ライフサイエンスコーパス: antichymotrypsin

1 ytokine signaling-3, lipocalin-2, and alpha1-antichymotrypsin.

2 tors, alpha1-proteinase inhibitor and alpha1-antichymotrypsin.

3 ed for variants in coding regions of alpha-1-antichymotrypsin.

4 to detect genes for alpha(1)-antitrypsin and antichymotrypsin.

5 ing of the product identified it as alpha(1)-antichymotrypsin.

6 complex with the protease inhibitor, alpha-1-antichymotrypsin.

7 with the serine protease inhibitor alpha(1)-antichymotrypsin.(1,2) However, it is unknown whether th

8 raised concentrations (16% higher for alpha1-antichymotrypsin, 18% for alpha1-acid-glycoprotein, 25%

9 GR/MYOC, a serine protease inhibitor (alpha1-antichymotrypsin), a neuroprotective factor (pigment epi

10 n G can also be completely blocked by alpha1 antichymotrypsin, a specific inhibitor of chymotrypsin-l

11 alpha1-Antichymotrypsin (AACT) is a major component of the amyl

12 rticosteroid-binding globulin (CBG), alpha 1-antichymotrypsin (AACT), and protein C inhibitor (PCI) a

13 rations of two acute-phase proteins, alpha 1-antichymotrypsin (ACT) and alpha 2-macroglobulin (MAC),

14 ition of human chymase by the serpins alpha1-antichymotrypsin (ACT) and alpha1-proteinase inhibitor (

15 ursor protein (APP), A beta protein, alpha 1-antichymotrypsin (ACT) and ubiquitin.

16 based on immunochemical detection of alpha1-antichymotrypsin (ACT) in amyloid plaques from the hippo

17 alpha-1-Antichymotrypsin (ACT) is present in neuritic plaques in

18 cs identified significant changes in alpha-1-antichymotrypsin (ACT) levels during LVAD support.

19 14q32.1 allow a single gene encoding alpha1-antichymotrypsin (ACT) to be expressed in astrocytes and

20 logue HTJ1 and its interaction with alpha(1)-antichymotrypsin (ACT), a member of the serine proteinas

21 Additionally, alpha1-antichymotrypsin (ACT), a serpin family inhibitor tightl

22 astase (HNE) could be transferred to alpha-1-antichymotrypsin (ACT), a serpin that does not inhibit H

23 Alpha(1)-antichymotrypsin (ACT), an acute-phase inflammatory prot

24 agment deposition, reactive gliosis, alpha-1-antichymotrypsin (ACT), and apolipoprotein E (APOE).

25 hat are known to interact with Abeta: alpha1-antichymotrypsin (ACT), interleukin-1beta (IL-1beta), S1

26 rine proteinase inhibitor (serpin), alpha(1)-antichymotrypsin (ACT), is encoded by a gene located wit

27 erine proteinase inhibitor (serpin) alpha(1)-antichymotrypsin (ACT), which is the dominant form of PS

28 chromosome 14, presenilin 1 (PS1) and alpha1-antichymotrypsin (ACT), with the risk of sporadic Alzhei

29 ein is the serine protease inhibitor alpha-1-antichymotrypsin (ACT).

30 Chtr within the complex that Chtr forms with antichymotrypsin (ACT).

31 cently we presented evidence that the serpin antichymotrypsin (ACT, I) reacts with the serine protein

32 rams/L), and the acute-phase protein alpha 1-antichymotrypsin (ACT; 0.06 g/L).

33 Then we determined that alpha-1-antichymotrypsin (alpha-ACT), an acute-phase factor abun

34 between granzyme M and the serpins alpha(1)-antichymotrypsin, alpha(1)-proteinase inhibitor, and pro

35 liver, including alpha1-antitrypsin, alpha1-antichymotrypsin, alpha-fetal protein, ceruloplasmin, IG

36 H dependence of the conversion of the alpha1-antichymotrypsin.alpha-chymotrypsin encounter complex, E

37 alpha1-Antichymotrypsin (alpha1-ACT), a member of the serpin fa

38 und by protease inhibitors, primarily alpha1-antichymotrypsin, although a fraction is inactivated in

39 tified as the C-terminal fragment of alpha-1 antichymotrypsin and a 28 kDa protein was determined as

40 lerated by seeding with polymers of alpha(1)-antichymotrypsin and a complex of alpha(1)-antichymotryp

41 d induces transcription through the alpha(1)-antichymotrypsin and C-reactive protein promoter.

42 lobin, but stimulates production of alpha(1)-antichymotrypsin and induces transcription through the a

43 response modifier A, and the human serpins, antichymotrypsin and squamous cell carcinoma antigen 1 (

44 otects cathepsin G from inhibition by alpha1-antichymotrypsin and squamous cell carcinoma antigen 2 a

45 the distance between residue P1' in alpha(1)-antichymotrypsin and the amino terminus of chymotrypsin

46 o be alpha(1)-proteinase inhibitor, alpha(1)-antichymotrypsin, and alpha(2)-macroglobulin.

47 hibitors alpha1-proteinase inhibitor, alpha1-antichymotrypsin, and alpha2-macroglobulin function as c

48 ions of antithrombin, C1 inhibitor, alpha(1)-antichymotrypsin, and heparin cofactor II cause a simila

49 etory leukocyte protease inhibitor, alpha(1)-antichymotrypsin, and monocyte-neutrophil elastase inhib

50 her proteins (such as antithrombin, alpha(1)-antichymotrypsin, and plasminogen activator inhibitor-1)

51 , cyclin D3, tissue transglutaminase, alpha1-antichymotrypsin, and STAT1), which have not previously

52 rongly for desmin, alphaB-crystallin, alpha1-antichymotrypsin, and ubiquitin and variably for gelsoli

53 alphaB-crystallin, SLIM1, gelsolin, alpha(1)-antichymotrypsin, and ubiquitin.

54 Together alpha-1 antichymotrypsin, Apo A1, and the unidentified 5191 Da p

55 protease inhibitors alpha(1)-antitrypsin and antichymotrypsin are present in human milk, but little i

56 esults suggest that alpha(1)-antitrypsin and antichymotrypsin are produced by the mammary gland and a

57 t derivatives of cysteine variants of alpha1-antichymotrypsin at the P11 and P13 residues.

58 , alpha(1)-acid glycoprotein (AGP), alpha(1)-antichymotrypsin, C-reactive protein (CRP), haptoglobin,

59 e proteins (alpha1-acid-glycoprotein, alpha1-antichymotrypsin, C-reactive protein, or serum amyloid A

60 prostate specific antigen (PSA), PSA-alpha1-antichymotrypsin, carcinoembryonic antigen and mucin-1,

61 h endopin 1 possesses homology with alpha(1)-antichymotrypsin, chymotrypsin was not inhibited.

62 Alpha(1)-antitrypsin and antichymotrypsin concentrations were high in early milk

63 alpha(1)-Antitrypsin and antichymotrypsin concentrations were measured in milk sa

64 mbin, beta amyloid precursor protein, alpha1-antichymotrypsin, cystic fibrosis transmembrane conducta

65 psin with a fluorescent derivative of alpha1-antichymotrypsin (derivatized at position P7 of the reac

66 active site (Leu-358) of the serpin alpha(1)-antichymotrypsin either one residue closer (P2) or furth

67 The recombinant PSA was inhibited by alpha1-antichymotrypsin, forming an equimolar complex with a mo

68 We show here that wildtype alpha(1)-antichymotrypsin forms polymers between the reactive cen

69 whether the increased expression of alpha(1)-antichymotrypsin found in AD brains counteracts or contr

70 ic protein gene(3) to express human alpha(1)-antichymotrypsin (hACT) in astrocytes of transgenic mice

71 The mean concentration of alpha(1)-antichymotrypsin in human plasma is 7 micrometer.

72 y be important in the deposition of alpha(1)-antichymotrypsin in the plaques of Alzheimer's disease.

73 on, we report the crystal structure of A349R antichymotrypsin in the reactive loop cleaved state at 2

74 At this concentration, alpha(1)-antichymotrypsin inhibits both macrophage enzymes.

75 alpha(1)-Antichymotrypsin is a member of the serine proteinase in

76 Alpha(1)-antichymotrypsin is an acute phase plasma protein and a

77 An alpha1-antichymotrypsin-like serpin has been implicated in Alzh

78 n hypothesized that alpha(1)-antitrypsin and antichymotrypsin may modulate digestion in the infant gu

79 ary gland expresses alpha(1)-antitrypsin and antichymotrypsin, measured alpha(1)-antitrypsin and anti

80 but not with reactive loop cleaved alpha(1)-antichymotrypsin or with polymers of other members of th

81 given cathepsin G/chymase inhibitors (alpha1-antichymotrypsin or Z-Gly-Leu-Phe-CH(2)Cl), were resista

82 Sonication of alpha(1)-antichymotrypsin polymers markedly increased the efficac

83 he structures of native ovalbumin and native antichymotrypsin, suggest that heparin may activate anti

84 we did not correlate any variants of alpha-1-antichymotrypsin, the human homologue of Spi2a, with acu

85 motrypsin, measured alpha(1)-antitrypsin and antichymotrypsin throughout lactation, assessed the resi

86 disassembly of myocardial proteins (alpha(1)-antichymotrypsin, ubiquitin, and gelsolin); (3) genes in

87 formation from alpha-chymotrypsin and alpha1-antichymotrypsin using two approaches: first, by stopped

88 alpha(1)-Antichymotrypsin variants were produced by mutation with

89 Alpha1-antichymotrypsin was a markedly ineffective inhibitor of

90 Abeta of another acute phase protein, alpha1-antichymotrypsin, was not active in preventing fibril fo

91 All APPs, except alpha(1)-antichymotrypsin, were significantly correlated with spl

92 so is inactivated more effectively by alpha1-antichymotrypsin, which features P1 Leu in the reactive

93 e inhibitors alpha-1-antitrypsin and alpha-1-antichymotrypsin, which may function as antimicrobials a

94 )-antichymotrypsin and a complex of alpha(1)-antichymotrypsin with an exogenous reactive loop peptide

95 other isoforms of endopins related to alpha1-antichymotrypsin, yet endopin 2C differs in its target p