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As one of the most common post-translational modifications (PTMs), protein phosphorylation plays an important role in various biological processes, such as signaling transduction, cellular metabolism, differentiation, growth, regulation and apoptosis. Protein phosphorylation is of great value not only in illustrating the underlying molecular mechanisms but also in treatment of diseases and design of new drugs. Recently, there is an increasing interest in automatically extracting phosphorylation information from biomedical literatures. However, it still remains a challenging task due to the tremendous volume of literature and circuitous modes of expression for protein phosphorylation. To address this issue, we propose a novel text-mining method for efficiently retrieving and extracting protein phosphorylation information from literature. By employing natural language processing (NLP) technologies, this method transforms each sentence into dependency parse trees that can precisely reflect the intrinsic relationship of phosphorylation-related key words, from which detailed information of substrates, kinases and phosphorylation sites is extracted based on syntactic patterns. Compared with other existing approaches, the proposed method demonstrates significantly improved performance, suggesting it is a powerful bioinformatics approach to retrieving phosphorylation information from a large amount of literature. A web server for the proposed method is freely available at http://bioinformatics.ustc.edu.cn/pptm/.
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http://dx.doi.org/10.1016/j.ymeth.2014.01.008 | DOI Listing |
Sci China Life Sci
September 2025
State Key Laboratory of Experimental Hematology, The Province and Ministry Co-sponsored Collaborative Innovation Center for Medical Epigenetics, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), Tianjin Medical University Cancer Institute and Hospital, Tianjin Key Labora
Histone arginine methylation by protein arginine methyltransferases (PRMTs) is crucial for transcriptional regulation and is implicated in cancers. Despite their therapeutic potential, some PRMTs present challenges as drug targets due to their context-dependent activities. Here, we demonstrate that hypoxia triggers the rapid condensation of PRMT2, which is essential for its histone H3R8 asymmetric dimethylation (H3R8me2a) activity.
View Article and Find Full Text PDFGeroscience
September 2025
Research Institute of the McGill University Health Centre, 2155 Guy Street, Suite 500, Montreal, QC, H3H 2R9, Canada.
Frailty, often linked to sarcopenia, involves reduced muscle strength and mass. While sarcopenia has multiple causes, impaired muscle protein synthesis may contribute. Leucine and resistance training (RT) are anabolic stimuli, but the long-term effects of leucine combined with RT in pre/frail older women remain unclear.
View Article and Find Full Text PDFBr J Cancer
September 2025
School of Life Science and Technology, Harbin Institute of Technology, Harbin, China.
Background: Activin A/Smad signaling plays an important role in promoting cancer stemness and chemoresistance in pancreatic ductal adenocarcinoma (PDAC), however the precise regulation on the termination of this pathway has not been fully understood.
Methods: LncRNA SLC7A11-AS1 interacting proteins were identified through RNA pull-down followed by LC-MS/MS. The protein interaction was analyzed by co-immunoprecipitation.
Commun Biol
September 2025
Department of Molecular Neurobiology, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.
Neuronal development and function are orchestrated by a plethora of regulatory mechanisms that control the abundance, localization, interactions, and function of proteins. A key role in this regard is assumed by post-translational protein modifications (PTMs). While some PTM types, such as phosphorylation or ubiquitination, have been explored comprehensively, PTMs involving ubiquitin-like modifiers (Ubls) have remained comparably enigmatic (Ubls).
View Article and Find Full Text PDFHandb Exp Pharmacol
September 2025
Department of Medicine, Duke University Medical Center, Durham, NC, USA.
GPCRs are known for their versatile signaling roles at the plasma membrane; however, recent studies have revealed that these receptors also function within various intracellular compartments, such as endosomes, the Golgi apparatus, and the endoplasmic reticulum. This spatially distinct signaling, termed location bias, allows GPCRs to initiate unique signaling cascades and influence cellular processes-including cAMP production, calcium mobilization, and protein phosphorylation-in a compartment-specific manner. By mapping the impact of GPCR signaling from these subcellular locations, this chapter emphasizes the mechanisms underlying signaling from intracellular receptor pools in diversifying receptor functionality.
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