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1 HGPRT-deficient fibroblast cells also exhibited the grea
2 After 1 h in D2O, HGPRT alone exchanges 160, HGPRT-GMP-Mg(2+) exchanges 154, the equilibrium complex
3 s study, we examined the ability of N2aTG, a HGPRT-deficient neuroblastoma and its HGPRT-positive cou
4 rse reactions were largely unchanged for all HGPRT constructs, except for a 4-5-fold decrease in the
7 ct molecular mass for HGPRT-I, HGPRT-II, and HGPRT-I.HGPRT-II and suggests that the predominant heter
11 he predicted amino acid sequences of certain HGPRT proteins from parasites of the Trypanosomatidae fa
15 These data demonstrate that the L. donovani HGPRT is compartmentalized exclusively within the glycos
17 and genetically for the Leishmania donovani HGPRT employing a combination of protein modifying reage
18 These data establish genetically that either HGPRT or XPRT is absolutely essential for purine acquisi
19 direct support to the hypothesis that either HGPRT or XPRT is crucial for purine salvage by the paras
20 eobase transport, the purine salvage enzymes HGPRT, XPRT and APRT were also upregulated, suggesting t
21 targeting signal had been deleted expressed HGPRT throughout the parasite, including subcellular org
23 veals species of distinct molecular mass for HGPRT-I, HGPRT-II, and HGPRT-I.HGPRT-II and suggests tha
24 se results to reaction coordinate motion for HGPRT suggests that bond formation between C1' of the nu
25 in the following article shows how T. gondii HGPRT is able to recognize guanine, hypoxanthine, and xa
28 GMP-Mg(2+) complex, the HGPRT-IMP-MgPPi <==> HGPRT-Hx-MgPRPP equilibrating mixture, and the transitio
33 705 and T-1105 are poor substrates for human HGPRT having Km(app) values of 6.4 and 4.1 mM, respectiv
35 p180 at the corresponding locations in human HGPRT and Giardia lamblia GPRT, respectively, may explai
36 namic and conformational properties of human HGPRT alone, the HGPRT-GMP-Mg(2+) complex, the HGPRT-IMP
37 compounds into the known structures of human HGPRT in complex with ANP-based inhibitors suggests reas
42 structure of T-705-RMP in complex with human HGPRT showed how this compound binds in the active site.
43 cture of this compound in complex with human HGPRT shows that it fills or partially fills three criti
44 structure of this ANbP in complex with human HGPRT was determined at 2.0 A resolution and shows that
45 cies of distinct molecular mass for HGPRT-I, HGPRT-II, and HGPRT-I.HGPRT-II and suggests that the pre
46 ular mass for HGPRT-I, HGPRT-II, and HGPRT-I.HGPRT-II and suggests that the predominant heterotetrame
48 ovani, null mutants genetically deficient in HGPRT and/or APRT were generated by targeted gene replac
49 An essential role for this Ser-Tyr dyad in HGPRT catalysis has now been verified biochemically and
51 vated c-MYC expression leads to an increased HGPRT mutation rate of Rat1 cells and an increase in the
52 aTG, a HGPRT-deficient neuroblastoma and its HGPRT-positive counterpart to proliferate and differenti
53 rising ability of mutant L. donovani lacking HGPRT, APRT, and/or AK to incorporate and grow in hypoxa
54 in T. foetus HGXPRT and Arg187 in S. mansoni HGPRT will be attractive targets for future studies.
56 nts containing amplified copies of a mutated HGPRT construct in which the Ser-Lys-Val COOH-terminal t
60 to the transition state analogue complex of HGPRT.ImmHP.MgPP(i) to determine the ionic states of the
62 ine definitively the intracellular milieu of HGPRT in these pathogens, polyclonal antiserum to the pu
67 he residue corresponding to Asp206, the only HGPRT amino acid that directly contacts the Mg(2+) ions,
69 oxanthine-guanine phosphoribosyltransferase (HGPRT) and Plasmodium falciparum (Pf) hypoxanthine-guani
70 oxanthine-guanine phosphoribosyltransferase (HGPRT) and significant homology with other HGPRT family
71 oxanthine-guanine phosphoribosyltransferase (HGPRT) and xanthine phosphoribosyltransferase (XPRT).
72 oxanthine guanine phosphoribosyltransferase (HGPRT) converts T-705 into its ribose-5'-monophosphate (
73 oxanthine-guanine phosphoribosyltransferase (HGPRT) have been determined at 1.65 and 1.90 A resolutio
74 oxanthine-guanine phosphoribosyltransferase (HGPRT) is a key enzyme in the purine salvage pathway of
75 oxanthine-guanine phosphoribosyltransferase (HGPRT) is the key enzyme in purine base salvage in human
77 oxanthine-guanine phosphoribosyltransferase (HGPRT) of the apicomplexan protozoan Toxoplasma gondii a
78 oxanthine-guanine phosphoribosyltransferase (HGPRT) proteins have implied that the translocation of a
79 oxanthine-guanine phosphoribosyltransferase (HGPRT), adenine phosphoribosyltransferase (APRT), and ad
80 oxanthine-guanine phosphoribosyltransferase (HGPRT)-xanthosine 5'-monophosphate (XMP)-pyrophosphate-M
84 clonal antiserum to the purified recombinant HGPRT from Leishmania donovani was generated in rabbits,
85 ichia coli indicated that wild type and S95T HGPRTs complemented bacterial phosphoribosyltransferase
86 ine PRT in our possession, only schistosomal HGPRT, the only other enzyme that contains an arginine r
89 encing of this EcoRI fragment confirmed that HGPRT and XPRT were organized in a head-to-tail arrangem
91 ational properties of human HGPRT alone, the HGPRT-GMP-Mg(2+) complex, the HGPRT-IMP-MgPPi <==> HGPRT
93 PRT alone, the HGPRT-GMP-Mg(2+) complex, the HGPRT-IMP-MgPPi <==> HGPRT-Hx-MgPRPP equilibrating mixtu
94 e that is conserved among all members of the HGPRT family is essential for phosphoribosylation of pur
95 rt null mutants in which both alleles of the HGPRT locus had been replaced by a drug-resistance casse
98 Two structural features important to the HGPRT mechanism, a previously unrecognized active site l
99 ith two subunits in the asymmetric unit; the HGPRT tetramer is completed by the application of 2-fold
103 rotetramer has enzymatic activity similar to HGPRT-II, and gel filtration chromatography demonstrates
104 xanthine-guanine phosphoribosyl-transferase (HGPRT) and xanthine phosphoribosyltransferase (XPRT) usi
105 human embryonic kidney 293T cells undergoing HGPRT-specific gene knockdown followed by influenza viru
107 bilities of 2-3 orders of magnitude, whereas HGPRTs containing conservative substitutions, S95C and S
108 ta hgprt knockout strain in which a wildtype HGPRT was amplified on an expression plasmid contained a
109 as a single copy gene that co-localized with HGPRT within a 4.3-kilobase pair (kb) EcoRI fragment, im
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