戻る
「早戻しボタン」を押すと検索画面に戻ります。 [閉じる]

コーパス検索結果 (left1)

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                                              SHMT also catalyzes the folate-independent retroaldol cl
2                                              SHMT catalyses interconversion of serine and glycine whi
3                                              SHMT enzymes are the major source of the one-carbon unit
4                                              SHMT is a pyridoxal 5'-phosphate-dependent enzyme that c
5                                              SHMT is crucial for deoxythymidylate biosynthesis and a
6                                              SHMT is involved in the penultimate step of thymidylate
7                                              SHMT is present in eukaryotic cells as mitochondrial SHM
8                                              SHMT requires both pyridoxal phosphate (PLP) and tetrahy
9                                              SHMT tetramers have surface charge distributions which s
10                                              SHMTs are emerging as a promising target for development
11 ers for (6S)-5,10-CH(2)-H(4)PteGlu(5) for an SHMT from any organism.
12 t) values for 5,10-CH(2)-H(4)PteGlu(5) of an SHMT from Arabidopsis thaliana.
13 ves incubating [2-3H]glycine, H4PteGlun, and SHMT for 3 min followed by a separation of the exchanged
14 o be inhibited by 5-CHO-H(4)PteGlu(n) as are SHMTs from other organisms.
15 alciparum (Pf) and Arabidopsis thaliana (At) SHMT in target assays and PfNF54 strains in cell-based a
16 ed into a rapid and sensitive assay for both SHMT and H4PteGlun and the one-carbon derivatives of H4P
17  for folate-dependent reactions catalyzed by SHMT.
18             In this method, serine formed by SHMT activity is reacted with 4-fluoro-7-nitro-2,1,3-ben
19 ofolate is a property of other characterized SHMTs.
20 in strains lacking SHMT activity, confirming SHMT as the in vivo source of 5-CHO-THF.
21                                  Cytoplasmic SHMT (cSHMT) has been postulated to channel one-carbon s
22 es cerevisiae, mitochondrial and cytoplasmic SHMT isozymes are encoded by distinct nuclear genes (SHM
23 e of the inactive form of murine cytoplasmic SHMT (cSHMT), lacking only the polyglutamate tail of the
24 ture at 2.8 A resolution of rabbit cytosolic SHMT (rcSHMT) in two forms: one with the PLP covalently
25 ydropteroylpolyglutamate on rabbit cytosolic SHMT.
26  site mutant homotetrameric rabbit cytosolic SHMTs identified lysine residues that contribute to the
27 that lacks mitochondrial, but not cytosolic, SHMT activity.
28 ted by a futile cycle comprising the enzymes SHMT and 5,10-methenyltetrahydrofolate synthetase (MTHFS
29 teGlu5 has a 300-fold increased affinity for SHMT compared to 5-CHO-H4PteGlu.
30  not readily available for use in assays for SHMT activity.
31 n donor formate generally rescues cells from SHMT inhibition, but paradoxically increases the inhibit
32 ure closely resembles the structure of human SHMT, confirming its similarity to the alpha-class of PL
33 r measuring serine hydroxymethyltransferase (SHMT) activity toward formation of serine and (6S)-H(4)P
34 tochondrial serine hydroxymethyltransferase (SHMT) activity.
35 activity of serine hydroxymethyltransferase (SHMT) and strongly inhibits SHMT and other folate-depend
36             Serine hydroxymethyltransferase (SHMT) catalyzes the reversible and THF-dependent convers
37             Serine hydroxymethyltransferase (SHMT) catalyzes the reversible cleavage of serine to for
38             Serine hydroxymethyltransferase (SHMT) catalyzes the reversible cleavage of serine to gly
39             Serine hydroxymethyltransferase (SHMT) catalyzes the reversible interconversion of serine
40             Serine hydroxymethyltransferase (SHMT) from all sources tested catalyzes the slow exchang
41             Serine hydroxymethyltransferase (SHMT) from plant mitochondria was shown to be inhibited
42 MTHFD1) and serine hydroxymethyltransferase (SHMT) generate 5,10-methylenetetrahydrofolate for de nov
43             Serine hydroxymethyltransferase (SHMT) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme
44             Serine hydroxymethyltransferase (SHMT) is a pyridoxal phosphate-dependent enzyme that cat
45   Mammalian serine hydroxymethyltransferase (SHMT) is a tetrameric, pyridoxal phosphate-dependent enz
46             Serine hydroxymethyltransferase (SHMT) is the major provider of one-carbon units in the c
47 richia coli serine hydroxymethyltransferase (SHMT) showed that the final rate determining folding ste
48 r cytosolic serine hydroxymethyltransferase (SHMT) were determined by a combination of isothermal tit
49 se (MTHFR), serine hydroxymethyltransferase (SHMT), and cystathionine beta-synthase (CBS) genes and t
50 tochondrial serine hydroxymethyltransferase (SHMT), combined with glycine decarboxylase, catalyzes an
51  the enzyme serine hydroxymethyltransferase (SHMT), designed to improve microsomal metabolic stabilit
52 theless for serine hydroxymethyltransferase (SHMT), one of the key enzymes of this cycle, efficient i
53 the enzymes serine hydroxymethyltransferase (SHMT), thymidylate synthase (TYMS), and dihydrofolate re
54 nhibitor of serine hydroxymethyltransferase (SHMT), was enriched in nuclei, accounting for 35% of fol
55 atalyzed by serine hydroxymethyltransferase (SHMT).
56 ICARFT) and serine hydroxymethyltransferase (SHMT).
57 abolized by serine hydroxymethyltransferase (SHMT)2 in the mitochondria and generates glycine and C1
58 hat targets serine hydroxymethyltransferase (SHMT)2 in the mitochondria and SHMT1 and de novo purine
59             Serine hydroxymethyltransferase (SHMT; EC 2.1.2.1) catalyzes the reversible interconversi
60  cytosolic serine hydroxymethyltransferases (SHMT) confirmed their close similarity in tertiary and d
61 ne or both serine hydroxymethyltransferases (SHMT) or at the genes encoding one or both methylenetetr
62            Serine hydroxymethyltransferases (SHMTs) reversibly transform serine into glycine in a rea
63   The enzyme serine hydroxymethyltransferse (SHMT) converts serine into glycine and a tetrahydrofolat
64 midylate (dTMP) synthesis through changes in SHMT expression is causative in folate-responsive NTDs.
65 se data establish that 5-CHO-THF can inhibit SHMT in vivo and thereby influence glycine pool size.
66 thyltransferase (SHMT) and strongly inhibits SHMT and other folate-dependent enzymes in vitro.
67 hat especially polyglutamylated PTX inhibits SHMTs in vivo.
68 -CHO-THF was undetectable in strains lacking SHMT activity, confirming SHMT as the in vivo source of
69  first structure of a ligand-bound mammalian SHMT allows identification of amino acid residues involv
70                                Mitochondrial SHMT mRNA levels in MCF-7 cells did not vary during the
71 is mitochondrial in plants and mitochondrial SHMT is central to photorespiration, we examined the imp
72 present in eukaryotic cells as mitochondrial SHMT and cytoplasmic (cSHMT) isozymes that are encoded b
73 lly conserved within the human mitochondrial SHMT gene.
74 gnated shm1-1) is defective in mitochondrial SHMT activity and displays a lethal photorespiratory phe
75                          Since mitochondrial SHMT is crucial to photorespiration, 5-FCL may help prev
76       This study suggests that mitochondrial SHMT-derived one-carbon units are essential for folate-m
77  and glycine were present, the mitochondrial SHMT made a significant contribution of one-carbon units
78 ffects SHM1, which encodes the mitochondrial SHMT required for photorespiration.
79     When grown on glycine, the mitochondrial SHMT was the predominant isozyme catalyzing the synthesi
80      Analyzed by the single-hit multitarget (SHMT) model, F1, F5, and F7, like camptothecin, induce R
81  both a Gly and Ala residue, and each mutant SHMT was purified and characterized with respect to kine
82 s in its configuration, and the P258A mutant SHMT showed reduced thermal stability.
83                                           No SHMT has been purified from a nonmethanogenic Archaea st
84 xplaining previous observations that nuclear SHMT is not a robust source of one-carbons for de novo d
85 bes the purification and characterization of SHMT from the thermophilic organism Sulfolobus solfatari
86 xploit antifolate scaffold in development of SHMT inhibitors because it seems likely that especially
87              In the presence of an excess of SHMT the exchange rate is directly proportional to the c
88 in maintaining the structure and function of SHMT and a possible role in pyridoxal 5'-phosphate addit
89                                     Glu75 of SHMT is clearly involved in the reaction mechanism; it i
90 estigation on species-specific inhibition of SHMT for antimalarial drug development.
91 redominant physiological binder/inhibitor of SHMT.
92 e rate is proportional to nanogram levels of SHMT.
93 ns the properties of several site mutants of SHMT and offers testable hypotheses for a more detailed
94     Studies of wild-type and site mutants of SHMT have failed to clearly establish the mechanism of t
95 upplemented media indicated that the role of SHMT in the KinB pathway is to feed the pool of C1 units
96 ycine formation is the rate-limiting step of SHMT catalysis.
97 ation significantly changed the structure of SHMT, the spectral properties of its complexes, or the k
98 ificant similarity with those of peptides of SHMTs from two methanogens.
99 that only two of the four catalytic sites on SHMT are catalytically competent and that the cSHMT-glyc
100 s and complex formation for photorespiratory SHMT activity demonstrates more complicated regulation o
101 nteraction is necessary for photorespiratory SHMT activity.
102 a pyrazolopyran scaffold that inhibits plant SHMT, we identify small-molecule dual inhibitors of huma
103                        On the basis of plant SHMT inhibitors from an herbicide optimization program,
104 tal structures of MTX and PTX bound to plant SHMT isozymes from cytosol and mitochondria-human isozym
105 um falciparum (Pf) and Plasmodium vivax (Pv) SHMT with a pyrazolopyran core structure were identified
106  co-localization of dihydrofolate reductase, SHMT, and thymidylate synthase to the nuclear lamina, in
107 n 6 genes (MTHFR, MTRR, FOLH1, CbetaS, RFC1, SHMT) involved in folate absorption and metabolism were
108 adiation employ the single hit multi-target (SHMT) algorithm, which yields a single value, the D0, as
109 nism for previous studies demonstrating that SHMT expression is rate-limiting for de novo thymidylate
110 thase to the nuclear lamina, indicating that SHMT serves as scaffold protein that is essential for co
111            Phylogenetic analysis showed that SHMT genes are divided into four classes reflecting thei
112 s work presents a comprehensive study of the SHMT gene family members, including synteny, phylogeny,
113 Mapping of the identified mutations onto the SHMT structural model uncovered key residues for structu
114                            In addition, this SHMT also catalyzed the cleavage of both allo-threonine
115 THF levels do not much affect fluxes through SHMT or any other folate-dependent reaction, i.e. that 5
116 tive inhibitors of 5-CHO-H4PteGlu binding to SHMT, showing that anions compete for the polyglutamate
117                Binding of 5-CHO-H4PteGlun to SHMT exhibits both positive enthalpy and entropy, showin
118 ives of 5-CHO-H4PteGlun were cross-linked to SHMT by a carbodiimide reaction to Lys-450 which resides
119 t B-cell lines are particularly sensitive to SHMT inhibition.
120  our human serine hydroxymethyl transferase (SHMT) 2 and glycinamide ribonucleotide formyltransferase
121 coding the serine hydroxymethyl transferase (SHMT).
122  to investigate the contributions of the two SHMT isozymes to the production of glycine and one-carbo
123 ines, rendering them uniquely dependent upon SHMT enzymatic activity to meet glycine demand.
124 set of patients that can be identified using SHMT analysis of PDO radiation responses.
125 drofolate in complexes of these species with SHMT.
126 gs such as methotrexate that synergized with SHMT inhibitors.

 
Page Top