ArticleAnalytical chemistry2018
Identification of Helicase Proteins as Clients for HSP90.
Article in Analytical chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- Regulation of RNA-binding proteins by small biomolecules.Nature reviews. Molecular cell biology · 2026Review
- Article
- Aha1 Is an Autonomous Chaperone for SULT1A1.Chemical research in toxicology · 2022Article
- Quantitative Proteomic Analysis Revealed Broad Roles ofJournal of proteome research · 2021Article
- A Targeted Quantitative Proteomic Method Revealed a Substantial Reprogramming of Kinome during Melanoma Metastasis.Scientific reports · 2020Article
- High-Throughput Targeted Quantitative Analysis of the Interaction between HSP90 and Kinases.Analytical chemistry · 2019Article
- Parallel-Reaction-Monitoring-Based Proteome-Wide Profiling of Differential Kinase Protein Expression during Prostate Cancer Metastasis in Vitro.Analytical chemistry · 2019Article
- SLIRP Interacts with Helicases to Facilitate 2'-Journal of the American Chemical Society · 2019Article
- Quantitative Interrogation of the Human Kinome Perturbed by Two BRAF Inhibitors.Journal of proteome research · 2019Article
- Targeted Quantitative Kinome Analysis Identifies PRPS2 as a Promoter for Colorectal Cancer Metastasis.Journal of proteome research · 2019Article
- Imatinib-Induced Changes in Protein Expression and ATP-Binding Affinities of Kinases in Chronic Myelocytic Leukemia Cells.Analytical chemistry · 2019Article
- Targeted Profiling of Heat Shock Proteome in Radioresistant Breast Cancer Cells.Chemical research in toxicology · 2019Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The 90-kDa heat shock protein (HSP90) is a molecular chaperone that maintains the proper folding of its client proteins including protein kinases and steroid hormone receptors. Helicases are a group of nucleic acid-binding ATPases that can unwind DNA and/or RNA and function in almost every aspect of nucleic acid metabolism. Not much, however, is known about the interactions between HSP90 and helicase proteins. Herein, we developed a parallel-reaction monitoring (PRM)-based targeted proteomic method that allows for quantifying >80% of the human helicase proteome. By employing this method, we demonstrated that a large number of helicase proteins exhibited diminished expression in cultured human cells upon treatment with two small-molecule inhibitors of HSP90. We further introduced a tandem affinity tag to the C-terminus of endogenous HSP90β protein by using the CRISPR-Cas9 genome editing method. Affinity purification followed by LC-PRM analysis revealed an enrichment of 40 out of the 66 quantified helicases from the lysate of cells expressing tagged HSP90β. Together, we developed a high-throughput targeted proteomic method for assessing quantitatively the human helicase proteome, and our results support that helicases may constitute an important group of client proteins for HSP90.
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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.