Identification of Ubiquitin Genes and Their Expression Patterns in Pinus massoniana Under Infection Stress from the Pinewood Nematode [PDF]
PlantsUbiquitins (Ubs) play a crucial role in plant–pathogen interactions, particularly the RPL40 family, which is essential for protein synthesis. While Pinus massoniana is highly susceptible to pine wilt disease (PWD) caused by Bursaphelenchus xylophilus ...
Qingyang Chen +7 more
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Ubiquitination and deubiquitination as critical modulators of NSCLC tumorigenesis and drug resistance [PDF]
Discover OncologyUbiquitination and deubiquitination are biological mechanisms that including the addition and removal ubiquitin molecules from proteins, which are associated with NSCLC.
Prasanna Srinivasan Ramalingam +12 more
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Multiple UBX proteins reduce the ubiquitin threshold of the mammalian p97-UFD1-NPL4 unfoldase
eLife, 2022 The p97/Cdc48 ATPase and its ubiquitin receptors Ufd1-Npl4 are essential to unfold ubiquitylated proteins in many areas of eukaryotic cell biology.
Ryo Fujisawa +2 more
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To Be or Not to Be...Ubiquitinated? [PDF]
Cell Cycle, 2004 Levels of p21, a cyclin-dependent kinase (CDK) inhibitor, are controlled in part at the post-translational level by protein degradation. Although the signaling pathways leading to p21 degradation have not yet been fully elucidated, it is evident that p21 ubiquitination is an essential factor in its degradation.
Joanna, Bloom, Michele, Pagano
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Neutron-encoded diubiquitins to profile linkage selectivity of deubiquitinating enzymes
Nature Communications, 2023 Most insights into deubiquitinase (DUB) substrate specificity originate from studies with isolated di-ubiquitins (diUb), but in cells diUbs with different linkage types coexist.
Bianca D. M. van Tol +13 more
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Ubiquitylation functions in the calcium carbonate biomineralization in the extracellular matrix. [PDF]
PLoS ONE, 2012 Mollusks shell formation is mediated by matrix proteins and many of these proteins have been identified and characterized. However, the mechanisms of protein control remain unknown.
Dong Fang +8 more
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Cracking the Ubiquitin Code: The Ubiquitin Toolbox [PDF]
Current Issues in Molecular Biology, 2019 Ubiquitination, a post-translational modification, regulates a vast array of fundamental biological processes with dysregulation of the dedicated enzymes giving rise to pathologies such as cancer and neurodegenerative diseases. Assembly and its ensuing removal of this post-translational modification, determining a large variety of biological functions,
Mulder, M.P.C., Witting, K.F., Ovaa, H.
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Role of the deubiquitylating enzyme DmUsp5 in coupling ubiquitin equilibrium to development and apoptosis in Drosophila melanogaster. [PDF]
PLoS ONE, 2015 Protein ubiquitylation is a dynamic process that affects the function and stability of proteins and controls essential cellular processes ranging from cell proliferation to cell death. This process is regulated through the balanced action of E3 ubiquitin
Levente Kovács +5 more
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Phosphoribosylation of Ubiquitin Promotes Serine Ubiquitination and Impairs Conventional Ubiquitination [PDF]
Cell, 2016 Conventional ubiquitination involves the ATP-dependent formation of amide bonds between the ubiquitin C terminus and primary amines in substrate proteins. Recently, SdeA, an effector protein of pathogenic Legionella pneumophila, was shown to mediate NAD-dependent and ATP-independent ubiquitin transfer to host proteins.
Bhogaraju, S. +6 more
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Nature Communications, 2023 Post-translational modification of proteins with polyubiquitin chains is a critical cellular signaling mechanism in eukaryotes with implications in various cellular states and processes.
Betsegaw Lemma +7 more
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