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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

28 arget pair deemed unsuitable: the von Hippel-Lindau (VHL) and BRD9, a bromodomain-containing subunit

29 ensive SAR studies exploring both von Hippel-Lindau (VHL) and cereblon (CRBN) E3 ligase ligands and a

30 two different ligands recruiting Von Hippel-Lindau (VHL) and cereblon (CRBN) E3 ubiquitin ligases, o

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

50 AC), that targets BCL-X(L) to the Von Hippel-Lindau (VHL) E3 ligase for degradation.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

70 von Hippel-Lindau (VHL) is a critical tumor suppressor in clear cel

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

72 Von Hippel-Lindau (VHL) is an E3 ubiquitin ligase that targets prot

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

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

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

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

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

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

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

80 ive regulation of HIFalpha by the von Hippel-Lindau (VHL) protein, the mechanisms underlying the comp

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 The von Hippel-Lindau (VHL) syndrome is a rare inherited cancer, caused

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

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

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

92 CI expression is regulated by the von Hippel-Lindau (VHL) tumor suppressor and is highly expressed in

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

94 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 with i

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

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

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

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

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

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

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

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

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

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

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

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

108 Loss of the von Hippel-Lindau (VHL) tumor suppressor is a hallmark feature of r

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

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

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

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

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

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

115 mutation, loss of function of the von Hippel-Lindau (VHL) tumor suppressor, provides a human pathogen

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

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

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 lease of molecular constraints on von Hippel-Lindau (VHL) ubiquitin ligase tumor suppressor function.

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

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

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

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

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

126 erstanding the growth kinetics of Von Hippel-Lindau (VHL)-associated clear cell renal cell carcinoma

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

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

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

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

131 on, which rises at birth, and the von Hippel-Lindau (VHL)-hypoxia-inducible factor 1alpha (Hif1alpha)

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

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

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

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

136 sly, we reported a first-in-class von Hippel-Lindau (VHL)-recruiting mitogen-activated protein kinase

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

138 on, which is largely regulated by von Hippel-Lindau (VHL; a protein component of a ubiquitin ligase c

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

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

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

142 ysis-targeting chimeras utilizing von Hippel-Lindau and cereblon ligands to hijack E3 ligases for PTK

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

163 molecular interventions in ocular von Hippel-Lindau disease.

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

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

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

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

168 69), with impaired binding to the von Hippel-Lindau E3 ligase and PRMT5, respectively.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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 ion CT screening of patients with von Hippel-Lindau syndrome can lead to substantial radiation exposu

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

252 (ccRCCs) have inactivation of the von Hippel-Lindau tumor suppressor protein (pVHL), resulting in the

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

271 ubiquitination via the E3 ligase von Hippel-Lindau tumor suppressor, which targets Hypoxia-Inducible

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

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

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

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

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

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

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

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

280 ally activated by mutation of the von Hippel-Lindau tumour suppressor, we observed marked excess over

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

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

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

284 genetic loss-of-function of VHL (von Hippel-Lindau) that leads to a highly vascularized tumor microe

285 retinib) and recruited E3 ligase (von Hippel-Lindau).

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

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

288 protein and recruit the E3 ligase Von Hippel-Lindau, resulting in ubiquitination and subsequent degra

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

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

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

292 he discovery of a novel E3 ligase von Hippel-Lindau-recruiting EGFR degrader, MS39 (compound 6), and

293 ponent for HIF destruction called von Hippel-Lindau.

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