Protein farnesylation and disease

@article{Novelli2011ProteinFA,
  title={Protein farnesylation and disease},
  author={Giuseppe Novelli and Maria Rosaria D'Apice},
  journal={Journal of Inherited Metabolic Disease},
  year={2011},
  volume={35},
  pages={917-926}
}
Prenylation consists of the addition of an isoprenoid group to a cysteine residue located near the carboxyl terminal of a protein. This enzymatic posttranslational modification is important for the maturation and processing of proteins. Both processes are necessary to mediate protein-protein and membrane-protein associations, in addition to regulating the localisation and function of proteins. The severe phenotype of animals deficient in enzymes involved in both prenylation and maturation… 
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45 Citations
Highly Influential Citations
1
Background Citations
17
Methods Citations
1

45 Citations

Production of Farnesylated and Methylated Proteins in an Engineered Insect Cell System.
TLDR
Protocols for extending work to produce authentically modified KRAS protein to other farnesylated and methylated substrates are described.
A New Schema to Identify S-farnesyl Cysteine Prenylation Sites with Substrate Motifs
TLDR
With a rapidly increasing number of experimentally verified S-farnesyl cysteine sites, there is still a lack of methods proposed for the prediction of S-methine prenylation sites, but this work is motivated in proposed new method for identifying S- farnesy cysteined prenolation sites.
Metabolic Stress Induces Caspase-3 Mediated Degradation and Inactivation of Farnesyl and Geranylgeranyl Transferase Activities in Pancreatic β-Cells
TLDR
These findings provide the first evidence to suggest that metabolic stress induced dysfunction of the islet β-cell may, in part, be due to defective protein prenylation signaling pathway.
Increased RhoA Prenylation in the loechrig (loe) Mutant Leads to Progressive Neurodegeneration
TLDR
It is shown that the loe mutation interferes with isoprenoid synthesis, leading to increased prenylation of the small GTPase Rho1, the fly orthologue of vertebrate RhoA, supporting findings in vertebrates that preNylation may play a role in neurodegenerative diseases like Alzheimer’s Disease.
Characterization of the Heavy-Metal-Associated Isoprenylated Plant Protein (HIPP) Gene Family from Triticeae Species
TLDR
It is proved that HIPP1-V positively regulates Cd tolerance in common wheat and genome-wide overview of the Triticeae HIPP genes is provided.
Innovative Target Therapies Are Able to Block the Inflammation Associated with Dysfunction of the Cholesterol Biosynthesis Pathway
TLDR
In this review, inhibitors of cholesterol synthesis, mitochondria-targeted drugs and inhibitors of the inflammasome are focused on.
Sterols and oxysterols in immune cell function
TLDR
This work reviews recent literature reporting on the biological functions of sterol intermediates and oxysterols, acting through transcription factors such as the liver X receptors, sterol regulatory element–binding proteins and the G protein–coupled receptor EBI2, in regulating the differentiation and population expansion of cells of the innate and adaptive immune systems.
Protein Farnesylation on Nasopharyngeal Carcinoma, Molecular Background and Its Potential as a Therapeutic Target
TLDR
An overview of the molecular pathogenesis of NPC in terms of the process of farnesylation is provided and the potential of anti-farnesylation therapy in the treatment of NPC is discussed.
Prenylation: From bacteria to eukaryotes
TLDR
The bioinformatics analyses suggest the possibility of prenylation for a number of Francisella genus proteins, and the current state of the knowledge about the preNylation of eukaryotic and prokaryotic proteins and prenolation inhibitors is described.
Isolation and characterisation of cDNA encoding a wheat heavy metal-associated isoprenylated protein involved in stress responses.
TLDR
Data indicate that TaHIPP1 is an important component in defence signalling pathways and may play a crucial role in the defence response of wheat to biotic and certain abiotic stresses.
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