posttranslational

Bacteriocins are classified according to their extent of posttranslational modification.

The latter often results from posttranslational modification of proteins.

It also has posttranslational modifications which are similar to those of the plasma-derived molecule.

Finally, the protein can undergo a variety of posttranslational modifications, which are briefly summarized here.

The carbohydrate is attached to the protein in a cotranslational or posttranslational modification.

Some enzymes act on other proteins to add or remove chemical groups in a process known as posttranslational modification.

Sulfation is also a possible posttranslational modification of protein.

CD44 function is controlled by its posttranslational modifications.

This is a reversible process and a major form of posttranslational modification of proteins.

Besides glycosylation, additional posttranslational modifications have been reported for CD36.

Posttranslational modification of proteins with phosphate groups has proven to be a key regulatory step throughout all biological systems.

Phosphoserine is a component of many proteins as the result of posttranslational modifications.

This posttranslational modification is necessary for proper folding and transport of the protein to the plasma membrane.

Further posttranslational modifications have been reported.

The threonine residue is susceptible to numerous posttranslational modifications.

Other posttranslational modifications at lysine residues include acetylation and ubiquitination.

These unusual amino acids are introduced by posttranslational modification of the precursor peptide.

Adenylylation is a posttranslational modification that can occur to molecules such as tyrosine residues.

Peptide autoinducers usually result from posttranslational modification of a larger precursor molecule.

The primary sequence of PrP is 253 amino acids long before posttranslational modification.

MAT regulation generally occurs through phosphorylation and posttranslational modification.

The presence of HMGB1 in the nucleus depends on posttranslational modifications.

Protein phosphorylation in particular plays a significant role in a wide range of cellular processes and is a very important posttranslational modification.

Dermorphin appears to be made in these through an unusual posttranslational modification carried out by an amino acid isomerase.

Release from the autoinhibitory restraints requires posttranslational modifications such as phosphorylation and interacting proteins.