Any process that modulates the frequency, rate or extent of cyclase activity.

The formation from simpler components of a deoxyribonucleoside diphosphate, a glycosamine consisting of a base linked to a deoxyribose sugar esterified with diphosphate on its glycose moiety.

Any process that modulates the frequency, rate or extent of the chemical reactions involving RNA.

The series of events by which a mechanical stimulus is received and converted into a molecular signal.

Any process that stops, prevents or reduces the rate of the chemical reactions involving RNA.

spermidine catabolism to deoxyhypusine, using deoxyhypusine synthase

The breakdown of spermidine to form deoxyhypusine by the enzyme [eIF-5A]-deoxyhypusine synthase. The reaction occurs in four steps: 1. spermidine + NAD+ = dehydrospermidine + NADH + H+; 2. dehydrospermidine + [enzyme]-lysine = 1,3-diaminopropane + [enzyme]-lysine-N6=CH(CH2)3NH2; 3. [enzyme]-lysine-N6=CH(CH2)3NH2 = [eIF-5A]-lysine-N6=CH(CH2)3NH2; 4. [eIF-5A]-lysine-N6=CH(CH2)3NH2 + NADH + H+ = [eIF-5A]-deoxyhypusine + NAD+.

The process of creating protein polymers, compounds composed of a large number of component monomers; polymeric proteins may be made up of different or identical monomers. Polymerization occurs by the addition of extra monomers to an existing poly- or oligomeric protein.

A heteromeric complex of flotillin 1, flotillin 2, caveolin 1 and caveolin 2 within the caveolar membrane.

The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of component monomers; protein oligomers may be composed of different or identical monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.

Interacting selectively with a tetratricopeptide repeat (TPR) domain of a protein, the consensus sequence of which is defined by a pattern of small and large hydrophobic amino acids and a structure composed of helices.

A series of molecular signals within the cell that are mediated by a member of the Rac family of proteins switching to a GTP-bound active state.