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1 1026_II1055 (bcaB), which encodes a putative prolyl 4-hydroxylase.
2  EGLN1, hypoxia-inducible gene 1 (HIG1), and prolyl 4-hydroxylase.
3  substrate for the collagen-modifying enzyme prolyl 4-hydroxylase.
4 -2, that encode alpha subunits of the enzyme prolyl 4-hydroxylase.
5 olding and assembly is distinct from that of prolyl 4-hydroxylase.
6 o human PHD2 and a Chlamydomonas reinhardtii prolyl-4-hydroxylase.
7  TET 5-methylcytosine hydroxylases, and EglN prolyl-4-hydroxylases.
8 ind to protein disulfide isomerase (PDI) and prolyl 4-hydroxylase 1 (P4H1).
9                                              Prolyl 4-hydroxylase-1 (P4H1) was previously implicated
10 e2Cre-mediated disruption of Egln1 (encoding prolyl-4 hydroxylase 2 [PHD2]; Egln1(Tie2)) in endotheli
11 ing RNA (siRNA) to silence murine HIF-1alpha-prolyl-4 hydroxylase-2 (PHD2).
12 c oxide synthase (eNOS), Akt, and HIF-1alpha-prolyl-4-hydroxylase-2 (PHD)2 expression were measured.
13                    For a third system, viral prolyl 4-hydroxylase (26 kDa), ECD showed that multiple
14  colocalization of antibodies to PGP 9.5 and prolyl-4-hydroxylase (a fibroblast marker) as well as co
15 PDI-2 is required for the normal function of prolyl 4-hydroxylase, a key collagen-modifying enzyme.
16 ated deletions within each gene to eliminate prolyl 4-hydroxylase activity from the animal.
17 1 target genes and discovered that the phy-2 prolyl 4-hydroxylase alpha subunit is critical for survi
18 peptide that acts as the beta-subunit in the prolyl 4-hydroxylase alpha(2)beta(2)-tetramer (P4H) and
19 K catalytic subunit (DNA-PKcs), HA95, Hsp27, prolyl 4-hydroxylase alpha-1 subunit, alpha-tubulin, and
20 ted that these 3 genes are apolipoprotein E, prolyl 4-hydroxylase alpha-subunit, and an unknown trans
21  physical map, and we show that it encodes a prolyl-4-hydroxylase alpha catalytic subunit.
22                                              Prolyl-4-hydroxylase alpha(I) (P4Halpha(I)) is the rate-
23 riptionally activates the alpha(II) collagen prolyl-4-hydroxylase [alpha(II)PH] gene, resulting in th
24 D44(+), SH2(+), SH3(+), and SH4(+); produced prolyl-4-hydroxylase, alpha-smooth muscle actin, fibrone
25 n, along with the alpha and beta subunits of prolyl 4-hydroxylase, an enzyme that modifies the collag
26 elopment and is mediated by a HIF-alpha type prolyl 4-hydroxylase and five sequentially acting cytopl
27 erved residues present in the active site of prolyl 4-hydroxylase and lysyl hydroxylase.
28 nase domains similar to the alpha-subunit of prolyl 4-hydroxylase and lysyl hydroxylases.
29 amily of O2-dependent HIF hydroxylases: four prolyl 4-hydroxylases and an asparaginyl hydroxylase.
30                                        Since prolyl-4-hydroxylase and protein disulfide isomerase coe
31 enes, (5) other HRGPs, glycosyl transferase, prolyl 4-hydroxylase, and peroxidase genes coexpressed w
32               Hypoxia-inducible factor (HIF) prolyl 4-hydroxylases are a family of iron- and 2-oxoglu
33 w molecular weight inhibitors of procollagen prolyl 4-hydroxylase as potential inhibitors of the HIF
34  D application, but there was an increase in prolyl-4-hydroxylase-beta expression, indicative of incr
35 oliferation, apoptosis, satellite cells, and prolyl-4-hydroxylase-beta expression.
36  an enzymatic activity distinct from that of prolyl 4-hydroxylase, but no amino acid sequences or gen
37                                     Collagen prolyl 4-hydroxylases (C-P4H) are required for formation
38                                     Collagen prolyl 4-hydroxylases (C-P4H-I, C-P4H-II, and C-P4H-III)
39                                     Collagen prolyl 4-hydroxylases (C-P4Hs) are key enzymes in collag
40                                     Collagen prolyl 4-hydroxylases (C-P4Hs) play a central role in th
41 a-(P4H-beta) subunits of the type I collagen prolyl-4-hydroxylase (C-P4H(I)).
42  show that hypoxia increases type I collagen prolyl-4-hydroxylase [C-P4H(I)], which leads to prolyl-h
43 synthesis at a post-translational level in a prolyl 4-hydroxylase-dependent manner that does not requ
44  in the kidney and liver and is regulated by prolyl-4-hydroxylase domain (PHD) dioxygenases PHD1, PHD
45                                          The prolyl-4-hydroxylase domain (PHD) enzymes are regarded a
46 F-1alpha in these cells is controlled by the prolyl-4-hydroxylase domain (PHD) family of proteins.
47 ulated in response to oxygen availability by prolyl-4-hydroxylase domain (PHD) proteins, with PHD2 be
48 e targeting to examine the von Hippel-Lindau/prolyl-4-hydroxylase domain (PHD)/HIF axis in cell-expre
49           Transfections with plasmids coding prolyl-4-hydroxylase domain protein 2 (PHD2) and ShPHD2
50                                              Prolyl-4-hydroxylase-domain (PHD) proteins regulate the
51 collagen is post-translationally modified by prolyl-4-hydroxylase (EC 1.14.11.2) before secretion and
52 f each of the hypoxia inducible factor (HIF) prolyl-4-hydroxylase enzymes (PHD1-3) in the first 24 h
53 rt for the animal-derived O2-sensor model of prolyl 4-hydroxylase function, in an organism that lacks
54                         Co-transfection with prolyl 4-hydroxylase generated homotrimers with stable p
55                                     Although prolyl 4-hydroxylase has been characterized as an alpha2
56                                        While prolyl-4-hydroxylase has been studied extensively by bio
57 gen VIII molecules expressed with or without prolyl 4-hydroxylase identified urea-sensitive high mole
58 t body morphology, consistent with a role of prolyl 4-hydroxylase in formation of the body cuticle.
59 us solution, azaquinolone inhibitors bind to prolyl 4-hydroxylase in two different orientations, as f
60 s the first report of a mutationally defined prolyl-4-hydroxylase in any animal.
61 e midleaflet and free edge and expression of prolyl-4-hydroxylase (indicating collagen synthesis) was
62 ells demonstrated expression of vimentin and prolyl-4-hydroxylase, indicating a mesenchymal phenotype
63  that prevention of fibrosis after MI with a prolyl 4-hydroxylase inhibitor (P4HI) would preserve LV
64                              Addition of the prolyl 4-hydroxylase inhibitor 2,2-dipyridyl, however, e
65 Cs that were cultured in the presence of the prolyl-4-hydroxylase inhibitor dimethyloxalylglycine (DM
66  factor (HIF) pathway under normoxia using a prolyl-4-hydroxylase inhibitor, dimethyloxalylglycine (D
67 ntified low molecular weight and peptide HIF prolyl 4-hydroxylase inhibitors as novel neurological th
68 We also showed that structurally diverse HIF prolyl 4-hydroxylase inhibitors prevent oxidative death
69                                              Prolyl 4-hydroxylases install a hydroxyl group in the 4R
70 , by inhibiting the hypoxia-inducible factor prolyl 4-hydroxylase isoform 1 (PHD1), an iron and 2-oxo
71 thylases, TET DNA demethylases, and collagen prolyl 4-hydroxylases, leading to accumulation of methyl
72                                      Ofd1, a prolyl 4-hydroxylase-like 2-oxoglutarate dioxygenase, co
73                     Ofd1, an uncharacterized prolyl 4-hydroxylase-like 2-oxoglutarate-Fe(II) dioxygen
74 (II)-dependent protein hydroxylases, such as prolyl 4-hydroxylase or lysyl hydroxylases.
75         Soluble cytosolic extracts have Skp1 prolyl 4-hydroxylase (P4H) activity, which can be measur
76 aperone and being a component of the enzymes prolyl 4-hydroxylase (P4H) and microsomal triglyceride t
77                                              Prolyl 4-hydroxylase (P4H) catalyzes the posttranslation
78                                              Prolyl 4-hydroxylase (P4H) is a nonheme iron dioxygenase
79                               In a screen of prolyl 4-hydroxylase (P4H) mutants, we found that geneti
80       An endoplasmic reticulum transmembrane prolyl 4-hydroxylase (P4H-TM) is able to hydroxylate the
81                                              Prolyl 4-hydroxylases (P4H) catalyze the post-translatio
82                                              Prolyl-4-hydroxylase (P4H) is a non-heme iron hydroxylas
83 two transient complexes in the reaction of a prolyl-4-hydroxylase (P4H), a functional homologue of hu
84 ium expresses, in all cells, an O2-dependent prolyl 4-hydroxylase (P4H1) required for O-glycosylation
85     Dictyostelium expresses an HIFalpha-type prolyl 4-hydroxylase (P4H1) whose levels affect the O(2)
86                                              Prolyl 4-hydroxylases (P4Hs) are mononuclear non-heme ir
87                                     Specific prolyl 4-hydroxylases (P4Hs) regulate the stability of t
88 nal modification (PTM) of HRGPs catalyzed by prolyl 4-hydroxylases (P4Hs), defines their subsequent O
89 h glycoproteins (HRGPs) that is catalyzed by prolyl 4-hydroxylases (P4Hs).
90                                  Cytoplasmic prolyl 4-hydroxylases (PHDs) have a primary role in O(2)
91                PHD1 belongs to the family of prolyl-4-hydroxylases (PHDs) that is responsible for pos
92 ma gondii is hydroxylated by an O2-dependent prolyl-4-hydroxylase (PhyA), and the resulting hydroxypr
93 g F-box and WD-40 domain protein (Fbxw7) and Prolyl 4-hydroxylase possessing a transmembrane domain (
94               Previous studies showed that a prolyl 4-hydroxylase related to animal HIFalpha prolyl h
95 stelium lacks HIFalpha, a mediator of animal prolyl 4-hydroxylase signaling, and P4H1 can hydroxylate
96 ular weight or peptide inhibitors of the HIF prolyl 4-hydroxylases stabilize HIF-1alpha and up-regula
97 not viable, suggesting an essential role for prolyl 4-hydroxylase that is normally accomplished by ei
98                          However, unlike the prolyl 4-hydroxylases that regulate mammalian hypoxia-in
99 , cellular hypoxic responses are mediated by prolyl 4-hydroxylases that use O(2) and alpha-ketoglutar
100 d PHD3, oxygen- and 2-oxoglutarate-dependent prolyl-4-hydroxylases that regulate HIF activity.
101         The ability of the inhibitors of HIF prolyl 4-hydroxylases to stabilize proteins involved in
102 ere mimicked by small-molecule inhibitors of prolyl 4-hydroxylase, validating the genetic results and
103 HIF-1 activation is controlled by HIF-1alpha-prolyl 4-hydroxylases, which target HIF-1alpha for ubiqu
104 ed by examining this required interaction of prolyl-4-hydroxylase with procollagen.

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