge. In this study, we report the development of an affinity reagent that permits identification of endogenous TFs at the proteome scale. The affinity reagent is composed of a synthetic DNA containing a concatenated tandem array of the consensus TFREs (catTFRE) for the majority of TF families. By using catTFRE to enrich TFs from cells, we were able to identify as many as 400 TFs from a single cell line and a total of 878 TFs from 11 cell types, covering more than 50% of the gene products that code for the DNA-binding TFs in the genome. We further demonstrated that catTFRE pull-downs could quantitatively measure proteome-wide changes in DNA binding activity of TFs in response to exogenous stimulation by using a label-free MS-based quantification approach. Applying catTFRE on the evaluation of drug effects, we described a panoramic view of TF activations and provided candidates for the elucidation of molecular mechanisms of drug actions. We anticipate that the catTFRE affinity strategy will find widespread applications in biomedical research.
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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.