Results 101 to 110 of about 540 (119)
Journal of Proteomics, 2022 The removal of (poly)ubiquitin chains at the proteasome is a key step in the protein degradation pathway that determines which proteins are degraded and ultimately decides cell fate. Three different deubiquitinating enzymes (DUBs) are associated to the human proteasome, PSMD14 (RPN11), USP14 and UCH37 (UCHL5).
Karel Bezstarosti, Jeroen A A Demmers
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Proteomic approaches to study ubiquitinomics
Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms, 2023As originally described some 40 years ago, protein ubiquitination was thought to serve primarily as a static mark for protein degradation. In the ensuing years, it has become clear that 'ubiquitination' is a structurally diverse and dynamic post-translational modification and is intricately involved in a myriad of signaling pathways in all eukaryote ...
Indrajit, Sahu +3 more
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Global Analysis of Host and Bacterial Ubiquitinome in Response to Salmonella Typhimurium Infection [PDF]
Molecular Cell, 2016 Ubiquitination serves as a critical signal in the host immune response to infection. Many pathogens have evolved strategies to exploit the ubiquitin (Ub) system to promote their own survival through a complex interplay between host defense machinery and bacterial virulence factors.
Evgenij Fiskin +2 more
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The global proteome and ubiquitinome of bacterial and viral co-infected bronchial epithelial cells
Journal of Proteomics, 2022 Viral infections facilitate bacterial trafficking to the lower respiratory tract resulting in bacterial-viral co-infections. Bacterial dissemination to the lower respiratory tract is enhanced by influenza A virus induced epithelial cell damage and dysregulation of immune responses.
Thomas Sura +2 more
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Molecular and Cellular Proteomics, 2019 Huntington's disease is caused by a polyglutamine repeat expansion in the huntingtin protein which affects the function and folding of the protein, and results in intracellular protein aggregates. Here, we examined whether this mutation leads to altered ubiquitination of huntingtin and other proteins in both soluble and insoluble fractions of brain ...
Karen A Sap +2 more
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Experimental Gerontology, 2006
Ubiquitination of endogenous proteins is one of the key regulatory steps of protein degradation followed by regulation of proteasome activity. During the last years evidence has increased that proteasome activity is decreased during the aging process in various model systems and that these changes might be causally related to aging and aging associated
Johannes Grillari +2 more
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Ubiquitination of endogenous proteins is one of the key regulatory steps of protein degradation followed by regulation of proteasome activity. During the last years evidence has increased that proteasome activity is decreased during the aging process in various model systems and that these changes might be causally related to aging and aging associated
Johannes Grillari +2 more
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Journal of Proteome Research, 2023
Phosphoproteomics and ubiquitinomics data-independent acquisition (DIA) mass spectrometry (MS) data is typically analyzed by using a data-dependent acquisition (DDA) spectral library. The performance of various library-free strategies for analyzing phosphoproteomics and ubiquitinomics DIA MS data has not been evaluated. In this study, we systematically
Chengwen Wen +10 more
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Phosphoproteomics and ubiquitinomics data-independent acquisition (DIA) mass spectrometry (MS) data is typically analyzed by using a data-dependent acquisition (DDA) spectral library. The performance of various library-free strategies for analyzing phosphoproteomics and ubiquitinomics DIA MS data has not been evaluated. In this study, we systematically
Chengwen Wen +10 more
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Hsp90 inhibition induces both protein-specific and global changes in the ubiquitinome
Journal of Proteomics, 2015Inhibition of the essential chaperone Hsp90 with drugs causes a global perturbation of protein folding and the depletion of direct substrates of Hsp90, also called clients. Ubiquitination and proteasomal degradation play a key role in cellular stress responses, but the impact of Hsp90 inhibition on the ubiquitinome has not been characterized on a ...
Quadroni M, Potts A, Waridel P
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Large-Scale Filter-Aided Sample Preparation Method for the Analysis of the Ubiquitinome
Analytical Chemistry, 2017Protein ubiquitination regulates key cellular functions, including protein homeostasis and signal transduction. The digestion of ubiquitinated proteins with trypsin yields a glycine-glycine remnant bound to the modified lysine residue (K-ε-GG) that can be recognized by specific antibodies for immunoaffinity purification (IAP) and subsequent ...
Albert Casanovas +3 more
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Decoding the ubiquitin landscape by cutting-edge ubiquitinomic approaches
Biochemical Society TransactionsFunctional consequences of protein ubiquitination have gone far beyond the degradation regulation as was initially imagined during its discovery 40 years back. The state-of-the-art has revealed the plethora of signaling pathways that are largely regulated by ubiquitination process in eukaryotes.
Brindhavanam P T, Indrajit Sahu
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