Results 1 to 10 of about 276 (130)
Regulation of protein prenylation
Prenyltransferases (PTases) are known to play a role in embryonic development, normal tissue homeostasis and cancer by posttranslationally modifying proteins involved in these processes. They are being discussed as potential drug targets in an increasing number of diseases, ranging from Alzheimer's disease to malaria.
Hagen Bachmann, Dominik Jung
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Protein Prenylation in Plant Stress Responses [PDF]
Protein prenylation is one of the most important posttranslational modifications of proteins. Prenylated proteins play important roles in different developmental processes as well as stress responses in plants as the addition of hydrophobic prenyl chains
Michal Hála, Viktor Žárský
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Biochemistry of protein prenylation.
Covalent modification by isoprenoid lipids (prenylation) is now recognized as a mechanism to promote membrane interactions and biological activities of a variety of cellular proteins. Both the 15-carbon farnesyl and 20-carbon geranylgeranyl isoprenoids are involved in these modifications, which occur on carboxyl-terminal cysteine residues of proteins ...
PJ Casey
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Protein Prenylation in Plants: Mechanisms and Functional Implications
Protein prenylation is a crucial post-translational modification that involves the formation of a covalent bond between isoprenoid lipids and the cysteine residues of specific proteins.
Chang Tian, Quan Wang
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Compromised Protein Prenylation as Pathogenic Mechanism in Mevalonate Kinase Deficiency
Mevalonate kinase deficiency (MKD) is an autoinflammatory metabolic disorder characterized by life-long recurring episodes of fever and inflammation, often without clear cause. MKD is caused by bi-allelic pathogenic variants in the MVK gene, resulting in
Frouwkje A. Politiek, Hans R. Waterham
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Inhibition of protein prenylation by patulin
The antibiotic patulin was found to inhibit protein prenylation in mouse FM3A cells. Thus, the agent reduced incorporation of [3H]mevalonate into proteins by 50% at a concentration of 7 μM. In a cell‐free assay, patulin inhibited rat brain farnesyl:protein transferase, one of the enzymes responsible for protein prenylation.
Keiji Hasumi
exaly +3 more sources
Chloroplastic prenylated proteins [PDF]
By in vivo [3H]mevalonate labelling of spinach combined with biochemical analysis, evidence is provided for the existence of protein prenylation in chloroplasts. Approximately 20 prenylated polypeptides were resolved by SDS‐PAGE followed by autoradiography.
Parmryd, Ingela +4 more
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Single prenyl-binding site on protein prenyl transferases [PDF]
Three distinct protein prenyl transferases, one protein farnesyl transferase (FTase) and two protein geranylgeranyl transferases (GGTase), catalyze prenylation of many cellular proteins. One group of protein substrates contains a C-terminal C AAX motif (C is Cys, A
L, Desnoyers, M C, Seabra
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Specific Disruption of Ras2 CAAX Proteolysis Alters Its Localization and Function
Many CAAX proteins, such as Ras GTPase, undergo a series of posttranslational modifications at their carboxyl terminus (i.e., cysteine prenylation, endoproteolysis of AAX, and carboxylmethylation).
Rajani Ravishankar +6 more
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The prenylated form of the human 2'-5'-oligoadenylate synthetase 1 (OAS1) protein has been shown to potently inhibit the replication of Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2), the virus responsible for the Coronavirus Disease 2019 ...
Spyros Lytras +11 more
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