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1 man AKR1B subfamily members (i.e. AKR1B1 and AKR1B10).
2 rated that aldo-keto reductase family 1 B10 (AKR1B10), a novel protein overexpressed in human hepatoc
3                             Mechanistically, AKR1B10 activates protein phosphatase 2A (PP2A) by preve
4                      These data suggest that AKR1B10 affects cell survival through modulating lipid s
5 acid protein with 91% amino acid identity to AKR1B10; AKR1B15.2 has a prolonged N terminus and consis
6 ntracellular fluorescent studies showed that AKR1B10 and ACCA proteins co-localize in the cytoplasm o
7                     This association between AKR1B10 and ACCA proteins was further confirmed by co-im
8 cantly increased the secretion of endogenous AKR1B10 and exogenous GFP-AKR1B10 fusion protein when co
9    We characterized the functional domain in AKR1B10 and found that helix 10 (amino acids 233-240), l
10 including 3 new markers of IM (ACE2, LGALS4, AKR1B10) and 3 of SPEM (OLFM4, LYZ, DPCR1).
11                  Co-immunoprecipitation with AKR1B10 antibody and protein mass spectrometry analysis
12          We identify the aldo-keto reductase AKR1B10 as a metastasis enhancer that has little impact
13 ed epithelium in keloid disease and identify AKR1B10 as a potential new target in future management o
14 tification of the aldo-keto reductase enzyme AKR1B10 as highly up-regulated in keloid epidermis sugge
15 n mass spectrometry analysis identified that AKR1B10 associates with acetyl-CoA carboxylase-alpha (AC
16                                The cytosolic AKR1B10 associates with and is translocated to lysosomes
17 determined the transcriptional start site of AKR1B10 at 320 bp upstream of the ATG translational star
18                The results demonstrated that AKR1B10 consists of 10 exons and 9 introns, stretching a
19                                      Loss of AKR1B10 disrupts this pathway, stabilizing c-Myc, which
20 ify aldo-keto reductase family 1 member B10 (AKR1B10), down-regulated in gastrointestinal cancers, as
21  addition, c-Myc transcriptionally represses AKR1B10, establishing a feedback loop that sustains its
22 on exchange chromatography demonstrated that AKR1B10 exists in two distinct forms, monomers (approxim
23  is known about the regulatory mechanisms of AKR1B10 expression.
24 tion of endogenous AKR1B10 and exogenous GFP-AKR1B10 fusion protein when cotransfected.
25 n this study, we determined the structure of AKR1B10 gene and characterized its promoter.
26  -4091 bp of the 5'-flanking fragment of the AKR1B10 gene was capable of driving GFP and luciferase r
27          Therefore, in the last two decades, AKR1B10 has attracted interest as a novel target for age
28                                              AKR1B10(High) tumour cells have reduced glycolytic capac
29 s, inhibition of fatty acid oxidation blocks AKR1B10(High)-enhanced metastatic colonisation with no i
30 namycin, a HSP90alpha inhibitor, dissociated AKR1B10-HSP90alpha complexes and significantly reduced A
31 ding is significant in exploiting the use of AKR1B10 in cancer clinics.
32      This study presents a novel function of AKR1B10 in tumorigenic mammary epithelial cells (RAO-3),
33                                              AKR1B10 inhibition results in apoptosis of tumor cells w
34 s exposing the HCT-8 cells to epalrestat, an AKR1B10 inhibitor, led to more than 2-fold elevation of
35                      These data suggest that AKR1B10 is a novel regulator of the biosynthesis of fatt
36           In this study, we demonstrate that AKR1B10 is critical to cell survival.
37    We further demonstrate that lysine-125 of AKR1B10 is essential for its interaction with PP2A-Calph
38              Under physiological conditions, AKR1B10 is expressed mainly in the gastrointestinal trac
39                                              AKR1B10 is highly expressed in several cancers and preca
40                                              AKR1B10 is involved in hepatocarcinogenesis via modulati
41         Our previous studies have shown that AKR1B10 is secreted through a lysosome-mediated nonclass
42                    Aldo-keto reductase 1B10 (AKR1B10) is a human enzyme that catalyzes the NADPH-depe
43     Aldo-keto reductase family 1 member B10 (AKR1B10) is overexpressed in human hepatocellular carcin
44     Aldo-keto reductase family 1 member B10 (AKR1B10) is primarily expressed in the normal human colo
45 nterestingly, small interfering RNA-mediated AKR1B10 knock down increased ACCA degradation through ub
46 ctively mitigates metastasis associated with AKR1B10 loss.
47 ed metastatic colonisation with no impact on AKR1B10(Low) cells.
48 covers an antimetastatic mechanism involving AKR1B10-mediated PP2A activation and highlights its pote
49         Our previous studies have shown that AKR1B10 mediates the ubiquitin-dependent degradation of
50           Consistent with previous findings, AKR1B10 mRNA and protein levels were higher in primary h
51      After analyzing the correlation between AKR1B10 mRNA expression in PHC tissues and the clinical
52                                     A higher AKR1B10 mRNA expression level is related to a shorter DF
53 tissues and the clinical data, we found that AKR1B10 mRNA expression was associated with serum alpha-
54 through identified potential targets namely, AKR1B10, NR3C1, PTGS2, and HER2.
55                Paracrine signals released by AKR1B10-overexpressing keratinocytes into conditioned me
56          Our recent studies have showed that AKR1B10 plays a critical role in the growth and prolifer
57 umor suppressor protein binding sites in the AKR1B10 promoter, including c-Ets-1, C/EBP, AP-1, and p5
58 ntibody and pulldown assays with recombinant AKR1B10 protein.
59                    Aldo-keto reductase 1B10 (AKR1B10) protein is a new tumor biomarker in humans.
60 (MUC13, OLFM4, CDH17, KRT20, MUC5AC, LGALS4, AKR1B10, REG4).
61 lipids like sphingosine-1-phosphate (S1P) in AKR1B10's oncogenic function.
62 increases QSG-7701's proliferation, in which AKR1B10-S1P signaling plays a pivotal role.
63 P90alpha complexes and significantly reduced AKR1B10 secretion in a dose-dependent manner.
64 r, our data suggest that HSP90alpha mediates AKR1B10 secretion through binding to its helix 10 domain
65 3-240), located at the C terminus, regulates AKR1B10 secretion.
66 tudy illuminates the regulatory mechanism of AKR1B10 secretion.
67 chanistic analysis supports a model in which AKR1B10 serves to limit the toxic side effects of oxidat
68                                              AKR1B10 silencing also increased the levels of alpha,bet
69 ls (NCI-H460), small-interfering RNA-induced AKR1B10 silencing resulted in caspase-3-mediated apoptos
70 , partially rescued the apoptosis induced by AKR1B10 silencing, whereas exposing the HCT-8 cells to e
71                           Here, we show that AKR1B10 transfection into normal human keratinocytes rep
72                                    Moreover, AKR1B10 up-regulation is strictly related to acquired re
73                            Cotransfection of AKR1B10 with a luciferase reporter plasmid showed reduce
74 s-240 in helix 10 mediate the interaction of AKR1B10 with HSP90alpha.