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Palmitoylation of Gephyrin Controls Receptor Clustering and Plasticity of GABAergic Synapses [1] In molecular biology, palmitoylation is the covalent attachment of fatty acids, such as palmitic acid, to cysteine (S-palmitoylation) and less frequently to serine and threonine (O-palmitoylation) residues of proteins, which are typically membrane ...
The protein palmitoylation is a reversible process. ... "Palmitoyl acyltransferase assays and inhibitors (Review)". Molecular Membrane Biology. 26 (1): 5 ...
In palmitoleoylation, a palmitoleoyl group (derived from palmitoleic acid, pictured above) is added.. Palmitoleoylation is type of protein lipidation where the monounsaturated fatty acid palmitoleic acid is covalently attached to serine or threonine residues of proteins.
RU-SKI 43 inhibits the activity of SHHat, an enzyme that catalyzes the palmitoylation of Shh. [56] Since palmitoylation is essential for the activity of Shh, [57] inhibition of SHHat by RU-SKI 43 inhibits Shh signaling in cancer cells. [58] [59] 5E1, a monoclonal antibody against Shh, has been shown to inhibit medulloblastoma growth in mouse ...
An example in which palmitoylation of a protein plays a role in cell signaling pathways is in the clustering of proteins in the synapse. When the postsynaptic density protein 95 (PSD-95) is palmitoylated, it is restricted to the membrane and allows it to bind to and cluster ion channels in the postsynaptic membrane. Thus, palmitoylation can ...
Some members of the family such as ZDHHC3 and ZDHHC7 enhance palmitoylation of proteins such as PSD-95, SNAP-25, GAP43, Gαs. Others such as ZDHHC9 showed specificity only toward the H-Ras protein. [3] However, a recent study questions the involvement of classical enzyme-substrate recognition and specificity in the palmitoylation reaction. [4]
Ras, from "Rat sarcoma virus", is a family of related proteins that are expressed in all animal cell lineages and organs. All Ras protein family members belong to a class of protein called small GTPase, and are involved in transmitting signals within cells (cellular signal transduction).
Meng's work at Berkeley has suggested that thioredoxin h9 is associated with the plasma membrane and is capable of moving from cell to cell through two important protein post-translation modifications: myristoylation and palmitoylation. [2] She is the first to connect thioredoxin with the plasma membrane.