18 articles for thisTarget
The following articles (labelled with PubMed ID or TBD) are for your review
PMID
Data
Article Title
Organization
Design, synthesis, and structure-activity relationships of tetrahydroquinoline-based farnesyltransferase inhibitors.

Bristol-Myers Squibb Pharmaceutical Research Institute
Modeling of binding modes and inhibition mechanism of some natural ligands of farnesyl transferase using molecular docking.

University of Milan
Successful virtual screening of a chemical database for farnesyltransferase inhibitor leads.

Mayo Medical School and Mayo Clinic
Structure-activity relationships of cysteine-lacking pentapeptide derivatives that inhibit ras farnesyltransferase.

Warner-Lambert
Ras farnesyltransferase: a new therapeutic target.

Warner-Lambert
Phenolic replacements for cysteine in farnesyl transferase inhibitors based on CVFM

TBA
Constrained analogs of KCVFM with improved inhibitory properties against farnesyl transferase

TBA
Stereochemistry of the benzodiazepine based Ras farnesyltransferase inhibitors

TBA
Peptide based P21
RAS farnesyl transferase inhibitors: systematic modification of the tetrapeptide CA
1A
2X motif

TBA
Evaluation of amino acid-based linkers in potent macrocyclic inhibitors of farnesyl-protein transferase.

Merck Research Laboratories
Diaryl ether inhibitors of farnesyl-protein transferase.

Merck Research Laboratories
Discovery of a series of cyclohexylethylamine-containing protein farnesyltransferase inhibitors exhibiting potent cellular activity.

Abbott Laboratories
Solid-phase synthesis of novel inhibitors of farnesyl transferase.

Institute of Cancer Research
A new class of highly potent farnesyl diphosphate-competitive inhibitors of farnesyltransferase.

Tsukuba Research Institute
C-terminal modifications of histidyl-N-benzylglycinamides to give improved inhibition of Ras farnesyltransferase, cellular activity, and anticancer activity in mice.

Warner-Lambert
Novel benzimidazole phosphonates as potential inhibitors of protein prenylation.

University of Iowa
2-substituted piperazines as constrained amino acids. Application to the synthesis of potent, non carboxylic acid inhibitors of farnesyltransferase.

Merck Research Laboratories
Interrogating the Roles of Post-Translational Modifications of Non-Histone Proteins.

Temple University