prenylation

Prenylation may increase the potential activity of its original flavonoid.

Prenylation was initially believed to be important only for membrane attachment.

However, another role for prenylation appears to be its importance in protein-protein interactions.

Small molecules can also undergo prenylation, such as in the case of prenylflavonoids.

Defects in protein prenylation can cause pathologies such as choroideremia.

Proteins that undergo prenylation include Ras, which plays a central role in the development of cancer.

There is no known enzyme activity that can carry out the prenylation reaction with the isoprenoid alcohol.

One form of C-terminal modification is prenylation.

The decreased length of the open reading frame results in the loss of 2 prenylation sites and 1 amidation site.

Prenylation is the attachment of lipid chains to proteins to facilitate their interaction with the cell membrane.

The prenylation of these adenines is carried out by tRNA-isopentenyltransferase.

"Refinement and prediction of protein prenylation motifs".

Isoprenoid biosynthesis may be inhibited by fosmidomycin which in turn reduces protein prenylation.

The REPs are essential for the prenylation of Rab proteins.

This suggests that inhibitors of prenylation enzymes (e.g., farnesyltransferase) may influence tumor growth.

This process, called prenylation, causes prenylated proteins to become membrane-associated due to the hydophobic nature of the prenyl group.

The nucleophilic thiol group allows cysteine to conjugate to other groups, e.g., in prenylation.

During prenylation, a farnesyl- or geranylgeranyl-isoprenoid membrane anchor is added to a cysteine residue near the C-terminus.

After 2-succinylbenzoic acid has been produced, a cyclization, a prenylation, a methylation, and an oxidation occur which yields a napthoquinone.

RhoV/Chp depends on palmitoylation rather than prenylation for association with plasma and intracellular membranes.

(See also prenylation.)

However, there is increasing evidence that statins (which inhibit the mevalonate pathway) may be clinically useful because they affect these other molecules (including protein prenylation).

Following these important advances, their team of dedicated researchers elucidated the role of lipid modification of proteins (protein prenylation) in cancer.

Dimethylallyl pyrophosphate is then obtained from the deoxyxylulose pathway, where prenylation of the benzenoid occurs, yielding humulone.

In addition to changes in guanine nucleotide state, the posttranslational prenylation of Rab proteins plays an important role in the cycling mechanism.