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| http://dx.doi.org/10.1038/leu.2013.347 | DOI Listing |
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Rapid Microwave Fixation of the Brain Reveals Seasonal Changes in the Phosphoproteome of Hibernating Thirteen-Lined Ground Squirrels.
ACS Chem Neurosci
January 2025
Department of Chemistry, University of Nebraska-Lincoln, Lincoln, Nebraska 68588, United States.
Hibernating mammals such as the thirteen-lined ground squirrel () experience significant reductions in oxidative metabolism and body temperature when entering a state known as torpor. Animals entering or exiting torpor do not experience permanent loss of brain function or other injuries, and the processes that enable such neuroprotection are not well understood. To gain insight into changes in protein function that occur in the dramatically different physiological states of hibernation, we performed quantitative phosphoproteomics experiments on thirteen-lined ground squirrels that are summer-active, winter-torpid, and spring-active.
View Article and Find Full Text PDFEmpirical Comparison and Analysis of Artificial Intelligence-Based Methods for Identifying Phosphorylation Sites of SARS-CoV-2 Infection.
Int J Mol Sci
December 2024
Center for Informational Biology, School of Life Science and Technology, University of Electronic Science and Technology of China, Chengdu 611731, China.
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a member of the large coronavirus family with high infectivity and pathogenicity and is the primary pathogen causing the global pandemic of coronavirus disease 2019 (COVID-19). Phosphorylation is a major type of protein post-translational modification that plays an essential role in the process of SARS-CoV-2-host interactions. The precise identification of phosphorylation sites in host cells infected with SARS-CoV-2 will be of great importance to investigate potential antiviral responses and mechanisms and exploit novel targets for therapeutic development.
View Article and Find Full Text PDFIn-Depth Analysis of Tissue Phosphoproteomics with TiO Enrichment and Fractionation with High-pH Reversed-Phase Chromatography.
Methods Mol Biol
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Laboratory of Proteomics, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
Protein phosphorylation is an important post-translational modification that regulates almost all cellular processes, such as cellular metabolism, growth, differentiation, signal transduction, and gene regulation. Mass spectrometry, which acts as an automated and sensitive method, enables global analysis of protein phosphorylation. However, several technical challenges need to be addressed when analyzing protein phosphorylation in a global manner.
View Article and Find Full Text PDFAdvancements in Global Phosphoproteomics Profiling: Overcoming Challenges in Sensitivity and Quantification.
Proteomics
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Institute of Chemistry, Academia Sinica, Taipei, Taiwan.
Protein phosphorylation introduces post-genomic diversity to proteins, which plays a crucial role in various cellular activities. Elucidation of system-wide signaling cascades requires high-performance tools for precise identification and quantification of dynamics of site-specific phosphorylation events. Recent advances in phosphoproteomic technologies have enabled the comprehensive mapping of the dynamic phosphoproteomic landscape, which has opened new avenues for exploring cell type-specific functional networks underlying cellular functions and clinical phenotypes.
View Article and Find Full Text PDFLongitudinal phosphoproteomics reveals the PI3K-PAK1 axis as a potential target for recurrent colorectal liver metastases.
Cell Rep
December 2024
Laboratory of Proteomics for Drug Discovery, Center for Drug Design Research, National Institute of Biomedical Innovation, Health and Nutrition, Osaka 567-0085, Japan; Laboratory of Proteomics and Drug Discovery, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan. Electronic address:
The resistance of colorectal cancer liver metastases (CRLMs) to 5-fluorouracil (5-FU) chemotherapy remains a significant global health challenge. We investigated the phosphoproteomic dynamics of serial tissue sections obtained from initial metastases and recurrent tumors collected from 24 patients to address this unmet need for innovative therapeutic strategies for patients with CRLM with a poor prognosis. Our analysis revealed the activation of PAK kinase in patients with CRLM with a poor prognosis.
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