Sentence examples for multiple ubiquitin molecules from inspiring English sources

After several cycles of ubiquitination, multiple ubiquitin molecules are attached to the substrate which is then quickly recognized and subsequently degraded by the 26S proteasome.

Ubiquitination is a posttranslational modification in which single or multiple ubiquitin molecules are attached to a protein.

UPS-dependent proteolysis requires the attachment of multiple ubiquitin molecules to a target protein, which results in the subsequent degradation of the polyubiquitinated target protein through the 26S proteasome complex (Fig. 1a 3,1a 31a 3,1a 3

Protein ubiquitination involves the concerted action of the E1 ubiquitin-activating enzyme, an E2 ubiquitin-conjugating enzyme and an E3 ubiquitin-protein ligase, the last of which delivers multiple ubiquitin molecules to the target protein [9] [11].

Proteins are marked for removal by the covalent attachment of multiple ubiquitin molecules and are subsequently degraded by the 26S proteasome or the lysosome (Ciechanover 1994; Ciechanover 1998).

The UPS pathway includes two key steps: covalent attachment of multiple ubiquitin molecules to the protein substrate and degradation of the ubiquitylated protein by the 26S proteasome complex.

Upon further inspection, the Survivin stability assay suggested that ubiquitinated Survivin in the nucleus could lead to possible increase in sizes due to multiple conjugations of ubiquitin molecules.

Proteins are degraded by the ubiquitin proteasome pathway via two distinct steps: the covalent attachment of multiple monomers of ubiquitin molecules to a protein substrate and degradation of the tagged protein by the 26S proteasome [ 8, 9].

Among the cases of poly-ubiquitination, conjugation with a few ubiquitin molecules is called oligo-ubiquitination. Ubiquitination is sequentially achieved by the cooperation of three enzymes: ubiquitin activating enzyme (E1), ubiquitin conjugating enzyme (E2), and ubiquitin ligase (E3).

Adaptor proteins, which contain ubiquitin binding domains (UBD) such as the ubiquitin-interacting motif (UIM) can recognise the ubiquitin molecules on the ubiquitinated EGFR.

Conjugation with one ubiquitin molecule and with tandem repeated ubiquitin molecules is defined as mono- and poly-ubiquitination, respectively.