ライフサイエンスコーパス: HMG

1 HMG Co-A reductase negatively regulates eNOS, and the PL

2 HMG domain transcription factor, Sox2, is a critical gen

3 HMG-CoA lyase (HMGCL) is crucial to ketogenesis, and inh

4 HMG-CoA reductase (HMGR) catalyzes a rate-limiting step

5 HMG-CoA reductase (HMGR) undergoes feedback-regulated de

6 HMG-CoA reductase catalyzes the four-electron reduction

7 HMG-CoA reductase inhibitors (statins) improve cutaneous

8 HMG-CoA reductase inhibitors or statins are associated w

9 HMG-CoA reductase inhibitors such as statins are cholest

10 HMG-coA reductase inhibitors, commonly known as statins,

11 HMG-CoA reductase levels are regulated in response to st

12 HMG-CoAR is the central enzyme of the mevalonate pathway

13 HMG-CoAR regulates the oncogenic Hippo transducers TAZ/Y

14 HMG-CoAR was positively associated with the expression o

15 HMG-D and ZmHMGB1 differ from HMGB1 in having phosphoryl

16 ested that the transcription factor Sox11, a HMG-domain containing protein that is highly expressed i

17 cells increased expression of KLF2 through a HMG-CoA/prenylation-dependent pathway.

18 olog of 3-hydroxy-methylglutaryl coenzyme A (HMG CoA) lyase (HCL1).

19 beta-hydroxy-beta-methylglutaryl coenzyme A (HMG CoA) reductase inhibitors (statins) within 60 days a

20 ) and 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR)) has been linked to cholestero

21 le of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase and alphaPix.

22 f the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase and subsequently the isoprenylation o

23 ular 3-hydroxy-3-methyl-glutaryl-coenzyme A (HMG-CoA) reductase inhibitor (statin) treatment for dysl

24 ntly, 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase inhibitors (statins) have been the ma

25 RBs), 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase inhibitors (statins), and selective s

26 the 3-hydroxyl-3-methylglutaryl coenzyme A (HMG-CoA) reductase inhibitors known as statins have anti

27 Hydroxy-methyl-glutaryl-coenzyme A (HMG-CoA) reductase inhibitors or statins are well tolera

28 s, or 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase inhibitors, have anti-inflammatory ef

29 le or 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase.

30 nate [3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase] pathway synthesizes lipids for G-pro

31 ds to 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) synthase and irreversibly inhibits HMG-CoA synt

32 levels of hydroxymethylglutaryl-coenzyme A (HMG-CoA) synthase, squalene epoxidase, and acyl-CoA:chol

33 Antibodies against HMG-CoA reductase apparently provoke SINAM.

34 An autoantibody directed against HMG-CoA reductase (HMGCR), the pharmacologic target of s

35 Treatment with small interfering RNA against HMG-CoA synthase led to a substantial reduction in HCV r

36 Although HMG Co-A reductase inhibitors ("statins") may prevent ca

37 eptor (IGF1R) inhibitor, and fluvastatin, an HMG-CoA reductase inhibitor, as potential chemopreventiv

38 Amphoterin is an HMG protein (HMGB1) that has been shown to have extranuc

39 SOX9 is an HMG-box transcription factor that plays an essential rol

40 Simvastatin, an HMG-coA reductase inhibitor, is known to attenuate infla

41 SOX2, an HMG box transcription factor, plays an essential role in

42 f cholesterol biosynthesis using statins (an HMG-CoA reductase inhibitor) significantly increased the

43 plementary activity between these agents and HMG-CoA reductase inhibitors (statins) based on their ab

44 nd Tip60 interact directly via the ATXN1 and HMG-box protein 1 (AXH) domain of ATXN1.

45 Sp100 isoforms contain SAND, PHD, Bromo, and HMG domains and are highly sumoylated, all characteristi

46 and spliced into four isoforms (A, B, C, and HMG), which differentially regulate transcription.

47 oteins 1c and 2, acetyl-CoA carboxylase, and HMG-CoA reductase mRNAs/proteins and inactive non-phosph

48 ylglycerol, diacylglycerol, malonyl-CoA, and HMG-CoA.

49 edback response, which upregulates HMGCR and HMG-CoA synthase 1 (HMGCS1) following statin treatment.

50 rol synthesis, HMG CoA synthase (HMGCS1) and HMG CoA reductase (HMGCR), were also reduced in PGC1alph

51 ensin-converting enzyme (ACE) inhibitors and HMG CoA reductase inhibitors (statins) have more than do

52 ered N-terminal region consisting of PHD and HMG domains and receptor-binding motifs.

53 PKG phosphorylates K-RAS and HMG CoA reductase inhibitors reduce K-RAS farnesylation

54 hepatic low-density lipoprotein receptor and HMG-CoA reductase expression in ApoE-p50-DKO but not in

55 SREBP cleavage-activating protein (SCAP) and HMG-CoA reductase (HMGR) both possess SSDs required for

56 red for the feedback inhibition of SREBP and HMG-CoA reductase (HMGR).

57 e rescued by cholesterol supplementation and HMG Co-A reductase inhibition.

58 Anti-HMG-CoA reductase-positive patients can be further subdi

59 -associated myopathy, statin-associated anti-HMG-CoA reductase-positive autoimmune myopathy, and stat

60 e autoimmune myopathy, and statin-naive anti-HMG-CoA reductase-positive myopathy.

61 Statins are HMG-CoA reductase inhibitors that are known to inhibit c

62 served ER-anchored ubiquitin ligases such as HMG-CoA reductase degradation1 (Hrd1).

63 rast, the effects of hymeglusin on bacterial HMG-CoA synthase, mvaS, have been minimally characterize

64 larly to the DNA-binding faces of both basic HMG boxes.

65 ist in dynamic assemblies in which the basic HMG boxes and linkers associate with their intrinsically

66 A positive relationship emerged between HMG-CoAR, hormone receptors and TAZ/YAP, suggesting a co

67 erol uptake (LDL receptor) and biosynthesis (HMG-CoA reductase).

68 Statins block HMG-CoA reductase (HMGCR), the rate-limiting enzyme of t

69 nce assignments from the NMR spectra of both HMG-boxes of TFAM.

70 In yeast, the membrane-bound HMG-CoA reductase degradation (HRD) ubiquitin-ligase com

71 a nucleus-encoded, high-mobility-group-box (HMG-box) protein that regulates transcription of the mit

72 insights into the binding mechanisms used by HMG boxes to recognize varied DNA structures and sequenc

73 was characterized and demonstrated to cleave HMG-CoA to acetoacetate and acetyl-CoA with catalytic an

74 th elevated 3-hydroxy-3-methyl-glutaryl-CoA (HMG-CoA) reductase activity and mRNA levels.

75 hat inhibit 3-hydroxy-3-methyl-glutaryl-CoA (HMG-CoA) reductase, the rate-limiting enzyme in the synt

76 ident enzyme 3-hydroxy-3-methylglutaryl CoA (HMG-CoA) reductase catalyzes the rate-limiting step in s

77 3-Hydroxy-3-methylglutaryl-CoA (HMG-CoA) lyase (HMGL) is involved in branched-chain amin

78 cedented (R)-3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) stereospecific route in nature.

79 homologues, 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) synthase and the fatty acid biosynthesis enzyme

80 erivatives, such as acetyl-CoA, butyryl-CoA, HMG-CoA, and malonyl-CoA, as well as NADPH but not NADP(

81 CSA13 inhibited colonic HMG-CoA reductase activity in an FPRL1-dependent manner.

82 omatic residue (position 15 of the consensus HMG box) that is invariant among SRY-related HMG box tra

83 e we describe a role of the highly conserved HMG-box transcription factor SOX-2 in postmitotic specif

84 a disprove the hypothesis that the conserved HMG box domain is the only functional domain of Sry, and

85 roteins are composed of one or two conserved HMG box domains, each forming three alpha-helices that f

86 mphoid enhancer factor (LEF) factors contain HMG domains and bind to related consensus sites.

87 finger domains (ZF1-3) and the corresponding HMG DNA-binding domain of TCF3/4 factors.

88 edded ubiquitin ligases, in yeast Hrd1/Der3 (HMG-CoA reductase degradation/degradation of the ER) and

89 experiments show that the drug can displace HMG box-containing proteins essential for kDNA function

90 tion in Npc1a weakens the ability of ectopic HMG Coenzyme A reductase (Hmgcr) to induce germ cell mig

91 We found that two out of eight HMG samples showed trisomy of chromosome 1q, which encom

92 sumoylation state of Caenorhabditis elegans HMG-CoA synthase (HMGS-1).

93 treatment and variants in the gene encoding HMG-CoA reductase are associated with reductions in both

94 BIAD1 to the cholesterol biosynthetic enzyme HMG CoA reductase (HMGCR), thereby inhibiting its endopl

95 BIAD1 to the cholesterol biosynthetic enzyme HMG CoA reductase, which is subject to sterol-accelerate

96 ERAD of the cholesterol biosynthetic enzyme HMG-CoA reductase.

97 pathway, including the rate-limiting enzyme HMG-CoA reductase.

98 re better in patients whose tumors expressed HMG-CoAR (p = 0.044 and p = 0.043).

99 y of TFAM is mainly contributed by its first HMG-box, while the second HMG-box has low-DNA-binding ca

100 ible wavelength spectrophotometric assay for HMG-CoA synthase has been developed.

101 225 MBC samples were immunostained for HMG-CoAR and 124 were considered eligible for exploring

102 lky tryptophan opposite the binding site for HMG Box A at both 12- and 23-spacer recombination signal

103 NA levels of the cholesterol synthesis genes HMG CoA reductase, squalene synthase, and FPP synthase b

104 le and multiple 3-hydroxy-3-methyl-glutaryl (HMG) substitutions.

105 d expression of 3-hydroxy-3-methyl-glutaryl (HMG)-CoA reductase (Hmg1) under iron starvation, reduced

106 an inhibitor of 3-hydroxy-3-methyl-glutaryl (HMG)-CoA reductase and the N-bisphosphonate zoledronic a

107 y prepared from isolated human milk glycans (HMGs), and our studies on their recognition by viruses,

108 support for the role of the N-terminal gp59 HMG motif in fork binding and the interaction of the C-t

109 Y comprises a conserved high-mobility group (HMG) box DNA-binding domain and poorly conserved regions

110 a DNA sequence-specific high-mobility group (HMG) box that binds Wnt response elements (WREs).

111 sisting of a quartet of high-mobility group (HMG) box transcription factors, SOX4, SOX13, TCF1, and L

112 e Y chromosome)-related high mobility group (HMG) box) proteins require the calcium-binding protein c

113 ions cluster in the SRY high mobility group (HMG) box, a conserved motif of specific DNA binding and

114 inding is mediated by a high mobility group (HMG) box.

115 on factor A (TFAM) is a high-mobility group (HMG) protein at the nexus of mitochondrial DNA (mtDNA) r

116 chondria (TFAM), a dual high-mobility group (HMG) protein involved in maintenance and compaction of t

117 ning DNA, whereas three high-mobility group (HMG) proteins (i.e., HMGB1, HMGB2, and mitochondrial tra

118 High mobility group (HMG) proteins concentrate in the nucleus, interacting wi

119 tural homology with the high mobility group (HMG) proteins from eukaryotic organisms.

120 Here we show that the high-mobility group (HMG) transcription factors Tcf1 and Lef1 are essential f

121 e the expression of the high mobility group (HMG)-box transcription factor SOX-2 for the specificatio

122 proteins belong to the high-mobility-group (HMG) domain-containing transcription factors, and functi

123 e linker histone H1 and high-mobility-group (HMG) proteins with nucleosomes leads to changes in chrom

124 ng WDHD1 (WD repeat and high mobility group [HMG]-box DNA-binding protein), one of the genes that was

125 Hemimegalencephaly (HMG) is a developmental brain disorder characterized by

126 undant vertebrate chromosomal protein HMGB1 (HMG-D and ZmHMGB1, respectively) differ from HMGB1 in ha

127 The HRD (HMG-CoA reductase degradation) pathway is a conserved ro

128 amino acids are normally conserved in human HMG proteins and 27 are conserved in the human Sox sub-f

129 ollection as a previously unidentified human HMG-CoA lyase (HMGCL).

130 Hydroxmethylglutaryl (HMG)-coenzyme A (CoA) reductase inhibitors (statins) low

131 n vitro results with 24S-hydroxycholesterol, HMG CoA reductase and squalene synthase mRNA levels were

132 diminution of sterol synthesis, identifying HMG-CoA synthase as a potential drug target and suggesti

133 A total of 33 amino acids in HMG proteins are known to have natural variants in disea

134 lso causes a 65% protein content decrease in HMG-CoA reductase (HMGR) and a 28% decrease in sterol sy

135 addition, both fungi and humans deficient in HMG CoA lyase accumulate acidic intermediates as a conse

136 ovascular risk parameters via a reduction in HMG-CoA reductase activity, along with an increase in ar

137 ly, deletion of SET1 leads to a reduction in HMG-CoA reductase protein and total cellular ergosterol.

138 Numerous natural variants in HMG proteins are associated with disease phenotypes.

139 hen administered at a high dosage (including HMG-CoA reductase inhibitors >75 mg/day/adult).

140 ore rapidly after mTOR inhibition, including HMG-CoA synthase, whose enhanced degradation probably li

141 15(S)-HETE by inducing HMG-CoA reductase expression caused increased farnesylat

142 risk reduction from medications that inhibit HMG-CoA reductase; further research is needed to underst

143 Statins lower cholesterol by inhibiting HMG-CoA reductase, the rate-limiting enzyme of the metab

144 (HMG-CoA) synthase and irreversibly inhibits HMG-CoA synthase in a dose-dependent manner.

145 Interestingly, HMG-CoA reductase, the rate-limiting enzyme in cholester

146 DNA looping assays in vivo that an isolated HMG box A domain derived from human HMGB2 folds poorly a

147 these lncRNAs with high affinity through its HMG DNA-binding domain in vitro.

148 trate that TFAM is phosphorylated within its HMG box 1 (HMG1) by cAMP-dependent protein kinase in mit

149 The E3 ubiquitin ligase HMG-coA reductase degradation 1 homolog (Hrd1) and, cons

150 requirement for mitochondrial OPA3 to limit HMG-CoA-derived MGC and protect the electron transport c

151 Duplication of the mating type matA(HMG) gene in this haploid organism triggers Mat-induced

152 s as a specific feature associated with matA(HMG) regulation during sexual development.

153 m (ER)-localized 3-hydroxy-3-methylglutaryl (HMG) CoA reductase.

154 Mammalian 3-hydroxy-3-methylglutaryl (HMG)-CoA reductase (HMGR) undergoes sterol-dependent, en

155 3-Hydroxy-3-methylglutaryl (HMG)-CoA reductase (HMGR), the rate-limiting enzymes of

156 eptor-binding motifs, SET methyltransferase, HMG and PHD domains.

157 pa3 mutants derives from extra-mitochondrial HMG-CoA through a non-canonical pathway.

158 d protein analysis identified, mitochondrial HMG-CoA synthase, aldehyde dehydrogenase, and catalase a

159 articularly high levels of the mitochondrial HMG-CoA synthase 2 (Hmgcs2) compared with all other tiss

160 enhanced when the USD is fused with the MLL4 HMG-box.

161 Moreover, HMG-CoAR expression may be a favorable prognostic indica

162 ion, revealed the features of a noncanonical HMG box.

163 te myocardin function, we identified a novel HMG box-containing protein HMG2L1 (high mobility group 2

164 were similar to each other and to other NSS HMG-box proteins.

165 haromyces pombe, where the nucleocytoplasmic HMG protein Oxs1 acts cooperatively with Pap1 to regulat

166 d a unique signature implicating activity of HMG (TCF) and RHD (NF-kappaB) transcription factor famil

167 W-FO) on serum and liver lipids, activity of HMG-CoA reductase in liver microsomes and EPA+DHA incorp

168 The activity of HMG-CoA reductase was reduced (p<0.05) in the FVW-FO fed

169 anti-HCV effects are reversed by addition of HMG-CoA, mevalonic acid, or geranylgeraniol.

170 Statins, a class of HMG-CoA reductase inhibitors, display pleiotropic immuno

171 cated in the sterol-regulated degradation of HMG-CoA reductase and Insig-1 through ER-associated degr

172 the robust sterol-accelerated degradation of HMG-CoA reductase.

173 ole in the sterol-accelerated degradation of HMG-CoA reductase.

174 The DNA binding domain of HMG proteins is known to be important in many diseases,

175 ate, an inhibitor of an enzyme downstream of HMG-CoA reductase, and to gliotoxin, an inhibitor acting

176 de of geranyl lipid production downstream of HMG-CoA reductase.

177 ive study designed to evaluate the effect of HMG-CoA reductase inhibitors on atherosclerosis.

178 ngly, renal as well as hepatic expression of HMG-CoA synthase 2 increased with prolonged starvation.

179 in many diseases, with the Sox sub-family of HMG proteins of particular significance.

180 genetic variant known to mimic inhibition of HMG-CoA reductase (the intended drug target) with the sa

181 posure was genetically proxied inhibition of HMG-CoA reductase and secondary exposures were genetical

182 maging sensor, we confirm that inhibition of HMG-CoA reductase blocks MYC phosphorylation in vivo.

183 Here, we show that inhibition of HMG-CoA reductase by atorvastatin (AT) blocks both MYC p

184 3 silencing or pharmacological inhibition of HMG-CoA reductase in these cells decreases protein isopr

185 The inhibition of HMG-CoA reductase may be a useful target for the treatme

186 Finally, we show that inhibition of HMG-CoA reductase suppresses MYC phosphorylation through

187 Genetically proxied inhibition of HMG-CoA reductase was significantly associated with lowe

188 were used to proxy therapeutic inhibition of HMG-CoA reductase, Niemann-Pick C1-Like 1 (NPC1L1) and p

189 rs blocks their sensitivity to inhibition of HMG-CoA reductase.

190 s its anti-HCV effects through inhibition of HMG-CoA synthase.

191 Simvastatin, a potent inhibitor of HMG-CoA reductase, suppressed 15(S)-HETE-induced Rac1 ac

192 The interaction of HMG proteins with chromatin is dynamic.

193 nsmembrane span ER-resident Hmg2p isozyme of HMG-CoA reductase fused to GFP, which undergoes regulate

194 l fibrosis via FPRL1-dependent modulation of HMG-CoA reductase pathway.

195 pplementation with the enzymatic products of HMG-CoA reductase functionally rescued lymphangiogenic s

196 ase catalyzes the four-electron reduction of HMG-CoA to mevalonate and is an enzyme of considerable b

197 er increase in SREBP2 and down-regulation of HMG-CoA reductase protein.

198 ar free cholesterol, causing upregulation of HMG Co-A reductase, the rate-limiting enzyme in choleste

199 reased capture of ZOL and by upregulation of HMG-CoA synthase and reductase transcription.

200 sights into diverse recognition functions of HMGs and show the utility of the SGM approach and MAGS a

201 Further identification of serine ADPr on HMG proteins and hundreds of other targets indicates tha

202 Statins, or HMG CoA (3-hydroxy-3-methylglutaryl-coenzyme A) reductas

203 In other organisms, HMG CoA lyase catalyzes the last step in the leucine cat

204 of the rate-limiting enzyme in the pathway, HMG-CoA reductase (HMGCR).

205 olesterol metabolism proteins such as PCSK9, HMG-CoA reductase, ATP citrate lyase, and NPC1L1.

206 l components of red mold fermented products, HMG-CoA reductase inhibitors, did not exacerbate pre-exi

207 In the primary analysis, genetically proxied HMG-CoA reductase inhibition equivalent to a 1-mmol/L (3

208 CA1/2 mutation carriers, genetically proxied HMG-CoA reductase inhibition was associated with lower o

209 hypolipidemic property of FVW-FO and reduced HMG-CoA reductase activity which is proportional to the

210 droxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase) by statins has shown potential effica

211 droxy-3-methylglutaryl-coenzime A reductase (HMG-CoA) reductase.

212 actor sex-determining region Y (SRY)-related HMG box 2 (SOX2) in regulating the epigenetic landscape

213 iments indicated that the LSC is SRY-related HMG box transcription factor 9 positive (Sox9(+) ) and c

214 HMG box) that is invariant among SRY-related HMG box transcription factors (the SOX family) and conse

215 Sox genes code for SRY-related HMG domain-bearing transcription factors involved in var

216 The SRY-related HMG-box 5 (SOX5) gene encodes a member of the SOX family

217 The SRY-related HMG-box family of transcription factors member SOX2 regu

218 ciated transcription factor, and SRY-related HMG-box gene 10).

219 SOX6 belongs to a family of 20 SRY-related HMG-box-containing (SOX) genes that encode transcription

220 , including sex-determining region Y-related HMG box 2 (Sox2), a well established regulator of stem c

221 a and Sox9 (sex determining region Y-related HMG box transcription factor 9).

222 We studied resected HMG tissue to test whether the condition might reflect s

223 etoacetate synthesis when incubated with (S)-HMG-CoA.

224 buted by its first HMG-box, while the second HMG-box has low-DNA-binding capability.

225 t stem cells specifically recognized several HMGs that were then further structurally defined as nove

226 of Mice also specifically recognized several HMGs.

227 The total neutral and sialylated HMGs were derivatized with a bifunctional fluorescent ta

228 egion Y) encode proteins containing a single HMG (high-mobility group) domain.

229 a protein that bent DNA similar to a single HMG box and only at higher protein concentrations.

230 tively) differ from HMGB1 in having a single HMG box, as well as basic and acidic flanking regions th

231 argeting activities of Oct4 (POU DBD), Sox2 (HMG box DBD), Klf4 (zinc finger DBD), and c-Myc (bHLH DB

232 umably normal development, but 12 other SOX4 HMG-domain missense variants are recorded and all demons

233 ether, these findings point to specific SOX4 HMG-domain missense variants as the cause of a character

234 r that is a fungal ortholog of the hSRY/SOX9 HMG box proteins.

235 in the highly conserved, SOX family-specific HMG domain, but each alters a different residue.

236 Basal protein levels of SREBP2, HMG-CoA reductase, and steroidogenic acute regulatory pr

237 We found that Sry HMG box protein 9-positive (Sox9(+)) epithelial cell adh

238 nt, and hybrid MatA protein carrying the SRY HMG box is fully capable of driving both early and late

239 Statins (HMG-CoA reductase inhibitors) are the most prescribed cl

240 y deficient HMGCL R41M mutant with substrate HMG-CoA have been determined to 2.4 and 2.2 A, respectiv

241 -limiting enzymes for cholesterol synthesis, HMG CoA synthase (HMGCS1) and HMG CoA reductase (HMGCR),

242 binding protein HMGB1 consists of two tandem HMG-box domains joined by a basic linker to a C-terminal

243 in-induced upregulation of the statin target HMG-CoA reductase.

244 ns are cholesterol-lowering drugs, targeting HMG-CoA reductase, thereby reducing the risk of coronary

245 sive and cooperative binding of the two TFAM HMG-box domains and the linker between them.

246 vere growth defect in BMDMs, indicating that HMG CoA lyase gene function is critical for macrophage c

247 There is experimental evidence to show that HMG-CoA reductase inhibitors (statins) may inhibit proli

248 analyses for 10-year survival suggested that HMG-CoAR expression is a protective factor (HR 0.50, 95%

249 findings demonstrate for the first time that HMG-CoA reductase plays a determinant role in 12/15-Lox-

250 The HMG box has structural conservation between the first tw

251 The HMG box transcription factor SOX4 involved in neuronal d

252 The HMG domain within HMGB2 is crucial for interaction with

253 The HMG-box transcription factor LEF1 controls many developm

254 The HMG-Box transcription factor SOX2 is expressed in neural

255 The HMG-COA reductase degradation 1 (HRD1) and degradation o

256 The HMG-CoA reductase inhibitors (statins) are widely prescr

257 /LSP complexes are dynamic entities, and the HMG boxes induce the U-turn against the tendency of the

258 ch are presumably displaced from DNA and the HMG boxes, respectively, in the HMGB1-nucleosome complex

259 ed with the PKG activator sildenafil and the HMG CoA reductase inhibitor atorvastatin to further redu

260 es the PWWP domain of LEDGF proteins and the HMG domain of SSRP1.

261 ith the DNA-binding proteins Rsc3/30 and the HMG protein, Hmo1, to remodel partially-unwrapped nucleo

262 We also show that BCL11A and the HMG-box-containing transcription factor SOX6 interact ph

263 Minor-groove DNA binding by the HMG box results in substantial DNA bending toward the ma

264 adult pituitary progenitors that express the HMG box transcription factors SOX2 and SOX9.

265 ondensation with acetoacetyl-CoA to form the HMG-CoA product.

266 Here we identify the HMG-box transcription factor TOX as a central regulator

267 Two of these variants are located in the HMG domain and abolish SOX6 transcriptional activity in

268 Proteins in the HMG family are important transcription factors.

269 tion elsewhere in the protein, including the HMG box.

270 ulates DNA binding and bending by one of the HMG boxes in the FL protein.

271 oteins, including a divergent version of the HMG domain.

272 Individual sub-groups of the HMG family have specificity in the location of the third

273 Helices alpha1 and alpha2 of the HMG-box constitute the main p53-binding region.

274 to dissect the ERK-dependent control of the HMG-box repressor Capicua (Cic), which plays critical ro

275 LDLR SRE was observed in the presence of the HMG-CoA reductase inhibitor, lovastatin, when PP2A activ

276 The up-regulation of the HMG-CoA reductase pathway in the endothelium is the majo

277 d the binding capacity depends mainly on the HMG box-A domain of TFAM.

278 nerves during embryogenesis and rely on the HMG domain containing Sox10 transcription factor for spe

279 ain and poorly conserved regions outside the HMG box.

280 Missense variants primarily target the HMG domain, the SOX hallmark that mediates DNA binding a

281 arteriovenous angiogenesis by targeting the HMG-CoA reductase (HMGCR) pathway.

282 et al., in this issue, demonstrates that the HMG-CoA reductase inhibitor lovastatin can normalize pro

283 ructure with fork DNA has suggested that the HMG-like domain could bind to the duplex DNA ahead of th

284 iposomes ([S]-LIP), that are loaded with the HMG-CoA reductase inhibitor simvastatin [S], were evalua

285 hyl-beta-cyclodextrin, 2) treatment with the HMG-CoA reductase inhibitor simvastatin, and 3) shRNA-me

286 were partially rescued by treatment with the HMG-CoA reductase inhibitor simvastatin.

287 ts of AT are blocked by cotreatment with the HMG-CoA reductase product mevalonate.

288 Therefore, HMG-CoA reductase is a critical regulator of MYC phospho

289 ay inhibitors targeting downstream enzyme to HMG-CoA reductase (upstream enzyme) and farnesyl-pyropho

290 HMGB1 contains two HMG boxes that bind and bend DNA (the A box and the B bo

291 nitor cells (CPCs) that express the Sry-type HMG box gene Sox17 from embryonic day (E) 7.5 to E8.5 sp

292 sociated degradation (ERAD) of ubiquitinated HMG CoA reductase (HMGCR), the rate-limiting enzyme of t

293 Understanding HMG-CoA reductase regulation has tremendous implications

294 ction in HCV replication, further validating HMG-CoA synthase as an enzyme essential for HCV replicat

295 We show that despite these variations, HMG-D and ZmHMGB1 exist in dynamic assemblies in which t

296 evalonate, implying a dependence on vascular HMG-CoA reductase inhibition.

297 of low-density lipoprotein cholesterol with HMG-CoA reductase inhibitors (statins).

298 In comparison with HMG-CoA (CoA) synthase, the homologous enzyme from prima

299 Overall survival was longer in patients with HMG-CoAR-positive tumors compared with their negative co

300 The yeast HMG-CoA reductase isozyme Hmg2, like its mammalian count