ライフサイエンスコーパス: APX

1 APX eliminated PP binding sites in the DVC as assessed b

2 APX has a unique substrate binding site near the heme pr

3 APX or sham procedures were performed in anesthetized ma

4 APX partially reversed PP inhibition of basal protein se

5 APX reduced the pancreatic fluid (54%) and protein (46%)

6 APX-1/Delta acts in surrounding cells including the non-

7 nd drinking bouts may increase in size after APX, because the feedback inhibition provided by those s

8 In order to convert CCP into an APX, the ascorbate-binding loop and critical arginine we

9 ntral M lineage cells, its ligands LAG-2 and APX-1 are asymmetrically localized in cells adjacent to

10 edundant function of GLP-1 ligands LAG-2 and APX-1.

11 cal formation on Trp51, as seen for KatG and APX, is implicated; this is supported by QM/MM calculati

12 costerone and plasma glucose in both SHM and APX rats for up to 4 h after drug treatment.

13 Dawley rats with lesions centered on the AP (APX) and sham-operated (SHM) rats administered paraquat

14 We hypothesize that the removal of the AP (APX) will alter the effects of PP on pancreatic secretio

15 DTNB-modified APX (APX-TNB) exhibits only 1.3% wild-type activity when asco

16 g either DFEN or amylin was examined in both APX and sham operated groups.

17 SOD and its optimum level was maintained by APX.

18 a different ligand related to delta, called APX-1.

19 cent to the proximal His heme ligand in CCP, APX, and LmP.

20 r ascorbate levels in absence of chloroplast APX activity are detrimental to the cell during excess l

21 We conclude that chloroplast APX proteins in Arabidopsis can be effectively compensat

22 enzymes such as cytosolic and chloroplastic APXs.

23 sham operated controls but, unlike controls, APX rats did not reduce total intake in the two-bottle p

24 nteraction for the cyanide-bound derivative (APX-CN) is consistent with a 1:1 stoichiometry and is ch

25 The reaction of ferric APX with the suicide substrate phenylhydrazine yields pr

26 ot methyl viologen or Rose Bengal, and GPXs, APX, and MSRA2 genes (encoding glutathione peroxidase, a

27 in terms of our current understanding of how APX catalyzes oxidation of different types of substrates

28 s residues at positions 160, 203, and 204 in APX with methionine should stabilize a Trp179 radical in

29 g response in SHM rats that was abolished in APX animals.

30 d Trp(208), respectively, which is absent in APX.

31 Arg172 in APX hydrogen bonds with one of the heme propionates.

32 nk from Trp51 to the heme is observed, as in APX.

33 lly competent binding sites for ascorbate in APX.

34 ue that is required for ascorbate binding in APX is Asn in CCP.

35 is42 is critical for Compound I formation in APX; (b) confirmation that titration of His42 controls C

36 ed site is nearly identical to that found in APX.

37 was blunted with PP at 100 pmol/kg per h in APX rats, possibly related to the stimulatory effect of

38 eaction with H(2)O(2) to form Compound I; in APX, the radical is located on the porphyrin ring.

39 Increases in APX and GPX activity, as well as total protein contents

40 y greater c-fos activation of NTS neurons in APX rats than sham rats, despite the apparent absence of

41 to the stimulatory effect of high-dose PP in APX rats without 2-DG.

42 hionine should stabilize a Trp179 radical in APX compound I.

43 al modification of the single Cys residue in APX with Ellman's reagent (DTNB) blocks the ability of A

44 heme pocket to the corresponding residues in APX dramatically decreased the stability of the Trp191 r

45 r of 2-DG-stimulated pancreatic secretion in APX rats.

46 tioned flavor aversion to DEN was similar in APX and sham operated controls but, unlike controls, APX

47 ison with the naturally occurring K+ site in APX.

48 mal heme pocket, Trp191 in CcP and Trp179 in APX, only Trp191 in CcP forms a stable cation radical wh

49 behavior of rats with area postrema lesions (APX) was monitored electronically every 6 s for 23 hr.

50 Area postrema lesions (APX) were produced by vacuum aspiration in adult male ra

51 Rats with such lesions (APX) displayed normal anorexia following administration

52 icient in thylakoid or stromal/mitochondrial APXs were not more sensitive to the stress combination t

53 DTNB-modified APX (APX-TNB) exhibits only 1.3% wild-type activity when

54 While wild-type CCP shows no APX activity, CCP2APX catalyzes the peroxidation of asco

55 similar structures, and yet neither CCP nor APX exhibits each other's activities with respect to red

56 llman's reagent (DTNB) blocks the ability of APX to oxidize ascorbate but not other small aromatic ph

57 en the non-exchangeable substrate protons of APX-CN and the haem iron were determined by paramagnetic

58 ced Fos-ir was reduced greatly in the PVN of APX rats, but appeared normal in several other regions s

59 We have previously shown that reaction of APX with peroxide leads, over long time scales, to forma

60 was reduced in many rostral brain regions of APX rats.

61 The 2.0 A X-ray crystal structure of APX-TNB shows clear electron density for the TNB group c

62 te molecule interact with different sites on APX.

63 wer catalase (CAT) and ascorbate peroxidase (APX) activities, leading to fruits with lower decay.

64 Cytochrome c (CcP) and ascorbate peroxidase (APX) are heme peroxidases which have very similar active

65 smutase (CuZn-SOD) and ascorbate peroxidase (APX) constitute first line of defence against oxidative

66 the proximal pocket of ascorbate peroxidase (APX) could be engineered into cytochrome c peroxidase (C

67 roximal heme pocket of ascorbate peroxidase (APX) could be successfully engineered into the closely h

68 c peroxidase (CCP) and ascorbate peroxidase (APX) have very similar structures, and yet neither CCP n

69 Peroxisomal ascorbate peroxidase (APX) is a carboxyl tail-anchored, type II (N(cytosol)-C(

70 peroxisomal isoform of ascorbate peroxidase (APX) is a novel membrane isoform that functions in the r

71 des a 32-kD subunit of ascorbate peroxidase (APX) with a single, putative membrane-spanning region ne

72 raction of recombinant ascorbate peroxidase (APX) with its physiological substrate, ascorbate, has be

73 ted that overexpressed ascorbate peroxidase (APX), a peroxisomal membrane protein, sorted indirectly

74 Ascorbate peroxidase (APX), cytochrome c peroxidase (CcP), and the catalase-pe

75 oxide dismutase (SOD), ascorbate peroxidase (APX), guaiacol peroxidase (GPX) and glutathione reductas

76 nvestigate the role of ascorbate peroxidase (APX), guaiacol peroxidase (GPX), polysaccharides, and pr

77 ogous to that found in ascorbate peroxidase (APX), was engineered into cytochrome c peroxidase (CcP)

78 P) and plant cytosolic ascorbate peroxidase (APX).

79 orbate binding site in ascorbate peroxidase (APX).

80 hloramphenicol acetyltransferase-peroxisomal APX (CAT-pAPX) fusion protein accumulated only in the re

81 zation of endogenous Arabidopsis peroxisomal APX (AtAPX) in cultured wild-type Arabidopsis cells (Ara

82 cently we showed that cottonseed peroxisomal APX was sorted post-translationally from the cytosol to

83 d proteins) abolished sorting of peroxisomal APX to peroxisomes via pER.

84 id transmembrane domain (TMD) of peroxisomal APX was sufficient for sorting.

85 ular localization and sorting of peroxisomal APX were examined both in vivo and in vitro.

86 ediate in the sorting pathway of peroxisomal APX.

87 med in response to overexpressed peroxisomal APX, portions of rough ER (pER) in wild-type cells serve

88 Thus, plant peroxisomal APX, a representative enzymatic peroxisomal membrane pro

89 signals responsible for sorting peroxisomal APX.

90 ng of constitutively synthesized peroxisomal APX.

91 Epitope-tagged peroxisomal APX, which was expressed transiently in tobacco BY-2 cel

92 tive sorting sequences) plus the peroxisomal APX C-terminal tail also sorted chloramphenicol acetyltr

93 mes via pER, indicating that the peroxisomal APX TMD does not possess essential sorting information.

94 Replacement of the peroxisomal APX TMD with an artificial TMD (devoid of putative sorti

95 However, in vitro, peroxisomal APX inserted post-translationally into the ER but not in

96 harged domain to function within peroxisomal APX as an overlapping pER sorting signal and a membrane

97 with lesions centered on the area postrema (APX) and sham-operated (SHM) rats administered 2DG (200

98 Rats with lesions of the area postrema (APX) or sham lesions were trained to associate flavored

99 We propose that APX-1 is part or all of the P2 signal that induces ABp t

100 In this report, we show that APX-1 protein is expressed in the P2 blastomere and that

101 Stopped-flow studies show that APX-TNB reacts normally with peroxide to give compound I

102 The APX rats were similar to controls in learning preference

103 In contrast, the APX rats displayed impaired aversion learning for flavor

104 , and this region was entirely absent in the APX rats.

105 te, chromate, and arsenate produce transient APX intermediates that are sufficiently long-lived to be

106 1 in CcP forms a stable cation radical while APX forms the more traditional porphyrin pi-cation radic

107 Similarly enhanced water intake by rats with APX also was observed when marked hypovolemia was induce

108 solution after food deprivation by rats with APX also were considerably larger than those of control

109 d each day in 16.3 distinct bouts, rats with APX ate comparable amounts of food (28.6 g) in much fewe

110 M NaCl daily in 7.0 bouts, whereas rats with APX consumed 9 times as much saline (45.5 ml) in more bo

111 water daily in 17.8 bouts, whereas rats with APX consumed more than twice as much water (101.5 ml) in

112 ese and other results suggest that rats with APX experience less inhibition of ingestion while drinki

113 icantly more water was consumed by rats with APX than by intact control rats.