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 inactivation occurs in von

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

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 (Pro-402/564) of HIFalpha was abolished in a von Hippel-Lindau-dependent manner in cells exposed to n

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

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

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

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

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

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

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

29 role in the pathogenesis of renal cancer and von Hippel-Lindau disease.

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

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

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

33 litated diffusion' model of Berg, Winter and von Hippel, showing how non-specific DNA-protein interac

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

50 Generally, von Hippel-Lindau (VHL) disease is caused by a germline

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

66 pel-Lindau (VHL) gene inactivation occurs in von Hippel-Lindau (VHL) disease.

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

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

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

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

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

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

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

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

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

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

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

78 of quadruplexes and according to the McGhee-von Hippel model is 1.3 x 10(6) M(-)(1) in terms of pote

79 s of quadruplexes and in terms of the McGhee-von Hippel model is 2.4 x 10(6) M(-)(1) in terms of pote

80 CuTMpyP4 and (1)(4) is four using the McGhee-von Hippel model.

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

82 The multiprotein von Hippel-Lindau (VHL) tumor suppressor and Skp1-Cul1-F

83 nt Hif1a (inability to form HIF-1) or mutant von Hippel-Lindau gene (Vhlh; constitutively active HIF-

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

106 1/2alpha mRNA levels and increased levels of von Hippel-Lindau E3 ligase in TRPM2-S-expressing cells.

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

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

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

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

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

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

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

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

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

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

117 acterized by homozygous mutation (598C>T) of von Hippel-Lindau gene (VHL), a negative regulator of hy

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

136 m of autoimmune polyendocrinopathy syndrome, von Hippel-Lindau syndrome, and congenital polycythemia.

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

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

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

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

141 The von Hippel-Lindau (VHL) E3 ubiquitin ligase binds HIF-1a

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

143 The von Hippel-Lindau (VHL) gene is the major renal cancer g

144 The von Hippel-Lindau (VHL) gene product, pVHL, targets the

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

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

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

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

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

150 The von Hippel-Lindau gene product (pVHL) targets the alpha

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

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

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

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

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

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

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

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

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

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

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

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

163 T heterodimer), proline hydroxylase, and the von Hippel-Lindau protein.

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

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

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

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

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

169 1alpha and targets it for recognition by the von Hippel-Lindau tumor suppressor and consequent degrad

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

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

172 indau (VHL) tumor suppressor gene causes the von Hippel-Lindau hereditary cancer syndrome, and somati

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

189 homozygous for an Arg200Trp mutation in the von Hippel-Lindau (VHL) gene.

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

191 Mutations in the von Hippel-Lindau (VHL) tumor suppressor gene cause tiss

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

193 ervous system (CNS) hemangioblastomas in the von Hippel-Lindau (VHL) tumor suppressor gene syndrome,

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

212 Germline inactivation of the von Hippel-Lindau (VHL) tumor suppressor gene causes the

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

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

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

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

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

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

219 mib-induced apoptosis, and expression of the von Hippel-Lindau (VHL) tumor suppressor protein downreg

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

251 1 was identified as a protein partner of the von Hippel-Lindau tumor suppressor pVHL.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

284 elevant published literature regarding VEGF, von Hippel-Lindau (VHL) gene inactivation and VEGF overe

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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