コーパス検索結果 (１語後でソート)
通し番号をクリックするとPubMedの該当ページを表示します
1 Tipifarnib is an inhibitor of human protein farnesyltransferase.
2 to determine the structure of the Zn site in protein farnesyltransferase.
3 of partially purified Plasmodium falciparum protein farnesyltransferase.
4 tide substrates in the crystal structures of protein farnesyltransferase.
5 distinct specificity compared with mammalian protein farnesyltransferase.
6 Cys, which are good substrates for mammalian protein farnesyltransferase.
7 the CVIM tetrapeptide substrate of mammalian protein farnesyltransferase, a series of imidazole-conta
8 tipifarnib analogues that no longer bind to protein farnesyltransferase and display increased potenc
11 ALA encodes the alpha-subunit shared between protein farnesyltransferase and protein geranylgeranyltr
12 B farnesylation in vitro can be catalyzed by protein farnesyltransferase and that the peptidomimetic
14 eping sickness (Trypanosoma brucei), and the protein farnesyltransferase appears to be a good target
17 vestigate the thiol substrate specificity of protein farnesyltransferase by demonstrating that a vari
18 he detailed catalytic mechanism of mammalian protein farnesyltransferase by measuring the effect of m
25 ribe the molecular identification of a plant protein farnesyltransferase (FTase) and evidence for its
28 carried out by a pair of cytosolic enzymes, protein farnesyltransferase (FTase) and protein geranylg
29 cognition motif for two prenylation enzymes, protein farnesyltransferase (FTase) and protein geranylg
30 carried out by the CaaX prenyltransferases, protein farnesyltransferase (FTase) and protein geranylg
34 identified as very potent dual inhibitors of protein farnesyltransferase (FTase) and protein geranylg
38 h for new cancer therapeutics has identified protein farnesyltransferase (FTase) as a promising drug
51 study, the developmental expression of a pea protein farnesyltransferase (FTase) gene was examined us
52 he Cys-Val-Ile-Met tetrapeptide substrate of protein farnesyltransferase (FTase) have been designed a
58 noid lipid (a process termed prenylation) by protein farnesyltransferase (FTase) or geranylgeranyltra
59 ear the C terminus of a substrate protein by protein farnesyltransferase (FTase) or protein geranylge
60 attachment of an isoprenoid lipid by either protein farnesyltransferase (FTase) or protein geranylge
61 the covalent attachment of a lipid group by protein farnesyltransferase (FTase) or protein geranylge
65 tors of the potential anticancer drug target protein farnesyltransferase (FTase), but these compounds
67 ent substrate (apparent Km = 0.8 microM) for protein farnesyltransferase (FTase), while modification
73 have proven to be both potent inhibitors of protein-farnesyltransferase (FTase) and valuable probes
75 ubnanomolar concentrations and are devoid of protein farnesyltransferase inhibition were discovered.
77 These phenotypes can be ameliorated with a protein farnesyltransferase inhibitor (FTI), suggesting
78 gle-arm clinical trial demonstrated that the protein farnesyltransferase inhibitor lonafarnib amelior
83 ber transferase, the effects of two types of protein farnesyltransferase inhibitors, several chaetome
84 potentially relevant to the long-term use of protein farnesyltransferase inhibitors, which lead to an
85 eld a sequence that is a known substrate for protein farnesyltransferase; irradiation of the NDBF-cag
87 soma cruzi, and Leishmania mexicana and that protein farnesyltransferase (PFT) activity can be detect
88 ein geranylgeranyltransferase-I (PGGT-I) and protein farnesyltransferase (PFT) attach geranylgeranyl
91 Here, we report a new class of antimalarial protein farnesyltransferase (PFT) inhibitors, designed w
93 ERA1 gene, which encodes the beta-subunit of protein farnesyltransferase (PFT), exhibit pleiotropic e
94 Tipifarnib (R115777), an inhibitor of human protein farnesyltransferase (PFT), is shown to be a high
99 otential off-target inhibition of the enzyme protein farnesyltransferase (PFTase) by commercially ava
102 exploited the high specificity of the enzyme protein farnesyltransferase (PFTase) to site-specificall
106 recombinant proteins have a C-terminal CVIX protein farnesyltransferase recognition motif that allow
107 Efficient product formation catalyzed by protein farnesyltransferase requires an enzyme-bound zin
108 ed the alpha- and beta-subunits of T. brucei protein farnesyltransferase (TB-PFT) using nucleic acid
112 n a screening effort against the drug target protein farnesyltransferase, we identified a series of d
WebLSDに未収録の専門用語（用法）は "新規対訳" から投稿できます。