ubiquitin

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u·biq·ui·tin

 (yo͞o-bĭk′wĭ-tĭn)
n.
A small protein found in all eukaryotic cells that attaches to other proteins, thereby regulating their activity or location or marking them for degradation.

ubiquitin

(juːˈbɪkwɪtɪn)
n
(Biochemistry) biochem a small polypeptide, found in most eukaryotic cells, that combines with other proteins to make them susceptible to degradation
[C20: from ubiquitous + -in]
uˌbiquitiˈnation n
References in periodicals archive ?
Ubiquitins are essentially molecular tags that are found everywhere in the cell.
On the other hand, ubiquitins have a subtle trick up their sleeves - they can tag other tags.
NF-kB activity increases when TRAF3 has the homing targets, called ubiquitins, attached to it and is destroyed by the proteasome, a complex of proteins that hunts down ubiquitin-decorated proteins.
When TRAF3 evades attack, it turns that same destructive mechanism against NIK, a protein that is central to NF-kB activity, by tagging it with ubiquitins.
SMD simulations (17) qualitatively reproduced the differences between these mechanical unfolding patterns and additionally showed, that the major unfolding barrier of extension by force for both C-to-N linked and C-to-Lys 48 linked ubiquitin was formed by the rupture of hydrogen bonds between specific [beta]-strands: two parallel [beta]-strands (I and V) in C-to-N linked ubiquitin and two antiparallel [beta]-strands (III and V) in C-to-Lys 48 linked ubiquitins.
The researchers showed that KEAP1, short for the tongue-twisting Kelch-like ECH-associated protein 1, binds to IKKB and attaches molecules known as ubiquitins to the oncoprotein, which targets it for dissolution by the cell's proteasome complex.
Ubiquitins are small regulatory proteins that attach to other target proteins allowing their destruction and recycling.
By attaching a string of targeting proteins known as ubiquitins to the phosphorylated tumor suppressor, MDM2 marks it for destruction by the ubiquitin-proteasome degradation pathway.
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