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1 ncluding uncoupling protein 2, catalase, and copper zinc superoxide dismutase.
2 l killing was abrogated by 1,000 units/ml of copper-zinc superoxide dismutase.
3  oxidative damage in cells lacking cytosolic copper/zinc superoxide dismutase.
4 tivities of either glutathione peroxidase or copper/zinc superoxide dismutase.
5 having a point mutation in the gene encoding copper/zinc superoxide dismutase.
6                        Similarly, two mutant copper zinc superoxide dismutase 1 (mSOD1) mouse models
7 otective role in mice harboring mutations of copper-zinc superoxide dismutase 1 (SOD1) in familial am
8 d in the reduced accumulation of chloroplast copper/zinc superoxide dismutase 1 (HvSOD1), whereas los
9 d in the reduced accumulation of chloroplast copper/zinc superoxide dismutase 1 (HvSOD1), whereas los
10                             Mutations in the copper/zinc superoxide dismutase 1 (SOD-1) gene have pre
11                                 Mutations in copper/zinc superoxide dismutase 1 (SOD1) are found in a
12 rosis, FALS) associated with the most common copper/zinc superoxide dismutase 1 (SOD1) mutation, an a
13 ions confer one or more toxic function(s) on copper/zinc superoxide dismutase 1 (SOD1) that impair mo
14                                 Mutations in copper/zinc superoxide dismutase 1 (SOD1), a genetic cau
15                                 Mutations in copper/zinc superoxide dismutase 1 (SOD1), primary cause
16                                          The copper-zinc superoxide dismutase-1 (SOD1) is a highly st
17                                  Addition of copper-zinc superoxide dismutase (3,000 units/ml), which
18  constitutive ACHN proteins were identified: copper zinc superoxide dismutase, 60S acidic ribosomal p
19 t LSD1 and LOL1 have antagonistic effects on copper-zinc superoxide dismutase accumulation, consisten
20                                    Cytosolic copper zinc superoxide dismutase activity also increased
21 genic (Tg) rats with a five-fold increase in copper zinc superoxide dismutase activity.
22 l TH was not nitrated in mice overexpressing copper/zinc superoxide dismutase after MPTP administrati
23 tant for maintaining mitochondrial function (copper/zinc superoxide dismutase, aldehyde oxidase, and
24                            Subpopulations of copper-zinc superoxide dismutase also localize to mitoch
25                   Significant differences in copper zinc superoxide dismutase and catalase activities
26 rable with the level of protection seen with copper/zinc superoxide dismutase and the anti-apoptotic
27 regulation of one of its target genes, CSD2 (copper/zinc superoxide dismutase), and thereby helps pla
28 t abundant copper proteins, plastocyanin and copper/zinc superoxide dismutase, are found in chloropla
29 t is perhaps the most perplexing question in copper-zinc superoxide dismutase-associated familial ALS
30 metry at the active site of bovine and human copper,zinc-superoxide dismutases (bSOD1 and hSOD1) trea
31 sed (P<0.01) manganese superoxide-dismutase, copper-zinc superoxide-dismutase, catalase, and glutathi
32 d be found between cell growth and levels of copper/zinc superoxide dismutase, catalase, or glutathio
33 rophic lateral sclerosis-linked mutations in copper-zinc superoxide dismutase cause motor neuron deat
34                                 Mutations in copper-zinc superoxide dismutase cause the neurodegenera
35  for two genes encoding antioxidant enzymes, copper zinc superoxide dismutase (Cu/Zn SOD) and glutath
36  transgenic mice that under- or over-express copper, zinc superoxide dismutase (Cu,Zn-SOD; SOD-1).
37  space, which contains a recently identified copper, zinc superoxide dismutase (Cu,ZnSOD).
38                                              Copper,zinc superoxide dismutase (Cu,Zn-SOD) catalyzes t
39                                 Mutations of copper,zinc-superoxide dismutase (cu,zn SOD) are found i
40           H. ducreyi expresses a periplasmic copper-zinc superoxide dismutase (Cu, Zn SOD) that prote
41                                              Copper-zinc superoxide dismutase (Cu,ZnSOD) is the antio
42   Haemophilus ducreyi produces a periplasmic copper-zinc superoxide dismutase (Cu-Zn SOD), which is t
43 milies to mutations in the gene encoding for copper-zinc superoxide dismutase (Cu/Zn-SOD), a key enzy
44 riments showed a decrease in basal levels of copper/zinc superoxide dismutase (Cu/Zn SOD) and glutath
45                                              Copper/zinc superoxide dismutase (Cu/Zn SOD) is a first-
46 on basal activity of the antioxidant enzymes copper/zinc superoxide dismutase (Cu/Zn SOD), manganese
47                       Inclusion of exogenous copper/zinc superoxide dismutase (Cu/ZnSOD, 100 microg/m
48  manganese superoxide dismutase (Mn-SOD) and copper-zinc superoxide dismutase (CuZn-SOD) and of L-fer
49                                 Mutations in copper-zinc superoxide dismutase (CuZn-SOD) have been im
50                                              Copper-zinc superoxide dismutase (CuZn-SOD) is believed
51 ) that delivers copper to the active site of copper-zinc superoxide dismutase (CuZn-SOD, a product of
52  whether transgenic (Tg) mice overexpressing copper/zinc-superoxide dismutase (CuZn-SOD) are protecte
53                                              Copper zinc superoxide dismutase (CuZnSOD) is an essenti
54                                              Copper-zinc superoxide dismutase (CuZnSOD) acquires its
55                                 Mutations in copper-zinc superoxide dismutase (CuZnSOD) cause 25% of
56     The three-dimensional structure of yeast copper-zinc superoxide dismutase (CuZnSOD) has been dete
57                                  Deletion of copper-zinc superoxide dismutase (CuZnSOD) in Sod1(-/-)
58 er ion at the active site of human wild type copper-zinc superoxide dismutase (CuZnSOD) is essential
59 ction cycle is proposed for the mechanism of copper-zinc superoxide dismutase (CuZnSOD) that involves
60 imed to determine if the expression of human copper-zinc superoxide dismutase (CuZnSOD) within the lu
61      Manganese superoxide-dismutase (MnSOD), copper-zinc superoxide dismutase (CuZnSOD), and heme oxy
62                                Yeast lacking copper-zinc superoxide dismutase (CuZnSOD), manganese su
63 inherited mutations in the gene that encodes copper-zinc superoxide dismutase (CuZnSOD).
64 re due to lesions in SOD1, the gene encoding copper-zinc superoxide dismutase (CuZnSOD).
65 ieved to deliver copper ions specifically to copper-zinc superoxide dismutase (CuZnSOD).
66                                              Copper-zinc superoxide dismutase (CuZnSOD, SOD1 protein)
67          Mutations of the SOD1 gene encoding copper/zinc superoxide dismutase (CuZnSOD) cause an inhe
68                                              Copper/zinc superoxide dismutase (CuZnSOD; SOD1) is wide
69                                              Copper-zinc superoxide dismutases (CuZnSODs) are infrequ
70 lative amounts of copper-containing forms of copper-zinc superoxide dismutase (EC 1.15.1.1) from bovi
71               Mutations in the gene encoding copper/zinc superoxide dismutase enzyme produce an anima
72                       The down-regulation of copper/zinc superoxide dismutase expression in response
73  copper in native polyacrylamide gels of the copper-zinc superoxide dismutase from purified preparati
74           A series of mutant human and yeast copper-zinc superoxide dismutases has been prepared, wit
75 sistent with these findings, the activity of copper-zinc superoxide dismutase in these tissues was eq
76 n is essential for photo-autotrophic growth, copper/zinc superoxide dismutase is dispensable and in p
77  of the main free radical scavenging enzymes copper/zinc superoxide dismutase, manganese superoxide d
78                                              Copper/zinc superoxide dismutase, manganese superoxide d
79                             Mutations in the copper/zinc superoxide dismutase (mSOD1) gene are associ
80 motor neuron degeneration produced by mutant copper/zinc superoxide dismutase (mSOD1), the only prove
81               In addition, mice deficient in copper-zinc superoxide dismutase or cellular glutathione
82 ntified, of which five [i.e., alpha-amylase; copper zinc superoxide dismutase; protein disulfide isom
83                        Over 130 mutations to copper, zinc superoxide dismutase (SOD) are implicated i
84                                 Mutations in copper, zinc superoxide dismutase (SOD) have been implic
85                                 Mutations in copper,zinc-superoxide dismutase (SOD) have been implica
86 ies reported that H(2)O(2) is metabolized by copper,zinc-superoxide dismutase (SOD) to form (.)OH tha
87                                              Copper-zinc superoxide dismutase (SOD) is of fundamental
88 zable substrates, the peroxidase reaction of copper-zinc superoxide dismutase (SOD) oxidizes SOD itse
89 ant SV expressing the O-2 scavenging enzyme, copper/zinc superoxide dismutase (SOD), potentiates SV-i
90 oavailability to support the activity of the copper/zinc superoxide dismutase Sod1 and that loss of S
91 re associated with mutations in the gene for copper/zinc superoxide dismutase ( SOD1 ), which catalys
92 ite (NO2(-)) and nitrate (NO3(-)) ions using copper, zinc superoxide dismutase (SOD1) and nitrate red
93 for copper loading of the antioxidant enzyme copper, zinc superoxide dismutase (SOD1) by its partner
94 ALS) cases are due to known mutations in the copper, zinc superoxide dismutase (SOD1) gene.
95 sts for the increased peroxidase activity of copper, zinc superoxide dismutase (SOD1) in oxidant-indu
96                                              Copper, zinc superoxide dismutase (SOD1) is activated in
97 on (HCO(3)(-)) on the peroxidase activity of copper, zinc superoxide dismutase (SOD1) was investigate
98 ied out using antibodies against the enzymes copper, zinc superoxide dismutase (SOD1), or manganese s
99  of identified linkages in the gene encoding copper, zinc-superoxide dismutase (SOD1).
100 elivers the essential copper ion cofactor to copper,zinc superoxide dismutase (SOD1), a key enzyme in
101                                              Copper,zinc-superoxide dismutase (SOD1) was shown to be
102 peroxide dismutase (Ccs1) activates immature copper-zinc superoxide dismutase (Sod1) by delivering co
103         Mutations in the gene encoding human copper-zinc superoxide dismutase (SOD1) cause a dominant
104                           Mutations in human copper-zinc superoxide dismutase (SOD1) cause an inherit
105 ver 100 mutations in the gene encoding human copper-zinc superoxide dismutase (SOD1) cause an inherit
106               Mutations in the metalloenzyme copper-zinc superoxide dismutase (SOD1) cause one form o
107 e dissociation of apo- and metal-bound human copper-zinc superoxide dismutase (SOD1) dimers induced b
108                More than 90 mutations in the copper-zinc superoxide dismutase (SOD1) gene cause a sub
109 eral sclerosis (ALS)-linked mutations in the copper-zinc superoxide dismutase (SOD1) gene cause motor
110                               Aggregation of copper-zinc superoxide dismutase (SOD1) is a defining fe
111 eral sclerosis (fALS) caused by mutations in copper-zinc superoxide dismutase (SOD1) is characterized
112 ously shown that several familial ALS-linked copper-zinc superoxide dismutase (SOD1) mutants (A4V, G8
113                          We show that mutant copper-zinc superoxide dismutase (SOD1) overexpression i
114 eroxide can interact with the active site of copper-zinc superoxide dismutase (SOD1) to generate a po
115                                  Delivery of copper-zinc superoxide dismutase (SOD1), an efficient RO
116 o determine the misfolding pathway of mutant copper-zinc superoxide dismutase (SOD1), the protein kno
117 of bicarbonate on the peroxidase activity of copper-zinc superoxide dismutase (SOD1), using the nitri
118            In the course of studies on human copper-zinc superoxide dismutase (SOD1), we observed a m
119 binding to metal-free (apo) human and bovine copper-zinc superoxide dismutases (SOD1) were measured u
120                                 Mutations in copper/zinc superoxide dismutase (SOD1) are causative fo
121                        Yeast strains lacking copper/zinc superoxide dismutase (SOD1) are sensitive to
122 type (WT) and 14 different variants of human copper/zinc superoxide dismutase (SOD1) associated with
123 d that 14 biologically metallated mutants of copper/zinc superoxide dismutase (SOD1) associated with
124  cell death as a consequence of mutations in copper/zinc superoxide dismutase (SOD1) associated with
125  "cage"-like nano-formulation (nanozyme) for copper/Zinc superoxide dismutase (SOD1) by polyion conde
126 orted that oxidative damage in yeast lacking copper/zinc superoxide dismutase (SOD1) can be alleviate
127 city in Saccharomyces cerevisiae lacking the copper/zinc superoxide dismutase (SOD1) can be suppresse
128                                 Mutations in copper/zinc superoxide dismutase (SOD1) cause a subset o
129  At least 119 mutations in the gene encoding copper/zinc superoxide dismutase (SOD1) cause amyotrophi
130  90 different mutations in the gene encoding copper/zinc superoxide dismutase (SOD1) cause approximat
131             Yeast deficient in the cytosolic copper/zinc superoxide dismutase (SOD1) exhibit metaboli
132                             Mutations in the copper/zinc superoxide dismutase (SOD1) gene produce an
133 ts in the gene encoding the enzyme cytosolic copper/zinc superoxide dismutase (SOD1) have been report
134  mature animal, immature mice transgenic for copper/zinc superoxide dismutase (SOD1) have greater bra
135                                              Copper/zinc superoxide dismutase (SOD1) is an abundant i
136 onstrate here that the delivery of copper to copper/zinc superoxide dismutase (SOD1) is mediated thro
137      We have reported that overexpression of copper/zinc superoxide dismutase (SOD1) reduced superoxi
138      We have reported that overexpression of copper/zinc superoxide dismutase (SOD1) reduces apoptoti
139 tly inherited mutations in the gene encoding copper/zinc superoxide dismutase (SOD1) result in the fa
140                 The cDNA encoding the equine copper/zinc superoxide dismutase (SOD1) was cloned from
141  (ALS) is mutation in ubiquitously expressed copper/zinc superoxide dismutase (SOD1), but the mechani
142 copper into the essential antioxidant enzyme copper/zinc superoxide dismutase (SOD1).
143  using transgenic (Tg) mice that overexpress copper/zinc superoxide dismutase (SOD1).
144 ve previously shown that a fraction of yeast copper/zinc-superoxide dismutase (SOD1) and its copper c
145 urthermore, transgenic mice that overexpress copper/zinc-superoxide dismutase (SOD1) show decreased l
146  in the absence of any Pb-induced changes in copper/zinc-superoxide dismutase (SOD1), manganese-SOD (
147                                      Whereas copper, zinc-superoxide dismutase, SOD1, efficiently dis
148                                Yeast lacking copper-zinc superoxide dismutase (sod1Delta) show a prof
149 milial ALS (FALS) are caused by mutations of copper/zinc superoxide dismutase type 1.
150         Several of the ALS-associated mutant copper-zinc superoxide dismutases were also found to be
151 on of spheres, the association of the enzyme copper-zinc superoxide dismutase with superoxide anion,
152 structure, and intracellular localization of copper,zinc superoxide dismutase, with relevance to amyo

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