ArticleProceedings of the National Academy of Sciences of the United States of America2016
Mass spectrometry-based absolute quantification reveals rhythmic variation of mouse circadian clock proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers, 1 of them a synthesis that pooled it.
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Who cites it
47 citing papers in PubMed, 1 synthesis or guideline pooled it, 76 citations in OpenAlex.
- Cell-Free Approach for Non-canonical Amino Acids Incorporation Into Polypeptides.Frontiers in bioengineering and biotechnology · 2020Pooled it
- Targeted quantification assays for DNA repair and handling proteins and interactions in Huntington's disease models.bioRxiv : the preprint server for biology · 2026Article
- Nuclear CK1δ as a critical determinant of PER:CRY complex dynamics and circadian period.eLife · 2026Article
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- Multilayer Timing of Cardiac Circadian Regulation Informs Prevention and Treatment of Cardiovascular Disease.Vascular health and risk management · 2026Article
- Serum fucosylated receptor expression-enhancing protein 5 as a biomarker for early stage pancreatic cancer.Oncology letters · 2025Article
- Absolute Quantitation of Phosphopeptides and Glycopeptides Using Coulometric Mass Spectrometry.ACS measurement science au · 2025Article
- CRYing for balance: a repressor lingers through peak circadian transcription.The EMBO journal · 2025Article
- Abundant clock proteins point to missing molecular regulation in the plant circadian clock.Molecular systems biology · 2025Article
- Elucidation of the mechanism of amyloid A and transthyretin formation using mass spectrometry-based absolute quantification.Virchows Archiv : an international journal of pathology · 2024Article
- Circadian period is compensated for repressor protein turnover rates in single cells.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Mammalian circadian clock proteins form dynamic interacting microbodies distinct from phase separation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Mammalian circadian clock proteins form dynamic interacting microbodies distinct from phase separation.bioRxiv : the preprint server for biology · 2023Article
- Circadian ribosome profiling reveals a role for theProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Identification of CD14 and lipopolysaccharide-binding protein as novel biomarkers for sarcoidosis using proteomics of serum extracellular vesicles.International immunology · 2022Article
- Mathematical analysis of robustness of oscillations in models of the mammalian circadian clock.PLoS computational biology · 2022Article
- Cell-Free PURE System: Evolution and Achievements.Biodesign research · 2022Review
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- Live-cell imaging of circadian clock protein dynamics in CRISPR-generated knock-in cells.Nature communications · 2021Article
- Proteomic analysis of urinary and tissue-exudative extracellular vesicles to discover novel bladder cancer biomarkers.Cancer science · 2021Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Absolute values of protein expression levels in cells are crucial information for understanding cellular biological systems. Precise quantification of proteins can be achieved by liquid chromatography (LC)-mass spectrometry (MS) analysis of enzymatic digests of proteins in the presence of isotope-labeled internal standards. Thus, development of a simple and easy way for the preparation of internal standards is advantageous for the analyses of multiple target proteins, which will allow systems-level studies. Here we describe a method, termed MS-based Quantification By isotope-labeled Cell-free products (MS-QBiC), which provides the simple and high-throughput preparation of internal standards by using a reconstituted cell-free protein synthesis system, and thereby facilitates both multiplexed and sensitive quantification of absolute amounts of target proteins. This method was applied to a systems-level dynamic analysis of mammalian circadian clock proteins, which consist of transcription factors and protein kinases that govern central and peripheral circadian clocks in mammals. Sixteen proteins from 20 selected circadian clock proteins were successfully quantified from mouse liver over a 24-h time series, and 14 proteins had circadian variations. Quantified values were applied to detect internal body time using a previously developed molecular timetable method. The analyses showed that single time-point data from wild-type mice can predict the endogenous state of the circadian clock, whereas data from clock mutant mice are not applicable because of the disappearance of circadian variation.
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