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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

31 igase-target pair deemed unsuitable: the von Hippel-Lindau (VHL) and BRD9, a bromodomain-containing s

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

33 s, onto two different ligands recruiting Von Hippel-Lindau (VHL) and cereblon (CRBN) E3 ubiquitin lig

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

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

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

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

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

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

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

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

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

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

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

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

59 -1alpha and/or HIF-2alpha due to loss of von Hippel-Lindau (VHL) function.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

74 von Hippel-Lindau (VHL) is a critical tumor suppressor in cl

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

76 Von Hippel-Lindau (VHL) is an E3 ubiquitin ligase that targe

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

85 -sensitive regulation of HIFalpha by the von Hippel-Lindau (VHL) protein, the mechanisms underlying t

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

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

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

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

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

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

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

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

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

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

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

97 ore, NICI expression is regulated by the von Hippel-Lindau (VHL) tumor suppressor and is highly expre

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

113 Loss of the von Hippel-Lindau (VHL) tumor suppressor is a hallmark featu

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

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

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

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

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

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

120 ssical mutation, loss of function of the von Hippel-Lindau (VHL) tumor suppressor, provides a human p

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

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

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

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

125 the release of molecular constraints on von Hippel-Lindau (VHL) ubiquitin ligase tumor suppressor fu

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

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

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

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

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

131 in understanding the growth kinetics of Von Hippel-Lindau (VHL)-associated clear cell renal cell car

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

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

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

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

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

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

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

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

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

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

142 entration, which is largely regulated by von Hippel-Lindau (VHL; a protein component of a ubiquitin l

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

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

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

146 proteolysis-targeting chimeras utilizing von Hippel-Lindau and cereblon ligands to hijack E3 ligases

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

172 1 (MS4369), with impaired binding to the von Hippel-Lindau E3 ligase and PRMT5, respectively.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

264 161 also increased HIF-1alpha binding to von Hippel-Lindau tumor suppressor protein, an E3 ligase com

265 of the 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

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

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

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

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

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

272 sequent ubiquitination via the E3 ligase von Hippel-Lindau tumor suppressor, which targets Hypoxia-In

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

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

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

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

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

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

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

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

281 iologically activated by mutation of the von Hippel-Lindau tumour suppressor, we observed marked exce

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

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

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

285 cRCC is genetic loss-of-function of VHL (von Hippel-Lindau) that leads to a highly vascularized tumor

286 ead (foretinib) and recruited E3 ligase (von Hippel-Lindau).

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

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

289 R-ABL1 protein and recruit the E3 ligase Von Hippel-Lindau, resulting in ubiquitination and subsequen

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

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

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

293 ribed the discovery of a novel E3 ligase von Hippel-Lindau-recruiting EGFR degrader, MS39 (compound 6

294 ase component for HIF destruction called von Hippel-Lindau.

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