ReviewFrontiers in genetics2014
Exploiting holistic approaches to model specificity in protein phosphorylation.
Review in Frontiers in genetics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Multiple Site-Specific Phosphorylation of IDPs Monitored by NMR.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Large-scale Discovery of Substrates of the Human Kinome.Scientific reports · 2019Article
- Kinome-wide identification of phosphorylation networks in eukaryotic proteomes.Bioinformatics (Oxford, England) · 2019Article
- Predicting CK2 beta-dependent substrates using linear patterns.Biochemistry and biophysics reports · 2015Article
- Kinase-interacting substrate screening is a novel method to identify kinase substrates.The Journal of cell biology · 2015Article
- A prismatic view of protein phosphorylation in health and disease.Frontiers in genetics · 2015Article
- Counteracting Protein Kinase Activity in the Heart: The Multiple Roles of Protein Phosphatases.Frontiers in pharmacology · 2015Review
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphate plays a chemically unique role in shaping cellular signaling of all current living systems, especially eukaryotes. Protein phosphorylation has been studied at several levels, from the near-site context, both in sequence and structure, to the crowded cellular environment, and ultimately to the systems-level perspective. Despite the tremendous advances in mass spectrometry and efforts dedicated to the development of ad hoc highly sophisticated methods, phosphorylation site inference and associated kinase identification are still unresolved problems in kinome biology. The sequence and structure of the substrate near-site context are not sufficient alone to model the in vivo phosphorylation rules, and they should be integrated with orthogonal information in all possible applications. Here we provide an overview of the different contexts that contribute to protein phosphorylation, discussing their potential impact in phosphorylation site annotation and in predicting kinase-substrate specificity.
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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.