ライフサイエンスコーパス: Hippel

1 Binding is modeled using the McGhee-von Hippel formalism for the cooperative binding of ligands

2 Von Hippel-Landau (VHL) protein is a potent tumor suppressor

3 2alpha to destabilize HIF by binding the von Hippel-Landau tumour suppressor protein (pVHL).

4 Von Hippel Lindau (VHL) is a tumour suppressor that is lost

5 tivation of the tumor suppressor protein von Hippel Lindau (VHL) leads to an increase in VPF/VEGF exp

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

7 Aberrant von Hippel Lindau (VHL) protein function is the underlying d

8 von Hippel Lindau (Vhl) protein, encoded by a tumor suppress

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

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

11 verexpressed because of mutations in the von Hippel Lindau (VHL) tumor suppressor protein.

12 nactivation of the tumor suppressor gene von-Hippel Lindau (VHL), which activates the hypoxia-inducib

13 thway controlled by the tumor suppressor von Hippel Lindau (VHL).

14 functional loss of the tumor suppressor von Hippel Lindau (VHL).

15 e Prefoldin subunit counterpart of human von Hippel Lindau binding-protein 1.

16 BCR-ABL by recruiting either Cereblon or Von Hippel Lindau E3 ligases is reported.

17 ere was no change in HIF-1alpha mRNA and von Hippel Lindau E3 ubiquitin ligase (VHL) protein expressi

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

19 ect to their effects on PHD2 binding and von Hippel Lindau interaction.

20 Von Hippel Lindau protein (pVHL) and hypoxia inducible facto

21 We find that GCs limit the expression of Von Hippel Lindau protein (pVHL), a negative regulator of HI

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

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

24 his provides a recognition motif for the von Hippel Lindau protein, a component of an E3 ubiquitin li

25 ptide ligand for the E3 ubiquitin ligase von Hippel Lindau protein.

26 difference in uptake among patients with von Hippel Lindau syndrome (VHL; n = 19), succinate dehydrog

27 cinoma (RCC) is characterized by loss of von Hippel Lindau tumor suppressor gene activity, resulting

28 lpha protein levels are regulated by the von Hippel Lindau tumor suppressor gene, VHL, which targets

29 Inactivation of the VHL (Von Hippel Lindau) tumour suppressor has long been recognise

30 by enhancing its interactions with VHL (von Hippel Lindau), thus promoting its ubiquitination and de

31 ts of the hypoxia inducible factor (HIF)/von Hippel Lindau/hydroxylase pathway, including specific ro

32 egulation by oxygen requires the protein von Hippel-Lindau (pVhl) and pVhl disruption results in cons

33 omas (ccRCC) exhibit inactivation of the von Hippel-Lindau (pVHL) tumor suppressor, establishing it a

34 are usually associated with mutations in von Hippel-Lindau (VHL) and subsequent normoxic stabilizatio

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

36 nactivation of the tumor suppressor gene von Hippel-Lindau (VHL) are major causes of clear-cell renal

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

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

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

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

41 ral and functional progression of ocular von Hippel-Lindau (VHL) disease and analysis of patient fact

42 ble for the autosomal dominant condition von Hippel-Lindau (VHL) disease and is implicated in most sp

43 von Hippel-Lindau (VHL) disease is a dominantly inherited fa

44 von Hippel-Lindau (VHL) disease is a rare familial cancer pr

45 von Hippel-Lindau (VHL) disease is caused by germ-line mutat

46 Von Hippel-Lindau (VHL) disease is caused by germline mutati

47 von Hippel-Lindau (VHL) disease is caused by germline mutati

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

49 nt polycystic kidney disease (ADPKD) and von Hippel-Lindau (VHL) disease lead to large kidney cysts t

50 von Hippel-Lindau (VHL) disease results from germline and so

51 hemangioblastomas (RCH) associated with von Hippel-Lindau (VHL) disease treated with systemic suniti

52 mas of the CNS are a cardinal feature of von Hippel-Lindau (VHL) disease, a dominantly inherited mult

53 ajor cause of mortality in patients with von Hippel-Lindau (VHL) disease, which is caused by germ lin

54 is model, overexpression was achieved by Von Hippel-Lindau (Vhl) disruption in a liver-specific tempo

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

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

57 ucible factor-1alpha, which binds to the Von-Hippel-Lindau (VHL) E3 ubiquitin ligase complex, linked

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

59 nent of the E3 ubiquitin ligase complex, von Hippel-Lindau (VHL) facilitates oxygen-dependent polyubi

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

61 -1alpha and/or HIF-2alpha due to loss of von Hippel-Lindau (VHL) function.

62 egins with an intragenic mutation in the von Hippel-Lindau (VHL) gene and loss of 3p (where VHL is lo

63 Mutations in the von Hippel-Lindau (VHL) gene are pathogenic in VHL disease,

64 Mutations in the human von Hippel-Lindau (VHL) gene are the cause of VHL disease th

65 s have identified functional loss of the von Hippel-Lindau (VHL) gene as a frequent and crucial event

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

67 The von Hippel-Lindau (VHL) gene is lost in approximately 70% of

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

69 Von Hippel-Lindau (VHL) gene loss is an important factor in

70 von Hippel-Lindau (VHL) gene mutations are associated with c

71 Germline von Hippel-Lindau (VHL) gene mutations underlie dominantly i

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

73 ll carcinoma (CC-RCC) is the loss of the von Hippel-Lindau (VHL) gene, which results in stabilization

74 cterized by frequent inactivation of the von Hippel-Lindau (VHL) gene.

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

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

77 ia-inducible factors (HIFs) secondary to von Hippel-Lindau (VHL) mutations that occur in over 90% of

78 C), inactivation of the tumor suppressor von Hippel-Lindau (VHL) occurs in the majority of the tumors

79 von Hippel-Lindau (VHL) patients develop multiple central ne

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

81 lecular Cell, Roe et al. report that the von Hippel-Lindau (VHL) protein is a positive regulator of p

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

83 of hypoxia signaling by knockdown of the von-Hippel-Lindau (VHL) protein led to reversal of the effec

84 motes its binding to a ubiquitin ligase, von Hippel-Lindau (VHL) protein, through a proline hydroxyla

85 rs promoted the degradation of the human von Hippel-Lindau (VHL) protein, which is an unfolded protei

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

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

88 se binders targeting cereblon (CRBN) and Von Hippel-Lindau (VHL) proteins.

89 eneration of a transgenic mouse model of von Hippel-Lindau (VHL) renal cancer termed the TRACK model

90 osis of the disease independent of their von Hippel-Lindau (VHL) status.

91 radation by the prolyl hydroxylase (PHD)/von Hippel-Lindau (VHL) system.

92 s frequently associated with loss of the von Hippel-Lindau (VHL) tumor suppressor (pVHL), which inhib

93 a component of the ElonginB/C-CUL2-RBX-1-Von Hippel-Lindau (VHL) tumor suppressor complex that ubiqui

94 etween HIF1 and mTORC1 in the absence of von Hippel-Lindau (VHL) tumor suppressor expression.

95 Inactivating mutations of the von Hippel-Lindau (VHL) tumor suppressor gene are associated

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

97 duals bearing germ line mutations in the Von Hippel-Lindau (VHL) tumor suppressor gene are predispose

98 Loss of the von Hippel-Lindau (VHL) tumor suppressor gene contributes to

99 Loss of von Hippel-Lindau (VHL) tumor suppressor gene function occur

100 The von Hippel-Lindau (VHL) tumor suppressor gene is inactivated

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

102 esulting from the hereditary loss of the von Hippel-Lindau (VHL) tumor suppressor gene is the leading

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

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

105 carcinoma (RCC), cells deficient in the von Hippel-Lindau (VHL) tumor suppressor gene use glutamine

106 (CCRCC) evolves due to mutations in the Von Hippel-Lindau (VHL) tumor suppressor gene.

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

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

109 ypified by biallelic inactivation of the von Hippel-Lindau (VHL) tumor suppressor gene.

110 von Hippel-Lindau (VHL) tumor suppressor loss is associated

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

112 Mutation of the von Hippel-Lindau (VHL) tumor suppressor protein at codon 20

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

114 The Von Hippel-Lindau (VHL) tumor suppressor protein regulates V

115 ubiquitin ligase complex containing the von Hippel-Lindau (VHL) tumor suppressor protein, which resu

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

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

118 ubiquitin ligase complex containing the von Hippel-Lindau (VHL) tumor suppressor.

119 characterized by an inactivation of the von Hippel-Lindau (VHL) tumor-suppressor gene with subsequen

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

121 iR-155 in angiogenesis through targeting von Hippel-Lindau (VHL) tumour suppressor in breast cancer.

122 oxia inducible factor (HIF), whereas the von Hippel-Lindau (VHL) ubiquitin ligase as well as the oxyg

123 F (Skp1, Cullin, F-box protein) and VCB (von Hippel-Lindau (VHL), Cullin and Elongin B/C) E3 ubiquiti

124 ghtly controlled by the tumor suppressor von Hippel-Lindau (VHL), deletion of VHL results in constitu

125 e transcription and a down-regulation of von Hippel-Lindau (VHL), the E3 ubiquitin ligase that mediat

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

127 Von Hippel-Lindau (VHL)-associated hemangioblastomas (VHL-HB

128 In order to examine the role of HIF in von Hippel-Lindau (VHL)-associated vascular tumorigenesis, w

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

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

131 differentially regulated by hypoxia in a von Hippel-Lindau (VHL)-dependent manner both in RCC cell cu

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

133 N-gamma induces prolyl hydroxylation and von Hippel-Lindau (VHL)-mediated proteasomal degradation, wh

134 Von Hippel-Lindau (VHL)-null 786-O, RCC4 and A498 Renal Cell

135 In von Hippel-Lindau (VHL)-null kidney cancer cell lines, we re

136 ediated by prolyl hydroxylase (PHD), the von Hippel-Lindau (VHL)/Elongin-C/Elongin-B E3 ubiquitin lig

137 n = 4) (SDH is succinate dehydrogenase); von Hippel-Lindau (VHL; n = 2); RET (n = 12); neurofibromin

138 els, we demonstrate that deletion of the von Hippel-Lindau (Vhlh) gene (encoding an E3 ubiquitin liga

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

140 cell carcinoma include the discovery of von Hippel-Lindau associated mechanisms involved in renal cy

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

142 he HIF-1alpha binding with its E3 ligase von Hippel-Lindau but enhanced the binding affinity between

143 Patients with von Hippel-Lindau disease (VHL) are at risk to develop multi

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

145 endocrine tumors (PNETs) associated with von Hippel-Lindau disease (VHL) is challenging because of th

146 Von Hippel-Lindau disease (VHL) is one of the most common in

147 von Hippel-Lindau disease (VHL) patients develop highly vasc

148 c sac tumors (ELSTs) are associated with von Hippel-Lindau disease and cause irreversible sensorineur

149 e and serial evaluation of patients with von Hippel-Lindau disease and ELSTs at the National Institut

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

151 Patients affected with von Hippel-Lindau disease are at risk of developing multiple

152 e disease may inform us as to how ocular von Hippel-Lindau disease arises, and help guide molecular i

153 tive clinical characterization of ocular von Hippel-Lindau disease has been limited by small patient

154 von Hippel-Lindau disease is an inherited, multisystemic can

155 a full characterization of the impact of von Hippel-Lindau disease on eye health and visual function.

156 rformed on postmortem tissues from three von Hippel-Lindau disease patients (not in the clinical seri

157 related with the clinical findings in 16 von Hippel-Lindau disease patients with 22 CNS hemangioblast

158 c resonance imaging (MRI) is obtained in von Hippel-Lindau disease patients, hemangioblastomas provid

159 with clinically and genetically defined von Hippel-Lindau disease was systemically characterized in

160 ne mutation in the VHL gene leads to the von Hippel-Lindau disease, a familial syndrome characterized

161 ressor protein (pVHL) is associated with von Hippel-Lindau disease, an inherited cancer syndrome, as

162 ation of renal cancer syndromes includes von Hippel-Lindau disease, Birt-Hogg-Dube syndrome, heredita

163 apies targeting the molecular biology of von Hippel-Lindau disease, some of which are presently being

164 guide molecular interventions in ocular von Hippel-Lindau disease.

165 hese mutants may rescue pVHL function in von Hippel-Lindau disease.

166 characterization and treatment of ocular von Hippel-Lindau disease.

167 esis, which can occur sporadically or in von Hippel-Lindau disease.

168 angioma with or without association with von Hippel-Lindau disease.

169 lpha mRNA levels and increased levels of von Hippel-Lindau E3 ligase in TRPM2-S-expressing cells.

170 blasts through selective deletion of the von Hippel-Lindau gene (Vhl) expressed high levels of Vegf a

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

172 oxic conditions, through the loss of the Von Hippel-Lindau gene (VHL).

173 Inactivation of the von Hippel-Lindau gene in clear-cell renal cell carcinomas (

174 Von Hippel-Lindau gene inactivation is observed in most clea

175 Correlations between the nature of von Hippel-Lindau gene mutations and the ocular phenotype we

176 Von Hippel-Lindau gene mutations were detected in four (22%)

177 We have examined the status of the von Hippel-Lindau gene product (pVHL) that is responsible fo

178 Here, we report that the Von Hippel-Lindau gene product, pVHL, physically interacts w

179 Mutations in the von Hippel-Lindau gene upregulate expression of the central

180 bed in association with mutations in the von Hippel-Lindau gene.

181 Loss of von Hippel-Lindau is not sufficient for neoplastic transform

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

183 correlations between the genotype of the von Hippel-Lindau mutation and the phenotype of eye disease

184 ent of the function of tumor suppressors von Hippel-Lindau or p53 or the degradation of HIF-alpha.

185 protein accumulation independent of the von Hippel-Lindau pathway.

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

187 The von Hippel-Lindau protein (pVHL) bound directly to hydroxyla

188 referentially interacted with PHD1-3 and von Hippel-Lindau protein (pVHL) during normoxia but not in

189 evious observations that deletion of the von Hippel-Lindau protein (pVHL) in juxtaglomerular (JG) cel

190 The tumor suppressor von Hippel-Lindau protein (pVHL) is critical for cellular mo

191 The von Hippel-Lindau protein (pVHL) is the substrate recognitio

192 IF-1 hydroxylation, and interaction with von Hippel-Lindau protein (pVHL), resulting in HIF-1alpha de

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

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

195 tin and collagen network is regulated by von Hippel-Lindau protein (pVHL).

196 iquitination by a complex containing the von Hippel-Lindau protein (pVHL).

197 F, resulting in high-affinity binding to Von Hippel-Lindau protein (pVHL).

198 Von Hippel-Lindau protein (VHL) is the E3 ubiquitin ligase t

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

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

201 lase PHD2 is required for binding of the von Hippel-Lindau protein (VHL), leading to ubiquitination a

202 on, which is required for binding of the von Hippel-Lindau protein (VHL), the recognition component o

203 d the first small molecule targeting the von Hippel-Lindau protein (VHL), the substrate recognition s

204 tion promotes binding of HIFalpha to the von Hippel-Lindau protein (VHL)-elongin B/C complex, thus si

205 ylation leading to ubiquitination by the von Hippel-Lindau protein (VHL)-Elongin C ubiquitin-ligase c

206 bunit is mediated by prolyl hydroxylase, von Hippel-Lindau protein (VHL)/Elongin-C E3 ubiquitin ligas

207 gh Pax8-rtTA-based inducible knockout of von Hippel-Lindau protein (VHL-KO), protects from rhabdomyol

208 additional TRiC-binding domain from the von Hippel-Lindau protein (vTBD), at the N-terminus of Stat3

209 and reducing HIF2alpha affinity for the von Hippel-Lindau protein and its degradation.

210 KSHV) targets the HIF-1alpha suppressors von Hippel-Lindau protein and p53 for degradation via its su

211 dentification of loss of function of the von Hippel-Lindau protein as the basis for clear cell RCC, i

212 In additional, von Hippel-Lindau protein expression was significantly incre

213 providing clues as to how disruptions in von Hippel-Lindau protein function may result in eye disease

214 Because pVHL (von Hippel-Lindau protein) directs the proteolysis of Hif-1a

215 is constitutively ubiquitinated by pVHL (von Hippel-Lindau protein) followed by proteasomal degradati

216 The tumor suppressor VHL (von Hippel-Lindau protein) serves as a negative regulator of

217 LF2 promoted HIF-1alpha degradation in a von Hippel-Lindau protein-independent but proteasome-depende

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

219 al activation was partially inhibited by von Hippel-Lindau protein.

220 e to renal cell carcinoma (RCC), such as Von Hippel-Lindau syndrome and tuberous sclerosis complex.

221 r and cystic kidney disease, miR-92a and von Hippel-Lindau syndrome, and alterations in LIN28-LET7 ex

222 e pseudo-hypoxic drive, just as it is in von Hippel-Lindau syndrome.

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

224 ers characterized by inactivation of the von Hippel-Lindau tumor suppressor (pVHL).

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

226 Inactivation of the von Hippel-Lindau tumor suppressor (VHL) is an early event i

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

228 (USP33)/VDU1, originally identified as a von Hippel-Lindau tumor suppressor (VHL) protein-interacting

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

230 effect of astrocyte-targeted deletion of von Hippel-Lindau tumor suppressor (Vhl), hypoxia-inducible

231 ents were in known ccRCC genes including von Hippel-Lindau tumor suppressor (VHL), polybromo 1 (PBRM1

232 characterized by loss of function of the von Hippel-Lindau tumor suppressor (VHL), which negatively r

233 F-1 reporter activity are independent of von Hippel-Lindau tumor suppressor (VHL)-1, whereas VHL-1 is

234 ha and targets it for recognition by the von Hippel-Lindau tumor suppressor and consequent degradatio

235 ansactivation potential independently of von Hippel-Lindau tumor suppressor and p53 function indicate

236 e characterized by biallelic loss of the von Hippel-Lindau tumor suppressor and subsequent constituti

237 ongin BC-box protein family includes the von Hippel-Lindau tumor suppressor and suppressor of cytokin

238 ongin C-containing ubiquitin ligase, the von Hippel-Lindau tumor suppressor complex, promotes Pol II

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

240 The von Hippel-Lindau tumor suppressor gene (VHL) has attracted

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

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

243 Here we show that loss of the Von Hippel-Lindau tumor suppressor gene (VHL) sensitizes kid

244 Mutations in von Hippel-Lindau tumor suppressor gene (VHL) underlie the V

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

246 fects on tumor cells occur regardless of von Hippel-Lindau tumor suppressor gene status and hypoxia-i

247 Inactivation of the von Hippel-Lindau tumor suppressor gene, VHL, is an archetyp

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

249 The Caenorhabditis elegans von Hippel-Lindau tumor suppressor homolog VHL-1 is a cullin

250 through tubule-specific knockdown of the von Hippel-Lindau tumor suppressor increased cyst size in th

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

252 l carcinoma (ccRCC), inactivation of the von Hippel-Lindau tumor suppressor is nearly universal; thus

253 of oxygen-sensing pathway including the von Hippel-Lindau tumor suppressor protein (pVHL) and the hy

254 The von Hippel-Lindau tumor suppressor protein (pVHL) is frequen

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

256 al epithelium-specific disruption of the von Hippel-Lindau tumor suppressor protein (VHL) resulted in

257 pecific disruption of genes encoding the von Hippel-Lindau tumor suppressor protein (Vhl), hypoxia-in

258 ology, intestinal-specific disruption of von Hippel-Lindau tumor suppressor protein (Vhl), hypoxia-in

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

260 the nucleus, where it co-localized with von Hippel-Lindau tumor suppressor protein and the HIF hydro

261 Furthermore, the down-regulation of the von Hippel-Lindau tumor suppressor protein by RNA interferen

262 The von Hippel-Lindau tumor suppressor protein is the substrate

263 The ability of von Hippel-Lindau tumor suppressor protein to form the E3 ub

264 Here, we use the von Hippel-Lindau tumor suppressor protein VHL as a model su

265 s did not differ, but HIF-1alpha and the von Hippel-Lindau tumor suppressor protein were overexpresse

266 161 also increased HIF-1alpha binding to von Hippel-Lindau tumor suppressor protein, an E3 ligase com

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

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

269 The von Hippel-Lindau tumor suppressor pVHL regulates the stabil

270 reviously shown that inactivation of the von Hippel-Lindau tumor suppressor pVHL, which targets both

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

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

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

274 es that were wild-type or mutant for the Von Hippel-Lindau tumor suppressor, in characterizing higher

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

276 nephron via induced inactivation of the von Hippel-Lindau tumor suppressor, which targets the HIF-al

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

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

279 Inactivation of von Hippel-Lindau tumor-suppressor protein (pVHL) is associa

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

281 e HIF-1alpha pathway through deletion of von Hippel-Lindau tumor-suppressor protein or pharmacologic

282 characterized by loss of function of the von Hippel-Lindau tumour suppressor (VHL) and unrestrained a

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

284 In particular, the von Hippel-Lindau tumour suppressor protein (pVhl) controls

285 rmore, renal cell lines deficient in the von Hippel-Lindau tumour suppressor protein preferentially u

286 bsequent proteasomal degradation via the von Hippel-Lindau ubiquitin ligase.

287 rast, over-expression of Vhl (Drosophila von Hippel-Lindau) generated a range of phenotypes, includin

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

289 deletions that harbor the ccRCC-related von Hippel-Lindau, PBRM1, BAP1, and SETD2 tumor suppressor g

290 We identified Von Hippel-Lindau, pVHL, as the protein that governs KLF4 tu

291 without altering its protein levels in a von Hippel-Lindau-deficient cell line, indicating a discrete

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

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

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

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

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

297 Dysregulation of the von Hippel-Lindau/hypoxia-inducible transcription factor (HI

298 Here we establish that the von Hippel-Lindau/hypoxia-inducible transcription factor (VH

299 onditional gene targeting to examine the von Hippel-Lindau/prolyl-4-hydroxylase domain (PHD)/HIF axis

300 In the established Berg-von Hippel model for this search process, the TF alternates