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Ln-M4B3T-DOTA - a new sterically overcrowded LCT for protein pseudocontact shift NMR spectroscopy.
Matt A, Häussinger D.
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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 ...
David Komander, Kirby N Swatek
exaly +3 more sources
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The measurement of ubiquitin and ubiquitinated proteins
Electrophoresis, 1999Ubiquitination of key cellular proteins involved in signal transduction, gene transcription and cell-cycle regulation usually condemns those proteins to proteasomal or lysosomal degradation. Additionally, cycles of reversible ubiquitination regulate the function of certain proteins in a manner analogous to phosphorylation.
E G, Mimnaugh, P, Bonvini, L, Neckers
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Ubiquitin and ubiquitin conjugates in human lens
Experimental Eye Research, 1992Ubiquitin, an 8.5 kDa polypeptide found almost universally in plants and animals, is a normal component in the lens. The best documented function for ubiquitin involves its conjugation to proteins as a signal to initiate degradation. Conjugates for ubiquitin-dependent degradation tend to be of very high molecular mass and are rapidly degraded.
J, Jahngen-Hodge +3 more
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Annual Review of Biochemistry, 1998
The selective degradation of many short-lived proteins in eukaryotic cells is carried out by the ubiquitin system. In this pathway, proteins are targeted for degradation by covalent ligation to ubiquitin, a highly conserved small protein. Ubiquitin-mediated degradation of regulatory proteins plays important roles in the control of numerous processes ...
Aaron Ciechanover, Avram Hershko
exaly +3 more sources
The selective degradation of many short-lived proteins in eukaryotic cells is carried out by the ubiquitin system. In this pathway, proteins are targeted for degradation by covalent ligation to ubiquitin, a highly conserved small protein. Ubiquitin-mediated degradation of regulatory proteins plays important roles in the control of numerous processes ...
Aaron Ciechanover, Avram Hershko
exaly +3 more sources
Annual Review of Biochemistry, 2012
The posttranslational modification with ubiquitin, a process referred to as ubiquitylation, controls almost every process in cells. Ubiquitin can be attached to substrate proteins as a single moiety or in the form of polymeric chains in which successive ubiquitin molecules are connected through specific isopeptide bonds.
David Komander, Michael Rape
exaly +3 more sources
The posttranslational modification with ubiquitin, a process referred to as ubiquitylation, controls almost every process in cells. Ubiquitin can be attached to substrate proteins as a single moiety or in the form of polymeric chains in which successive ubiquitin molecules are connected through specific isopeptide bonds.
David Komander, Michael Rape
exaly +3 more sources

