• Archives of Pharmacal Research
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• v.28 no.2
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• pp.169-171
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• 2005

The methanolic extract of the aerial parts of Persicaria thunbergii was found to show inhibitory activity on Farnesyl Protein Transferase (FPTase). Bioassay-guided fractionation of the methanolic extract resulted in the isolation of isorhamnetin, as an inhibitor on FPTase. This compound inhibited FPTase activity in a dose-dependent manner, and the $IC_{50}$ value of isorhamnetin was $37.5\;{\mu}M$.

• Archives of Pharmacal Research
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• v.29 no.1
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• pp.64-66
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• 2006

The methanolic extract of the aerial parts of Centipeda minima was found to show inhibitory activity on farnesyl protein transferase (FPTase). Bioassay-guided fractionation of the methanolic extract resulted in the isolation of 6-O-angeloylprenolin, as an inhibitor on FPTase. This compound inhibited FPTase activity in a dose-dependent manner, and the $IC_{50}$ value of 6-O-angeloylprenolin was 18.8 ${\mu}M$.

• Natural Product Sciences
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• v.13 no.4
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• pp.328-331
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• 2007

The methanolic extract of the roots of Lithospermum erythrorhizon (Boraginaceae) was found to show inhibitory activity towards farnesyl protein transferase (FPTase). Bioassay-guided fractionation of the methanolic extract resulted in the isolation of three naphthoquinone compounds, as inhibitors of FPTase. These compounds inhibited the FPTase activity in a dose-dependent manner.

• Korean Journal of Pharmacognosy
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• v.42 no.3
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• pp.218-222
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• 2011

The purpose of this research is to study of inhibitory activity of protostane type triterpens against farnesyl-protein transferase (FPTase). The ingredients of Alismatis Rhizoma, alisol B 23-acetate, C 23-acetate, alisols B and A 24-acetate, and thirteen synthetic analogues from alisol B 23-acetate exhibited inhibition activity against FPTase by scintillation proximity assay method. As a result, alisol C 23-acetate, one of the constituents of Alismatis Rhizoma, the synthetic analogues carboxylated and hydroxylated on branch chain of protostane exhibited a significant inhibitory activity. However, the compounds significantly lowered the inhibitory activity, when there is no 3 position keto on protostane skeletone.

• Proceedings of the PSK Conference
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• 2003.04a
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• pp.265.2-265.2
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• 2003

Diarylheptanoids [curcumin (1), demethoxycurcumin (2), bisdemethoxycurcumin (3), bisdimethoxymethylcurcumin (4), and 1,2-dihydrobis(de-O-methyl)curcumin (5)] were isolated from the methanolic extract of Curcuma longa L. and A new cyclic diarylheptanoiid (6) and a known compound 7 were isolated from fruits of Alnus japonica S. Diarylheptanoids (1-3) inhibited farnesyl protein transferase (FTPase) with an IC50 of 29-50 $\mu\textrm{m}$. (omitted)

• Journal of Life Science
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• v.20 no.2
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• pp.202-207
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• 2010

Ras genes are responsible for up to 30% of human tumor mutations and are composed of three isoforms: H-Ras, K-Ras and N-Ras. The post-translational modification of the CAAX motif of the Ras protein is essential in Ras actions. In the present study, we studied the effects of novel farnesyl transferase inhibitors (FTIs), YH3938 and YH3945, on the actions of oncogenic mutants of H-Ras, K-Ras and N-Ras. YH3938 and YH3945 completely reverted the proliferation and morphology of oncogenic H-Ras-transformed Rat2 cells, but not of oncogenic K-Ras-transformed Rat2 cells. Oncogenic N-Ras-transformed Rat2 cells were slightly affected. Activation of SRE promoters by oncogenic H-Ras and N-Ras, but not by K-Ras, were inhibited by treatment with YH3938 and YH3945. Using bandshift analysis, YH3938 suppressed the processing of oncogenic H-Ras and N-Ras, but not that of oncogenic K-Ras protein. YH3945 only inhibited the processing of H-Ras. From these results, we conclude that YH3938 and YH3945 specifically inhibit actions of oncogenic H-Ras through inhibition of its farnesylation, that YH3938 also inhibits N-Ras activity in a dose-dependent manner, and that these drugs have no effect on oncogenic K-Ras activity.

• Applied Biological Chemistry
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• v.43 no.2
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• pp.95-99
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• 2000

A series of hetero ring (X) substitued chalcone derivatives with farnesyl protein transferase (FPTase) inhibition activities $(pI_{50})$ values determined in vitro is analyzed by modified Free-Wilson (F-W) and Hansch method for quantitative structure activity relationship (QSARs). On the basis of F-W analysis on the FPTase inhibitory activity of a training set of the compounds, none of the (X)-substituents were not contribute the activity. But the net charge of ${\alpha}$ carbon atom is contribute the activity than that of ${\beta}$ carbon atom. And the relative orders of the (Y)-substituents on the activity are ortho>meta>para-substituents. According to Hansch approach, the activities would depend largely on the optimal, $(R_{opt.}=-0.35)$ resonance effect with ortho substituted $(I_o>0)$ electron donating group (R<0) and STERIMOL parameter, $B_1$ constant. The inhibition activity between hetro ring substituents have been a proportioned with each others and none substituent(H), 45 showed the highest FPTase inhibition $(pI_{50}=4.30)$ activity.

• BMB Reports
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• v.28 no.3
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• pp.197-203
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• 1995

Famesyl protein transferase involved in the first step of post-translational modification of $p21^{ras}$ proteins transfers the famesyl moiety from famesyl pyrophosphate to a cysteine residue in $p21^{ras}$ proteins. The enzyme was first purified 30,000-fold from bovine testis by use of 30~50% ammonium sulfate fractionation, DEAE-Sephacel ion exchange chromatography, Sephacryl S-300 gel filtration chromatography, Sephacryl S-200 gel filtration chromatography, and hexapeptide (Lys-Lys-Cys-Val-Ile-Met) affinity chromatography. The molecular weight of the purified enzyme was estimated to be ~100 kDa by gel filtration and SDS-polyacrylamide gels showed two closely spaced bands of ~50 kDa protein. These indicate that the enzyme consists of two nonidentical subunits, a and 13, which have slightly different molecular weights. The enzyme was inhibited by hexapeptide (Lys-Lys-Cys-Val-Ile-Met), which acted as an alternative substrate that competed for famesylation. Kinetic analysis by measuring initial velocities showed that famesyl protein transferase is a very slow enzyme. EDTA-treated famesyl protein transferase showed little activity with $Mg^{2+}$ or $Zn^{2+}$ alone, but required both $Mg^{2+}$ and $Zn^{2+}$ for the catalytic activity.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1995.04a
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• pp.63-63
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• 1995

Farnesyl Protein Transferase (FPTase) catalyses a post-translational modification of Ras that is obligatory for the cell transforming activity of this oncogene protein. The screening of natural products to identify inhibitors of this enzyme as a potential anticancer agents, has led to the isolation of a novel lactone, from the hydroid Solanderia secunda. Solandelactone G has been isolated from the hydroid Solanderia secunda collected along the offshore of Jaejudo and Keomunde. The structure of the compound has been determined as cyclopropane containing C$\_$22/ fatty acid lactone on the basis of the combined spectral and chemical methods

• Proceedings of the Zoological Society Korea Conference
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• 1998.10b
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• pp.304.1-304
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• 1998

No Abstract, See Full Text