Results 71 to 80 of about 27,627 (205)
Ubiquitylation in ERAD: reversing to go forward? [PDF]
PLoS Biology, 2011 Proteins are co-translationally inserted into the endoplasmic reticulum (ER) where they undergo maturation. Homeostasis in the ER requires a highly sensitive and selective means of quality control.
Yien Che Tsai, Allan M Weissman
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Optimal enzyme rhythms in cells [PDF]
arXiv, 2016 Cells can use periodic enzyme activities to adapt to periodic environments or existing internal rhythms and to establish metabolic cycles that schedule biochemical processes in time. A periodically changing allocation of the protein budget between reactions or pathways may increase the overall metabolic efficiency.
arxiv
Enzyme localization can drastically affect signal amplification in signal transduction pathways [PDF]
, 2007 Push-pull networks are ubiquitous in signal transduction pathways in both prokaryotic and eukaryotic cells. They allow cells to strongly amplify signals via the mechanism of zero-order ultrasensitivity. In a push-pull network, two antagonistic enzymes control the activity of a protein by covalent modification.
arxiv +1 more source
On the reproducibility of enzyme reactions and kinetic modelling [PDF]
arXiv, 2021 Enzyme reactions are highly dependent on reaction conditions. To ensure reproducibility of enzyme reaction parameters, experiments need to be carefully designed and kinetic modelling meticulously executed. Furthermore, to enable the judgement of the quality of enzyme reaction parameters, the experimental conditions, the modelling process as well as the
arxiv
Deciphering the substrate specificity of ubiquitin conjugating enzymes
, 2014 Presentation of my 3rd rotation project on the Wellcome Trust PhD programme. Work supervised by Prof. Ronald T. Hay (Gene Regulation and Expression, College of Life Sciences, University of Dundee).
Madeira, Fábio, Hay, Ronald T.
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A Ubiquitin-Conjugating Enzyme Is Essential for Developmental Transitions inDictyostelium [PDF]
Molecular Biology of the Cell, 1997 We have identified a developmentally essential gene,UbcB, by insertional mutagenesis. The encoded protein (UBC1) shows very high amino acid sequence identity to ubiquitin-conjugating enzymes from other organisms, suggesting that UBC1 is involved in protein ubiquitination and possibly degradation during Dictyostelium development.
Anson Nomura +3 more
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Covalent protein modification with ISG15 via a conserved cysteine in the hinge region. [PDF]
PLoS ONE, 2012 The ubiquitin-like protein ISG15 (interferon-stimulated gene of 15 kDa) is strongly induced by type I interferons and displays antiviral activity. As other ubiquitin-like proteins (Ubls), ISG15 is post-translationally conjugated to substrate proteins by ...
Veronika N Bade +3 more
doaj +1 more source
A human ubiquitin-conjugating enzyme homologous to yeast UBC8.
Journal of Biological Chemistry, 1994 Ubiquitin-conjugating enzymes catalyze the covalent attachment of ubiquitin to cellular substrates. Here we describe the isolation of a novel ubiquitin-conjugating enzyme from human placenta and the cloning of the corresponding cDNA. DNA sequencing revealed that this gene, UbcH2, encodes a protein with significant sequence similarity to yeast UBC8.
Peter K. Kaiser +8 more
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Cell Reports, 2019 Summary: Ubiquitin and ubiquitin-like chains are finely balanced by conjugating and de-conjugating enzymes. Alterations in this balance trigger the response to stress conditions and are often observed in pathologies.
Aymeric P. Bailly +8 more
doaj
Robust cullin-RING ligase function is established by a multiplicity of poly-ubiquitylation pathways
eLife, 2019 The cullin-RING ligases (CRLs) form the major family of E3 ubiquitin ligases. The prototypic CRLs in yeast, called SCF enzymes, employ a single E2 enzyme, Cdc34, to build poly-ubiquitin chains required for degradation. In contrast, six different human E2
Spencer Hill +15 more
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