Results 171 to 180 of about 3,218 (202)
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Bioorganic & Medicinal Chemistry Letters, 2003
Phosphonoacetamido(oxy) groups have proven to be good mimics of the diphosphate portion in geranylgeranyl protein transferase I (GGTase I) inhibitors. The introduction of small alkyl groups (Me, Et) into the diphosphate mimic moiety caused a further decrease in collateral farnesyl protein transferase (FTase) inhibitory activity, thereby improving ...
Filippo, Minutolo +10 more
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Phosphonoacetamido(oxy) groups have proven to be good mimics of the diphosphate portion in geranylgeranyl protein transferase I (GGTase I) inhibitors. The introduction of small alkyl groups (Me, Et) into the diphosphate mimic moiety caused a further decrease in collateral farnesyl protein transferase (FTase) inhibitory activity, thereby improving ...
Filippo, Minutolo +10 more
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A Fluorescence Assay for Geranylgeranyl Transferase Type I
Analytical Biochemistry, 1995A new fluorescence assay for measuring the activity of geranylgeranyl transferase (type I) is described. It does not require the use of either radiolabeled geranylgeranyl diphosphate or the purified recombinant Ras protein substrate with the carboxy terminal sequence of CVLL. Dansyl GCVLL and unlabeled geranylgeranyl diphosphate are used as substrates.
W C, Pickett +5 more
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Digeranyl bisphosphonate inhibits geranylgeranyl pyrophosphate synthase
Biochemical and Biophysical Research Communications, 2007A primary cellular target of the clinical nitrogenous bisphosphonates is the isoprenoid biosynthetic pathway. Specifically these drugs inhibit the enzyme farnesyl pyrophosphate synthase and deplete cells of larger isoprenoids. Inhibition of this enzyme results in impaired processing of both farnesylated and geranylgeranylated proteins.
Andrew J, Wiemer +3 more
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Geranylgeranyl Diphosphate Synthase: An Emerging Therapeutic Target
Clinical Pharmacology & Therapeutics, 2011Proteins modified post-translationally by geranylgeranylation have been implicated in numerous cellular processes related to human disease. In recent years, the study of protein geranylgeranylation has advanced tremendously in both cellular and animal models.
A J, Wiemer, D F, Wiemer, R J, Hohl
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Geranylgeranyl diphosphate synthase genes in entomopathogenic fungi
Applied Microbiology and Biotechnology, 2009Based on comparative amino-acid sequence alignment of geranylgeranyl diphosphate (GGPP) synthase from filamentous fungi, degenerated oligonucleotide primers were designed for searching GGPP synthase gene(s) in entomopathogenic fungi. Polymerase chain reaction with the designed primers amplified GGPP synthase homologues from five representative ...
Suthitar, Singkaravanit +3 more
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Human Geranylgeranyl Diphosphate Synthase is an Octamer in Solution
Journal of Biochemistry, 2007A recombinant geranylgeranyl diphosphate synthase (GGPS) was analysed to be a mixture of octamer, hexamer and dimer by gel filtration using a Superdex 200 column followed by the blue native polyacrylamide gel electrophoresis. The hexamer and dimer were each converted to an octamer by treating with dithiothreitol (DTT).
Yukino, Miyagi +2 more
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Biochemical Society Transactions, 1992
J A, Glomset, M H, Gelb, C C, Farnsworth
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J A, Glomset, M H, Gelb, C C, Farnsworth
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THE EXPRESSION AND PURIFICATION OF GERANYLGERANYLATED KRAS4B
2016Wildtype KRAS4b is post-translationally modified by cells to include a 15-carbon farnesyl lipid and a methyl group at its C-terminus. The modifications function to anchor KRAS4b on the inner leaflet of the plasma membrane where it serves as a molecular switch to regulate cellular signaling pathways.
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[Protein farnesyl and geranylgeranyl transferases].
Comptes rendus des seances de la Societe de biologie et de ses filiales, 1992Posttranslational prenylation of proteins synthesized as soluble precursors enhances their hydrophobicity and enables them to bind biological membranes. These modifications consist in the attachment of a C15 farnesyl or a C20 geranylgeranyl moiety to the cysteine residue(s) of proteins bearing CAAX, CC or CXC C-terminal sequences (where C = cysteine, A
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