Publication for Hmgcr and Ldlr

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
mmu	Hmgcr	3-hydroxy-3-methylglutaryl-Coenzyme A reductase	15357			[link]
mmu	Ldlr	low density lipoprotein receptor	16835

Pubmed ID	Priority	Text
27824334	0.98	LDLR transgene was shown to be sensitive to sterols, statins, and RNAi knockdown of HMG-CoA Reductase (Hmgcr) (the rate limiting enzyme in intracellular cholesterol biosynthesis), all of which modify the activity of the LDLR promoter.
	0.98	Hmgcr in mouse upregulates Ldlr expression.
	0.97	Hmgcr transcripts in vivo, leading to an increase in LDLR transgene expression.
	0.97	Hmgcr mRNA, and led to an increase in endogenous Ldlr expression.
	0.97	LDLR protein expression was also found to be significantly increased in liver tissues following suppression of endogenous Hmgcr 4 weeks postdelivery of vectors.
	0.96	Hmgcr mRNA, which led to profound upregulation of endogenous Ldlr protein expression in vivo.
	0.96	Hmgcr expression, driving induction of the LDLR promoter.
	0.95	LDLR-Hmgcr-RNAi vector treatment in hypercholesterolaemic Ldlr-/- mice results in sustained Hmgcr knockdown, leading to further LDLR upregulation
	0.95	LDLR transgene expression was improved through knockdown of endogenous Hmgcr, which induced the LDLR promoter leading to significant upregulation of LDLR transgene expression.
	0.94	LDLR to provide prolonged expression of LDLR through targeted knockdown of Hmgcr.
	0.94	LDLR-Hmgcr-RNAi vector has a synergistic effect in lowering plasma cholesterol in Ldlr-/- mice fed a refined high-cholesterol diet.
	0.92	LDLR-miR82-injected animals showed a significant reduction in Hmgcr protein levels, as compared to uninjected animals, and control groups injected with the pLDLR-LDLR-miRNT or pLDLR-LDLR vector (Figure 4c).
	0.91	LDLR-miR82-injected animals had significantly reduced levels of Hmgcr protein as compared to controls (0.414 +- 0.12-fold) (Figure 3c).
	0.91	LDLR-miR82 vector reduces Hmgcr and elevates LDLR expression in vitro and in vivo.
	0.90	LDLR-miR82 vector decreases Hmgcr and increases LDLR expression in HC-fed Ldlr-/- mice.
	0.85	LDLR-Hmgcr-RNAi vector treatment results in long-term lipid lowering and reduced atherosclerosis
	0.77	LDLR-Hmgcr-RNAi vector lowers plasma cholesterol to a greater extent than of our original LDLR mini-gene vector lacking the miRNA component.
	0.67	LDLR-Hmgcr-RNAi vector contains the oriP/EBNA-1 long-term retention elements from EBV, which may be replaced by mammalian DNA episomal retention systems, such as those that utilise Scaffold Matrix Attachment Region (S/MAR) suitable for ensuring long-term LDLR expression.
	0.67	Ldlr-/- mice injected with pLDLR-LDLR-miR82 show (c) decreased Hmgcr protein expression, and (d) increased LDLR protein expression, as compared to control.
	0.55	Hmgcr and expression of LDLR from a single plasmid.
28515432	0.98	Hmgcr), lipid endocytosis (Ldlr), and lipid esterification (Dgat2, Mogat2 and Plin2).
	0.98	Hmgcr, Ldlr, and Fabp5).
	0.98	Hmgcr, Ldlr, and Fabp5, indicate a negative feedback mechanism from Ldlr and Fabp5 with expression of Lep, showing the complicated regulatory mechanism of lipid metabolism involving both intake and cellular lipid metabolism in reducing fat deposition in adipose tissue in response to HS intake.
	0.97	Hmgcr, Ldlr and Fabp5).
	0.97	Ldlr and Hmgcr yet CREB1 is also regulated by Agt and Egf, involved in the RAS.
	0.97	Hmgcr, and Ldlr and Egf negatively regulates the expression of Lep.
	0.97	Ldlr and Hmgcr, and CREB1 was, in part, regulated by Agt and Egf, both of which involved the RAS.
	0.93	Hmgcr, Ldlr, Dgat2, Mogat2, Plin2, and Fabp5) in the HS mice were significantly decreased (P < 0.05 or P < 0.01, Fig. 5B), and the expression of Acsl6 in the HS mice was significantly increased (P < 0.01, Fig. 5B).
	0.92	Hmgcr, Ldlr and Fabp5 genes in lipid metabolism; calcium ion inhibited intake by the change expression of Lep and there was a negative feedback mechanism involving Lep on the expression of Ldlr and Fabp5.
28808191	0.98	LDLR gene and HMGCR gene promotes transcription of the mRNAs, ultimately resulting in increased LDLR protein on the cell surface and increased HMGCR protein in the ER membrane.
	0.98	HMGCR and INSIG1 (lowering endogenous synthetic levels of cholesterol), stimulate the expression of IDOL to degrade LDLR, and stimulate the expression of ABCA1/ABCG1 to promote cholesterol removal from the cell, thereby acting as an effective foil to the SREBP2 pathway.
	0.98	HMGCR, LDLR (increasing cellular cholesterol levels through endogenous and exogenous pathways) and upregulation of PCSK9 (decreasing cell surface levels of LDLR).
	0.98	LDLR and HMGCR (similar to CR-derived cholesterol) suggesting that esterification of LDL-derived cholesterol is an essential step in its redirection from the regulatory pool.
	0.98	LDLR and HMGCR (among others).
	0.97	LDLR and HMGCR expression and clearly enters the regulatory pathway.
	0.86	HMGCR and LDLR gene transcription are shut down, closing the cycle.
	0.78	LDLR and HMGCR also occurs.
	0.70	LDLR but not HMGCR.
30940698	0.98	Hmgcr]), import (e.g., low-density lipoprotein receptor [Ldlr]), and efflux (e.g., AbcA1).
	0.98	Hmgcr, the other proteins in the cholesterol biogenesis cascade (Fig. S5A) and the low-density lipoprotein receptor (Ldlr), as well as proprotein convertase subtilisin/kexin type 9 (Pcsk9), which antagonizes Ldlr (Fig. 2A), were found in increased abundance during the expansion phase of infection compared to their levels in mock-infected control mice.
	0.98	Hmgcr, Ldlr, and Pcsk9 is regulated by the transcription factor SREBP2, expression of Abca1, Abcg5, and the inducible degrader of the low-density lipoprotein (LDL) receptor (Idol) is regulated by liver X receptor (LXR), transcription factors which are considered to be mutually antagonistic.
	0.96	Hmgcr, Pcsk9, and Ldlr) was not induced until 8 DPI, although the corresponding proteins were found in higher abundance in infected IECs than in controls.
	0.90	Ldlr or Pcsk9 was seen at either expansion phase time points compared to their expression in mock-infected mice, yet a significant increase in the expression of Hmgcr, Ldlr, and Pcsk9 was detected at 8 DPI (Fig. 2D and E).
	0.85	Hmgcr (C), Ldlr (D), Pcsk9 (E), Abca1 (F), Abcg5 (G), and Idol (H) revealed expression levels in IECs enriched from mock-infected or C. rodentium-infected colons.
	0.71	Hmgcr and Ldlr were in significantly higher abundance at 4 DPI (log2 fold changes [log2FC], 1.53 and 1.11, respectively), with a more exaggerated increase at 6 DPI (log2FC, 2.04 and1.33, respectively).
31239739	0.98	HMGCR is the key enzyme for cholesterol synthesis and low density lipoprotein receptor (LDLr) is the mediator of cholesterol uptake, the two key proteins which are predominantly regulated by SREBP-2.
	0.98	HMGCR and LDLr is mediated via a negative feedback mechanism that is tightly controlled by the other two proteins, SREBP-2 and SREBP SCAP, which are important for keeping a balance of cholesterol at cell and systemic level.
	0.98	LDLr negative feedback system is disrupted by damage factors, the increasing HMGCR-mediated cholesterol synthesis and LDLr-mediated cholesterol uptake may exacerbate cholesterol accumulation in kidneys, subsequently causing renal injuries mediated by lipids.
	0.97	LDLr, SREBP2, and SCAP expression, the renal expression of HMGCR protein was down-regulated with an increasing dose of quercetin in db/db mice as compared with diabetic controls after treatment for 10 weeks, and the differences were statistically significant (P<0.05, Figure 8B).
	0.96	LDLr, HMGCR, SREBP-2, and SCAP subsequently attenuated the renal lipid profile change and lipid droplet accumulation, resulting in the alleviation of renal injury of db/db mice.
	0.94	LDLr signaling pathway and the expression of HMGCR in the kidneys, could be therapeutic mechanisms for ameliorating early stage DN.
31547031	0.98	HMG-CoA reductase, SREBP-2, and LDL receptor were decreased by AHR treatment (Figure 5).
	0.97	3-hydroxy-3-methylglutaryl (HMG)-CoA reductase, and low-density lipoprotein (LDL)-receptor in the liver.
	0.97	HMG-CoA reductase, SREBP-2, and LDL-receptor than HFD-fed control mice.
	0.96	3-hydroxy-3-methylglutaryl CoA reductase, sterol regulatory element-binding transcription factor (SREBP)-2, and low-density lipoprotein receptor, as well as fatty acid synthesis genes, such as SREBP-1c and fatty acid synthase.
	0.95	HMG-CoA reductase, SREBP1/2, FAS, and LDL receptor.
	0.58	HMG-CoA reductase (A), SREBP-2 (B), and LDL receptor (C) in HFD-induced obese mice.
25804527	0.98	Ldlr and Hmgcr, was found markedly increased at 4 h TPA exposure in the skin of Tm7sf2+/+ mice (Fig. 1F).
	0.98	LDLR and HMGCR expression, suggesting a pivotal role for this orphan receptor in the regulation of cholesterol metabolism.
	0.97	3-hydroxy-3-methylglutaryl-CoA reductase (Hmgcr), (ii) increased uptake of circulating cholesterol via the low-density lipoprotein receptor (Ldlr), and (iii) decreased cellular cholesterol efflux via the ATP-binding cassette transporter (Abca1).
	0.97	Hmgcr and Ldlr only in the skin of Tm7sf2+/+ mice (Fig. 1C and D).
	0.97	Hmgcr) and cholesterol uptake (Ldlr), as well as increased expression of the transcription factor (Srebp-2) responsible for driving expression of these genes detected in wild type animals, were all lost in Tm7sf2-/- mice.
27892461	0.98	Ldlr, Pcsk9 and Hmgr, while a slight increase in Srebf1c expression was observed (Supplementary Fig. 6I).
	0.98	HMG-CoA reductase (HMGR) by statins, inhibition of liver ACL by ETC-1002-CoA results in the suppression of cholesterol synthesis and compensatory LDLR upregulation and LDL particle clearance from the blood.
	0.97	HMGR, PCSK9 and LDLR mRNA, with maximum effects reaching 1.4, 1.3, 1.5 and 2.3-fold, respectively (Fig. 5f).
	0.97	LDL receptor activity (Fig. 5i), and in support of our clinical findings, the addition of ETC-1002 to atorvastatin increased LDL receptor activity above atorvastatin treatment alone, supporting that the co-suppression of ACL and HMG-CoA reductase activity is complementary (Fig. 5i).
25275627	0.98	LDLr and oxidized LDLr (LOX1), LPL, Abca1 and HMGCR were altered in the hearts during T. cruzi infection.
	0.98	HMGCR and LDLr expression which results in endogenous cholesterol biosynthesis and LDL-mediated uptake of cholesterol.
	0.98	HMGCR and LDLr protein levels in the tissues when the cells already had elevated intracellular LDL/cholesterol levels due to parasite invasion suggesting that infection results in dysfunctional cholesterol homeostasis in tissues and changes in the regulation of these key cholesterol homeostasis genes.
28395113	0.98	HMGCR, HMGCS, and LDLR) but also ameliorated SREBP-2 gene expression at low cholesterol levels (Fig. 8B).
	0.97	HMGCR, HMGCS, squalene synthase, and LDLR) and other lipid transport genes (adenosine triphosphate-binding cassette transporter A 1 and ACAT2) was reduced in CRTC2-/- mice (Fig. 5D).
	0.97	HMGCR and LDLR.
30911291	0.98	HMG-CoA reductase inhibitors prevent Abeta accumulation-induced apoptosis and synaptic injury in neurons by ameliorating the LDLR downregulation induced by OGD damage in microglia, suppressing microglia activity by blocking the pIkappaBalpha/pNF-kappaB signaling pathway and decreasing downstream inflammatory cytokines such as TNF-alpha, IL-1beta, and COX2 and upregulating the anti-inflammatory cytokine IL-10 (Figure 8).
	0.97	HMG-CoA reductase inhibitors prevent Abeta accumulation-induced apoptosis and synaptic injury in neurons by ameliorating the LDLR downregulation induced by OGD damage in microglia, suppressing microglia activity by blocking the pIkappaBalpha/pNF-kappaB signaling pathway and decreasing downstream inflammatory cytokines such as TNF-alpha, IL-1beta, and COX2 and upregulating the anti-inflammatory cytokine IL-10.
	0.95	HMG-CoA reductase inhibitors suppressed the OGD-induced LDLR downregulation and Abeta accumulation and further protected neurons from apoptosis and synaptic injury.
32111832	0.98	3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGCR) and squalene epoxidase (SQLE), and the low-density lipoprotein receptor (LDLR).
	0.98	Hmgcr, Sqs, Dhcr24, Pcsk9, and Ldlr (Fig. 4c).
	0.97	HMGCR, LDLR, SQLE, and FASN in response to sterol-depletion, in Hap1-SPRINGKO cells basal expression of these genes was reduced and the response to sterol-depletion was largely abrogated.
18852694	0.98	LDLR and 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase, the rate-limiting enzyme for cholesterol synthesis (Brown and Goldstein, 1997; Shimano, 2001).
	0.90	HMG-CoA reductase and farnesyl pyrophosphate synthases, although the effect of fenofibrate on plasma cholesterol levels and expression of LDLR in the liver was not examined in this report.
19721697	0.98	HMGCR are key enzymes in cholesterol synthesis, and LDLR is responsible for the uptake of low-density lipoprotein (LDL)-cholesterol from the blood.
	0.97	Hmgcr, Low density lipoprotein receptor (Ldlr), and Acetoacetyl-CoA synthetase (Aacs) in Rev-KO and TgRev animals suggested that the activity of SREBP2 was affected in these animals as well (Figure 1D), in spite of the apparently normal Srebp2 mRNA accumulation (Figure S4A).
25352833	0.98	HMGCR and decreases LDLR synthesis.
	0.97	LDL receptor (LOX-1), carbohydrate-responsive element binding protein (ChREBP), fatty acid synthase (FAS), and acyl-CoA carboxylase (ACC) was detected, whereas expression of SREBP-1, SREBP-2, HMGCR, peroxisome proliferator-activated receptor alpha (PPAR-alpha), fatty acid binding protein (L-FABP), and carnitine palmitoyltransferase 1A (CPT1A) was decreased.
25440061	0.98	LDLR, PCSK9, and HMGCR (Figure 1A).
	0.94	LDLR or HMGCR suggesting that IDOL inhibition can modulate plasma LDL levels independent of those parameters (Figure 4F).
26520906	0.98	LDLR, as well as 3-hydroxy-3methylglutaryl coenzyme A reductase (HMGCR), the rate-limiting enzyme of cholesterol biosynthesis.
	0.98	HMGCR and the LDLR, thereby enhancing LDL clearance from the plasma and ensuring that intracellular cholesterol levels are maintained.
28301372	0.98	HMGCR levels were only elevated in Dab2-Arh double knockout mice and in Ldlr-/- mice, but not in Arh-/- mice, could suggest that LDLR expression in sinusoid endothelial cells has a significant role in the liver uptake and sensing of cholesterol to preserve homeostatic cholesterol levels.
	0.78	HMG-CoA reductase (HMGCR) and cholesterol increase in the liver of Dab2-Arh double knockout mice was comparable to that of Ldlr-/- mice.
28427397	0.98	HMGCR and LDLR.
	0.95	HMGCR, LPL, and apoB and increased that of LXR in the liver tissue of HCD-fed LDLR-/- mice.
21459323	0.98	LDLR-/- mice with the blockade of VLDL/LDL clearance, which is consistent with decreased hepatic SREBP-2 processing and HMGCS and HMGCR expression.
23021221	0.98	Hmgcr, Lss and Dhcr24, were down-regulated by the HCHF diet, especially in LDLR KO mice (Figure 2B), with Dhcr24 being the most suppressed transcript among the entire set of transcripts evaluated.
23344002	0.98	LDLR and cholesterol biosynthetic enzymes such as HMG-CoA reductase by downregulating SREBPs, important transcriptional factors, which results in LDLR reduction.
23469003	0.98	Hmg-CoA reductase upregulation, may explain the strong hepatic lipid accumulation in Ldlr-/- as apparent at day 5 post infection.
23554170	0.98	HMGCR), HMG-CoA synthase (HMGCS), low density lipoprotein receptor (LDLR) and SREBP1/2 itself.
25023731	0.98	LDLR expression is modulated by multiple pathways within the cell: LDLR transcription is regulated by the sterol response element binding proteins (SREBPs), and HMGcoA reductase inhibitors (statins) activate SREBPs by inhibiting cholesterol synthesis within hepatocytes.
26828754	0.98	HMGCR is the rate-limiting step in cholesterol synthesis, and the low-density lipoprotein receptor (LDLR) is the primary mechanism for uptake of extracellular cholesterol.
27694328	0.98	Hmgcr, Ldlr, and Pcsk9.
27707816	0.98	LDLR and HMGCR.
28166809	0.98	3-hydroxy-3-methyl-glutaryl-CoA reductase (HMG-CoA) activity, stimulates acyl-CoA cholesterol acyltransferase (ACAT) and regulates the LDLR activity by a feedback mechanism.
28178673	0.98	HMGCR), which are involved in cholesterol uptake and synthesis, respectively, were down-regulated in a dose-dependent manner, suggesting the possibility that acRoots inhibited cholesterol uptake and synthesis by altering LDLR and HMGCR expression in HCC.
29073233	0.98	HMGCR activity and protein levels of INSIGs, SREBFs, as well as LDLR could be achieved by ubiquitin-mediated degradation involving ubiquitin ligases GP78, HRD1, TRC8, FBW7, and IDOL.
29183708	0.98	HMGCR and the low-density lipoprotein receptor (LDLR), thus promoting cholesterol biosynthesis and uptake.
29899496	0.98	Ldlr-/-Sort1-/- mouse jejunum had reduced LXR-related (Nr1h3, Nr1h2, Rxra, Apoe, Abca1, Abcg1, Srebf1, Ppara, Sp1, Hnf4a) and sterol-related (Hmgcr, Hmgcs1, Cyp27a1, Vldlr) mRNA levels (Fig. 5a and Supplementary Fig. S3c).
30785396	0.98	HMGCR and other cholesterol biosynthetic enzymes as well as the low density lipoprotein (LDL) receptor that removes cholesterol-rich LDL from circulation.
31327168	0.98	Hmgcr, Acss2, Pmvk, Mvd, Fdft1, Ldlr, and Sqle (Figure 2A).
19260826	0.97	Hmgcr and Ldlr, two preferential SREBP-2 target genes, was suppressed by desmosterol.
	0.95	HMG-CoA reductase (Hmgcr), the LDL receptor (Ldlr) and Insig1 were lower in 25HC-treated cells than in controls (Figure 4B).
	0.95	Hmgcr, Ldlr and Insig1 mRNA levels (Figure 4B), although less potently than 25HC.
	0.95	Hmgcr, Ldlr and Insig1 expression (Supplementary Figure S2).
	0.94	Hmgcr and Ldlr mRNAs were paralleled by reductions of HMG-CoA reductase and LDL receptor protein levels (Figure 4C).
	0.80	HMG-CoA reductase and LDL receptor protein levels, although the effect on the former protein was null when cholesterol was added in ethanol (Figure 4C).
26167919	0.97	Hmgcr, Ldlr, Scarb1 in superovulated ovaries suggested hCG might accelerate the luneinaization.
	0.93	Hmgcr, Ldlr, Scarb1 in COH groups was accompanied by the up-regulation of Lhcgr, which suggested the correlation between cholesterol and hormone.
	0.91	HMG-CoA reductase (HMGCR), Scavenger receptor class B type I (SCARB1), low-density lipoprotein receptor (LDLR) and Lhcgr were shown in COH groups in ovaries 15h or 39h after hCG injection (Fig 3A and 3B).
	0.66	Hmgcr, Ldlr, Scarb1 in HCOH group were lower compared with those in LCOH group at 15h-post hCG injection.
26980316	0.97	LDLR regulatory elements, they showed that small interfering RNA oligonucleotides and microRNA (miRNA) specific for murine HMGCR transcripts increased LDLR promoter activity by 300-fold and 12-fold, respectively.
	0.96	HMGCR provides an effective complementary strategy for enhancing LDLR transgene expression.
	0.95	LDLR gene therapy with RNA silencing of HMGCR is a further strategy intended to enhance LDLR gene expression.
	0.80	HMGCR-specific miRNA plasmids with pLDLR-LDLR into Ldr-/- mice, they observed significantly lower LDL-C levels (-~1.5mmo/L, p=0.0036) in these mice as compared with controls that only received the pLDLR-LDLR plasmid.
28565758	0.97	HMG-CoAR, LDL-R, and CYP7A1, involved in cholesterol synthesis, absorption, and metabolism have been studied by measuring their expression at the level of mRNA using RT-PCR to determine the effect of apigenin on cholesterol metabolism.
	0.94	LDL-R is an important receptor that mediates liver uptake of LDL-C. It was shown in the present study that the mRNA levels of HMG-CoAR, CYP7A1, and LDL-R in the liver of mice of the model group decreased significantly following exposure to a high-fat diet compared with those in the normal control group.
	0.88	HMG-CoAR, CYP7A1, and LDL-R) were examined by RT-PCR.
	0.81	HMG-CoAR, CYP7A1 and LDL-R mRNA in the liver of mice with hyperlipidemia
28970592	0.97	3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase in LDLR+/- mice.
	0.97	3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase in LDLR+/- mice.
	0.95	HMG-CoA reductase and increases circulating levels of PCSK9 by as much as 30%, compared with placebo, making them somewhat self-limiting to further reduce LDL-C. This likely occurs because the transcription factor SREBP-2, that is indirectly up-regulated by statin, activates the Ldlr and Pcsk9 genes.
	0.82	Ldlr and Pcsk9 genes, and thus makes statin somewhat self-limiting to further reduce LDL-C. To assess the effect of PCSK9Qbeta-003 vaccine on lipid homeostasis in LDLR+/- mice, we evaluated the mRNA expression of SREBP-2, HNF-1alpha and HMG-CoA reductase in liver.
26042593	0.97	Hmgcr and Ppara expression, while in MCS diet-fed controls Ldlr expression was significantly attenuated.
	0.97	Ldlr (LDL uptake / clearance) and Hmgcr (rate-limiting enzyme in cholesterol synthesis) were attenuated by miR-155 deficiency in HFD model.
	0.96	Ldlr and Hmgcr mRNA expression in MCD diet-fed WT mice compared to MCS controls.
23840542	0.97	LDLR, SR-B1, apoA1, apoE, HMGCR, SREBP1c, LXRalpha and PPARgamma.
	0.87	LDLR, HMGCR, apoA1 and apoE expression notably abolished while making the down-regulation of DHC on SRA1 expression markedly compensated.
26226008	0.97	HMGCoA-R, HMGCoA-S1, methylsterol monoxygenase (SC4MOL), LDLR, and SRB1, and decreases cholesterol efflux and catabolism by suppressing ABCA1, ABCG1, ABCG5/G8, and CYP7A1.
	0.96	3-hydroxy-3-methylglutaryl CoA reductase (HMGCoA-R), 3-hydroxy-3-methylglutaryl CoA synthase 1 (HMGCoA-S1), LDL receptor (LDLR), and scavenger receptor B1 (SRB1).
22441164	0.97	HMGCR, FPPS, IDI1, SQS, squalene epoxidase (SQLE), lanosterol synthase (LSS), 7-dehydrocholesterol reductase (DHCR7), LDL receptor (LDLR) and Insig-1 were all significantly increased 1.6- to 4.7-fold in P0 129 Pex2-/- versus control mouse liver.
30510211	0.97	Ldlr-/- mice, and Cmpd 81 synergizes with lovastatin to further decrease lipid levels (Fig. 6e and Supplementary Fig. 7g), indicating that induced degradation of HMGCR may bring therapeutic benefit to treat NASH.
27499577	0.96	HMGCR, LDLR, CYP7alpha1 and PPAR-alpha proteins in the liver; and the SREBP-1, SCD-1, FAS, PPAR-alpha and adiponectin proteins in adipose tissue were reversed by PGBR.
	0.94	HMGCR (78%), and increase in LDLR (50%), CYP7alpha1 (66%) and PPARalpha (75%) protein levels compared with the HFD group (Fig. 1).
	0.92	HMGCR, increasing LDLR, CYP7alpha1 and recovering adiponectin through regulating PPARs.
	0.91	HMGCR, LDLR, CYP7alpha1, PPARalpha, and adiponectin in liver and adipose tissue were recovered by PGBR.
	0.90	HMGCR, LDLR, CYP7alpha1 and PPARalpha protein expressions in liver of high-fat diet (HFD) fed mice.
20498851	0.96	LDLR and HMGCoAR.
	0.94	LDLR and HMGCoAR at 24 h post-transfection (Figures 2 and 3 and S1), likely due to the down-regulation of SREBP activity in presence of lipids/sterols present in the lipofectamine reagent, as previously reported.
24506864	0.96	HMGCR in Ldlr-/-/Lrp6mut/mut vs. Ldlr-/- mice (Figure 5C and 5D).
27022257	0.96	HMG-CoA reductase inhibitors lead to an increase in LDL receptors, it is also possible that Simva could have further increased LDL-receptor overexpression, allowing the internalization of larger amounts of PTX associated with LDE into the melanoma tumor cells.
30582457	0.96	Ldlr, Pcsk9, Hmgcr or Srebf2 (Figure 6D-F).
30354208	0.95	LDLR mRNA levels in all tested HPHs, whereas mRNA levels of HMGCR, SREBP1 and SREBP2 were unchanged (Fig. 5A-C).
	0.94	Ldlr mRNA levels significantly to 1.7-fold of control, whereas other typical SREBP2-target genes such as Pcsk9 and Hmgcr were unaffected by OCA.
31767163	0.95	HMG-CoA reductase and squalene synthase enzymes, as well as of LDLR and LRP1 (HMGCR: t(4) = 9.38, p = 0.007; FDFT1: t(4) = 17.43, p < 0.0001; LDLR: t(4) = 11.80, p = 0.0003; LRP1; t(4) = 0.60, p = 0.58).
	0.92	LDLr also resulted in downregulation of HMGCR and FDFT1, albeit to a smaller extent.
24025456	0.95	3-hydroxy-3-methylglutaryl-Coenzyme A reductase (HMGCR), the LDL receptor (LDLR), or sterol regulatory element binding protein, type 2 (SREBP-2) as the major cholesterol-related transcriptional regulator, did identify sex differences in disruption of cholesterol homeostasis and disease outcome (e.g., in NAFLD).
30891077	0.95	LDLR and NPC1L1 ), synthesis (PPARalpha , SREBP1/2 , and HMGCR ), and excretion (CYP7A1 and ABCG5/8 ) in liver or small intestine.
24158514	0.91	HMGCR, PCSK9) in mouse primary hepatocytes were not affected by Ad-shHNRNPD infection (Figure 5C), thus confirming the specific targeting effect of the shRNA to hnRNP D. The reduction of hnRNP D by Ad-shHNRNPD transduction with a consequential increase in LDLR protein level was also observed in mouse hepatoma-derived cells (Figure 5D).
20470821	0.90	HMG-CoA reductase, the cholesterol transport protein apolipoprotein E (ApoE), the adenosine triphosphate (ATP) binding cassette (ABC) transporter proteins A1 and G1 (ABCA1, ABCG1), the low-density lipoprotein receptor (LDLR) and LDLR-related protein (LRP), the oxysterols 24S-hydroxycholesterol and 27-hydroxycholesterol to which cholesterol is converted in the brain and body, respectively, and the liver X-activated receptors (LXRs) for which oxysterols are ligands and that induce expression of ApoE and ABCA1 genes.
32084149	0.89	LDLR or HMGCoA reductase with ribose-cysteine treatment, suggesting no effect on LDL uptake or cholesterol synthesis via the SREPB2 pathway.
18771980	0.88	HMGCR and LDLR, and to study the correlations between the expression of these mediators.
	0.66	HMGCR pathway (and of LDLR) in the apoE+/-mat group underscores the validity of our hypothesis based on the current data.
19014463	0.83	HMG CoA reductase, LDL receptor and Egr-1 transcription factor gene, that are also activated by IGF-1 in this study.
29404461	0.81	LDLR mRNA.35, 36 However, these agents would not inhibit HMGCR mRNA expression.