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1                                              APX eliminated PP binding sites in the DVC as assessed b
2                                              APX expression restored APX single-knockout infectivity,
3                                              APX has a unique substrate binding site near the heme pr
4                                              APX or sham procedures were performed in anesthetized ma
5                                              APX overexpression in wild-type promastigotes reduced me
6                                              APX partially reversed PP inhibition of basal protein se
7                                              APX reduced the pancreatic fluid (54%) and protein (46%)
8                                              APX-1/Delta acts in surrounding cells including the non-
9                                              APX-null promastigotes could not be generated, and paras
10 nd drinking bouts may increase in size after APX, because the feedback inhibition provided by those s
11              In order to convert CCP into an APX, the ascorbate-binding loop and critical arginine we
12 ntral M lineage cells, its ligands LAG-2 and APX-1 are asymmetrically localized in cells adjacent to
13 edundant function of GLP-1 ligands LAG-2 and APX-1.
14              CAT (17), SOD (7), POD (8), and APX (29%) were increased with combined TiO(2)-NPs and mi
15 homologous gene block problem is NP-hard and APX-hard.
16 cal formation on Trp51, as seen for KatG and APX, is implicated; this is supported by QM/MM calculati
17 costerone and plasma glucose in both SHM and APX rats for up to 4 h after drug treatment.
18 arrying C allele showed higher antioxidants (APX, AsA, and GSH) and barley yield traits (GS, WGS, and
19 Dawley rats with lesions centered on the AP (APX) and sham-operated (SHM) rats administered paraquat
20   We hypothesize that the removal of the AP (APX) will alter the effects of PP on pancreatic secretio
21                           DTNB-modified APX (APX-TNB) exhibits only 1.3% wild-type activity when asco
22 e expression of stress-related genes such as APX, CAT, and P5CS, with strong induction observed under
23 g either DFEN or amylin was examined in both APX and sham operated groups.
24  SOD and its optimum level was maintained by APX.
25  a different ligand related to delta, called APX-1.
26  b, total Chl, proline and MDA content, CAT, APX and GPX activity and petal and seeds yields were det
27 P treatment weakened the levels of SOD, CAT, APX, AsA, GSH, TP, and TF, thereby exacerbating ROS outb
28 as the proline and MDA content, and the CAT, APX and GPX activities increased as salt levels increase
29 cent to the proximal His heme ligand in CCP, APX, and LmP.
30 r ascorbate levels in absence of chloroplast APX activity are detrimental to the cell during excess l
31                 We conclude that chloroplast APX proteins in Arabidopsis can be effectively compensat
32  enzymes such as cytosolic and chloroplastic APXs.
33 sham operated controls but, unlike controls, APX rats did not reduce total intake in the two-bottle p
34 nteraction for the cyanide-bound derivative (APX-CN) is consistent with a 1:1 stoichiometry and is ch
35                              Here we examine APX with spectroscopy-oriented QM/MM calculations and ex
36                       The reaction of ferric APX with the suicide substrate phenylhydrazine yields pr
37 esults also uncover a unique requirement for APX-mediated control of ROS levels for survival and succ
38    Collectively, our data support a role for APX-regulated mitochondrial H(2)O(2) in promoting differ
39 activity of antioxidant enzymes such as GPX, APX, CAT, SOD, and POD as well as the lowest amount of h
40 ot methyl viologen or Rose Bengal, and GPXs, APX, and MSRA2 genes (encoding glutathione peroxidase, a
41 in terms of our current understanding of how APX catalyzes oxidation of different types of substrates
42 l) form of ascorbate peroxidase compound II (APX-II) is a subject of debate.
43 s residues at positions 160, 203, and 204 in APX with methionine should stabilize a Trp179 radical in
44 g response in SHM rats that was abolished in APX animals.
45 d Trp(208), respectively, which is absent in APX.
46                                    Arg172 in APX hydrogen bonds with one of the heme propionates.
47 nk from Trp51 to the heme is observed, as in APX.
48 lly competent binding sites for ascorbate in APX.
49 ue that is required for ascorbate binding in APX is Asn in CCP.
50 is42 is critical for Compound I formation in APX; (b) confirmation that titration of His42 controls C
51 ed site is nearly identical to that found in APX.
52  was blunted with PP at 100 pmol/kg per h in APX rats, possibly related to the stimulatory effect of
53 eaction with H(2)O(2) to form Compound I; in APX, the radical is located on the porphyrin ring.
54                                 Increases in APX and GPX activity, as well as total protein contents
55 y greater c-fos activation of NTS neurons in APX rats than sham rats, despite the apparent absence of
56 to the stimulatory effect of high-dose PP in APX rats without 2-DG.
57 hionine should stabilize a Trp179 radical in APX compound I.
58 al modification of the single Cys residue in APX with Ellman's reagent (DTNB) blocks the ability of A
59 heme pocket to the corresponding residues in APX dramatically decreased the stability of the Trp191 r
60 r of 2-DG-stimulated pancreatic secretion in APX rats.
61 tioned flavor aversion to DEN was similar in APX and sham operated controls but, unlike controls, APX
62 ison with the naturally occurring K+ site in APX.
63 h in CcP (1.76 A) is notably shorter than in APX (1.87 A).
64 mal heme pocket, Trp191 in CcP and Trp179 in APX, only Trp191 in CcP forms a stable cation radical wh
65 , while expression of catalytically inactive APX drastically reduced virulence.
66                            It also increased APX, CAT, and SOD activities, delayed the decrease in th
67 nd that in L. amazonensis, the ROS-inducible APX is essential for survival of all life cycle stages.
68 behavior of rats with area postrema lesions (APX) was monitored electronically every 6 s for 23 hr.
69                       Area postrema lesions (APX) were produced by vacuum aspiration in adult male ra
70                      Rats with such lesions (APX) displayed normal anorexia following administration
71   Similar to what was reported for L. major, APX depletion in L. amazonensis enhanced differentiation
72 icient in thylakoid or stromal/mitochondrial APXs were not more sensitive to the stress combination t
73                                DTNB-modified APX (APX-TNB) exhibits only 1.3% wild-type activity when
74                 While wild-type CCP shows no APX activity, CCP2APX catalyzes the peroxidation of asco
75  similar structures, and yet neither CCP nor APX exhibits each other's activities with respect to red
76 llman's reagent (DTNB) blocks the ability of APX to oxidize ascorbate but not other small aromatic ph
77 strongly support the Fe(IV)=O formulation of APX-II and highlight unresolved discrepancies in the nat
78 en the non-exchangeable substrate protons of APX-CN and the haem iron were determined by paramagnetic
79 ced Fos-ir was reduced greatly in the PVN of APX rats, but appeared normal in several other regions s
80    We have previously shown that reaction of APX with peroxide leads, over long time scales, to forma
81 was reduced in many rostral brain regions of APX rats.
82 rther insight into the protonation status of APX-II, we examined the intermediate using a combination
83         The 2.0 A X-ray crystal structure of APX-TNB shows clear electron density for the TNB group c
84 te molecule interact with different sites on APX.
85 wer catalase (CAT) and ascorbate peroxidase (APX) activities, leading to fruits with lower decay.
86 xidase family, notably ascorbate peroxidase (APX) and cytochrome c peroxidase (CcP), as well as a mit
87 Cytochrome c (CcP) and ascorbate peroxidase (APX) are heme peroxidases which have very similar active
88 smutase (CuZn-SOD) and ascorbate peroxidase (APX) constitute first line of defence against oxidative
89 the proximal pocket of ascorbate peroxidase (APX) could be engineered into cytochrome c peroxidase (C
90 roximal heme pocket of ascorbate peroxidase (APX) could be successfully engineered into the closely h
91 c peroxidase (CCP) and ascorbate peroxidase (APX) have very similar structures, and yet neither CCP n
92 ions of compound II in ascorbate peroxidase (APX) have yielded conflicting conclusions regarding the
93            Peroxisomal ascorbate peroxidase (APX) is a carboxyl tail-anchored, type II (N(cytosol)-C(
94 peroxisomal isoform of ascorbate peroxidase (APX) is a novel membrane isoform that functions in the r
95                        Ascorbate Peroxidase (APX) was reached at its peak (1.93 +/- 0.01) at site 7 i
96 des a 32-kD subunit of ascorbate peroxidase (APX) with a single, putative membrane-spanning region ne
97 raction of recombinant ascorbate peroxidase (APX) with its physiological substrate, ascorbate, has be
98 ted that overexpressed ascorbate peroxidase (APX), a peroxisomal membrane protein, sorted indirectly
99 oxide dismutase (SOD), ascorbate peroxidase (APX), and glutathione reductase (GR), under salt stress.
100 uch as catalase (CAT), ascorbate peroxidase (APX), and guaiacol peroxidase (GPX) in maize leaves.
101 nzymes catalase (CAT), ascorbate peroxidase (APX), and guaiacol peroxidase (GPX) significantly increa
102 c antioxidants such as ascorbate peroxidase (APX), catalase (CAT), superoxide dismutase (SOD) and per
103 c peroxidase (CcP) and ascorbate peroxidase (APX), collected using the X-ray free electron laser at S
104                        Ascorbate peroxidase (APX), cytochrome c peroxidase (CcP), and the catalase-pe
105  well as activities of ascorbate peroxidase (APX), glutathione reductase (GR), monodehydroascorbate r
106 oxide dismutase (SOD), ascorbate peroxidase (APX), guaiacol peroxidase (GPX) and glutathione reductas
107 nvestigate the role of ascorbate peroxidase (APX), guaiacol peroxidase (GPX), polysaccharides, and pr
108 ogous to that found in ascorbate peroxidase (APX), was engineered into cytochrome c peroxidase (CcP)
109 orbate binding site in ascorbate peroxidase (APX).
110 P) and plant cytosolic ascorbate peroxidase (APX).
111 g a role for ascorbate-dependent peroxidase (APX), which degrades mitochondrial H(2)O(2) Earlier stud
112 hloramphenicol acetyltransferase-peroxisomal APX (CAT-pAPX) fusion protein accumulated only in the re
113 zation of endogenous Arabidopsis peroxisomal APX (AtAPX) in cultured wild-type Arabidopsis cells (Ara
114 cently we showed that cottonseed peroxisomal APX was sorted post-translationally from the cytosol to
115 d proteins) abolished sorting of peroxisomal APX to peroxisomes via pER.
116 id transmembrane domain (TMD) of peroxisomal APX was sufficient for sorting.
117 ular localization and sorting of peroxisomal APX were examined both in vivo and in vitro.
118 ediate in the sorting pathway of peroxisomal APX.
119 med in response to overexpressed peroxisomal APX, portions of rough ER (pER) in wild-type cells serve
120                      Thus, plant peroxisomal APX, a representative enzymatic peroxisomal membrane pro
121  signals responsible for sorting peroxisomal APX.
122 ng of constitutively synthesized peroxisomal APX.
123                   Epitope-tagged peroxisomal APX, which was expressed transiently in tobacco BY-2 cel
124 tive sorting sequences) plus the peroxisomal APX C-terminal tail also sorted chloramphenicol acetyltr
125 mes via pER, indicating that the peroxisomal APX TMD does not possess essential sorting information.
126               Replacement of the peroxisomal APX TMD with an artificial TMD (devoid of putative sorti
127               However, in vitro, peroxisomal APX inserted post-translationally into the ER but not in
128 harged domain to function within peroxisomal APX as an overlapping pER sorting signal and a membrane
129  with lesions centered on the area postrema (APX) and sham-operated (SHM) rats administered 2DG (200
130      Rats with lesions of the area postrema (APX) or sham lesions were trained to associate flavored
131 tron diffraction data obtained from putative APX-II crystals indicate a protonated oxygenic ligand at
132                      APX expression restored APX single-knockout infectivity, while expression of cat
133 e generated, and parasites carrying a single APX allele were impaired in their ability to infect macr
134 ates both thylakoidal APX (tAPX) and stromal APX (sAPX) through alternative splicing.
135                       Our data indicate that APX-II is an iron(IV) oxo species with an Fe-O bond dist
136                              We propose that APX-1 is part or all of the P2 signal that induces ABp t
137                 In this report, we show that APX-1 protein is expressed in the P2 blastomere and that
138               Stopped-flow studies show that APX-TNB reacts normally with peroxide to give compound I
139 ondrial H(2)O(2) Earlier studies showed that APX-null L. major parasites are viable, accumulate highe
140                                          The APX rats were similar to controls in learning preference
141                             In contrast, the APX rats displayed impaired aversion learning for flavor
142 , and this region was entirely absent in the APX rats.
143 e cpAPX gene that generates both thylakoidal APX (tAPX) and stromal APX (sAPX) through alternative sp
144 TcAPx-CcP is similar in overall structure to APX and CcP, but there are differences in the substrate-
145 te, chromate, and arsenate produce transient APX intermediates that are sufficiently long-lived to be
146 1 in CcP forms a stable cation radical while APX forms the more traditional porphyrin pi-cation radic
147 ition 36,665,559 bp which is associated with APX, AsA, GSH, GS, WGS, and TKW under n-K treatment.
148 Similarly enhanced water intake by rats with APX also was observed when marked hypovolemia was induce
149 solution after food deprivation by rats with APX also were considerably larger than those of control
150 d each day in 16.3 distinct bouts, rats with APX ate comparable amounts of food (28.6 g) in much fewe
151 M NaCl daily in 7.0 bouts, whereas rats with APX consumed 9 times as much saline (45.5 ml) in more bo
152 water daily in 17.8 bouts, whereas rats with APX consumed more than twice as much water (101.5 ml) in
153 ese and other results suggest that rats with APX experience less inhibition of ingestion while drinki
154 icantly more water was consumed by rats with APX than by intact control rats.

 
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