ライフサイエンスコーパス: Lindau

1 Von Hippel Lindau (VHL) is a tumour suppressor that is lost in the

2 n of the tumor suppressor protein von Hippel Lindau (VHL) leads to an increase in VPF/VEGF expression

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

4 Aberrant von Hippel Lindau (VHL) protein function is the underlying driver o

5 von Hippel Lindau (Vhl) protein, encoded by a tumor suppressor gene

6 ndocrine neoplasia type 1 (MEN1), von Hippel Lindau (VHL) syndrome, neurofibromatosis (NF-1), and pos

7 essed because of mutations in the von Hippel Lindau (VHL) tumor suppressor protein.

8 ontrolled by the tumor suppressor von Hippel Lindau (VHL).

9 onal loss of the tumor suppressor von Hippel Lindau (VHL).

10 ldin subunit counterpart of human von Hippel Lindau binding-protein 1.

11 by recruiting either Cereblon or Von Hippel Lindau E3 ligases is reported.

12 no change in HIF-1alpha mRNA and von Hippel Lindau E3 ubiquitin ligase (VHL) protein expression.

13 or type associated with wild-type von Hippel Lindau gene.

14 their effects on PHD2 binding and von Hippel Lindau interaction.

15 Von Hippel Lindau protein (pVHL) and hypoxia inducible factor (HIF)

16 that GCs limit the expression of Von Hippel Lindau protein (pVHL), a negative regulator of HIF, and

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

18 ha increases its affinity for the von Hippel Lindau protein elongin B/C (VCB) ubiquitin ligase comple

19 vides a recognition motif for the von Hippel Lindau protein, a component of an E3 ubiquitin ligase co

20 igand for the E3 ubiquitin ligase von Hippel Lindau protein.

21 nce in uptake among patients with von Hippel Lindau syndrome (VHL; n = 19), succinate dehydrogenase B

22 (RCC) is characterized by loss of von Hippel Lindau tumor suppressor gene activity, resulting in high

23 otein levels are regulated by the von Hippel Lindau tumor suppressor gene, VHL, which targets HIF-1al

24 The von Hippel Lindau tumor suppressor protein (pVHL) is a component of

25 Inactivation of the VHL (Von Hippel Lindau) tumour suppressor has long been recognised as ne

26 ancing its interactions with VHL (von Hippel Lindau), thus promoting its ubiquitination and degradati

27 he hypoxia inducible factor (HIF)/von Hippel Lindau/hydroxylase pathway, including specific roles for

28 ent insights into the role of the von-Hippel Lindau (VHL) tumor suppressor gene in hereditary and spo

29 tion of the tumor suppressor gene von-Hippel Lindau (VHL), which activates the hypoxia-inducible fact

30 on by oxygen requires the protein von Hippel-Lindau (pVhl) and pVhl disruption results in constitutiv

31 cRCC) exhibit inactivation of the von Hippel-Lindau (pVHL) tumor suppressor, establishing it as the m

32 ally associated with mutations in von Hippel-Lindau (VHL) and subsequent normoxic stabilization of hy

33 ions in the tumor-suppressor gene von Hippel-Lindau (VHL) are associated with a complex spectrum of c

34 tion of the tumor suppressor gene von Hippel-Lindau (VHL) are major causes of clear-cell renal cell c

35 lpha and their negative regulator von Hippel-Lindau (VHL) as well as astrocyte-specific deletion of t

36 TRC8/RNF139 and von Hippel-Lindau (VHL) both encode E3 ubiquitin (Ub) ligases mutat

37 ions of the tumor suppressor gene von Hippel-Lindau (VHL) can lead to benign and malignant tumors, in

38 ients with a germline mutation in von Hippel-Lindau (VHL) develop renal cell cancers and hypervascula

39 functional progression of ocular von Hippel-Lindau (VHL) disease and analysis of patient factors inf

40 the autosomal dominant condition von Hippel-Lindau (VHL) disease and is implicated in most sporadic

41 von Hippel-Lindau (VHL) disease is a dominantly inherited family ca

42 von Hippel-Lindau (VHL) disease is a rare familial cancer predispos

43 von Hippel-Lindau (VHL) disease is caused by germ-line mutations in

44 Von Hippel-Lindau (VHL) disease is caused by germline mutations in

45 von Hippel-Lindau (VHL) disease is caused by germline mutations of

46 The von Hippel-Lindau (VHL) disease is caused by VHL germ line mutation

47 cystic kidney disease (ADPKD) and von Hippel-Lindau (VHL) disease lead to large kidney cysts that sha

48 von Hippel-Lindau (VHL) disease results from germline and somatic m

49 ioblastomas (RCH) associated with von Hippel-Lindau (VHL) disease treated with systemic sunitinib mal

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

51 use of mortality in patients with von Hippel-Lindau (VHL) disease, which is caused by germ line mutat

52 l, overexpression was achieved by Von Hippel-Lindau (Vhl) disruption in a liver-specific temporal fas

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

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

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

56 the E3 ubiquitin ligase complex, von Hippel-Lindau (VHL) facilitates oxygen-dependent polyubiquitina

57 with an epidermal deletion of the von Hippel-Lindau (VHL) factor, a negative regulator of HIF, have i

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

59 ith an intragenic mutation in the von Hippel-Lindau (VHL) gene and loss of 3p (where VHL is located).

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

61 Mutations in the human von Hippel-Lindau (VHL) gene are the cause of VHL disease that disp

62 identified functional loss of the von Hippel-Lindau (VHL) gene as a frequent and crucial event in the

63 Mutations in the von Hippel-Lindau (VHL) gene give rise to renal cell carcinoma.

64 lished literature regarding VEGF, von Hippel-Lindau (VHL) gene inactivation and VEGF overexpression i

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

66 requently display inactivation of von Hippel-Lindau (VHL) gene leading to increased level of hypoxia-

67 Von Hippel-Lindau (VHL) gene loss is an important factor in the dev

68 von Hippel-Lindau (VHL) gene mutations are associated with clear ce

69 Germline von Hippel-Lindau (VHL) gene mutations underlie dominantly inherite

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

71 inoma (CC-RCC) is the loss of the von Hippel-Lindau (VHL) gene, which results in stabilization of hyp

72 d by frequent inactivation of the von Hippel-Lindau (VHL) gene.

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

74 ypoxia-regulated tumor-suppressor von Hippel-Lindau (VHL) is an E3 ligase that recognizes its substra

75 cible factors (HIFs) secondary to von Hippel-Lindau (VHL) mutations that occur in over 90% of ccRCC t

76 ctivation of the tumor suppressor von Hippel-Lindau (VHL) occurs in the majority of the tumors and is

77 von Hippel-Lindau (VHL) patients develop multiple central nervous s

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

79 Cell, Roe et al. report that the von Hippel-Lindau (VHL) protein is a positive regulator of p53, thu

80 von Hippel-Lindau (VHL) protein is known to destabilize myogenin vi

81 ts binding to a ubiquitin ligase, von Hippel-Lindau (VHL) protein, through a proline hydroxylation-in

82 oted the degradation of the human von Hippel-Lindau (VHL) protein, which is an unfolded protein in ye

83 e residues followed by binding of von Hippel-Lindau (VHL) protein.

84 ed by O2-dependent binding of the von Hippel-Lindau (VHL) protein.

85 ers targeting cereblon (CRBN) and Von Hippel-Lindau (VHL) proteins.

86 on of a transgenic mouse model of von Hippel-Lindau (VHL) renal cancer termed the TRACK model (transg

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

88 n by the prolyl hydroxylase (PHD)/von Hippel-Lindau (VHL) system.

89 ently associated with loss of the von Hippel-Lindau (VHL) tumor suppressor (pVHL), which inhibits ubi

90 nent of the ElonginB/C-CUL2-RBX-1-Von Hippel-Lindau (VHL) tumor suppressor complex that ubiquitinates

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

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

93 tic and epigenetic changes in the von Hippel-Lindau (VHL) tumor suppressor gene are common in sporadi

94 earing germ line mutations in the Von Hippel-Lindau (VHL) tumor suppressor gene are predisposed to th

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

96 Loss of von Hippel-Lindau (VHL) tumor suppressor gene function occurs in fa

97 The von Hippel-Lindau (VHL) tumor suppressor gene is inactivated in the

98 The von Hippel-Lindau (VHL) tumor suppressor gene is mutated as an earl

99 g from the hereditary loss of the von Hippel-Lindau (VHL) tumor suppressor gene is the leading cause

100 Inactivating mutations within the von Hippel-Lindau (VHL) tumor suppressor gene predispose patients t

101 Germline mutations in the von Hippel-Lindau (VHL) tumor suppressor gene predispose people to

102 oma (RCC), cells deficient in the von Hippel-Lindau (VHL) tumor suppressor gene use glutamine to gene

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

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

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

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

107 von Hippel-Lindau (VHL) tumor suppressor loss is associated with re

108 The R200W mutation in the von Hippel-Lindau (VHL) tumor suppressor protein (pVHL) is unique i

109 Mutation of the von Hippel-Lindau (VHL) tumor suppressor protein at codon 200 (R200

110 The von Hippel-Lindau (VHL) tumor suppressor protein pVHL is commonly m

111 The Von Hippel-Lindau (VHL) tumor suppressor protein regulates VEGF gen

112 tin ligase complex containing the von Hippel-Lindau (VHL) tumor suppressor protein, which results in

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

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

115 tin ligase complex containing the von Hippel-Lindau (VHL) tumor suppressor.

116 terized by an inactivation of the von Hippel-Lindau (VHL) tumor-suppressor gene with subsequent stabi

117 articular the inactivation of the von Hippel-Lindau (VHL) tumour suppressor gene (TSG).

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

119 ducible factor (HIF), whereas the von Hippel-Lindau (VHL) ubiquitin ligase as well as the oxygen-sens

120 , Cullin, F-box protein) and VCB (von Hippel-Lindau (VHL), Cullin and Elongin B/C) E3 ubiquitin ligas

121 ontrolled by the tumor suppressor von Hippel-Lindau (VHL), deletion of VHL results in constitutive HI

122 cription and a down-regulation of von Hippel-Lindau (VHL), the E3 ubiquitin ligase that mediates the

123 the loss of the tumor suppressor von Hippel-Lindau (VHL), which causes hypoxia-inducible factor (HIF

124 Von Hippel-Lindau (VHL)-associated hemangioblastomas (VHL-HB) arise

125 der to examine the role of HIF in von Hippel-Lindau (VHL)-associated vascular tumorigenesis, we utili

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

127 HIF-2alpha is stabilized in von Hippel-Lindau (VHL)-deficient renal cell carcinoma through mech

128 ntially regulated by hypoxia in a von Hippel-Lindau (VHL)-dependent manner both in RCC cell culture a

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

130 induces prolyl hydroxylation and von Hippel-Lindau (VHL)-mediated proteasomal degradation, whereas h

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

132 In von Hippel-Lindau (VHL)-null kidney cancer cell lines, we reported

133 by prolyl hydroxylase (PHD), the von Hippel-Lindau (VHL)/Elongin-C/Elongin-B E3 ubiquitin ligase com

134 (SDH is succinate dehydrogenase); von Hippel-Lindau (VHL; n = 2); RET (n = 12); neurofibromin 1 (NF1;

135 demonstrate that deletion of the von Hippel-Lindau (Vhlh) gene (encoding an E3 ubiquitin ligase impl

136 The E3 ligase von Hippel-Lindau and autophagy receptor protein p62 are required f

137 arcinoma include the discovery of von Hippel-Lindau associated mechanisms involved in renal cyst form

138 ved that hMSH4 interacts with the von Hippel-Lindau binding protein 1 (VBP1), a partner of the VHL ub

139 1alpha binding with its E3 ligase von Hippel-Lindau but enhanced the binding affinity between the HIF

140 Patients with von Hippel-Lindau disease (VHL) are at risk to develop multiple tum

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

142 ne tumors (PNETs) associated with von Hippel-Lindau disease (VHL) is challenging because of the malig

143 Von Hippel-Lindau disease (VHL) is one of the most common inherited

144 von Hippel-Lindau disease (VHL) patients develop highly vascular tu

145 umors (ELSTs) are associated with von Hippel-Lindau disease and cause irreversible sensorineural hear

146 erial evaluation of patients with von Hippel-Lindau disease and ELSTs at the National Institutes of H

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

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

149 se may inform us as to how ocular von Hippel-Lindau disease arises, and help guide molecular interven

150 inical characterization of ocular von Hippel-Lindau disease has been limited by small patient numbers

151 von Hippel-Lindau disease is an inherited, multisystemic cancer syn

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

153 on postmortem tissues from three von Hippel-Lindau disease patients (not in the clinical series).

154 with the clinical findings in 16 von Hippel-Lindau disease patients with 22 CNS hemangioblastomas (1

155 ance imaging (MRI) is obtained in von Hippel-Lindau disease patients, hemangioblastomas provide an op

156 linically and genetically defined von Hippel-Lindau disease was systemically characterized in a singl

157 tion in the VHL gene leads to the von Hippel-Lindau disease, a familial syndrome characterized by ben

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

159 f renal cancer syndromes includes von Hippel-Lindau disease, Birt-Hogg-Dube syndrome, hereditary papi

160 argeting the molecular biology of von Hippel-Lindau disease, some of which are presently being invest

161 molecular interventions in ocular von Hippel-Lindau disease.

162 tants may rescue pVHL function in von Hippel-Lindau disease.

163 erization and treatment of ocular von Hippel-Lindau disease.

164 hich can occur sporadically or in von Hippel-Lindau disease.

165 with or without association with von Hippel-Lindau disease.

166 NA levels and increased levels of von Hippel-Lindau E3 ligase in TRPM2-S-expressing cells.

167 through selective deletion of the von Hippel-Lindau gene (Vhl) expressed high levels of Vegf and deve

168 t SCAs contained mutations of the von Hippel-Lindau gene (VHL), a key component of the VHL ubiquitin

169 nditions, through the loss of the Von Hippel-Lindau gene (VHL).

170 Inactivation of the von Hippel-Lindau gene in clear-cell renal cell carcinomas (RCC) le

171 Von Hippel-Lindau gene inactivation is observed in most clear cell

172 orrelations between the nature of von Hippel-Lindau gene mutations and the ocular phenotype were also

173 Von Hippel-Lindau gene mutations were detected in four (22%) of 18

174 e have examined the status of the von Hippel-Lindau gene product (pVHL) that is responsible for HIF-1

175 Here, we report that the Von Hippel-Lindau gene product, pVHL, physically interacts with KLF

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

177 association with mutations in the von Hippel-Lindau gene.

178 Loss of von Hippel-Lindau is not sufficient for neoplastic transformation,

179 eficiency of the tumor suppressor von Hippel-Lindau leads to constitutively active hypoxia-inducible

180 tions between the genotype of the von Hippel-Lindau mutation and the phenotype of eye disease may inf

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

182 n accumulation independent of the von Hippel-Lindau pathway.

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

184 The von Hippel-Lindau protein (pVHL) bound directly to hydroxylated Akt

185 tially interacted with PHD1-3 and von Hippel-Lindau protein (pVHL) during normoxia but not in hypoxia

186 observations that deletion of the von Hippel-Lindau protein (pVHL) in juxtaglomerular (JG) cells of t

187 The tumor suppressor von Hippel-Lindau protein (pVHL) is critical for cellular molecular

188 The von Hippel-Lindau protein (pVHL) is the substrate recognition subun

189 droxylation, and interaction with von Hippel-Lindau protein (pVHL), resulting in HIF-1alpha degradati

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

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

192 collagen network is regulated by von Hippel-Lindau protein (pVHL).

193 ation by a complex containing the von Hippel-Lindau protein (pVHL).

194 lting in high-affinity binding to Von Hippel-Lindau protein (pVHL).

195 Von Hippel-Lindau protein (VHL) is the E3 ubiquitin ligase that tar

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

197 myocyte-specific deletion of the von Hippel-Lindau protein (VHL), an essential component of an E3 ub

198 D2 is required for binding of the von Hippel-Lindau protein (VHL), leading to ubiquitination and prot

199 ch is required for binding of the von Hippel-Lindau protein (VHL), the recognition component of an E3

200 irst small molecule targeting the von Hippel-Lindau protein (VHL), the substrate recognition subunit

201 omotes binding of HIFalpha to the von Hippel-Lindau protein (VHL)-elongin B/C complex, thus signallin

202 leading to ubiquitination by the von Hippel-Lindau protein (VHL)-Elongin C ubiquitin-ligase complex

203 s mediated by prolyl hydroxylase, von Hippel-Lindau protein (VHL)/Elongin-C E3 ubiquitin ligase, and

204 -rtTA-based inducible knockout of von Hippel-Lindau protein (VHL-KO), protects from rhabdomyolysis-in

205 onal TRiC-binding domain from the von Hippel-Lindau protein (vTBD), at the N-terminus of Stat3, furth

206 ducing HIF2alpha affinity for the von Hippel-Lindau protein and its degradation.

207 argets the HIF-1alpha suppressors von Hippel-Lindau protein and p53 for degradation via its suppresso

208 cation of loss of function of the von Hippel-Lindau protein as the basis for clear cell RCC, in addit

209 In additional, von Hippel-Lindau protein expression was significantly increased in

210 ng clues as to how disruptions in von Hippel-Lindau protein function may result in eye disease.

211 Because pVHL (von Hippel-Lindau protein) directs the proteolysis of Hif-1alpha un

212 titutively ubiquitinated by pVHL (von Hippel-Lindau protein) followed by proteasomal degradation unde

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

214 moted HIF-1alpha degradation in a von Hippel-Lindau protein-independent but proteasome-dependent mann

215 or HIF-1alpha, HIF-2alpha, or the von Hippel-Lindau protein.

216 vation was partially inhibited by von Hippel-Lindau protein.

217 nal cell carcinoma (RCC), such as Von Hippel-Lindau syndrome and tuberous sclerosis complex.

218 ystic kidney disease, miR-92a and von Hippel-Lindau syndrome, and alterations in LIN28-LET7 expressio

219 o-hypoxic drive, just as it is in von Hippel-Lindau syndrome.

220 ficant reduction in expression of von Hippel-Lindau tumor suppressor (100 vs 40; P < .001) and C-MET

221 racterized by inactivation of the von Hippel-Lindau tumor suppressor (pVHL).

222 etabolism correlated with loss of von Hippel-Lindau tumor suppressor (VHL) and a potential activation

223 Inactivation of the von Hippel-Lindau tumor suppressor (VHL) is an early event in >60%

224 ed by conditional deletion of the von Hippel-Lindau tumor suppressor (VHL) protein in the forkhead bo

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

226 The von Hippel-Lindau tumor suppressor (VHL) represses TRPM3 directly t

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

228 re in known ccRCC genes including von Hippel-Lindau tumor suppressor (VHL), polybromo 1 (PBRM1), SET

229 erized by loss of function of the von Hippel-Lindau tumor suppressor (VHL), which negatively regulate

230 orter activity are independent of von Hippel-Lindau tumor suppressor (VHL)-1, whereas VHL-1 is requir

231 targets it for recognition by the von Hippel-Lindau tumor suppressor and consequent degradation.

232 vation potential independently of von Hippel-Lindau tumor suppressor and p53 function indicates that

233 cterized by biallelic loss of the von Hippel-Lindau tumor suppressor and subsequent constitutive acti

234 C-box protein family includes the von Hippel-Lindau tumor suppressor and suppressor of cytokine signa

235 -containing ubiquitin ligase, the von Hippel-Lindau tumor suppressor complex, promotes Pol II polyubi

236 lic inactivating mutations of the von Hippel-Lindau tumor suppressor gene (VHL) are a hallmark of cle

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

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

239 Loss of function of the von Hippel-Lindau tumor suppressor gene (VHL) predisposes renal epi

240 Here we show that loss of the Von Hippel-Lindau tumor suppressor gene (VHL) sensitizes kidney can

241 Mutations in von Hippel-Lindau tumor suppressor gene (VHL) underlie the VHL here

242 nctions have been assigned to the von Hippel-Lindau tumor suppressor gene product (pVHL), including t

243 n tumor cells occur regardless of von Hippel-Lindau tumor suppressor gene status and hypoxia-inducibl

244 Inactivation of the von Hippel-Lindau tumor suppressor gene, VHL, is an archetypical tu

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

246 The Caenorhabditis elegans von Hippel-Lindau tumor suppressor homolog VHL-1 is a cullin E3 ubi

247 tubule-specific knockdown of the von Hippel-Lindau tumor suppressor increased cyst size in the embry

248 Purpose The von Hippel-Lindau tumor suppressor is inactivated in the majority o

249 noma (ccRCC), inactivation of the von Hippel-Lindau tumor suppressor is nearly universal; thus, the b

250 gen-sensing pathway including the von Hippel-Lindau tumor suppressor protein (pVHL) and the hypoxia i

251 The von Hippel-Lindau tumor suppressor protein (pVHL) is frequently mut

252 The von Hippel-Lindau tumor suppressor protein (pVHL) is one of these p

253 helium-specific disruption of the von Hippel-Lindau tumor suppressor protein (VHL) resulted in consti

254 disruption of genes encoding the von Hippel-Lindau tumor suppressor protein (Vhl), hypoxia-inducible

255 intestinal-specific disruption of von Hippel-Lindau tumor suppressor protein (Vhl), hypoxia-inducible

256 s targeted for degradation by the von Hippel-Lindau tumor suppressor protein (VHL).

257 cleus, where it co-localized with von Hippel-Lindau tumor suppressor protein and the HIF hydroxylases

258 required for its binding with the von Hippel-Lindau tumor suppressor protein and the subsequent prote

259 rmore, the down-regulation of the von Hippel-Lindau tumor suppressor protein by RNA interference incr

260 The von Hippel-Lindau tumor suppressor protein is the substrate binding

261 The ability of von Hippel-Lindau tumor suppressor protein to form the E3 ubiquitin

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

263 ot differ, but HIF-1alpha and the von Hippel-Lindau tumor suppressor protein were overexpressed in HA

264 o increased HIF-1alpha binding to von Hippel-Lindau tumor suppressor protein, an E3 ligase component

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

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

267 The von Hippel-Lindau tumor suppressor pVHL regulates the stability of

268 ly shown that inactivation of the von Hippel-Lindau tumor suppressor pVHL, which targets both HIFs fo

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

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

271 -inducible factor-1alpha with the von Hippel-Lindau tumor suppressor, and in an estrogen receptor int

272 were wild-type or mutant for the Von Hippel-Lindau tumor suppressor, in characterizing higher-grade

273 Inactivation of the von Hippel-Lindau tumor suppressor, pVHL, is associated with both h

274 n via induced inactivation of the von Hippel-Lindau tumor suppressor, which targets the HIF-alpha sub

275 tin ligase complex containing the von Hippel-Lindau tumor suppressor.

276 The von Hippel-Lindau tumor-suppressor gene (VHL) is lost in most clear

277 Inactivation of von Hippel-Lindau tumor-suppressor protein (pVHL) is associated wit

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

279 alpha pathway through deletion of von Hippel-Lindau tumor-suppressor protein or pharmacologic inducer

280 erized by loss of function of the von Hippel-Lindau tumour suppressor (VHL) and unrestrained activati

281 racterized by inactivation of the von Hippel-Lindau tumour suppressor gene (VHL).

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

283 renal cell lines deficient in the von Hippel-Lindau tumour suppressor protein preferentially use redu

284 t proteasomal degradation via the von Hippel-Lindau ubiquitin ligase.

285 ver-expression of Vhl (Drosophila von Hippel-Lindau) generated a range of phenotypes, including block

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

287 ons that harbor the ccRCC-related von Hippel-Lindau, PBRM1, BAP1, and SETD2 tumor suppressor genes, a

288 We identified Von Hippel-Lindau, pVHL, as the protein that governs KLF4 turnover

289 altering its protein levels in a von Hippel-Lindau-deficient cell line, indicating a discrete activi

290 lases and subsequent evasion from von Hippel-Lindau-dependent degradation.

291 We show that von Hippel-Lindau-dependent down-regulation of Dicer is key to the

292 4) of HIFalpha was abolished in a von Hippel-Lindau-dependent manner in cells exposed to nickel(II) o

293 ydrolase-L1 (UCHL1) abrogates the von Hippel-Lindau-mediated ubiquitination of HIF-1alpha, the regula

294 one during the elucidation of the von Hippel-Lindau/clear cell RCC pathway.

295 esult, LMP1 prevents formation of von Hippel-Lindau/HIF1alpha complex, as shown by coimmunoprecipitat

296 Dysregulation of the von Hippel-Lindau/hypoxia-inducible transcription factor (HIF) sign

297 Here we establish that the von Hippel-Lindau/hypoxia-inducible transcription factor (VHL/HIF)

298 nal gene targeting to examine the von Hippel-Lindau/prolyl-4-hydroxylase domain (PHD)/HIF axis in cel

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

300 xia signaling by knockdown of the von-Hippel-Lindau (VHL) protein led to reversal of the effects of M