ライフサイエンスコーパス: von Hippel

1 von Hippel Lindau (Vhl) protein, encoded by a tumor supp

2 von Hippel-Lindau (VHL) disease is a dominantly inherite

3 von Hippel-Lindau (VHL) disease is a rare familial cance

4 von Hippel-Lindau (VHL) disease is caused by germ-line m

5 von Hippel-Lindau (VHL) disease is caused by germline mu

6 von Hippel-Lindau (VHL) disease results from germline an

7 von Hippel-Lindau (VHL) gene mutations are associated wi

8 von Hippel-Lindau (VHL) is a critical tumor suppressor i

9 von Hippel-Lindau (VHL) patients develop multiple centra

10 von Hippel-Lindau (VHL) protein is known to destabilize

11 von Hippel-Lindau (VHL) tumor suppressor loss is associa

12 von Hippel-Lindau disease (VHL) is an autosomal-dominant

13 von Hippel-Lindau disease (VHL) patients develop highly

14 von Hippel-Lindau disease is an inherited, multisystemic

15 correlated with the clinical findings in 16 von Hippel-Lindau disease patients with 22 CNS hemangiob

16 33 (USP33)/VDU1, originally identified as a von Hippel-Lindau tumor suppressor (VHL) protein-interac

17 nhances the ubiquitylation of HIF1alpha by a von Hippel-Lindau protein (pVHL)-dependent mechanism.

18 is differentially regulated by hypoxia in a von Hippel-Lindau (VHL)-dependent manner both in RCC cel

19 y, KLF2 promoted HIF-1alpha degradation in a von Hippel-Lindau protein-independent but proteasome-dep

20 ity without altering its protein levels in a von Hippel-Lindau-deficient cell line, indicating a disc

21 Carbonic anhydrase IX is a von Hippel-Lindau (VHL)-mediated enzyme expressed in the

22 Aberrant von Hippel Lindau (VHL) protein function is the underlyi

23 In additional, von Hippel-Lindau protein expression was significantly i

24 so preferentially interacted with PHD1-3 and von Hippel-Lindau protein (pVHL) during normoxia but not

25 uster and cystic kidney disease, miR-92a and von Hippel-Lindau syndrome, and alterations in LIN28-LET

26 minant polycystic kidney disease (ADPKD) and von Hippel-Lindau (VHL) disease lead to large kidney cys

27 respect to their effects on PHD2 binding and von Hippel Lindau interaction.

28 : IFN-gamma induces prolyl hydroxylation and von Hippel-Lindau (VHL)-mediated proteasomal degradation

29 t there was no change in HIF-1alpha mRNA and von Hippel Lindau E3 ubiquitin ligase (VHL) protein expr

30 TRC8/RNF139 and von Hippel-Lindau (VHL) both encode E3 ubiquitin (Ub) li

31 In the established Berg-von Hippel model for this search process, the TF alterna

32 ibe our extensive SAR studies exploring both von Hippel-Lindau (VHL) and cereblon (CRBN) E3 ligase li

33 tional activation was partially inhibited by von Hippel-Lindau protein.

34 concentration, which is largely regulated by von Hippel-Lindau (VHL; a protein component of a ubiquit

35 onectin and collagen network is regulated by von Hippel-Lindau protein (pVHL).

36 ligase component for HIF destruction called von Hippel-Lindau.

37 Previously, we reported a first-in-class von Hippel-Lindau (VHL)-recruiting mitogen-activated pro

38 omponent of the E3 ubiquitin ligase complex, von Hippel-Lindau (VHL) facilitates oxygen-dependent pol

39 onsible for the autosomal dominant condition von Hippel-Lindau (VHL) disease and is implicated in mos

40 h mutations in SDH complex subunits B and D, von Hippel-Lindau (VHL), RET, and neurofibromin 1 (NF1).

41 ents with clinically and genetically defined von Hippel-Lindau disease was systemically characterized

42 HD (n = 4) (SDH is succinate dehydrogenase); von Hippel-Lindau (VHL; n = 2); RET (n = 12); neurofibro

43 contrast, over-expression of Vhl (Drosophila von Hippel-Lindau) generated a range of phenotypes, incl

44 Mgr interacts with Drosophila von Hippel Lindau protein (Vhl).

45 The Caenorhabditis elegans von Hippel-Lindau tumor suppressor homolog VHL-1 is a cu

46 Mutations in VHL, which encodes von Hippel-Lindau tumor suppressor (VHL), are associated

47 lyl hydroxylases and subsequent evasion from von Hippel-Lindau-dependent degradation.

48 Mutations in the tumor-suppressor gene von Hippel-Lindau (VHL) are associated with a complex sp

49 ic inactivation of the tumor suppressor gene von Hippel-Lindau (VHL) are major causes of clear-cell r

50 Mutations of the tumor suppressor gene von Hippel-Lindau (VHL) can lead to benign and malignant

51 result of loss of the tumor suppressor gene von Hippel-Lindau (VHL) have yet to be fully elucidated.

52 th inactivation of the tumor suppressor gene von-Hippel Lindau (VHL), which activates the hypoxia-ind

53 Germline von Hippel-Lindau (VHL) gene mutations underlie dominant

54 onents of the hypoxia inducible factor (HIF)/von Hippel Lindau/hydroxylase pathway, including specifi

55 s the Prefoldin subunit counterpart of human von Hippel Lindau binding-protein 1.

56 Mutations in the human von Hippel-Lindau (VHL) gene are the cause of VHL diseas

57 actors promoted the degradation of the human von Hippel-Lindau (VHL) protein, which is an unfolded pr

58 a subunit is mediated by prolyl hydroxylase, von Hippel-Lindau protein (VHL)/Elongin-C E3 ubiquitin l

59 In von Hippel-Lindau (VHL)-null kidney cancer cell lines, w

60 ed, providing clues as to how disruptions in von Hippel-Lindau protein function may result in eye dis

61 of these mutants may rescue pVHL function in von Hippel-Lindau disease.

62 In order to examine the role of HIF in von Hippel-Lindau (VHL)-associated vascular tumorigenesi

63 to be pseudo-hypoxic drive, just as it is in von Hippel-Lindau syndrome.

64 Patients with a germline mutation in von Hippel-Lindau (VHL) develop renal cell cancers and h

65 ses are usually associated with mutations in von Hippel-Lindau (VHL) and subsequent normoxic stabiliz

66 Mutations in von Hippel-Lindau tumor suppressor gene (VHL) underlie t

67 netic resonance imaging (MRI) is obtained in von Hippel-Lindau disease patients, hemangioblastomas pr

68 ogenesis, which can occur sporadically or in von Hippel-Lindau disease.

69 We show in von Hippel-Lindau (VHL)-defective renal carcinoma cells

70 HIF-2alpha is stabilized in von Hippel-Lindau (VHL)-deficient renal cell carcinoma t

71 erization of renal cancer syndromes includes von Hippel-Lindau disease, Birt-Hogg-Dube syndrome, here

72 elements were in known ccRCC genes including von Hippel-Lindau tumor suppressor (VHL), polybromo 1 (P

73 A key regulator of HIF-1alpha is von Hippel-Lindau protein (pVHL), which mediates the oxy

74 The E3 ligase von Hippel-Lindau and autophagy receptor protein p62 are

75 ct the HIF-1alpha binding with its E3 ligase von Hippel-Lindau but enhanced the binding affinity betw

76 subsequent ubiquitination via the E3 ligase von Hippel-Lindau tumor suppressor, which targets Hypoxi

77 described the discovery of a novel E3 ligase von Hippel-Lindau-recruiting EGFR degrader, MS39 (compou

78 a peptide ligand for the E3 ubiquitin ligase von Hippel Lindau protein.

79 warhead (foretinib) and recruited E3 ligase (von Hippel-Lindau).

80 promotes its binding to a ubiquitin ligase, von Hippel-Lindau (VHL) protein, through a proline hydro

81 Binding is modeled using the McGhee-von Hippel formalism for the cooperative binding of liga

82 multiple endocrine neoplasia type 1 (MEN1), von Hippel Lindau (VHL) syndrome, neurofibromatosis (NF-

83 f eye disease may inform us as to how ocular von Hippel-Lindau disease arises, and help guide molecul

84 help guide molecular interventions in ocular von Hippel-Lindau disease.

85 uctural and functional progression of ocular von Hippel-Lindau (VHL) disease and analysis of patient

86 titative clinical characterization of ocular von Hippel-Lindau disease has been limited by small pati

87 cal characterization and treatment of ocular von Hippel-Lindau disease.

88 The ability of von Hippel-Lindau tumor suppressor protein to form the E

89 ed between HIF1 and mTORC1 in the absence of von Hippel-Lindau (VHL) tumor suppressor expression.

90 ific proline residues followed by binding of von Hippel-Lindau (VHL) protein.

91 therapies targeting the molecular biology of von Hippel-Lindau disease, some of which are presently b

92 the effect of astrocyte-targeted deletion of von Hippel-Lindau tumor suppressor (Vhl), hypoxia-induci

93 f the HIF-1alpha pathway through deletion of von Hippel-Lindau tumor-suppressor protein or pharmacolo

94 enal cell carcinoma include the discovery of von Hippel-Lindau associated mechanisms involved in rena

95 echnology, intestinal-specific disruption of von Hippel-Lindau tumor suppressor protein (Vhl), hypoxi

96 ) and significant reduction in expression of von Hippel-Lindau tumor suppressor (100 vs 40; P < .001)

97 astomas of the CNS are a cardinal feature of von Hippel-Lindau (VHL) disease, a dominantly inherited

98 As a result, LMP1 prevents formation of von Hippel-Lindau/HIF1alpha complex, as shown by coimmun

99 ble a full characterization of the impact of von Hippel-Lindau disease on eye health and visual funct

100 mas (RCC) frequently display inactivation of von Hippel-Lindau (VHL) gene leading to increased level

101 Inactivation of von Hippel-Lindau tumor-suppressor protein (pVHL) is ass

102 n HIF-1 reporter activity are independent of von Hippel-Lindau tumor suppressor (VHL)-1, whereas VHL-

103 a transactivation potential independently of von Hippel-Lindau tumor suppressor and p53 function indi

104 hrough Pax8-rtTA-based inducible knockout of von Hippel-Lindau protein (VHL-KO), protects from rhabdo

105 1/2alpha mRNA levels and increased levels of von Hippel-Lindau E3 ligase in TRPM2-S-expressing cells.

106 Loss of von Hippel Lindau (VHL) protein function is a key driver

107 carcinoma (RCC) is characterized by loss of von Hippel Lindau tumor suppressor gene activity, result

108 HIF-1alpha and/or HIF-2alpha due to loss of von Hippel-Lindau (VHL) function.

109 Loss of von Hippel-Lindau (VHL) tumor suppressor gene function o

110 Loss of von Hippel-Lindau is not sufficient for neoplastic trans

111 of ccRCC metabolism correlated with loss of von Hippel-Lindau tumor suppressor (VHL) and a potential

112 he generation of a transgenic mouse model of von Hippel-Lindau (VHL) renal cancer termed the TRACK mo

113 Correlations between the nature of von Hippel-Lindau gene mutations and the ocular phenotyp

114 t effects on tumor cells occur regardless of von Hippel-Lindau tumor suppressor gene status and hypox

115 gene transcription and a down-regulation of von Hippel-Lindau (VHL), the E3 ubiquitin ligase that me

116 g to the release of molecular constraints on von Hippel-Lindau (VHL) ubiquitin ligase tumor suppresso

117 degradation by the prolyl hydroxylase (PHD)/von Hippel-Lindau (VHL) system.

118 inactivation of the tumor suppressor protein von Hippel Lindau (VHL) leads to an increase in VPF/VEGF

119 if regulation by oxygen requires the protein von Hippel-Lindau (pVhl) and pVhl disruption results in

120 Because pVHL (von Hippel-Lindau protein) directs the proteolysis of Hi

121 pha is constitutively ubiquitinated by pVHL (von Hippel-Lindau protein) followed by proteasomal degra

122 and HIF-2alpha and their negative regulator von Hippel-Lindau (VHL) as well as astrocyte-specific de

123 e 3p deletions that harbor the ccRCC-related von Hippel-Lindau, PBRM1, BAP1, and SETD2 tumor suppress

124 ole-genome sequencing on 40 tumours from six von Hippel-Lindau patients.

125 e pathway controlled by the tumor suppressor von Hippel Lindau (VHL).

126 de a functional loss of the tumor suppressor von Hippel Lindau (VHL).

127 ccRCC), inactivation of the tumor suppressor von Hippel-Lindau (VHL) occurs in the majority of the tu

128 s tightly controlled by the tumor suppressor von Hippel-Lindau (VHL), deletion of VHL results in cons

129 way of RCC, the loss of the tumor suppressor von Hippel-Lindau (VHL), which causes hypoxia-inducible

130 Deficiency of the tumor suppressor von Hippel-Lindau leads to constitutively active hypoxia

131 The tumor suppressor von Hippel-Lindau protein (pVHL) is critical for cellula

132 The hypoxia-regulated tumor-suppressor von Hippel-Lindau (VHL) is an E3 ligase that recognizes

133 us (KSHV) targets the HIF-1alpha suppressors von Hippel-Lindau protein and p53 for degradation via it

134 pendent of the function of tumor suppressors von Hippel-Lindau or p53 or the degradation of HIF-alpha

135 of miR-155 in angiogenesis through targeting von Hippel-Lindau (VHL) tumour suppressor in breast canc

136 We show that von Hippel-Lindau-dependent down-regulation of Dicer is

137 The von Hippel Lindau tumor suppressor protein (pVHL) is a c

138 The von Hippel-Lindau (VHL) disease is caused by VHL germ li

139 The von Hippel-Lindau (VHL) gene is lost in approximately 70

140 The von Hippel-Lindau (VHL) protein controls the degradation

141 The von Hippel-Lindau (VHL) syndrome is a rare inherited can

142 The von Hippel-Lindau (VHL) tumor suppressor gene is inactiv

143 The von Hippel-Lindau (VHL) tumor suppressor gene is mutated

144 The von Hippel-Lindau (VHL) tumor suppressor protein pVHL is

145 The von Hippel-Lindau (VHL) tumor suppressor pVHL is lost in

146 The von Hippel-Lindau protein (pVHL) bound directly to hydro

147 The von Hippel-Lindau protein (pVHL) is the substrate recogn

148 The von Hippel-Lindau tumor suppressor (VHL) represses TRPM3

149 The von Hippel-Lindau tumor suppressor gene (VHL) has attrac

150 The von Hippel-Lindau tumor suppressor protein (pVHL) is fre

151 The von Hippel-Lindau tumor suppressor protein (pVHL) is one

152 The von Hippel-Lindau tumor suppressor protein is the substr

153 The von Hippel-Lindau tumor suppressor pVHL is an E3 ligase

154 The von Hippel-Lindau tumor suppressor pVHL regulates the st

155 The von Hippel-Lindau tumor-suppressor gene (VHL) is lost in

156 -terminal hydrolase-L1 (UCHL1) abrogates the von Hippel-Lindau-mediated ubiquitination of HIF-1alpha,

157 ated in the presence of oxygen, allowing the von Hippel-Lindau (VHL) E3 ubiquitin ligase to interact

158 xygen tension, which rises at birth, and the von Hippel-Lindau (VHL)-hypoxia-inducible factor 1alpha

159 entas did not differ, but HIF-1alpha and the von Hippel-Lindau tumor suppressor protein were overexpr

160 by hypoxia-inducible factors (HIFs) and the von Hippel-Lindau tumor suppressor VHL.

161 HIF-2alpha to destabilize HIF by binding the von Hippel-Landau tumour suppressor protein (pVHL).

162 F-1alpha protein levels are regulated by the von Hippel Lindau tumor suppressor gene, VHL, which targ

163 ygen-sensitive regulation of HIFalpha by the von Hippel-Lindau (VHL) protein, the mechanisms underlyi

164 hermore, NICI expression is regulated by the von Hippel-Lindau (VHL) tumor suppressor and is highly e

165 droxylation leading to ubiquitination by the von Hippel-Lindau protein (VHL)-Elongin C ubiquitin-liga

166 1alpha and targets it for recognition by the von Hippel-Lindau tumor suppressor and consequent degrad

167 lated and is targeted for degradation by the von Hippel-Lindau tumor suppressor protein (VHL).

168 targeting the latter for degradation by the von Hippel-Lindau tumor-suppressor protein (VHL).

169 or a ubiquitin ligase complex containing the von Hippel-Lindau (VHL) tumor suppressor protein, which

170 by a ubiquitin ligase complex containing the von Hippel-Lindau (VHL) tumor suppressor.

171 lyubiquitination by a complex containing the von Hippel-Lindau protein (pVHL).

172 the ubiquitin ligase complex containing the von Hippel-Lindau tumor suppressor.

173 ne-specific disruption of genes encoding the von Hippel-Lindau tumor suppressor protein (Vhl), hypoxi

174 ed conditional gene targeting to examine the von Hippel-Lindau/prolyl-4-hydroxylase domain (PHD)/HIF

175 of HIF-alpha increases its affinity for the von Hippel Lindau protein elongin B/C (VCB) ubiquitin li

176 This provides a recognition motif for the von Hippel Lindau protein, a component of an E3 ubiquiti

177 omposed of two instances of a ligand for the von Hippel-Lindau (VHL) E3 ligase.

178 The Vhlh gene codes for the von Hippel-Lindau protein (VHL), a tumor suppressor that

179 pha, and reducing HIF2alpha affinity for the von Hippel-Lindau protein and its degradation.

180 g an additional TRiC-binding domain from the von Hippel-Lindau protein (vTBD), at the N-terminus of S

181 is overexpressed because of mutations in the von Hippel Lindau (VHL) tumor suppressor protein.

182 e, begins with an intragenic mutation in the von Hippel-Lindau (VHL) gene and loss of 3p (where VHL i

183 Mutations in the von Hippel-Lindau (VHL) gene are pathogenic in VHL disea

184 Mutations in the von Hippel-Lindau (VHL) gene give rise to renal cell car

185 Genetic and epigenetic changes in the von Hippel-Lindau (VHL) tumor suppressor gene are common

186 Germline mutations in the von Hippel-Lindau (VHL) tumor suppressor gene predispose

187 cell carcinoma (RCC), cells deficient in the von Hippel-Lindau (VHL) tumor suppressor gene use glutam

188 The R200W mutation in the von Hippel-Lindau (VHL) tumor suppressor protein (pVHL)

189 Mutations in the von Hippel-Lindau gene upregulate expression of the cent

190 scribed in association with mutations in the von Hippel-Lindau gene.

191 Most renal cancers have defects in the von Hippel-Lindau tumor suppressor pVHL.

192 rthermore, renal cell lines deficient in the von Hippel-Lindau tumour suppressor protein preferential

193 e Elongin BC-box protein family includes the von Hippel-Lindau tumor suppressor and suppressor of cyt

194 bers of oxygen-sensing pathway including the von Hippel-Lindau tumor suppressor protein (pVHL) and th

195 e elongin C-containing ubiquitin ligase, the von Hippel-Lindau tumor suppressor complex, promotes Pol

196 rcinomas (ccRCC) exhibit inactivation of the von Hippel-Lindau (pVHL) tumor suppressor, establishing

197 sely, mice with an epidermal deletion of the von Hippel-Lindau (VHL) factor, a negative regulator of

198 udies have identified functional loss of the von Hippel-Lindau (VHL) gene as a frequent and crucial e

199 The functional loss of the von Hippel-Lindau (VHL) gene occurs in 90% of CC-RCC, dr

200 l cell carcinoma (CC-RCC) is the loss of the von Hippel-Lindau (VHL) gene, which results in stabiliza

201 haracterized by frequent inactivation of the von Hippel-Lindau (VHL) gene.

202 ely regulated by O2-dependent binding of the von Hippel-Lindau (VHL) protein.

203 C) is frequently associated with loss of the von Hippel-Lindau (VHL) tumor suppressor (pVHL), which i

204 Inactivating mutations of the von Hippel-Lindau (VHL) tumor suppressor gene are associ

205 Loss of the von Hippel-Lindau (VHL) tumor suppressor gene contribute

206 C) resulting from the hereditary loss of the von Hippel-Lindau (VHL) tumor suppressor gene is the lea

207 re typified by biallelic inactivation of the von Hippel-Lindau (VHL) tumor suppressor gene.

208 are linked to biallelic inactivation of the von Hippel-Lindau (VHL) tumor suppressor gene.

209 EGF) due to the mutation/inactivation of the von Hippel-Lindau (VHL) tumor suppressor gene.

210 Loss of the von Hippel-Lindau (VHL) tumor suppressor is a hallmark f

211 Mutation of the von Hippel-Lindau (VHL) tumor suppressor protein at codo

212 cinomas (CC-RCCs) is loss-of-function of the von Hippel-Lindau (VHL) tumor suppressor protein.

213 classical mutation, loss of function of the von Hippel-Lindau (VHL) tumor suppressor, provides a hum

214 RCC) characterized by an inactivation of the von Hippel-Lindau (VHL) tumor-suppressor gene with subse

215 nisms, in particular the inactivation of the von Hippel-Lindau (VHL) tumour suppressor gene (TSG).

216 models, we demonstrate that deletion of the von Hippel-Lindau (Vhlh) gene (encoding an E3 ubiquitin

217 steoblasts through selective deletion of the von Hippel-Lindau gene (Vhl) expressed high levels of Ve

218 of the eight SCAs contained mutations of the von Hippel-Lindau gene (VHL), a key component of the VHL

219 Inactivation of the von Hippel-Lindau gene in clear-cell renal cell carcinom

220 We have examined the status of the von Hippel-Lindau gene product (pVHL) that is responsibl

221 ing correlations between the genotype of the von Hippel-Lindau mutation and the phenotype of eye dise

222 and protein accumulation independent of the von Hippel-Lindau pathway.

223 f previous observations that deletion of the von Hippel-Lindau protein (pVHL) in juxtaglomerular (JG)

224 ith cardiac myocyte-specific deletion of the von Hippel-Lindau protein (VHL), an essential component

225 roxylase PHD2 is required for binding of the von Hippel-Lindau protein (VHL), leading to ubiquitinati

226 lation, which is required for binding of the von Hippel-Lindau protein (VHL), the recognition compone

227 he identification of loss of function of the von Hippel-Lindau protein as the basis for clear cell RC

228 cancers characterized by inactivation of the von Hippel-Lindau tumor suppressor (pVHL).

229 Inactivation of the von Hippel-Lindau tumor suppressor (VHL) is an early eve

230 was achieved by conditional deletion of the von Hippel-Lindau tumor suppressor (VHL) protein in the

231 is characterized by loss of function of the von Hippel-Lindau tumor suppressor (VHL), which negative

232 ) are characterized by biallelic loss of the von Hippel-Lindau tumor suppressor and subsequent consti

233 Biallelic inactivating mutations of the von Hippel-Lindau tumor suppressor gene (VHL) are a hall

234 Biallelic inactivation of the von Hippel-Lindau tumor suppressor gene (VHL) is linked

235 Loss of function of the von Hippel-Lindau tumor suppressor gene (VHL) predispose

236 Inactivation of the von Hippel-Lindau tumor suppressor gene, VHL, is an arch

237 Biallelic inactivation of the von Hippel-Lindau tumor suppressor gene, VHL, occurs in

238 ion through tubule-specific knockdown of the von Hippel-Lindau tumor suppressor increased cyst size i

239 cell carcinoma (ccRCC), inactivation of the von Hippel-Lindau tumor suppressor is nearly universal;

240 carcinomas (ccRCCs) have inactivation of the von Hippel-Lindau tumor suppressor protein (pVHL), resul

241 stinal epithelium-specific disruption of the von Hippel-Lindau tumor suppressor protein (VHL) resulte

242 Furthermore, the down-regulation of the von Hippel-Lindau tumor suppressor protein by RNA interf

243 ause of the frequent loss of function of the von Hippel-Lindau tumor suppressor protein.

244 ve previously shown that inactivation of the von Hippel-Lindau tumor suppressor pVHL, which targets b

245 Inactivation of the von Hippel-Lindau tumor suppressor, pVHL, is associated

246 imal nephron via induced inactivation of the von Hippel-Lindau tumor suppressor, which targets the HI

247 is characterized by loss of function of the von Hippel-Lindau tumour suppressor (VHL) and unrestrain

248 RCC) is characterized by inactivation of the von Hippel-Lindau tumour suppressor gene (VHL).

249 physiologically activated by mutation of the von Hippel-Lindau tumour suppressor, we observed marked

250 the work done during the elucidation of the von Hippel-Lindau/clear cell RCC pathway.

251 Dysregulation of the von Hippel-Lindau/hypoxia-inducible transcription factor

252 ted genes for HIF-1alpha, HIF-2alpha, or the von Hippel-Lindau protein.

253 In particular, the von Hippel-Lindau tumour suppressor protein (pVhl) contr

254 is mediated by prolyl hydroxylase (PHD), the von Hippel-Lindau (VHL)/Elongin-C/Elongin-B E3 ubiquitin

255 Purpose The von Hippel-Lindau tumor suppressor is inactivated in the

256 rated the first small molecule targeting the von Hippel-Lindau protein (VHL), the substrate recogniti

257 f Molecular Cell, Roe et al. report that the von Hippel-Lindau (VHL) protein is a positive regulator

258 We found that the von Hippel-Lindau (VHL) protein, an E3 ubiquitin ligase

259 Here we establish that the von Hippel-Lindau/hypoxia-inducible transcription factor

260 rmline mutation in the VHL gene leads to the von Hippel-Lindau disease, a familial syndrome character

261 nd 21 (MS4369), with impaired binding to the von Hippel-Lindau E3 ligase and PRMT5, respectively.

262 xylation promotes binding of HIFalpha to the von Hippel-Lindau protein (VHL)-elongin B/C complex, thu

263 Many functions have been assigned to the von Hippel-Lindau tumor suppressor gene product (pVHL),

264 a ligase-target pair deemed unsuitable: the von Hippel-Lindau (VHL) and BRD9, a bromodomain-containi

265 Here, we use the von Hippel-Lindau tumor suppressor protein VHL as a mode

266 d subsequent proteasomal degradation via the von Hippel-Lindau ubiquitin ligase.

267 hypoxia inducible factor (HIF), whereas the von Hippel-Lindau (VHL) ubiquitin ligase as well as the

268 ously observed that hMSH4 interacts with the von Hippel-Lindau binding protein 1 (VBP1), a partner of

269 f HIF-1 is required for its binding with the von Hippel-Lindau tumor suppressor protein and the subse

270 of hypoxia-inducible factor-1alpha with the von Hippel-Lindau tumor suppressor, and in an estrogen r

271 Inactivating mutations within the von Hippel-Lindau (VHL) tumor suppressor gene predispose

272 Recent insights into the role of the von-Hippel Lindau (VHL) tumor suppressor gene in heredit

273 ion of hypoxia signaling by knockdown of the von-Hippel-Lindau (VHL) protein led to reversal of the e

274 rognosis of the disease independent of their von Hippel-Lindau (VHL) status.

275 s performed on postmortem tissues from three von Hippel-Lindau disease patients (not in the clinical

276 Once hydroxylated, HIFalpha subunits bind to von Hippel-Lindau (VHL) E3 ligases and are degraded.

277 D184161 also increased HIF-1alpha binding to von Hippel-Lindau tumor suppressor protein, an E3 ligase

278 ypoxia-inducible factors (HIFs) secondary to von Hippel-Lindau (VHL) mutations that occur in over 90%

279 pRCC, a tumor type associated with wild-type von Hippel Lindau gene.

280 TK2 proteolysis-targeting chimeras utilizing von Hippel-Lindau and cereblon ligands to hijack E3 liga

281 f SCF (Skp1, Cullin, F-box protein) and VCB (von Hippel-Lindau (VHL), Cullin and Elongin B/C) E3 ubiq

282 of ccRCC is genetic loss-of-function of VHL (von Hippel-Lindau) that leads to a highly vascularized t

283 The tumor suppressor VHL (von Hippel-Lindau protein) serves as a negative regulato

284 The tumor suppressor VHL (von Hippel-Lindau) protein is a substrate receptor for U

285 sion by enhancing its interactions with VHL (von Hippel Lindau), thus promoting its ubiquitination an

286 Patients affected with von Hippel-Lindau disease are at risk of developing mult

287 lary hemangioblastomas (RCH) associated with von Hippel-Lindau (VHL) disease treated with systemic su

288 euroendocrine tumors (PNETs) associated with von Hippel-Lindau disease (VHL) is challenging because o

289 hatic sac tumors (ELSTs) are associated with von Hippel-Lindau disease and cause irreversible sensori

290 suppressor protein (pVHL) is associated with von Hippel-Lindau disease, an inherited cancer syndrome,

291 hemangioma with or without association with von Hippel-Lindau disease.

292 e, HIF-1 hydroxylation, and interaction with von Hippel-Lindau protein (pVHL), resulting in HIF-1alph

293 than the nucleus, where it co-localized with von Hippel-Lindau tumor suppressor protein and the HIF h

294 ant difference in uptake among patients with von Hippel Lindau syndrome (VHL; n = 19), succinate dehy

295 a major cause of mortality in patients with von Hippel-Lindau (VHL) disease, which is caused by germ

296 screening and surveillance of patients with von Hippel-Lindau (VHL) syndrome.

297 Patients with von Hippel-Lindau disease (VHL) are at risk to develop m

298 ctive and serial evaluation of patients with von Hippel-Lindau disease and ELSTs at the National Inst

299 Thirty-five patients with von Hippel-Lindau disease and ELSTs in 38 ears (3 bilate

300 Conclusion CT screening of patients with von Hippel-Lindau syndrome can lead to substantial radia