ライフサイエンスコーパス: SH group

1 iginating from the oxidation of the cysteine SH group.

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

3 nol caused a significant decrease of protein SH groups.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

50 -5-maleimide) as a label for the cytoplasmic SH groups on band 3 (AE1), combined with data showing th

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

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

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

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

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

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

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

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

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

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

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

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

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

64 Titration of SH groups was strongly inhibited by carboxymethylation a

65 The SH groups were oxidized to disulphide bonds when higher

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

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

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

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

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