Results 31 to 40 of about 353,107 (313)
Ubiquitin-dependent and -independent proteasomal protein degradation.
, 2023 A. UPS protein degradation resulting from (1) ubiquitin system targeting followed by (2) proteasomal protein degradation. B. Proteins with ubiquitin-independent degrons are directly bound and degraded by the proteasome without ubiquitin system targeting.
Frank W. Albert (7879037) +2 more
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Cells, 2019 The ubiquitin proteasome system (UPS) plays an important role in regulating numerous cellular processes, and a dysfunctional UPS is thought to contribute to motor neuron disease.
Monique Bax +12 more
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Resolving the Complexity of Ubiquitin Networks
Frontiers in Molecular Biosciences, 2020 Ubiquitination regulates nearly all cellular processes by coordinated activity of ubiquitin writers (E1, E2, and E3 enzymes), erasers (deubiquitinating enzymes) and readers (proteins that recognize ubiquitinated proteins by their ubiquitin-binding ...
Katarzyna Kliza, Koraljka Husnjak
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, 2011 In this chapter, we describe a method for detecting the ubiquitination status of G protein-coupled receptors (GPCRs). This involves co-expression of a GPCR with an epitope-tagged ubiquitin construct in a -heterologous mammalian expression system. Stimulus-dependent modification of the GPCR by -ubiquitin is detected by immunoprecipitation and subsequent
Adriana, Caballero, Adriano, Marchese
openaire +2 more sources
The molecular basis of CRL4 ubiquitin ligase architecture, targeting and regulation [PDF]
, 2013 Members of the CUL4-RBX1-DDB1 (CRL4) E3 ubiquitin ligase family regulate multiple cellular processes including development, transcription, and DNA repair.
Fischer, Eric Sebastian
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Ubiquitin-dependent and independent pathways of mitophagy.
, 2023 (A) Canonical ubiquitin-dependent mitophagy. In basal conditions, the PINK1 serine/threonine protein kinase precursor is targeted to healthy mitochondria thanks to its MTS, allowing its interaction with the TOMM complex and its import from the OMM to the
Jérémy Verbeke (5396666) +2 more
core +1 more source
Cells, 2019 Ubiquitin is a highly conserved small eukaryotic protein. It is generated by proteolytic cleavage of precursor proteins in which it is fused either to itself, constituting a polyubiquitin precursor of head-to-tail monomers, or as a single N-terminal ...
Sara Martín-Villanueva +3 more
doaj +1 more source
Pharmaceuticals, 2021 Background: The mTOR signaling pathway is inactivated by AMPK’s tumor-suppressing function. It is recognized that ubiquitin conjugating enzyme 2O (UBE2O), which directly targets AMPK for ubiquitination and degradation, is intensified in human cancers ...
Jae-Heon Kim +12 more
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Regulation of ubiquitin and ubiquitin‐like modifiers by phosphorylation [PDF]
The FEBS Journal, 2021 The regulatory influence of ubiquitin is vast, encompassing all cellular processes, by virtue of its central roles in protein degradation, membrane trafficking, and cell signaling. But how does ubiquitin, a 76 amino acid peptide, carry out such diverse, complex functions in eukaryotic cells? Part of the answer is rooted in the high degree of complexity
Nathaniel L. Hepowit +4 more
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The fanconi anemia DNA repair pathway is regulated by an interaction between ubiquitin and the E2-like fold domain of FANCL [PDF]
, 2015 The Fanconi Anemia (FA) DNA repair pathway is essential for the recognition and repair of DNA interstrand crosslinks (ICL). Inefficient repair of these ICL can lead to leukemia and bone marrow failure.
Howard, Mark J. +8 more
core +1 more source