Results 161 to 170 of about 6,054 (206)

Protein farnesylation and disease

Journal of Inherited Metabolic Disease, 2012
AbstractPrenylation 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 ...
NOVELLI, GIUSEPPE, D'APICE, MARIA ROSARIA   +1 more
openaire   +4 more sources

Farnesyl Diphosphate-Based Inhibitors of Ras Farnesyl Protein Transferase

Journal of Medicinal Chemistry, 1995
The rational design, synthesis, and biological activity of farnesyl diphosphate (FPP)-based inhibitors of the enzyme Ras farnesyl protein transferase (FPT) is described. Compound 3, wherein a beta-carboxylic phosphonic acid type pyrophosphate (PP) surrogate is connected to the hydrophobic farnesyl group by an amide linker, was found to be a potent (I50(
D V, Patel, R J, Schmidt, S A, Biller, E M, Gordon, S S, Robinson, V, Manne   +5 more
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Photoaffinity Analogues of Farnesyl Pyrophosphate Transferable by Protein Farnesyl Transferase

Journal of the American Chemical Society, 2002
Farnesylation is a posttranslational lipid modification in which a 15-carbon farnesyl isoprenoid is linked via a thioether bond to specific cysteine residues of proteins in a reaction catalyzed by protein farnesyltransferase (FTase). We synthesized analogues (3-6) of farnesyl pyrophosphate (FPP) to probe the range of modifications possible to the FPP ...
Kareem A H, Chehade, Katarzyna, Kiegiel, Richard J, Isaacs, Jennifer S, Pickett, Katherine E, Bowers, Carol A, Fierke, Douglas A, Andres, H Peter, Spielmann   +7 more
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Stereochemistry‐dependent inhibition of RAS farnesylation by farnesyl phosphonic acids

Lipids, 1998
AbstractThis investigation compares the effects of three farnesyl pyrophosphate analogs on selected aspects of isoprenoid metabolism. E,E‐α‐Hydroxyfarnesylphosphonate was prepared by an improved variation on a literature synthesis, which also gave access to the new Z,E‐α‐hydroxyfarnesyl‐ and α‐hydroxygeranylphosphonates.
R J, Hohl, K A, Lewis, D M, Cermak, D F, Wiemer   +3 more
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Characterization of Farnesyl Diphosphate Farnesyl Transferase 1 ( FDFT1 ) Expression In Cancer

Personalized Medicine, 2018
To help characterize the FDFT1 gene and protein expression in cancer. Cholesterol represents an important structural component of lipid rafts. These specializations can be involved in pathways stimulating cell growth, survival and other processes active in cancer.
Tüzmen, Şükrü, Hostetter, Galen, Watanabe, Aprill, Ekmekçi, Cumhur, Carrigan, Patricia E., Shechter, Ishaiahu, Kallioniemi, Olli, Miller, Laurence J., Mousses, Spyro   +8 more
openaire   +5 more sources

Phosphonate and bisphosphonate analogues of farnesyl pyrophosphate as potential inhibitors of farnesyl protein transferase

Bioorganic & Medicinal Chemistry, 1998
Several phosphonate and bisphosphonate analogues of farnesyl pyrophosphate have been prepared for an examination of their ability to inhibit farnesyl protein transferase (FPTase). A Horner-Wadsworth-Emmons condensation of farnesal or geranial with tetraethyl methylenediphosphonate gave the desired vinyl phosphonates, while alkylation of the dimethyl ...
S A, Holstein, D M, Cermak, D F, Wiemer, K, Lewis, R J, Hohl   +4 more
openaire   +2 more sources

Activation of TRPA1 by Farnesyl Thiosalicylic Acid

Molecular Pharmacology, 2008
The nonselective cation channel TRPA1 (ANKTM1, p120) is a potential mediator of pain, and selective pharmacological modulation of this channel may be analgesic. Although several TRPA1 activators exist, these tend to be either reactive or of low potency and/or selectivity.
Maher, Michael, Ao, Hong, Banke, Tue, Nasser, Nadia, Wu, Nyan-Tsz, Breitenbucher, J Guy, Chaplan, Sandra R, Wickenden, Alan D   +7 more
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Inhibition of farnesyl protein transferase by new farnesyl phosphonate derivatives of phenylalanine

Bioorganic & Medicinal Chemistry Letters, 1996
Abstract New farnesyl phosphonate derivatives of phenylalanine have been prepared as inhibitors of farnesyl-protein transferase (FPT). Enzyme inhibition studies with bovine brain FPT and rat liver squalene synthase show that compound 3a is a new, potent and selective FPT inhibitor.
M. Lamothe, D. Perrin, D. Blotières, M. Leborgne, S. Gras, D. Bonnet, B.T. Hill, S. Halazy   +7 more
openaire   +1 more source

Expression cloning of farnesylated proteins

2001
Publisher Summary The identification of novel prenylated proteins has most often involved the labeling of cultured cells with [3H] mevalonolactone that is enzymatically converted to [3H] farnesyl pyrophosphate (FPP) and [3H] geranylgeranyl pyrophosphate (GGPP) prior to being incorporated into protein.
openaire   +2 more sources

Protein farnesylation negatively regulates brassinosteroid signaling via reducing BES1 stability in Arabidopsis thaliana

Journal of Integrative Plant Biology, 2021
Hongyong Shi, Jia Li
exaly