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1 uding Lh2b (lysyl oxidase-like 2b) and P4ha (prolyl 4-hydroxylase).
2 substrate for the collagen-modifying enzyme prolyl 4-hydroxylase.
3 -2, that encode alpha subunits of the enzyme prolyl 4-hydroxylase.
4 olding and assembly is distinct from that of prolyl 4-hydroxylase.
5 1026_II1055 (bcaB), which encodes a putative prolyl 4-hydroxylase.
6 EGLN1, hypoxia-inducible gene 1 (HIG1), and prolyl 4-hydroxylase.
7 o human PHD2 and a Chlamydomonas reinhardtii prolyl-4-hydroxylase.
8 TET 5-methylcytosine hydroxylases, and EglN prolyl-4-hydroxylases.
11 e2Cre-mediated disruption of Egln1 (encoding prolyl-4 hydroxylase 2 [PHD2]; Egln1(Tie2)) in endotheli
12 encoding for hypoxia-inducible factor (HIF) prolyl-4-hydroxylase 2 (PHD2), cause erythrocytosis and
14 c oxide synthase (eNOS), Akt, and HIF-1alpha-prolyl-4-hydroxylase-2 (PHD)2 expression were measured.
16 colocalization of antibodies to PGP 9.5 and prolyl-4-hydroxylase (a fibroblast marker) as well as co
17 PDI-2 is required for the normal function of prolyl 4-hydroxylase, a key collagen-modifying enzyme.
20 1 target genes and discovered that the phy-2 prolyl 4-hydroxylase alpha subunit is critical for survi
21 peptide that acts as the beta-subunit in the prolyl 4-hydroxylase alpha(2)beta(2)-tetramer (P4H) and
22 ading enzymes, and decreased LOX, LOXL2, and prolyl 4-hydroxylase alpha-1 (P4HA1) for ECM processing
23 K catalytic subunit (DNA-PKcs), HA95, Hsp27, prolyl 4-hydroxylase alpha-1 subunit, alpha-tubulin, and
24 nuclear YAP1 accumulation and expression of prolyl 4-hydroxylase alpha-2 (P4HA2) which increases col
25 ted that these 3 genes are apolipoprotein E, prolyl 4-hydroxylase alpha-subunit, and an unknown trans
28 riptionally activates the alpha(II) collagen prolyl-4-hydroxylase [alpha(II)PH] gene, resulting in th
29 D44(+), SH2(+), SH3(+), and SH4(+); produced prolyl-4-hydroxylase, alpha-smooth muscle actin, fibrone
30 n, along with the alpha and beta subunits of prolyl 4-hydroxylase, an enzyme that modifies the collag
31 elopment and is mediated by a HIF-alpha type prolyl 4-hydroxylase and five sequentially acting cytopl
34 amily of O2-dependent HIF hydroxylases: four prolyl 4-hydroxylases and an asparaginyl hydroxylase.
36 y collagen prolyl 3-hydroxylase and collagen prolyl 4-hydroxylase, and is essential for normal cell f
37 enes, (5) other HRGPs, glycosyl transferase, prolyl 4-hydroxylase, and peroxidase genes coexpressed w
39 w molecular weight inhibitors of procollagen prolyl 4-hydroxylase as potential inhibitors of the HIF
40 , we identified carbonyl modification of the prolyl-4-hydroxylase beta subunit (P4Hb) that is respons
41 D application, but there was an increase in prolyl-4-hydroxylase-beta expression, indicative of incr
43 an enzymatic activity distinct from that of prolyl 4-hydroxylase, but no amino acid sequences or gen
50 show that hypoxia increases type I collagen prolyl-4-hydroxylase [C-P4H(I)], which leads to prolyl-h
51 synthesis at a post-translational level in a prolyl 4-hydroxylase-dependent manner that does not requ
52 in the kidney and liver and is regulated by prolyl-4-hydroxylase domain (PHD) dioxygenases PHD1, PHD
53 iminates between the inhibition of HIF-alpha prolyl-4-hydroxylase domain (PHD) enzymes and HIF-alpha
55 F-1alpha in these cells is controlled by the prolyl-4-hydroxylase domain (PHD) family of proteins.
56 ulated in response to oxygen availability by prolyl-4-hydroxylase domain (PHD) proteins, with PHD2 be
57 e targeting to examine the von Hippel-Lindau/prolyl-4-hydroxylase domain (PHD)/HIF axis in cell-expre
61 collagen is post-translationally modified by prolyl-4-hydroxylase (EC 1.14.11.2) before secretion and
62 f each of the hypoxia inducible factor (HIF) prolyl-4-hydroxylase enzymes (PHD1-3) in the first 24 h
63 e collagen prolyl 3-hydroxylase and collagen prolyl 4-hydroxylase families as potentially important r
65 P4HA3 in a subset of melanomas, the collagen prolyl 4-hydroxylase family members P4HA1, P4HA2, and P4
66 n of the fibroblast markers type I collagen, prolyl-4-hydroxylase, fibroblast specific protein-1, and
67 rt for the animal-derived O2-sensor model of prolyl 4-hydroxylase function, in an organism that lacks
69 hat expression of hypoxia-regulated collagen prolyl-4-hydroxylase genes P4HA1 and P4HA2 is significan
75 gen VIII molecules expressed with or without prolyl 4-hydroxylase identified urea-sensitive high mole
76 t body morphology, consistent with a role of prolyl 4-hydroxylase in formation of the body cuticle.
77 us solution, azaquinolone inhibitors bind to prolyl 4-hydroxylase in two different orientations, as f
79 e midleaflet and free edge and expression of prolyl-4-hydroxylase (indicating collagen synthesis) was
80 ells demonstrated expression of vimentin and prolyl-4-hydroxylase, indicating a mesenchymal phenotype
81 that prevention of fibrosis after MI with a prolyl 4-hydroxylase inhibitor (P4HI) would preserve LV
83 Cs that were cultured in the presence of the prolyl-4-hydroxylase inhibitor dimethyloxalylglycine (DM
84 factor (HIF) pathway under normoxia using a prolyl-4-hydroxylase inhibitor, dimethyloxalylglycine (D
85 ntified low molecular weight and peptide HIF prolyl 4-hydroxylase inhibitors as novel neurological th
86 We also showed that structurally diverse HIF prolyl 4-hydroxylase inhibitors prevent oxidative death
87 inhibition with multiple selective collagen prolyl 4-hydroxylase inhibitors reduces proliferation an
89 uggest that selective inhibition of collagen prolyl 4-hydroxylase is an attractive strategy to reduce
91 , by inhibiting the hypoxia-inducible factor prolyl 4-hydroxylase isoform 1 (PHD1), an iron and 2-oxo
92 thylases, TET DNA demethylases, and collagen prolyl 4-hydroxylases, leading to accumulation of methyl
97 aperone and being a component of the enzymes prolyl 4-hydroxylase (P4H) and microsomal triglyceride t
101 l hydroxylation (CPH), which is catalyzed by prolyl 4-hydroxylase (P4H), is the most prevalent posttr
107 two transient complexes in the reaction of a prolyl-4-hydroxylase (P4H), a functional homologue of hu
108 ium expresses, in all cells, an O2-dependent prolyl 4-hydroxylase (P4H1) required for O-glycosylation
109 Dictyostelium expresses an HIFalpha-type prolyl 4-hydroxylase (P4H1) whose levels affect the O(2)
114 nal modification (PTM) of HRGPs catalyzed by prolyl 4-hydroxylases (P4Hs), defines their subsequent O
116 els of HIF-1alpha transcripts, low levels of prolyl-4-hydroxylases (PHD2 and PHD3), and a low cellula
117 ne such environmental factor and cytoplasmic prolyl 4-hydroxylases (PHDs) are evolutionarily conserve
120 ma gondii is hydroxylated by an O2-dependent prolyl-4-hydroxylase (PhyA), and the resulting hydroxypr
121 g F-box and WD-40 domain protein (Fbxw7) and Prolyl 4-hydroxylase possessing a transmembrane domain (
123 stelium lacks HIFalpha, a mediator of animal prolyl 4-hydroxylase signaling, and P4H1 can hydroxylate
124 ular weight or peptide inhibitors of the HIF prolyl 4-hydroxylases stabilize HIF-1alpha and up-regula
125 sed levels of the miRNA biogenesis molecules prolyl 4-hydroxylase subunit alpha 1 (P4HA1) and Ago2 al
126 s in mitochondrial metabolism as elicited by prolyl 4-hydroxylase subunit alpha 1 (P4HA1) to T cell e
127 odel wherein conditional genetic ablation of prolyl 4-hydroxylase subunit beta (P4HB), the gene that
128 not viable, suggesting an essential role for prolyl 4-hydroxylase that is normally accomplished by ei
130 , cellular hypoxic responses are mediated by prolyl 4-hydroxylases that use O(2) and alpha-ketoglutar
134 ere mimicked by small-molecule inhibitors of prolyl 4-hydroxylase, validating the genetic results and
135 HIF-1 activation is controlled by HIF-1alpha-prolyl 4-hydroxylases, which target HIF-1alpha for ubiqu