ライフサイエンスコーパス: GART

1 ble amount of information is available about GART, while less is known about the GARS and AIRS domain

2 ) cells transfected with the human GARS-AIRS-GART gene, we show that this gene encodes not only the t

3 he expression of both the GARS and GARS-AIRS-GART proteins are regulated during development of the hu

4 lum development while the GARS and GARS-AIRS-GART proteins become undetectable in this tissue shortly

5 In contrast, the GARS and GARS-AIRS-GART proteins continue to be expressed during the postna

6 essed genes included HPRT, IMPDH, PAICS, and GART, all of which were expressed at a significantly low

7 cinamide transformylase (also abbreviated as GART), and phosphoribosylaminoimidazole synthetase (AIRS

8 fferences between human and Escherichia coli GART, previously used as a model for the human enzyme, w

9 ates that under physiological pH conditions, GART exists as a mixture of monomer and dimer in solutio

10 that (1) except the known 1C targets (DHFR, GART, and TYMS), MTHFD2 emerges as good drug target, esp

11 In the pH range 6.8 to 7.5, dimeric GART reversibly dissociates into a monomeric form as dem

12 vitro nuclease cleavage 3' to the Drosophila GART gene co-localized with the signal required for term

13 in the wild-type protein also occur in E70A GART.

14 se mutations on mRNA and protein content for GART and GARS.

15 onstrate a previously unappreciated role for GART in T cell-dependent antibody-producing B cell diffe

16 lycinamide ribonucleotide formyltransferase (GART) but do not induce detectable levels of DNA strand

17 lycinamide ribonucleotide formyltransferase (GART) enzymatic activities.

18 lycinamide-ribonucleotide formyltransferase (GART) genes from Escherichia coli (purN) and human (hGAR

19 lycinamide ribonucleotide formyltransferase (GART) locus is known to produce two functional proteins,

20 lycinamide ribonucleotide formyltransferase (GART).

21 The compounds were found to have human GART KiS ranging from 30 microM to 2 nM.

22 d using the X-ray crystal structure of human GART.

23 lectrostatic surface potentials of the human GART domain and Escherichia coli enzyme explain differen

24 complex is the first structure of the human GART domain that is bound at both the substrate and cosu

25 The human GART gene has two potential polyadenylation signals with

26 functional polyadenylation site in the human GART gene was virtually identical in sequence to a simil

27 onic polyadenylation mechanism for the human GART locus.

28 Monomeric GART reversibly associates into a dimeric form as a func

29 The GART activity of GART requires 10-formyltetrahydrofolate and has been a t

30 took a study of the pH-dependent behavior of GART in solution to determine whether side-chain ionizat

31 ), disrupts the pH-dependent dimerization of GART based on dynamic light scattering and gel filtratio

32 rotein that contains only the GARS domain of GART as a functional protein.

33 y for both the wild-type and mutant forms of GART indicates that a tyrosine residue(s) undergoes a ch

34 specific, pH-dependent assembly reaction of GART, although pH-dependent conformational changes prese

35 apoenzyme represents the first structure of GART, from any source, with a completely unoccupied subs

36 53 pathway is intact and that the utility of GART inhibitors would not be limited to p53-negative tum

37 The GART activity of GART requires 10-formyltetrahydrofolate

38 The GART gene is located on human chromosome 21 and is aberr

39 The GART inhibitors have been proposed previously to be cyto

40 chanisms by which mutations inactivating the GART protein might arise in CHO-K1 cells.

41 The three-dimensional structure of the GART domain from the human trifunctional enzyme has been

42 lyadenylation signal within an intron of the GART gene provides clues to this process and might also

43 enes (PAXBP1, IFNAR2, OAS1, OAS3, TNFAIP8L1, GART) were differentially expressed in immune cells from

44 obust initial response of the p53 pathway to GART inhibitors is not transcriptionally propagated to t

45 he phosphoribosylglycinamide transformylase (GART) gene encodes a trifunctional protein carrying out

46 n glycinamide ribonucleotide transformylase (GART) (EC 2.1.2.2) is a validated target for cancer chem

47 f glycinamide ribonucleotide transformylase (GART) are described.

48 Glycinamide ribonucleotide transformylase (GART) exhibits closely packed dimers in all crystal form

49 Glycinamide ribonucleotide transformylase (GART; 10-formyltetrahydrofolate:5'-phosphoribosylglycina

50 n HCT116, MCF7, or A549 carcinoma cells upon GART inhibition, but, surprisingly, transcription of sev