Opinion: Searching for the elusive targets of farnesyltransferase inhibitors (Q75312802)

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17 November 2019

review article

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title

Opinion: Searching for the elusive targets of farnesyltransferase inhibitors (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:14737124%20AND%20SRC:MED&resulttype=core&format=json

17 November 2019

author name string

Saïd M Sebti

series ordinal

1

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:14737124%20AND%20SRC:MED&resulttype=core&format=json

17 November 2019

Channing J Der

series ordinal

2

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:14737124%20AND%20SRC:MED&resulttype=core&format=json

17 November 2019

publication date

1 December 2003

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17 November 2019

published in

Nature Reviews Cancer

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17 November 2019

volume

3

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17 November 2019

issue

12

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17 November 2019

page(s)

945-951

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Understanding Ras: 'it ain't over 'til it's over'.

17 November 2019

cites work

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K- and N-Ras are geranylgeranylated in cells treated with farnesyl protein transferase inhibitors

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Direct demonstration of geranylgeranylation and farnesylation of Ki-Ras in vivo

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Effect of farnesyltransferase inhibitor FTI-276 on established lung adenomas from A/J mice induced by 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone

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Farnesyltransferase inhibitors are potent lung cancer chemopreventive agents in A/J mice with a dominant-negative p53 and/or heterozygous deletion of Ink4a/Arf

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The geranylgeranyltransferase-I inhibitor GGTI-298 arrests human tumor cells in G0/G1 and induces p21(WAF1/CIP1/SDI1) in a p53-independent manner

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Farnesyl transferase inhibitors block the farnesylation of CENP-E and CENP-F and alter the association of CENP-E with the microtubules

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The farnesyltransferase inhibitor, FTI-2153, blocks bipolar spindle formation and chromosome alignment and causes prometaphase accumulation during mitosis of human lung cancer cells.

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The farnesyltransferase inhibitor, FTI-2153, inhibits bipolar spindle formation during mitosis independently of transformation and Ras and p53 mutation status.

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Farnesyltransferase inhibitors induce cytochrome c release and caspase 3 activation preferentially in transformed cells

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The phosphoinositide 3-OH kinase/AKT2 pathway as a critical target for farnesyltransferase inhibitor-induced apoptosis

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Geranylgeranylated RhoB is sufficient to mediate tissue-specific suppression of Akt kinase activity by farnesyltransferase inhibitors

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Selective inhibition of ras-dependent transformation by a farnesyltransferase inhibitor

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Benzodiazepine peptidomimetics: potent inhibitors of Ras farnesylation in animal cells

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High affinity for farnesyltransferase and alternative prenylation contribute individually to K-Ras4B resistance to farnesyltransferase inhibitors

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Four human ras homologs differ in their abilities to activate Raf-1, induce transformation, and stimulate cell motility

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CAAX geranylgeranyl transferase transfers farnesyl as efficiently as geranylgeranyl to RhoB

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Farnesyltransferase inhibitors alter the prenylation and growth-stimulating function of RhoB

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RhoB alteration is necessary for apoptotic and antineoplastic responses to farnesyltransferase inhibitors

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Both farnesylated and geranylgeranylated RhoB inhibit malignant transformation and suppress human tumor growth in nude mice

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RhoB prenylation is driven by the three carboxyl-terminal amino acids of the protein: evidenced in vivo by an anti-farnesyl cysteine antibody

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The expression of rho proteins decreases with human brain tumor progression: potential tumor markers

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Rho GTPases in human breast tumours: expression and mutation analyses and correlation with clinical parameters

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A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of ras proteins.

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Specific isoprenoid modification is required for function of normal, but not oncogenic, Ras protein

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RhoA prenylation is required for promotion of cell growth and transformation and cytoskeleton organization but not for induction of serum response element transcription.

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Rheb binds tuberous sclerosis complex 2 (TSC2) and promotes S6 kinase activation in a rapamycin- and farnesylation-dependent manner

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Rheb is a direct target of the tuberous sclerosis tumour suppressor proteins

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Failure to farnesylate Rheb protein contributes to the enrichment of G0/G1 phase cells in the Schizosaccharomyces pombe farnesyltransferase mutant

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Drosophila Rheb GTPase is required for cell cycle progression and cell growth

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