Ubiquitin in a sentence

This compact globular beta-grasp fold is found in ubiquitin, UBLs, and proteins that comprise a ubiquitin-like domain, e.g. the S. cerevisiae spindle pole body duplication protein, Dsk2, and NER protein, Rad23, both contain N-terminal ubiquitin domains.

This is then transferred to E1's active-site cysteine residue in concert with the adenylylation of a second ubiquitin. citation This adenylylated ubiquitin is then transferred to a cysteine of a second enzyme, ubiquitin-conjugating enzyme (E2).

However, sometimes the proteasome breaks down proteins without the help of ubiquitin tags, leading researchers to suspect that there was another, ubiquitin-independent mechanism of protein degradation.

Following addition of a single ubiquitin moiety to a protein substrate, further ubiquitin molecules can be added to the first, yielding a polyubiquitin chain.

In the last step, a member of a highly diverse class of enzymes known as ubiquitin ligases (E3) recognizes the specific protein to be ubiquitinated and catalyzes the transfer of ubiquitin from E2 to this target protein.

K63 chains have also been well-characterised, whereas the function of other lysine chains, mixed chains, branched chains, M1-linked linear chains, and heterologous chains (mixtures of ubiquitin and other ubiquitin-like proteins) remains more unclear.

Once a protein is tagged with a single ubiquitin molecule, this is a signal to other ligases to attach additional ubiquitin molecules.

Poly-ubiquitination occurs when the C-terminus of another ubiquitin, will be linked to one of the seven lysine residues or the first methionine on the previously added ubiquitin molecule itself (for example on K48, K29 or M1), forming a chain.

Proteins can specifically bind to ubiquitin via ubiquitin-binding domains (UBDs).

The E1 binds both ATP and ubiquitin and catalyses the acyl-adenylation of the C-terminus of the ubiquitin molecule.

The protein modifications can be either a single ubiquitin protein (monoubiquitination) or a chain of ubiquitin (polyubiquitination).

These chains are made by linking the glycine residue of a ubiquitin molecule to a lysine of ubiquitin bound to a substrate.

The UBDs exploit this by having small spacers between ubiquitin-interacting motifs that bind lysine 48-linked chains (compact ubiquitin chains) and larger spacers for lysine 63-linked chains.

They can cleave both isopeptide (between ubiquitin and lysine) and peptide bonds (between ubiquitin and the N-terminus ).

This fold is called "ubiquitin fold" or sometimes called ubiquitin fold.

UBLs are structurally similar to ubiquitin and are processed, activated, conjugated, and released from conjugates by enzymatic steps that are similar to the corresponding mechanisms for ubiquitin.

UFMylation is an enigmatic QC pathway based on a protein post-translational modification that resembles ubiquitin and its functions are still being deciphered.

Ubiquitin—so named because it is found in virtually all types of cells—serves as a flag to mark proteins for degradation in a cellular garbage disposal called the proteasome.

This occurs when ubiquitin molecules mark old, defective, and toxic proteins for destruction by the cell’s protein-disposal unit, known as the 26S proteasome.

Soon after a brain injury, two biomarkers -- Ubiquitin Carboxy-terminal Hydrolase-L1 and Glial Fibrillary Acidic Protein -- are detected in the blood.