ライフサイエンスコーパス: copper-zinc superoxide dismutase

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 ound to contain ALS-associated mutations was copper/zinc superoxide dismutase 1 (SOD1), which is conf

17 The copper-zinc superoxide dismutase-1 (SOD1) is a highly st

18 Addition of copper-zinc superoxide dismutase (3,000 units/ml), which

19 constitutive ACHN proteins were identified: copper zinc superoxide dismutase, 60S acidic ribosomal p

20 t LSD1 and LOL1 have antagonistic effects on copper-zinc superoxide dismutase accumulation, consisten

21 Cytosolic copper zinc superoxide dismutase activity also increased

22 genic (Tg) rats with a five-fold increase in copper zinc superoxide dismutase activity.

23 l TH was not nitrated in mice overexpressing copper/zinc superoxide dismutase after MPTP administrati

24 tant for maintaining mitochondrial function (copper/zinc superoxide dismutase, aldehyde oxidase, and

25 Subpopulations of copper-zinc superoxide dismutase also localize to mitoch

26 Significant differences in copper zinc superoxide dismutase and catalase activities

27 rable with the level of protection seen with copper/zinc superoxide dismutase and the anti-apoptotic

28 regulation of one of its target genes, CSD2 (copper/zinc superoxide dismutase), and thereby helps pla

29 t abundant copper proteins, plastocyanin and copper/zinc superoxide dismutase, are found in chloropla

30 t is perhaps the most perplexing question in copper-zinc superoxide dismutase-associated familial ALS

31 metry at the active site of bovine and human copper,zinc-superoxide dismutases (bSOD1 and hSOD1) trea

32 sed (P<0.01) manganese superoxide-dismutase, copper-zinc superoxide-dismutase, catalase, and glutathi

33 d be found between cell growth and levels of copper/zinc superoxide dismutase, catalase, or glutathio

34 rophic lateral sclerosis-linked mutations in copper-zinc superoxide dismutase cause motor neuron deat

35 Mutations in copper-zinc superoxide dismutase cause the neurodegenera

36 for two genes encoding antioxidant enzymes, copper zinc superoxide dismutase (Cu/Zn SOD) and glutath

37 transgenic mice that under- or over-express copper, zinc superoxide dismutase (Cu,Zn-SOD; SOD-1).

38 space, which contains a recently identified copper, zinc superoxide dismutase (Cu,ZnSOD).

39 Copper,zinc superoxide dismutase (Cu,Zn-SOD) catalyzes t

40 Mutations of copper,zinc-superoxide dismutase (cu,zn SOD) are found i

41 H. ducreyi expresses a periplasmic copper-zinc superoxide dismutase (Cu, Zn SOD) that prote

42 Copper-zinc superoxide dismutase (Cu,ZnSOD) is the antio

43 Haemophilus ducreyi produces a periplasmic copper-zinc superoxide dismutase (Cu-Zn SOD), which is t

44 milies to mutations in the gene encoding for copper-zinc superoxide dismutase (Cu/Zn-SOD), a key enzy

45 riments showed a decrease in basal levels of copper/zinc superoxide dismutase (Cu/Zn SOD) and glutath

46 Copper/zinc superoxide dismutase (Cu/Zn SOD) is a first-

47 on basal activity of the antioxidant enzymes copper/zinc superoxide dismutase (Cu/Zn SOD), manganese

48 Inclusion of exogenous copper/zinc superoxide dismutase (Cu/ZnSOD, 100 microg/m

49 manganese superoxide dismutase (Mn-SOD) and copper-zinc superoxide dismutase (CuZn-SOD) and of L-fer

50 Mutations in copper-zinc superoxide dismutase (CuZn-SOD) have been im

51 Copper-zinc superoxide dismutase (CuZn-SOD) is believed

52 ) that delivers copper to the active site of copper-zinc superoxide dismutase (CuZn-SOD, a product of

53 whether transgenic (Tg) mice overexpressing copper/zinc-superoxide dismutase (CuZn-SOD) are protecte

54 Copper zinc superoxide dismutase (CuZnSOD) is an essenti

55 Copper-zinc superoxide dismutase (CuZnSOD) acquires its

56 Mutations in copper-zinc superoxide dismutase (CuZnSOD) cause 25% of

57 The three-dimensional structure of yeast copper-zinc superoxide dismutase (CuZnSOD) has been dete

58 Deletion of copper-zinc superoxide dismutase (CuZnSOD) in Sod1(-/-)

59 er ion at the active site of human wild type copper-zinc superoxide dismutase (CuZnSOD) is essential

60 ction cycle is proposed for the mechanism of copper-zinc superoxide dismutase (CuZnSOD) that involves

61 imed to determine if the expression of human copper-zinc superoxide dismutase (CuZnSOD) within the lu

62 Manganese superoxide-dismutase (MnSOD), copper-zinc superoxide dismutase (CuZnSOD), and heme oxy

63 Yeast lacking copper-zinc superoxide dismutase (CuZnSOD), manganese su

64 inherited mutations in the gene that encodes copper-zinc superoxide dismutase (CuZnSOD).

65 re due to lesions in SOD1, the gene encoding copper-zinc superoxide dismutase (CuZnSOD).

66 ieved to deliver copper ions specifically to copper-zinc superoxide dismutase (CuZnSOD).

67 Copper-zinc superoxide dismutase (CuZnSOD, SOD1 protein)

68 Mutations of the SOD1 gene encoding copper/zinc superoxide dismutase (CuZnSOD) cause an inhe

69 Copper/zinc superoxide dismutase (CuZnSOD; SOD1) is wide

70 Copper-zinc superoxide dismutases (CuZnSODs) are infrequ

71 lative amounts of copper-containing forms of copper-zinc superoxide dismutase (EC 1.15.1.1) from bovi

72 Mutations in the gene encoding copper/zinc superoxide dismutase enzyme produce an anima

73 The down-regulation of copper/zinc superoxide dismutase expression in response

74 copper in native polyacrylamide gels of the copper-zinc superoxide dismutase from purified preparati

75 A series of mutant human and yeast copper-zinc superoxide dismutases has been prepared, wit

76 sistent with these findings, the activity of copper-zinc superoxide dismutase in these tissues was eq

77 n is essential for photo-autotrophic growth, copper/zinc superoxide dismutase is dispensable and in p

78 of the main free radical scavenging enzymes copper/zinc superoxide dismutase, manganese superoxide d

79 Copper/zinc superoxide dismutase, manganese superoxide d

80 Mutations in the copper/zinc superoxide dismutase (mSOD1) gene are associ

81 motor neuron degeneration produced by mutant copper/zinc superoxide dismutase (mSOD1), the only prove

82 In addition, mice deficient in copper-zinc superoxide dismutase or cellular glutathione

83 ntified, of which five [i.e., alpha-amylase; copper zinc superoxide dismutase; protein disulfide isom

84 Over 130 mutations to copper, zinc superoxide dismutase (SOD) are implicated i

85 Mutations in copper, zinc superoxide dismutase (SOD) have been implic

86 Mutations in copper,zinc-superoxide dismutase (SOD) have been implica

87 ies reported that H(2)O(2) is metabolized by copper,zinc-superoxide dismutase (SOD) to form (.)OH tha

88 Copper-zinc superoxide dismutase (SOD) is of fundamental

89 zable substrates, the peroxidase reaction of copper-zinc superoxide dismutase (SOD) oxidizes SOD itse

90 se-mediated increases of antioxidants (i.e., copper/zinc superoxide dismutase (SOD) and extracellular

91 Copper/zinc superoxide dismutase (SOD) is a homodimeric

92 ant SV expressing the O-2 scavenging enzyme, copper/zinc superoxide dismutase (SOD), potentiates SV-i

93 oavailability to support the activity of the copper/zinc superoxide dismutase Sod1 and that loss of S

94 re associated with mutations in the gene for copper/zinc superoxide dismutase ( SOD1 ), which catalys

95 ite (NO2(-)) and nitrate (NO3(-)) ions using copper, zinc superoxide dismutase (SOD1) and nitrate red

96 for copper loading of the antioxidant enzyme copper, zinc superoxide dismutase (SOD1) by its partner

97 ALS) cases are due to known mutations in the copper, zinc superoxide dismutase (SOD1) gene.

98 sts for the increased peroxidase activity of copper, zinc superoxide dismutase (SOD1) in oxidant-indu

99 Copper, zinc superoxide dismutase (SOD1) is activated in

100 on (HCO(3)(-)) on the peroxidase activity of copper, zinc superoxide dismutase (SOD1) was investigate

101 ied out using antibodies against the enzymes copper, zinc superoxide dismutase (SOD1), or manganese s

102 of identified linkages in the gene encoding copper, zinc-superoxide dismutase (SOD1).

103 elivers the essential copper ion cofactor to copper,zinc superoxide dismutase (SOD1), a key enzyme in

104 Copper,zinc-superoxide dismutase (SOD1) was shown to be

105 peroxide dismutase (Ccs1) activates immature copper-zinc superoxide dismutase (Sod1) by delivering co

106 Mutations in the gene encoding human copper-zinc superoxide dismutase (SOD1) cause a dominant

107 Mutations in human copper-zinc superoxide dismutase (SOD1) cause an inherit

108 ver 100 mutations in the gene encoding human copper-zinc superoxide dismutase (SOD1) cause an inherit

109 Mutations in the metalloenzyme copper-zinc superoxide dismutase (SOD1) cause one form o

110 e dissociation of apo- and metal-bound human copper-zinc superoxide dismutase (SOD1) dimers induced b

111 More than 90 mutations in the copper-zinc superoxide dismutase (SOD1) gene cause a sub

112 eral sclerosis (ALS)-linked mutations in the copper-zinc superoxide dismutase (SOD1) gene cause motor

113 Aggregation of copper-zinc superoxide dismutase (SOD1) is a defining fe

114 eral sclerosis (fALS) caused by mutations in copper-zinc superoxide dismutase (SOD1) is characterized

115 ously shown that several familial ALS-linked copper-zinc superoxide dismutase (SOD1) mutants (A4V, G8

116 We show that mutant copper-zinc superoxide dismutase (SOD1) overexpression i

117 s to analyze the endogenous metal content of copper-zinc superoxide dismutase (SOD1) purified from mi

118 eroxide can interact with the active site of copper-zinc superoxide dismutase (SOD1) to generate a po

119 Delivery of copper-zinc superoxide dismutase (SOD1), an efficient RO

120 o determine the misfolding pathway of mutant copper-zinc superoxide dismutase (SOD1), the protein kno

121 of bicarbonate on the peroxidase activity of copper-zinc superoxide dismutase (SOD1), using the nitri

122 In the course of studies on human copper-zinc superoxide dismutase (SOD1), we observed a m

123 is caused by mutations in the metallo-enzyme copper-zinc superoxide dismutase (SOD1).

124 binding to metal-free (apo) human and bovine copper-zinc superoxide dismutases (SOD1) were measured u

125 Mutations in copper/zinc superoxide dismutase (SOD1) are causative fo

126 Yeast strains lacking copper/zinc superoxide dismutase (SOD1) are sensitive to

127 type (WT) and 14 different variants of human copper/zinc superoxide dismutase (SOD1) associated with

128 d that 14 biologically metallated mutants of copper/zinc superoxide dismutase (SOD1) associated with

129 cell death as a consequence of mutations in copper/zinc superoxide dismutase (SOD1) associated with

130 "cage"-like nano-formulation (nanozyme) for copper/Zinc superoxide dismutase (SOD1) by polyion conde

131 orted that oxidative damage in yeast lacking copper/zinc superoxide dismutase (SOD1) can be alleviate

132 city in Saccharomyces cerevisiae lacking the copper/zinc superoxide dismutase (SOD1) can be suppresse

133 Mutations in copper/zinc superoxide dismutase (SOD1) cause a subset o

134 At least 119 mutations in the gene encoding copper/zinc superoxide dismutase (SOD1) cause amyotrophi

135 90 different mutations in the gene encoding copper/zinc superoxide dismutase (SOD1) cause approximat

136 Yeast deficient in the cytosolic copper/zinc superoxide dismutase (SOD1) exhibit metaboli

137 Mutations in the copper/zinc superoxide dismutase (SOD1) gene produce an

138 ts in the gene encoding the enzyme cytosolic copper/zinc superoxide dismutase (SOD1) have been report

139 mature animal, immature mice transgenic for copper/zinc superoxide dismutase (SOD1) have greater bra

140 Copper/zinc superoxide dismutase (SOD1) is an abundant i

141 onstrate here that the delivery of copper to copper/zinc superoxide dismutase (SOD1) is mediated thro

142 We have reported that overexpression of copper/zinc superoxide dismutase (SOD1) reduced superoxi

143 We have reported that overexpression of copper/zinc superoxide dismutase (SOD1) reduces apoptoti

144 tly inherited mutations in the gene encoding copper/zinc superoxide dismutase (SOD1) result in the fa

145 The cDNA encoding the equine copper/zinc superoxide dismutase (SOD1) was cloned from

146 (ALS) is mutation in ubiquitously expressed copper/zinc superoxide dismutase (SOD1), but the mechani

147 copper into the essential antioxidant enzyme copper/zinc superoxide dismutase (SOD1).

148 using transgenic (Tg) mice that overexpress copper/zinc superoxide dismutase (SOD1).

149 ve previously shown that a fraction of yeast copper/zinc-superoxide dismutase (SOD1) and its copper c

150 urthermore, transgenic mice that overexpress copper/zinc-superoxide dismutase (SOD1) show decreased l

151 in the absence of any Pb-induced changes in copper/zinc-superoxide dismutase (SOD1), manganese-SOD (

152 Whereas copper, zinc-superoxide dismutase, SOD1, efficiently dis

153 Yeast lacking copper-zinc superoxide dismutase (sod1Delta) show a prof

154 milial ALS (FALS) are caused by mutations of copper/zinc superoxide dismutase type 1.

155 Several of the ALS-associated mutant copper-zinc superoxide dismutases were also found to be

156 on of spheres, the association of the enzyme copper-zinc superoxide dismutase with superoxide anion,

157 structure, and intracellular localization of copper,zinc superoxide dismutase, with relevance to amyo