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Namespace Prefixes

PrefixIRI
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n11http://linked.opendata.cz/resource/drugbank/drug/DB04960/identifier/chemspider/
n7http://bio2rdf.org/drugbank:
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n4http://linked.opendata.cz/resource/drugbank/property/
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Statements

Subject Item
n2:DB04960
rdf:type
n3:Drug
n3:description
R115777 is a substance that is being studied in the treatment of acute myeloid leukemia (AML) and other types of cancer. It belongs to the family of drugs called farnesyltransferase inhibitors. It is also called tipifarnib and Zarnestra.
n3:generalReferences
# Martin LA, Head JE, Pancholi S, Salter J, Quinn E, Detre S, Kaye S, Howes A, Dowsett M, Johnston SR: The farnesyltransferase inhibitor R115777 (tipifarnib) in combination with tamoxifen acts synergistically to inhibit MCF-7 breast cancer cell proliferation and cell cycle progression in vitro and in vivo. Mol Cancer Ther. 2007 Sep;6(9):2458-67. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17876043 # Wang CC, Liao YP, Mischel PS, Iwamoto KS, Cacalano NA, McBride WH: HDJ-2 as a target for radiosensitization of glioblastoma multiforme cells by the farnesyltransferase inhibitor R115777 and the role of the p53/p21 pathway. Cancer Res. 2006 Jul 1;66(13):6756-62. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/16818651
n3:group
investigational
n3:indication
Investigated for use/treatment in colorectal cancer, leukemia (myeloid), pancreatic cancer, and solid tumors.
owl:sameAs
n7:DB04960
dcterms:title
R115777
adms:identifier
n9:159324 n10:10253567 n11:140122 n12:DB04960
n3:mechanismOfAction
The farnesyltransferase inhibitors (FTIs) are a class of experimental cancer drugs that target protein farnesyltransferase with the downstream effect of preventing the proper functioning of the Ras protein, which is commonly abnormally active in cancer. After translation, RAS goes through four steps of modification: isoprenylation, proteolysis, methylation and palmitoylation. Isoprenylation involves the enzyme farnesyltransferase (FTase) transferring a farnesyl group from farnesyl pyrophosphate (FPP) to the pre-RAS protein. Also, a related enzyme geranylgeranyltransferase I (GGTase I) has the ability to transfer a geranylgeranyl group to K and N-RAS. Farnesyl is necessary to attach RAS to the cell membrane. Without attachment to the cell membrane, RAS is not able to transfer signals from membrane receptors (Reuter et al., 2000).
n3:synonym
Tipifarnib
n3:IUPAC-Name
n4:271B6146-363D-11E5-9242-09173F13E4C5
n3:InChI
n4:271B614C-363D-11E5-9242-09173F13E4C5
n3:Molecular-Formula
n4:271B614B-363D-11E5-9242-09173F13E4C5
n3:Molecular-Weight
n4:271B6148-363D-11E5-9242-09173F13E4C5
n3:Monoisotopic-Weight
n4:271B6149-363D-11E5-9242-09173F13E4C5
n3:SMILES
n4:271B614A-363D-11E5-9242-09173F13E4C5
n3:Water-Solubility
n4:271B6144-363D-11E5-9242-09173F13E4C5
n3:logP
n4:271B6142-363D-11E5-9242-09173F13E4C5 n4:271B6145-363D-11E5-9242-09173F13E4C5
n3:logS
n4:271B6143-363D-11E5-9242-09173F13E4C5
n3:H-Bond-Acceptor-Count
n4:271B6152-363D-11E5-9242-09173F13E4C5
n3:H-Bond-Donor-Count
n4:271B6153-363D-11E5-9242-09173F13E4C5
n3:InChIKey
n4:271B614D-363D-11E5-9242-09173F13E4C5
n3:Polar-Surface-Area--PSA-
n4:271B614E-363D-11E5-9242-09173F13E4C5
n3:Polarizability
n4:271B6150-363D-11E5-9242-09173F13E4C5
n3:Refractivity
n4:271B614F-363D-11E5-9242-09173F13E4C5
n3:Rotatable-Bond-Count
n4:271B6151-363D-11E5-9242-09173F13E4C5
n3:affectedOrganism
Humans and other mammals
n3:casRegistryNumber
192185-68-5
n3:category
n3:Bioavailability
n4:271B6157-363D-11E5-9242-09173F13E4C5
n3:Ghose-Filter
n4:271B6159-363D-11E5-9242-09173F13E4C5
n3:MDDR-Like-Rule
n4:271B615A-363D-11E5-9242-09173F13E4C5
n3:Number-of-Rings
n4:271B6156-363D-11E5-9242-09173F13E4C5
n3:Physiological-Charge
n4:271B6155-363D-11E5-9242-09173F13E4C5
n3:Rule-of-Five
n4:271B6158-363D-11E5-9242-09173F13E4C5
n3:Traditional-IUPAC-Name
n4:271B6147-363D-11E5-9242-09173F13E4C5
n3:pKa--strongest-basic-
n4:271B6154-363D-11E5-9242-09173F13E4C5