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Chemical Biology of Lipidated Proteins
- Source :
- ACS Chemical Biology. 7:87-99
- Publication Year :
- 2012
- Publisher :
- American Chemical Society (ACS), 2012.
-
Abstract
- Many signaling proteins such as the members of the Ras superfamily of GTPases are posttranslationally modified by covalent attachment of lipid groups, which is crucial for the correct localization and function of these proteins. Numerous lipidated proteins are oncogens often found mutated in several human cancers. Therefore, several therapeutic strategies have been developed based on the inhibition of the enzymes involved in these lipidation steps. Here, we will summarize the results on protein lipidation inhibition, mainly focusing on the small molecules targeting the isoprenylation and acylation of proteins.
- Subjects :
- Models, Molecular
Acylation
Lipoproteins
Lipoylation
Chemical biology
Antineoplastic Agents
Lipid-anchored protein
GTPase
Biology
Protein lipidation
Biochemistry
Inhibitory Concentration 50
Prenylation
Transferases
Neoplasms
Humans
Enzyme Inhibitors
General Medicine
Lipid Metabolism
Cell biology
ras Proteins
Molecular Medicine
lipids (amino acids, peptides, and proteins)
Signal transduction
Ras superfamily
Protein Processing, Post-Translational
Function (biology)
Signal Transduction
Subjects
Details
- ISSN :
- 15548937 and 15548929
- Volume :
- 7
- Database :
- OpenAIRE
- Journal :
- ACS Chemical Biology
- Accession number :
- edsair.doi.dedup.....08e74814537e355ea7e036ce9bff6b62