ライフサイエンスコーパス: SH group

1 s without structural heart disease (SHD) (no-SHD group).

2 iginating from the oxidation of the cysteine SH group.

3 cific bond of the probe with the accessible -SH groups.

4 is sensitive to redox modifications of its -SH groups.

5 nol caused a significant decrease of protein SH groups.

6 ily, appear to contain such redox-sensitive -SH groups.

7 other reactions of their thiol (sulfhydryl; -SH) groups.

8 nitrobenzoate) (DTNB)-titratable sulfhydryl (SH) groups.

9 Lipid lesions were increased in both SHS groups (54+/-5% [SEM] aorta and 66+/-4% pulmonary ar

10 n the presence of high concentrations of the SH group alkylating agent, N-ethylmaleimide, suggested t

11 Age among the SH group and BPRS-E affect-anxiety subscale among the V

12 t not alphaB-crystallin, which is devoid of -SH groups and thus does not participate in disulfide cro

13 duced Voc-T in the T7X group compared to the Sh group, and subsequent bilateral vagotomy abolished bo

14 Two -SH groups are titrated in the native form of the mitocho

15 That the irradiated GR showed de novo formed SH groups argues that UVA photolysis of GR leads to the

16 lation and KMnO4, suggesting the presence of SH groups at the active site(s).

17 in the microenvironment of the protein, some SH groups become more easily titratable, and at pH 9.0 t

18 d against heat treatment likely because free SH groups blocked by H(2)O(2).

19 Introducing free SH groups by adding 13.8 mumol glutathione/g protein inc

20 T is sensitive to redox modifications of its SH groups by reactive nitrogen species.

21 The -OMe and -SH groups cause a similar but smaller effect, whereas -O

22 um, electrophoretic mobility, and number of -SH groups comparable to those shown by control hemoglobi

23 n were detected in the HIF-1alpha-stabilized SHED group compared with the control SHED.

24 products (AOPP) content, total sulfhydryl (-SH) groups content, the activity of superoxide dismutase

25 The remaining seven inaccessible SH groups could be titrated only in the presence of 8 M

26 e glycoprotein was reduced with Bu3P and the SH groups covalently blocked with ABD-F, and the resulti

27 re (PTP) induced by either oxidative stress, SH group cross-linking, or high Ca2+ load, suggesting th

28 CaCY with the SH group either reduced, blocked or oxidized stays as a

29 as also been reported that NO reacts with ---SH groups, forming S-nitrosothiols.

30 imately = S atom in SCH(3) group > H atom in SH group > H atom in CH group > aromatic side chain > S

31 n CH group > aromatic side chain > S atom in SH group > NH(2) in side chain > N-terminal NH(2) > COOH

32 ctivates TPH by selective action on critical SH groups (i.e., cysteine residues) while sparing cataly

33 carrying the crosslinked moiety with a free SH group; (iii) adduct formation of the latter with the

34 ment with the expected pK(a) change for the -SH group in the presence of the metal.

35 Removal of free SH groups in glutenin by adding 2.3 mumol KBrO3 or KIO3

36 Therefore, S-nitrosylation of critical ---SH groups in GR by NO with consequent decreases in bindi

37 All SH groups in the cysteine residues are free, and the GIF

38 tudy highlights the necessity of sulfhydryl (SH) groups in maintaining the structural integrity of th

39 Mercapto (-SH) groups in these ligands interact with cationic metal

40 During the sol-gel transition the -SH groups initially present in the protein system decrea

41 During the sol-gel transition the -SH groups initially present in the protein system decrea

42 lete inhibition of activity, while only one -SH group is titrated in the cytosolic enzyme with no eff

43 bined with data showing that the cytoplasmic SH groups lie about 40 A from the cytoplasmic surface of

44 TLSB was formed by using -SH group-modified lignocellulose as a raw material, whic

45 eased from 4065.7 +/- 136.7 and 89.3 +/- 1.2 SH groups (mumol/g) to 31483.6 +/- 342.7 and 119.5 +/- 3

46 ol/g) to 31483.6 +/- 342.7 and 119.5 +/- 3.7 SH groups (mumol/g), respectively.

47 o conducted studies on the reactivity of the SH group of beta93Cys (a residue located in the region o

48 ribozymes that attack biotinyl-AMP using the SH group of CoA.

49 ll recombination activity indicates that the SH group of Cys-25 does not provide any critical contact

50 Carboxymethylation of the SH group of Cys-60 in the molecule resulted in the gener

51 However, the SH group of Cys75 of the intermediates was not modified

52 The reagent is attached to the SH group of cytoplasmic monocysteine rhodopsin mutants b

53 During editing, the side chain -SH group of homocysteine reacts with its activated carbo

54 at elevated temperatures indicate that the -SH group of N-acetylcysteine enhances the rate of its hy

55 ethiolsulfonate (SLMTS) is reacted with the -SH groups of cysteinyl residues incorporated into a prot

56 AgNPs have been immobilized on SH groups of GQDs via bonding formation of Ag-S and anti

57 into the fingers nor the modification of the SH groups of these residues with photoaffinity cross-lin

58 ather weak hydrogen bond between the thiol (-SH) group of cysteine and its first neighbor water molec

59 face hydrophobicity and reactive sulfhydryl (SH) groups of OVA samples significantly increased from 4

60 method for determination of free sulphydryl (SH) groups of wheat gluten performed with previous glute

61 -5-maleimide) as a label for the cytoplasmic SH groups on band 3 (AE1), combined with data showing th

62 olecule, Alexa-maleimide, to free (reduced) -SH groups on proteins or other molecules exposed on the

63 ation, apparently because it interacts with -SH groups on tubulin.

64 it microtubule assembly by interacting with -SH groups on tubulin.

65 ication of proteins by addition of a thiol (-SH) group onto reactive cysteine residues: a process kno

66 Aggregate formation was due to SH-group oxidation as the monomeric form of CnA was reco

67 higher in the RA and OPR groups than in the SH group (P <0.05).

68 y higher in the RA group than in the OPR and SH groups (P <0.05).

69 are probably over 63 A from the cytoplasmic SH groups, placing them near the middle or the external

70 In the native enzyme 1.0 SH group readily reacted with DTNB with no detectable lo

71 This -SH group serves as a proton donor, is responsible for th

72 emoglobin were significantly higher in the 2 SHS groups than the control group (P<0.001).

73 Compared with the no-SHD group, the COA+BAV subgroup had larger aortic root d

74 thylmaleimide blockade of maleimide-reactive SH groups, then reduction and fluorescein 5-maleimide la

75 Conversion of the Cys10 SH group to a mixed disulfide with the amino acid Cys, t

76 The conserved Cys47-SH group was shown to be the site of oxidation by H2O2.

77 Titration of SH groups was strongly inhibited by carboxymethylation a

78 The SH groups were oxidized to disulphide bonds when higher

79 for age, gender, and prescription drug use (SH group with 5 or more episodes vs control: -1.03 [95%

80 d to nonpainful stimuli, similarly adjusted (SH group with 5 or more episodes vs control: -1.73; 95%

81 Titration of -SH groups with 5,5'-dithiobis(2-nitrobenzoic acid) sugge

82 d that relies on mass-labeling of accessible SH groups with a large SH reagent, methoxy-polyethylene

83 Titration of the next 3.0 SH groups with DTNB resulted in a loss of activity of mo

84 me caused the increase in the amount of free SH groups, with more dynamic changes at 37 degrees C.

85 hotolysis caused the formation of additional SH groups within the enzyme, as shown by the incorporati