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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
4 acid protein with 91% amino acid identity to AKR1B10; AKR1B15.2 has a prolonged N terminus and consis
5 ntracellular fluorescent studies showed that AKR1B10 and ACCA proteins co-localize in the cytoplasm o
7 cantly increased the secretion of endogenous AKR1B10 and exogenous GFP-AKR1B10 fusion protein when co
8 We characterized the functional domain in AKR1B10 and found that helix 10 (amino acids 233-240), l
11 ed epithelium in keloid disease and identify AKR1B10 as a potential new target in future management o
12 tification of the aldo-keto reductase enzyme AKR1B10 as highly up-regulated in keloid epidermis sugge
13 n mass spectrometry analysis identified that AKR1B10 associates with acetyl-CoA carboxylase-alpha (AC
15 determined the transcriptional start site of AKR1B10 at 320 bp upstream of the ATG translational star
17 on exchange chromatography demonstrated that AKR1B10 exists in two distinct forms, monomers (approxim
21 -4091 bp of the 5'-flanking fragment of the AKR1B10 gene was capable of driving GFP and luciferase r
22 namycin, a HSP90alpha inhibitor, dissociated AKR1B10-HSP90alpha complexes and significantly reduced A
26 s exposing the HCT-8 cells to epalrestat, an AKR1B10 inhibitor, led to more than 2-fold elevation of
31 Aldo-keto reductase family 1 member B10 (AKR1B10) is overexpressed in human hepatocellular carcin
32 Aldo-keto reductase family 1 member B10 (AKR1B10) is primarily expressed in the normal human colo
33 nterestingly, small interfering RNA-mediated AKR1B10 knock down increased ACCA degradation through ub
38 tissues and the clinical data, we found that AKR1B10 mRNA expression was associated with serum alpha-
42 umor suppressor protein binding sites in the AKR1B10 promoter, including c-Ets-1, C/EBP, AP-1, and p5
49 r, our data suggest that HSP90alpha mediates AKR1B10 secretion through binding to its helix 10 domain
53 ls (NCI-H460), small-interfering RNA-induced AKR1B10 silencing resulted in caspase-3-mediated apoptos
54 , partially rescued the apoptosis induced by AKR1B10 silencing, whereas exposing the HCT-8 cells to e
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