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1 tors, alpha1-proteinase inhibitor and alpha1-antichymotrypsin.
2 ytokine signaling-3, lipocalin-2, and alpha1-antichymotrypsin.
3 to detect genes for alpha(1)-antitrypsin and antichymotrypsin.
4 ing of the product identified it as alpha(1)-antichymotrypsin.
5 ed for variants in coding regions of 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
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 (
16 based on immunochemical detection of alpha1-antichymotrypsin (ACT) in amyloid plaques from the hippo
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
22 astase (HNE) could be transferred to alpha-1-antichymotrypsin (ACT), a serpin that does not inhibit H
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
31 cently we presented evidence that the serpin antichymotrypsin (ACT, I) reacts with the serine protein
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 receptor 2 (sTNFR2) (0.354, p<0.005), alpha1-antichymotrypsin (alpha1-ACT) (1.217, p<0.005), IL-1beta
40 und by protease inhibitors, primarily alpha1-antichymotrypsin, although a fraction is inactivated in
41 tified as the C-terminal fragment of alpha-1 antichymotrypsin and a 28 kDa protein was determined as
42 lerated by seeding with polymers of alpha(1)-antichymotrypsin and a complex of alpha(1)-antichymotryp
44 lobin, but stimulates production of alpha(1)-antichymotrypsin and induces transcription through the a
45 response modifier A, and the human serpins, antichymotrypsin and squamous cell carcinoma antigen 1 (
46 otects cathepsin G from inhibition by alpha1-antichymotrypsin and squamous cell carcinoma antigen 2 a
47 the distance between residue P1' in alpha(1)-antichymotrypsin and the amino terminus of chymotrypsin
49 hibitors alpha1-proteinase inhibitor, alpha1-antichymotrypsin, and alpha2-macroglobulin function as c
50 ions of antithrombin, C1 inhibitor, alpha(1)-antichymotrypsin, and heparin cofactor II cause a simila
51 etory leukocyte protease inhibitor, alpha(1)-antichymotrypsin, and monocyte-neutrophil elastase inhib
52 her proteins (such as antithrombin, alpha(1)-antichymotrypsin, and plasminogen activator inhibitor-1)
53 , cyclin D3, tissue transglutaminase, alpha1-antichymotrypsin, and STAT1), which have not previously
54 rongly for desmin, alphaB-crystallin, alpha1-antichymotrypsin, and ubiquitin and variably for gelsoli
57 protease inhibitors alpha(1)-antitrypsin and antichymotrypsin are present in human milk, but little i
58 esults suggest that alpha(1)-antitrypsin and antichymotrypsin are produced by the mammary gland and a
60 , alpha(1)-acid glycoprotein (AGP), alpha(1)-antichymotrypsin, C-reactive protein (CRP), haptoglobin,
61 e proteins (alpha1-acid-glycoprotein, alpha1-antichymotrypsin, C-reactive protein, or serum amyloid A
62 prostate specific antigen (PSA), PSA-alpha1-antichymotrypsin, carcinoembryonic antigen and mucin-1,
67 mbin, beta amyloid precursor protein, alpha1-antichymotrypsin, cystic fibrosis transmembrane conducta
68 psin with a fluorescent derivative of alpha1-antichymotrypsin (derivatized at position P7 of the reac
69 active site (Leu-358) of the serpin alpha(1)-antichymotrypsin either one residue closer (P2) or furth
71 The recombinant PSA was inhibited by alpha1-antichymotrypsin, forming an equimolar complex with a mo
73 whether the increased expression of alpha(1)-antichymotrypsin found in AD brains counteracts or contr
74 ic protein gene(3) to express human alpha(1)-antichymotrypsin (hACT) in astrocytes of transgenic mice
76 y be important in the deposition of alpha(1)-antichymotrypsin in the plaques of Alzheimer's disease.
77 on, we report the crystal structure of A349R antichymotrypsin in the reactive loop cleaved state at 2
82 n hypothesized that alpha(1)-antitrypsin and antichymotrypsin may modulate digestion in the infant gu
83 ary gland expresses alpha(1)-antitrypsin and antichymotrypsin, measured alpha(1)-antitrypsin and anti
84 but not with reactive loop cleaved alpha(1)-antichymotrypsin or with polymers of other members of th
85 given cathepsin G/chymase inhibitors (alpha1-antichymotrypsin or Z-Gly-Leu-Phe-CH(2)Cl), were resista
87 he structures of native ovalbumin and native antichymotrypsin, suggest that heparin may activate anti
88 we did not correlate any variants of alpha-1-antichymotrypsin, the human homologue of Spi2a, with acu
89 motrypsin, measured alpha(1)-antitrypsin and antichymotrypsin throughout lactation, assessed the resi
90 disassembly of myocardial proteins (alpha(1)-antichymotrypsin, ubiquitin, and gelsolin); (3) genes in
91 formation from alpha-chymotrypsin and alpha1-antichymotrypsin using two approaches: first, by stopped
94 Abeta of another acute phase protein, alpha1-antichymotrypsin, was not active in preventing fibril fo
96 so is inactivated more effectively by alpha1-antichymotrypsin, which features P1 Leu in the reactive
97 e inhibitors alpha-1-antitrypsin and alpha-1-antichymotrypsin, which may function as antimicrobials a
98 )-antichymotrypsin and a complex of alpha(1)-antichymotrypsin with an exogenous reactive loop peptide
99 other isoforms of endopins related to alpha1-antichymotrypsin, yet endopin 2C differs in its target p