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1 yltransferases, farnesyltransferase (FT) and geranylgeranyltransferase-1 (GGT), in the pathogenesis o
4 (D44N) that, when geranylgeranylated by Rab:geranylgeranyltransferase (GGTase II) in cell-free syste
5 nase (MAPK), and preserves the processing of geranylgeranyltransferase (GGTase) I and GGTase II prote
6 (VSMCs), insulin stimulated the activity of geranylgeranyltransferase (GGTase) I and increased the a
7 hibitors for farnesyltransferase (FTase) and geranylgeranyltransferase (GGTase) I as well as combinat
13 Treatment of H-Ras transgenic mice with the geranylgeranyltransferase I (GGTase I) inhibitor GGTI-21
14 f oncogenic K-Ras4B is more sensitive to the geranylgeranyltransferase I (GGTase I) inhibitor GGTI-28
15 in action on farnesyltransferase (FTase) and geranylgeranyltransferase I (GGTase I) using Chinese ham
16 erase (FTase), while modification by protein geranylgeranyltransferase I (GGTase I) was not detected.
20 tein farnesyltransferase (FTase) and protein geranylgeranyltransferase I (GGTase-I), enzymes involved
21 nt and selective peptidomimetic inhibitor of geranylgeranyltransferase I (GGTI), GGTI-2418, and its m
22 omoted the phosphorylation and activation of geranylgeranyltransferase I (GGTI-I), increased the amou
23 Both can be prenylated by either protein geranylgeranyltransferase I (PGGT-I) or protein farnesyl
24 tif permits this protein to be prenylated by geranylgeranyltransferase I but not II both in cell-free
27 he activity of FTase, but not of the related geranylgeranyltransferase I enzyme, in peripheral blood
29 e have now examined the effect of insulin on geranylgeranyltransferase I in MCF-7 breast cancer cells
30 ransformed NIH3T3 cells both FTI-276 and the geranylgeranyltransferase I inhibitor GGTI-297 are requi
33 ibitor of prenyltransferases, but not by the geranylgeranyltransferase I inhibitor, GGTI-298, or the
34 ly, we have designed farnesyltransferase and geranylgeranyltransferase I inhibitors (FTI-277 and GGTI
37 ts farnesyltransferase inhibitors (FTIs) and geranylgeranyltransferase I inhibitors (GGTIs) upregulat
38 t known whether both farnesyltransferase and geranylgeranyltransferase I inhibitors are required for
39 nt with tipifarnib suppressed FTase (but not geranylgeranyltransferase I) in bone marrow and peripher
42 tein farnesyltransferase (FTase) and protein geranylgeranyltransferase-I (GGTase-I) catalyze the pren
44 we demonstrate that in human tumor cells the geranylgeranyltransferase-I (GGTase-I) inhibitor GGTI-29
50 mily of peptidomimetic inhibitors of protein geranylgeranyltransferase-I (PGGTase-I) are reported.
51 geranylgeranylation by the specific protein geranylgeranyltransferase-I inhibitor, GGTI-298, blocked
52 ween protein farnesyltransferase and protein geranylgeranyltransferase-I. plp mutants also have alter
53 ned the effect of insulin on the activity of geranylgeranyltransferase II (GGTase II) in 3T3-L1 fibro
54 ch delivers Rab to catalytic subunits of Rab geranylgeranyltransferase II, are clustered on one face
55 All nascent Rab proteins are prenylated by geranylgeranyltransferase II, which recognizes the Rab s
60 induced by inhibitors of HMG-CoA reductase, geranylgeranyltransferase, or RhoA kinase was blocked by
61 n farnesyltransferase (PFTase) and a protein geranylgeranyltransferase (PGGTase-I) alkylate cysteines
63 Here, we describe a novel and conserved Rab geranylgeranyltransferase (RabGGT)-alpha-like subunit th
64 ranylgeranyltransferase I (GGTase-I) and Rab geranylgeranyltransferase (RabGGTase) catalyze these mod
65 ab GTPases regulating vesicle traffic by Rab geranylgeranyltransferase (RabGGTase) requires a complex
67 witched to that of a closely related enzyme, geranylgeranyltransferase type I (GGTase I) by a single
68 tein farnesyltransferase (FTase) and protein geranylgeranyltransferase type I (GGTase I) catalyze the
69 tein farnesyltransferase (FTase) and protein geranylgeranyltransferase type I (GGTase I) catalyze the
72 n) by protein farnesyltransferase (FTase) or geranylgeranyltransferase type I (GGTase-I) is essential
82 sis, protein farnesyltransferase and protein geranylgeranyltransferase type I are not required for vi
85 otein farnesyltransferase (FTase) or protein geranylgeranyltransferase type I or II (GGTase-I and GGT
89 ranslational modification of Rab proteins by geranylgeranyltransferase type II requires that they fir
90 tein farnesyltransferase (FTase) and protein geranylgeranyltransferase type II, which require both Zn
91 otein farnesyltransferase (FTase) or protein geranylgeranyltransferase type-I (GGTase-I) for proper f
97 ltransferase (FNTA), which is also shared by geranylgeranyltransferase, was isolated as a specific cy
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