Results 41 to 50 of about 519,123 (352)
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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Solo or in Concert: SUMOylation in Pathogenic Fungi [PDF]
The Plant Pathology JournalSUMOylation plays a pivotal role in DNA replication and repair, transcriptional stability, and stress response. Although SUMOylation is a conserved post-translational modification (PTM) in eukaryotes, the number, type, and function of SUMOylation ...
You-Jin Lim, Yong-Hwan Lee
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Dss1 is a 26S proteasome ubiquitin receptor [PDF]
, 2014 The ubiquitin-proteasome system is the major pathway for protein degradation in eukaryotic cells. Proteins to be degraded are conjugated to ubiquitin chains that act as recognition signals for the 26S proteasome.
Arrigoni +35 more
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International Journal of Molecular Sciences, 2018 Ever since the discovery of ubiquitin in 1975[...]
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Phenotypic Characterization of the Arabidopsis ufm1 (Ubiquitin Fold Modifier) Gene Involved in Seed Development [PDF]
, 2016 Background and Objective: With the completion of the Arabidopsis genome sequencing, the next challenge is the determination ofgene function. Post-translational modifications of proteins by small polypeptide are implicated in plant growth and development ...
Cornejo, Paula +1 more
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Ubiquitin and Ubiquitin-Like Proteins in Protein Regulation [PDF]
Circulation Research, 2007 The discovery of the ubiquitin system was awarded with the Nobel Prize in Chemistry in 2004. Labeling of intracellular proteins for degradation by a multienzymatic complex, called the proteasome, was identified as the main function of this system. Subsequently, it was discovered that the attachment of ubiquitin to proteins can modify their function ...
Joerg, Herrmann +2 more
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Ubiquitin and ubiquitin-like conjugation systems in trypanosomatids
Current Opinion in Microbiology, 2022 In eukaryotic cells, reversible attachment of ubiquitin and ubiquitin-like modifiers (Ubls) to specific target proteins is conducted by multicomponent systems whose collective actions control protein fate and cell behaviour in precise but complex ways.
Rebecca J, Burge +2 more
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Frontiers in Cardiovascular Medicine, 2022 Ubiquitin carboxyl-terminal hydrolase L1 (UCHL1) is a deubiquitinase known to play essential roles in the nervous tissue. Myocardial upregulation of UCHL1 was observed in human dilated cardiomyopathy and several animal models of heart disease, but the ...
Penglong Wu +9 more
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Detection of sequential polyubiquitylation on a millisecond timescale [PDF]
, 2009 The pathway by which ubiquitin chains are generated on substrate through a cascade of enzymes consisting of an E1, E2 and E3 remains unclear. Multiple distinct models involving chain assembly on E2 or substrate have been proposed.
Deshaies, Raymond J. +3 more
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A Ubiquitin-like Protein Unleashes Ubiquitin Ligases [PDF]
Cell, 2008 Modification of cullin-RING ubiquitin ligases by the ubiquitin-like molecule Nedd8 promotes substrate ubiquitination. A crystal structure of a cullin modified by Nedd8 recently reported in Cell (Duda et al., 2008) and a biochemical study in Molecular Cell (Saha and Deshaies, 2008) reveal the dramatic impact on the ligase machinery by conjugation of ...
Saifee, Nabiha Huq, Zheng, Ning
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