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1                                              GGTase I, but not FTase, is inhibited in breast tumors a
2                                              GGTase-I catalyzes C-terminal lipidation of >100 protein
3                                              GGTase-I deficiency reduced the accumulation of choleste
4                                              GGTase-I discriminates against farnesyl diphosphate (FPP
5 equires both an FTase inhibitor as well as a GGTase I inhibitor, and that inhibition of human tumor g
6 th a specific GGTase II inhibitor, but not a GGTase I inhibitor, consistent with the effect being dep
7           We conclude that insulin activates GGTase I, increases the amounts of geranylgeranylated Rh
8  a selective, highly potent, and cell-active GGTase-I inhibitor, GGTI-DU40.
9 lybasic region does not significantly affect GGTase I-catalyzed reactions, as only minimal changes ar
10 a2X motif binds in the same location for all GGTase-I substrates, the X residue of FTase substrates c
11                                     Although GGTase-I inhibitors (GGTIs) have received less attention
12                  Insulin increased FTase and GGTase I activities and the amounts of prenylated Ras an
13 tely blocked the insulin effect on FTase and GGTase I activities without interfering with insulin sig
14 -stimulated phosphorylation of the FTase and GGTase I alpha-subunit activation of FTase and GGTase I
15 Tase I alpha-subunit activation of FTase and GGTase I and subsequent increases in prenylated Ras and
16                                    FTase and GGTase I differ in both their substrate specificity and
17               Substrate overlap of FTase and GGTase I has not been determined to be biologically sign
18 horylation of the alpha-subunit of FTase and GGTase I in CHO-hIR-WT cells, but was without effect in
19  the results demonstrate that both FTase and GGTase I inhibitors are required for inhibition of K-Ras
20 e prenylation sensitivities to the FTase and GGTase I inhibitors is variable.
21 receptor to the prenyltransferases FTase and GGTase I is mediated by the Shc pathway, but not the IRS
22 B-derived hexapeptides (TKCVIX) to FTase and GGTase I modestly.
23                                    FTase and GGTase I modify several important signaling and regulato
24                     In contrast to FTase and GGTase I, only a handful of RabGGTase inhibitors have be
25 ap1, proteins that are modified by FTase and GGTase I, respectively.
26 nd Cdc42Hs proteins, substrates of FTase and GGTase I, respectively.
27  and TC21, are substrates for both FTase and GGTase I.
28 y to mediate the insulin effect on FTase and GGTase I.
29                                    FTase and GGTase-I (also called the CaaX prenyltransferases) recog
30 adopt a common binding mode in the FTase and GGTase-I active site.
31                           Although FTase and GGTase-I are highly homologous, they are quite selective
32                         Thus, both FTase and GGTase-I are required for the homeostasis of skin kerati
33  have solved crystal structures of FTase and GGTase-I complexed with a total of eight cognate and cro
34                                    FTase and GGTase-I have attracted interest as therapeutic targets
35                                    FTase and GGTase-I have long been proposed to specifically recogni
36                           Although FTase and GGTase-I have very similar active sites, L-778,123 adopt
37 (which encode the beta-subunits of FTase and GGTase-I, respectively) and a keratin 14-Cre transgene t
38 ase:GG pyrophosphate (GGPP), FTase:GGPP, and GGTase-I:GGPP complexes show 1:1 (enzyme:GGPP) stoichiom
39 s position allowed FTase beta to function as GGTase I beta.
40  ability of mutant FTase beta to function as GGTase I beta.
41  to that of geranylgeranylation catalyzed by GGTase I.
42 s were viable despite the lack of detectable GGTase I activity but were morphologically abnormal.
43  conditional allele of the gene that encodes GGTase-I (see the related article beginning on page 1294
44 onditional loss of Rhoa or the gene encoding GGTase-I, Pggt1b, in IECs exhibit spontaneous chronic in
45                            We are evaluating GGTase I as a potential target for antimycotic therapy o
46 ), whereas GGTI-2154 is highly selective for GGTase I (21 nM) over FTase (IC50, 5600 nM).
47 dulated by a protein that is a substrate for GGTase I.
48 ogenesis in vivo and give strong support for GGTase I as a target for anticancer drug discovery.
49 roteins showed that their kcat/Km values for GGTase I substrate are increased about 20-fold compared
50            GGTI-DU40 is highly selective for GGTase-I both in vitro and in living cells.
51 nflammatory cell function are substrates for GGTase-I.
52 neslyltransferase as well as a substrate for GGTases I and II.
53  inhibiting their prenylating enzymes FTase, GGTase I, and RabGGTase.
54 erase (FTase) and geranylgeranyltransferase (GGTase) I as well as combinations of lovastatin with ger
55 the processing of geranylgeranyltransferase (GGTase) I and GGTase II protein substrates.
56 d the activity of geranylgeranyltransferase (GGTase) I and increased the amounts of geranylgeranylate
57 he type I protein geranylgeranyltransferase (GGTase-I), FTase can also geranylgeranylate methionine-
58                                   In humans, GGTase-I and the homologous protein farnesyltransferase
59                 Geranylgeranyltransferase I (GGTase I) catalyzes the transfer of a prenyl group from
60 c mice with the geranylgeranyltransferase I (GGTase I) inhibitor GGTI-2154 results not only in haltin
61 ensitive to the geranylgeranyltransferase I (GGTase I) inhibitor GGTI-286 than it is to FTI-277 in K-
62 ase (FTase) and geranylgeranyltransferase I (GGTase I) using Chinese hamster ovary (CHO) cells that o
63 tion by protein geranylgeranyltransferase I (GGTase I) was not detected.
64 s recognized by geranylgeranyltransferase I (GGTase I).
65 d family member geranylgeranyltransferase I (GGTase I).
66 se) or geranylgeranyl protein transferase I (GGTase I) were used to conjugate FPP and GGPP with fluor
67 zed by protein geranylgeranyl transferase I (GGTase I).
68 r geranylgeranyl-protein transferase type I (GGTase I) (K(i) = 0.06 microM, IC(50) = 20 microM) or sq
69 ed enzyme, geranylgeranyltransferase type I (GGTase I) by a single amino acid change at one of the th
70 nd protein geranylgeranyltransferase type I (GGTase I) catalyze the attachment of a farnesyl or geran
71 nd protein geranylgeranyltransferase type I (GGTase I) catalyze the attachment of lipid groups from f
72    Protein geranylgeranyltransferase type I (GGTase I) catalyzes the attachment of a geranylgeranyl l
73         Protein geranylgeranyltransferase I (GGTase-I) and Rab geranylgeranyltransferase (RabGGTase)
74 se) and protein geranylgeranyltransferase I (GGTase-I), enzymes involved in the prenylation of Ras.
75 se) and protein geranylgeranyltransferase-I (GGTase-I) catalyze the prenylation of proteins with a ca
76         Protein geranylgeranyltransferase-I (GGTase-I) catalyzes the transfer of a 20-carbon isopreno
77 tumor cells the geranylgeranyltransferase-I (GGTase-I) inhibitor GGTI-298 blocked cells in G0/G1, whe
78 nylation enzyme geranylgeranyltransferase-I (GGTase-I).
79 fied by protein geranylgeranyltransferase-I (GGTase-I).
80 nsferase enzyme geranylgeranyltransferase-I (GGTase-I).
81            Geranylgeranyltransferase type I (GGTase-I) inhibitors (GGTIs) have therapeutic potential
82 (FTase) or geranylgeranyltransferase type I (GGTase-I) is essential for the function of many signal t
83 of protein geranylgeranyltransferase type I (GGTase-I) is widely believed to promote membrane associa
84 nylated by geranylgeranyltransferase type I (GGTase-I), which normally target proteins to membranes f
85 ferase and geranylgeranyltransferase type I (GGTase-I).
86 nd protein geranylgeranyltransferase type I (GGTase-I).
87 e known as geranylgeranyltransferase type I (GGTase-I).
88 or protein geranylgeranyltransferase type I (GGTase-I).
89 e, protein geranylgeranyltransferase type I (GGTase-I).
90 or protein geranylgeranyltransferase type-I (GGTase-I) for proper function and for the transforming a
91 on enzyme geranylgeranyl transferase type-I (GGTase-I) in podocytes led to progressive albuminuria an
92    Protein geranylgeranyltransferase type-I (GGTase-I), one of two CaaX prenyltransferases, is an ess
93 ranylgeranyl (GG) by FTase or GGTase type-I (GGTase-I), respectively.
94 he enzyme geranylgeranyl transferase type-I (GGTase-I).
95 nd protein geranylgeranyltransferase type-I (GGTase-I).
96 tein geranylgeranyltransferase type I or II (GGTase-I and GGTase-II).
97                                           In GGTase I, lysine beta311 is substituted for this asparta
98                Mutation of lysine beta311 in GGTase I to alanine (Kbeta311A) or aspartate (Kbeta311D)
99           Macrophages that were deficient in GGTase I or p110delta exhibited constitutive release of
100 action between the aryl groups and Ser 48 in GGTase-I binding site could be one possible reason to ex
101 g, and reduces inflammation and arthritis in GGTase-I-deficient mice, as well as prevents statins fro
102 dc42, reverses inflammation and arthritis in GGTase-I-deficient mice.
103 Tase (T49beta and F324beta, respectively, in GGTase-I).
104 itive with the protein substrate, whereas in GGTase-I, L-778,123 is competitive with the lipid substr
105                            Insulin increased GGTase I activity 3-fold and augmented the amounts of ge
106  lysates, GGTI-DU40 was confirmed to inhibit GGTase-I activity in a dose-dependent manner.
107 esyltransferase (15-C prenyl substrate) into GGTase-I (20-C prenyl substrate) with a single point mut
108 dition of Mg(II) for Kbeta311A and Kbeta311D GGTase I 2-5-fold compared with wild type GGTase I with
109               Aortic lesions in mice lacking GGTase-I in macrophages (Pggt1btriangle up/triangle up)
110 serine, or glutamine (FTase), or to leucine (GGTase-I).
111       We used immunofluorescence to localize GGTase-I, which was expressed mainly by podocytes in the
112 e first structural information for mammalian GGTase-I, including a series of substrate and product co
113 ndence, where the activity of FTase, but not GGTase I, is activated by magnesium.
114 ng II in VSMCs by increasing the activity of GGTase I and the availability of geranylgeranylated Rho-
115 e results demonstrate that lysine beta311 of GGTase I partially replaces the catalytic function of Mg
116                    GGTI-286, an inhibitor of GGTase I, blocked both effects of insulin.
117 inhibited in the presence of an inhibitor of GGTase I, GGTI-286 (3 microm) or by an expression of a d
118  the insulin were blocked by an inhibitor of GGTase I, GGTI-286.
119 ino acid increases whereas the reactivity of GGTase I increases with the hydrophobicity of the X-grou
120               The alpha and beta subunits of GGTase I from Saccharomyces cerevisiae are encoded by RA
121 in substrate specificity of FTase to that of GGTase I can be accomplished by introducing a distinct s
122                                  Analyses of GGTase-I-deficient macrophages revealed upregulation of
123             However, conditional deletion of GGTase-I in mouse macrophages increases GTP-loading of R
124                                 Depletion of GGTase-I in podocytes in vivo resulted in FPE and concom
125 ese compounds exhibit specific inhibition of GGTase-I and act by competing with a substrate protein.
126 udied in vitro by knockdown or inhibition of GGTase-I.
127 nt, was a classical competitive inhibitor of GGTase-I and not a time-dependent inhibitor.
128     A selective small molecular inhibitor of GGTase-I, GGTI-DU40, was tested in this study to investi
129 acterization of small molecule inhibitors of GGTase-I (GGTI) with two novel scaffolds from a library
130 However, we recently showed that knockout of GGTase-I in macrophages activates RHO proteins and proin
131   The results also point to the potential of GGTase-I inhibitors as agents capable of restoring growt
132                               A reduction of GGTase-I activity in cultured podocytes disrupted RhoGTP
133 ther the increased inflammatory signaling of GGTase-I-deficient macrophages would influence the devel
134     Here we present the crystal structure of GGTase-I from C. albicans (CaGGTase-I) in complex with i
135 Dpr1 mutants can function as either FTase or GGTase I beta subunit in vivo, although some differences
136 ein/peptide confers specificity for FTase or GGTase I.
137  affect the activity of recombinant FTase or GGTase I.
138 re transgene to create mice lacking FTase or GGTase-I in skin keratinocytes.
139  of more specific inhibitors toward FTase or GGTase-I.
140 tor) and are highly selective for FTase over GGTase I (geranylgeranyltransferase I).
141 ghly selective for FTase (IC50, 1.4 nM) over GGTase I (IC50, 1700 nM), whereas GGTI-2154 is highly se
142                Two compounds that are potent GGTase I inhibitors in vitro but that have poor antifung
143 unds with novel scaffolds and high predicted GGTase-I inhibitory activities were tested in vitro, and
144 at lacked substrate overlap with the protein GGTase-I made possible an analysis of the role of substr
145 mmalian FTase and complexed with the related GGTase-I enzyme.
146 foot process effacement in podocyte-specific GGTase-I knockout mice.
147 in podocytes, we generated podocyte-specific GGTase-I knockout mice.
148                                    Targeting GGTase-I activates RHOA and leads to increased macrophag
149               These results demonstrate that GGTase-I inhibitors arrest cells in G0/G1 and induce acc
150 alidating in a genetic model the theory that GGTase-I is a good target for anti-cancer drug developme
151              They found that ablation of the GGTase-I-encoding gene in cells destined to produce lung
152                This study indicates that the GGTase-I enzyme is a promising molecular target for lowe
153 (when FTase is inhibited) in cancer therapy; GGTase I inhibitors (GGTIs) as antitumor agents; effects
154 both Zn(II) and Mg(II) for maximal turnover, GGTase I turnover is dependent only on Zn(II).
155          The subcellular distribution of two GGTase I substrates, Rho1p and Cdc42p, was shifted from
156 ylation rate constant catalyzed by wild type GGTase I (k(chem) = 0.18 +/- 0.02 s(-1)) is not dependen
157 1D GGTase I 2-5-fold compared with wild type GGTase I with K(Mg) of 140 +/- 10 mm and 6.4 +/- 0.8 mm,
158  C. albicans can be prenylated by FTase when GGTase I is absent or limiting and that elevation of the
159  the JCI, Khan et al. examined mice in which GGTase-I was conditionally deleted in macrophages.
160   In contrast, treatment of these cells with GGTase I inhibitor GGTI-298 strongly inhibited receptor
161 pressed intestinal inflammation in mice with GGTase-I-deficient IECs, our findings suggest new avenue

 
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