Results 11 to 20 of about 574,104 (383)
Cell Research, 2016 Protein ubiquitination is a dynamic multifaceted post-translational modification involved in nearly all aspects of eukaryotic biology. Once attached to a substrate, the 76-amino acid protein ubiquitin is subjected to further modifications, creating a multitude of distinct signals with distinct cellular outcomes, referred to as the 'ubiquitin code ...
Kirby N Swatek, David Komander
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International Journal of Molecular Sciences, 2018 Ever since the discovery of ubiquitin in 1975[...]
N. Nakamura
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An expanded lexicon for the ubiquitin code
Nature reviews. Molecular cell biology, 2022 Recent studies have expanded our understanding of the mechanisms and functions of ubiquitylation. Pathogens rewrite ubiquitylation to promote infection through unconventional ubiquitylation involving lipids and sugars, and structural studies have ...
I. Dikič, B. Schulman
semanticscholar +1 more source
Ubiquitin signalling in neurodegeneration: mechanisms and therapeutic opportunities
Cell Death and Differentiation, 2021 Neurodegenerative diseases are characterised by progressive damage to the nervous system including the selective loss of vulnerable populations of neurons leading to motor symptoms and cognitive decline.
Marlene Schmidt +3 more
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Ubiquitin Interacting Motifs: Duality Between Structured and Disordered Motifs
Frontiers in Molecular Biosciences, 2021 Ubiquitin is a small protein at the heart of many cellular processes, and several different protein domains are known to recognize and bind ubiquitin. A common motif for interaction with ubiquitin is the Ubiquitin Interacting Motif (UIM), characterized ...
Matteo Lambrughi +10 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.
Ivan Dikic +7 more
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To Ubiquitinate or Not to Ubiquitinate: TRIM17 in Cell Life and Death [PDF]
Cells, 2021 TRIM17 is a member of the TRIM family, a large class of RING-containing E3 ubiquitin-ligases. It is expressed at low levels in adult tissues, except in testis and in some brain regions. However, it can be highly induced in stress conditions which makes it a putative stress sensor required for the triggering of key cellular responses.
Meenakshi Basu-Shrivastava +3 more
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Ubiquitylation in immune disorders and cancer: from molecular mechanisms to therapeutic implications [PDF]
, 2012 Conjugation of ubiquitin to proteins (ubiquitylation) has emerged to be one of the most crucial post-translational modifications controlling virtually all cellular processes.
Fulda, Simone +2 more
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Risk1, a Phosphatidylinositol 3-Kinase Effector, Promotes
mBio, 2020 To establish a habitable intracellular niche, various pathogenic bacteria secrete effectors that target intracellular trafficking and modulate phosphoinositide (PI) metabolism.
Oliver H. Voss +6 more
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E3 ubiquitin ligases: styles, structures and functions
Molecular Biomedicine, 2021 E3 ubiquitin ligases are a large family of enzymes that join in a three-enzyme ubiquitination cascade together with ubiquitin activating enzyme E1 and ubiquitin conjugating enzyme E2.
Quan Yang +3 more
semanticscholar +1 more source