ライフサイエンスコーパス: ER-associated degradation

1 us ubiquitin (Ub)-dependent pathways such as ER-associated degradation.

2 asmic proteasomes through a process known as ER-associated degradation.

3 anchored Ubc6, makes a major contribution to ER-associated degradation.

4 duction in GPIb-IX complex expression due to ER-associated degradation.

5 xhibited defects in translocation but not in ER-associated degradation.

6 at involves the quality control mechanism of ER-associated degradation.

7 valosin-containing protein and necessary for ER-associated degradation.

8 checkpoints and can target ENaC subunits for ER-associated degradation.

9 graded by proteasomes via a process known as ER-associated degradation.

10 rA2 as a regulator of APP metabolism through ER-associated degradation.

11 FTR, causes ER retention and degradation via ER-associated degradation.

12 degraded by the proteasome, a process called ER-associated degradation.

13 charomyces cerevisiae) protein implicated in ER-associated degradation.

14 toward either correct folding or disposal by ER-associated degradation.

15 targeted for disposal in a process known as ER-associated degradation.

16 bind the ER chaperone BiP/Grp78, and undergo ER-associated degradation.

17 E1 and E2 not only regulate the UPR but also ER-associated degradation.

18 disposal of terminally unfolded proteins by ER-associated degradation.

19 ntrast, COPII is not used to deliver CFTR to ER-associated degradation.

20 tant CHO cells exhibiting increased rates of ER-associated degradation.

21 y; instead, they are ultimately targeted for ER-associated degradation.

22 are retained in the ER and can be removed by ER-associated degradation.

23 ght be involved in either protein folding or ER-associated degradation.

24 d protein with a reduced half-life caused by ER-associated degradation.

25 um (ER): translocation, protein folding, and ER-associated degradation.

26 Thus, ACD6 constitutively undergoes ER-associated degradation.

27 ired for protein folding and is connected to ER-associated degradation.

28 nduces classical ER stress and is removed by ER-associated degradation.

29 TA1 through the quality control mechanism of ER-associated degradation.

30 somal enzymes that are otherwise degraded in ER-associated degradation.

31 in a process known as endoplasmic reticulum (ER)-associated degradation.

32 y chains (HC) undergo endoplasmic reticulum (ER)-associated degradation.

33 units are degraded by endoplasmic reticulum (ER)-associated degradation.

34 to mediate protein retrotranslocation during ER-associated degradation (a process called ERAD).

35 tein C (SP-C) trigger endoplasmic reticulum (ER)-associated degradation, a pathway that segregates te

36 ndoplasmic reticulum (ER) are eliminated via ER-associated degradation, a process that dislocates mis

37 nt is a substrate for endoplasmic reticulum (ER)-associated degradation and causes a dominant negativ

38 which is involved in endoplasmic reticulum (ER)-associated degradation and nuclear envelope reassemb

39 wly synthesized apoB, endoplasmic reticulum (ER)-associated degradation and re-uptake from the cell s

40 previously linked to endoplasmic reticulum (ER)-associated degradation and to the control of triacyl

41 oplasmic reticulum (ER), is degraded by both ER-associated degradation and autophagy, and causes hepa

42 ulated genes involved in MUC2 folding and in ER-associated degradation and maintained correct folding

43 f the ubiquitin-proteasome system, including ER-associated degradation and the control of lipid compo

44 o the cytosol by the pathway established for ER-associated degradation and their derived peptides may

45 thy cells constitutively degrade BOK via the ER-associated degradation and ubiquitin-proteasome pathw

46 for sterol pathway signals to stimulate Hmg2 ER-associated degradation and was employed for detection

47 consistent with protein misfolding and rapid ER-associated degradation, and can be stabilized by hist

48 ytosolic stress-induced heat shock response, ER-associated degradation, and polyubiquitination.

49 proteins subjected to endoplasmic reticulum (ER)-associated degradation are extracted from membranes

50 o sterol-accelerated, endoplasmic reticulum (ER)-associated degradation augmented by the nonsterol is

51 sterol synthesis, for endoplasmic reticulum (ER)-associated degradation by 26 S proteasomes.

52 Thus, ER-associated degradation can occur by mechanisms that d

53 In the endoplasmic reticulum (ER), ER-associated degradation clears aberrant proteins from

54 ER-associated degradation clears the secretory pathway o

55 Destabilized JB12 was degraded by ER-associated degradation complexes that contained HERP,

56 2 participates in recruiting p97 ATPase into ER-associated degradation complexes.

57 es encoding chaperones, oxidoreductases, and ER-associated degradation components.

58 trolled at the level of protein stability by ER-associated degradation components.

59 horing domain and thereby identified several ER-associated degradation diseases candidates.

60 Mutant yeast strains with diminished ER-associated degradation do not secrete BPTI more effic

61 llular components for endoplasmic reticulum (ER)-associated degradation due to their role in substrat

62 Inhibition of ER-associated degradation (either HtrA2 or proteasome) p

63 has been proposed to have multiple roles in ER-associated degradation, ER-mitochondria tethering, an

64 of ERV29, a stress-induced gene required for ER associated degradation (ERAD), misfolded proteins acc

65 nces in the extent of endoplasmic reticulum (ER) associated degradation (ERAD) of apo(a) allelic vari

66 t can be selected for endoplasmic reticulum (ER)-associated degradation (ERAD) by molecular chaperone

67 HCs) are targeted for endoplasmic reticulum (ER)-associated degradation (ERAD) by the ubiquitin E3 li

68 COX-2 is degraded via endoplasmic reticulum (ER)-associated degradation (ERAD) following post-transla

69 quality control, and endoplasmic reticulum (ER)-associated degradation (ERAD) in yeast and mammals.

70 Endoplasmic reticulum (ER)-associated degradation (ERAD) is an integral part of

71 Endoplasmic reticulum (ER)-associated degradation (ERAD) is required for ubiqui

72 Endoplasmic reticulum (ER)-associated degradation (ERAD) is responsible for the

73 Endoplasmic reticulum (ER)-associated degradation (ERAD) is the major quality c

74 surprising feature of endoplasmic reticulum (ER)-associated degradation (ERAD) is the movement, or re

75 UPR) is essential for endoplasmic reticulum (ER)-associated degradation (ERAD) of misfolded secretory

76 s responsible for the endoplasmic reticulum (ER)-associated degradation (ERAD) of numerous ER-residen

77 ubiquitin-dependent, endoplasmic reticulum (ER)-associated degradation (ERAD) of numerous lumenal (E

78 Accelerated endoplasmic reticulum (ER)-associated degradation (ERAD) of the cholesterol bio

79 The endoplasmic reticulum (ER)-associated degradation (ERAD) pathway in the yeast S

80 d and targeted to the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway when it fails

81 proteins through the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway.

82 sion by hijacking the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway.

83 and components of the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway.

84 sion by hijacking the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway.

85 , to a lesser extent, endoplasmic reticulum (ER)-associated degradation (ERAD) pathways are required

86 We demonstrate that endoplasmic reticulum (ER)-associated degradation (ERAD) prevents native foldin

87 gradation (UPD) in an endoplasmic reticulum (ER)-associated degradation (ERAD) process.

88 misfolded proteins by endoplasmic reticulum (ER)-associated degradation (ERAD) requires concerted act

89 oes sterol-dependent, endoplasmic-reticulum (ER)-associated degradation (ERAD) that is mediated by IN

90 al component of yeast endoplasmic reticulum (ER)-associated degradation (ERAD) ubiquitin ligase (E3)

91 nnel proteins undergo endoplasmic reticulum (ER)-associated degradation (ERAD) via the ubiquitin-prot

92 rotein maturation and endoplasmic reticulum (ER)-associated degradation (ERAD), a quality control pat

93 During endoplasmic reticulum (ER)-associated degradation (ERAD), a relatively small nu

94 rocessed and prone to endoplasmic reticulum (ER)-associated degradation (ERAD), although the mechanis

95 activities, including endoplasmic reticulum (ER)-associated degradation (ERAD), ER/Golgi membrane dyn

96 which is required for endoplasmic reticulum (ER)-associated degradation (ERAD).

97 and drastic defect in endoplasmic reticulum (ER)-associated degradation (ERAD).

98 This occurs through endoplasmic reticulum (ER)-associated degradation (ERAD).

99 mponents required for endoplasmic reticulum (ER)-associated degradation (ERAD).

100 d targeting of CD4 to endoplasmic reticulum (ER)-associated degradation (ERAD).

101 his process is termed endoplasmic-reticulum (ER)-associated degradation (ERAD).

102 When tightly controlled, autophagy-dependent ER-associated degradation (ERAD(II)) allows the cell to

103 nRHR), a G protein-coupled receptor, between ER-associated degradation (ERAD) and an ERQC autophagy p

104 y destabilized TTR variants are subjected to ER-associated degradation (ERAD) and then only in certai

105 Cue1p) and E3 (Doa10p) machinery involved in ER-associated degradation (ERAD) are also responsible fo

106 membrane-bound E3 ubiquitin ligases promote ER-associated degradation (ERAD) by ubiquitinating a ret

107 or proteins that interact with SelK revealed ER-associated degradation (ERAD) components (p97 ATPase,

108 of Sre1 in the absence of Scp1 requires the ER-associated degradation (ERAD) components Ubc7, an E2

109 Quality control pathways such as ER-associated degradation (ERAD) employ a small number o

110 this issue of Immunity, demonstrate that the ER-associated degradation (ERAD) export pathway operates

111 e primary ubiquitin ligases that function in ER-associated degradation (ERAD) in yeast, target distin

112 Akey step in ER-associated degradation (ERAD) is dislocation of the s

113 ER-associated degradation (ERAD) is essential for protei

114 f the JCI, Shi et al. report that Sel1L-Hrd1 ER-associated degradation (ERAD) is responsible for the

115 E3 ubiquitin ligase and its participation in ER-associated degradation (ERAD) lost their ability to d

116 How the ER-associated degradation (ERAD) machinery accurately id

117 To investigate how the ER-associated Degradation (ERAD) machinery can accomplis

118 lytic CTA1 subunit hijacks components of the ER-associated degradation (ERAD) machinery to retrotrans

119 is thought to provide antigen access to the ER-associated degradation (ERAD) machinery, allowing cyt

120 and pCatD association with components of the ER-associated degradation (ERAD) machinery.

121 athepsin D, and vIL-6 with components of the ER-associated degradation (ERAD) machinery.

122 ld or assemble correctly, ultimately undergo ER-associated degradation (ERAD) mediated by the ubiquit

123 e endoplasmic reticulum (ER) and involved in ER-associated degradation (ERAD) of diverse substrates.

124 ER-associated degradation (ERAD) of glycoproteins depend

125 ated ubiquitination is an obligatory step in ER-associated degradation (ERAD) of HMG CoA reductase, a

126 contributes to ER protein quality control by ER-associated degradation (ERAD) of misfolded proteins t

127 in transport, oxidative protein folding, and ER-associated degradation (ERAD) of misfolded proteins,

128 doplasmic reticulum (ER) stress by promoting ER-associated degradation (ERAD) of misfolded proteins.

129 ated by ER stress and has been implicated in ER-associated degradation (ERAD) of multiple unfolded se

130 the endoplasmic reticulum (ER) lumen and in ER-associated degradation (ERAD) of proteins by cytosoli

131 UBIAD1 binding inhibits sterol-accelerated, ER-associated degradation (ERAD) of reductase, one of se

132 ocation, secretion, retro-translocation, and ER-associated degradation (ERAD) of secretory pathway pr

133 lize the protein's native folding leading to ER-associated degradation (ERAD) of the misfolded enzyme

134 We now show that the ER-associated degradation (ERAD) of two mutant proteins

135 Because proteasome inhibitors also blocked ER-associated degradation (ERAD) of unassembled AChR sub

136 otein biosynthesis requires ER-retention and ER-associated degradation (ERAD) of unassembled/misfolde

137 dicate an as yet undiscovered feature of the ER-associated degradation (ERAD) pathway and explain the

138 Most substrates of this ER-associated degradation (ERAD) pathway are constitutiv

139 um (ER) proteins that are substrates for the ER-associated degradation (ERAD) pathway are recognized

140 while functional disruption of the conserved ER-associated degradation (ERAD) pathway ATPase VCP/p97

141 In this study, we elucidated the role of the ER-associated degradation (ERAD) pathway during BKPyV in

142 Under stress, the ER-associated degradation (ERAD) pathway for misfolded p

143 The ER-associated degradation (ERAD) pathway involves the re

144 However, inhibition of the ER-associated degradation (ERAD) pathway using a proteos

145 the known yeast and animal regulators of the ER-associated degradation (ERAD) pathway, a process that

146 ticulum (ER) and subsequently cleared by the ER-associated degradation (ERAD) pathway.

147 ition of its degradation, independent of the ER-associated degradation (ERAD) pathway.

148 from the endoplasmic reticulum (ER) via the ER-associated degradation (ERAD) pathway.

149 , upon activation, become substrates for the ER-associated degradation (ERAD) pathway.

150 ll receptor, an established substrate of the ER-associated degradation (ERAD) pathway.

151 one, CMV gH and gL were degraded through the ER-associated degradation (ERAD) pathway.

152 ded molecules are sorted for disposal by the ER-associated degradation (ERAD) pathway.

153 o the cytosol is hypothesized to involve the ER-associated degradation (ERAD) pathway.

154 cytosol, possibly through the action of the ER-associated degradation (ERAD) pathway.

155 In ER-associated degradation (ERAD) pathways, Bag6 can inte

156 ependent proteasomal degradation (UPD) in an ER-associated degradation (ERAD) process.

157 ER-associated degradation (ERAD) removes defective and m

158 ER-associated degradation (ERAD) rids the early secretor

159 inal mannose unit to initiate a glycan-based ER-associated degradation (ERAD) signal.

160 For most ER-associated degradation (ERAD) substrates, ubiquitylat

161 associates with a number of ER proteins and ER-associated degradation (ERAD) substrates; however, an

162 proteasome-mediated degradation through the ER-associated degradation (ERAD) system.

163 subjecting them to glycosylation arrest and ER-associated degradation (ERAD) through the ubiquitin p

164 We found that promotion of ER-associated degradation (ERAD) through upregulation of

165 is unclear, but previous studies implicated ER-associated degradation (ERAD), a pathway that retrotr

166 c reticulum (ER) is traditionally handled by ER-associated degradation (ERAD), a process that require

167 ined in the ER and targeted for clearance by ER-associated degradation (ERAD), a sophisticated proces

168 central component of ER quality control and ER-associated degradation (ERAD), acts as a timer enzyme

169 We investigated over synthesis, lack of ER-associated degradation (ERAD), and defects in ER to G

170 ions are defective, including translocation, ER-associated degradation (ERAD), and ER-to-Golgi transp

171 event involves the quality control system of ER-associated degradation (ERAD), but the molecular deta

172 Unassembled and misfolded subunits undergo ER-associated degradation (ERAD), but this degradation p

173 tinct complexes can play unique roles during ER-associated degradation (ERAD), establishes a role for

174 ed genes encoding chaperones and elements of ER-associated degradation (ERAD), including EDEM1.

175 d associated proteins that are essential for ER-associated degradation (ERAD), including valosin-cont

176 E3 ubiquitin ligases, which are involved in ER-associated degradation (ERAD), lead to the decrease o

177 In this process, collectively termed ER-associated degradation (ERAD), misfolded proteins are

178 f the C-terminal fragment is followed by its ER-associated degradation (ERAD), providing the first ex

179 Consistent with its role in ER-associated degradation (ERAD), synthetic interactions

180 in the cytosol, a process that is similar to ER-associated degradation (ERAD), the pathway used for d

181 quitin-conjugating enzyme (E2) implicated in ER-associated degradation (ERAD), through a region disti

182 NPL4 and UBC7, which are major components of ER-associated degradation (ERAD), we furthermore were ab

183 bly are often disposed of by a process named ER-associated degradation (ERAD), which involves transpo

184 um (ER) are eliminated by a process known as ER-associated degradation (ERAD), which starts with misf

185 ) membrane and is involved in the process of ER-associated degradation (ERAD).

186 targets misfolded N-linked glycoproteins for ER-associated degradation (ERAD).

187 ries of pathways collectively referred to as ER-associated degradation (ERAD).

188 the retrotranslocation complex and promotes ER-associated degradation (ERAD).

189 l percentage of each subunit is targeted for ER-associated degradation (ERAD).

190 by exploiting the quality control system of ER-associated degradation (ERAD).

191 sms target terminally misfolded proteins for ER-associated degradation (ERAD).

192 tion of terminally misfolded ER proteins via ER-associated degradation (ERAD).

193 activated ER stress response but incomplete ER-associated degradation (ERAD).

194 by exploiting the quality control system of ER-associated degradation (ERAD).

195 into the cytosol using a pathway related to ER-associated degradation (ERAD).

196 or "retrotranslocated" into the cytosol for ER-associated degradation (ERAD).

197 easome, indicating that they are cleared via ER-associated degradation (ERAD).

198 the ER and the quality control mechanism of ER-associated degradation (ERAD).

199 nuclear envelope (NE), where it functions in ER-associated degradation (ERAD).

200 doplasmic reticulum (ER) and are degraded by ER-associated degradation (ERAD).

201 at involves the quality control mechanism of ER-associated degradation (ERAD).

202 sol through the quality control mechanism of ER-associated degradation (ERAD).

203 plasm and degraded by the 26S proteasome via ER-associated degradation (ERAD).

204 raded by the proteasome via a pathway called ER-associated degradation (ERAD).

205 to the cell surface and targeted instead for ER-associated degradation (ERAD).

206 o ubiquitin-dependent proteolysis, including ER-associated degradation (ERAD).

207 ic reticulum (ER) proteins are eliminated by ER-associated degradation (ERAD).

208 ature-sensitive mutant, hrd4-1, deficient in ER-associated degradation (ERAD).

209 eticulum (ER) via a conserved process termed ER-associated degradation (ERAD).

210 lded polypeptides across the ER membrane for ER-associated degradation (ERAD).

211 ins are retained and eventually selected for ER-associated degradation (ERAD).

212 amplified 9 (OS-9), a component involved in ER-associated degradation (ERAD).

213 oplasm for ubiquitination and elimination by ER-associated degradation (ERAD).

214 eins and directs them either to ER export or ER-associated degradation (ERAD).

215 d that mutant Akita proinsulin is triaged by ER-associated degradation (ERAD).

216 osol, a series of events collectively termed ER-associated degradation (ERAD).

217 es into the cytosol for proteasome-mediated, ER-associated degradation (ERAD).

218 -proteasome pathway through a process called ER-associated degradation (ERAD).

219 percentage of the channel being targeted for ER-associated degradation (ERAD).

220 in- and proteasome-mediated process known as ER-associated degradation (ERAD).

221 ion of HMG-CoA reductase and Insig-1 through ER-associated degradation (ERAD).

222 oplasmic reticulum (ER) in a process termed "ER-associated degradation" (ERAD).

223 In contrast to UPS-mediated, ER-associated degradation, few components involved in pQ

224 directly comparing the HRD dependency of the ER-associated degradation for various ER membrane protei

225 icroarray screens for genes involved in SP-C ER-associated degradation identified MKS3/TMEM67, a locu

226 ate endoplasmic reticulum (ER) chaperones or ER-associated degradation in response to DTT-mediated ER

227 We have identified a new pathway of ER-associated degradation in Saccharomyces cerevisiae th

228 ary ubiquitin ligases (E3s) participating in ER-associated degradation in Saccharomyces cerevisiae.

229 teins from the endoplasmic reticulum (ER) by ER-associated degradation involves substrate retrotransl

230 ER-associated degradation is a normal process by which m

231 One polytopic ER protein subjected to ER-associated degradation is Insig-1, a negative regulat

232 d, based on several experimental approaches, ER-associated degradation is not involved.

233 iquitinating enzyme previously implicated in ER-associated degradation, is among those affected.

234 and p97-dependent degradation, indicating an ER-associated degradation-like mechanism of calnexin tur

235 otein US2 hijacks the endoplasmic reticulum (ER)-associated degradation machinery to dispose of MHC c

236 by ligating cellular endoplasmic reticulum (ER)-associated degradation machinery.

237 The ER-associated degradation machinery compensated for dist

238 Through ER-associated degradation, misfolded substrates are targ

239 of Vpu can cause the endoplasmic reticulum (ER)-associated degradation of BST-2, we found no evidenc

240 etrotranslocation and endoplasmic reticulum (ER)-associated degradation of misfolded proteins in yeas

241 rather from enhanced endoplasmic reticulum (ER)-associated degradation of the nascent protein.

242 ER-associated degradation of a lumenal substrate, CPY*,

243 in partial ER retention of APP and enhanced ER-associated degradation of APP by the proteasome, with

244 iculum (ER) membrane where it contributes to ER-associated degradation of APP together with the prote

245 ndent cell toxicity by selectively promoting ER-associated degradation of ATZ and is thereby a potent

246 Thus ER-associated degradation of CFTR occurs via a membrane-

247 omal protein cathepsin D by promotion of the ER-associated degradation of ER-transiting, preproteolyt

248 bility that this E3 might be involved in the ER-associated degradation of nascent apoB.

249 eta subunits can independently contribute to ER-associated degradation of the cystic fibrosis transme

250 ed the relationship between biosynthesis and ER-associated degradation of the cystic fibrosis transme

251 to reductase leads to the ubiquitination and ER-associated degradation of the enzyme, thereby slowing

252 uctase, thus inducing the ubiquitination and ER-associated degradation of the enzyme.

253 al protein translocation, as well as for the ER-associated degradation of two substrates.

254 d-type Pma1, resulting in ubiquitylation and ER-associated degradation of wild-type Pma1.

255 by components of the endoplasmic reticulum (ER)-associated degradation pathway.

256 ulum (ER) are identified and degraded by the ER-associated degradation pathway (ERAD), a component of

257 proteins are misfolded and eliminated by the ER-associated degradation pathway (ERAD), which involves

258 radation required specific components of the ER-associated degradation pathway including the Cdc48 ad

259 ively targeted for removal by a well-studied ER-associated degradation pathway, or ERAD.

260 1 gene, which encodes a key component of the ER-associated degradation pathway, suggesting an alterna

261 nteracts with the cellular components of the ER-associated degradation pathway, we constructed chimer

262 tu1 interacts with Cdc48, a regulator of the ER-associated degradation pathway.

263 doplasmic reticulum (ER) are degraded by the ER-associated degradation pathway.

264 , gp78, is a bona fide E3 ligase in the apoB ER-associated degradation pathway.

265 state did not delay their degradation by the ER-associated degradation pathway.

266 models, ATZ was disposed of by autophagy and ER-associated degradation pathways.

267 Like other substrates for ER-associated degradation, Pma1-D378N is stabilized in m

268 C onto BiP promoting interactions with other ER-associated degradation proteins.

269 chaperones, vesicle transport proteins, and ER-associated degradation proteins.

270 ng, Grp94 was proposed to participate in the ER-associated degradation quality control pathway by int

271 Therefore, nascent apoB is subject to ER-associated degradation, re-uptake, and a third distin

272 n, active Smoothened mutants are targeted by ER-associated degradation, resulting in attenuation of i

273 ress, accumulation of endoplasmic reticulum (ER)-associated degradation substrates, and ER stress.

274 Grp94 triages mutant myocilin through ER-associated degradation, subverting autophagy.

275 tein regulated by the endoplasmic reticulum (ER)-associated degradation system and subcellular locali

276 activity of the CGalT enzyme via a distinct ER-associated degradation system involving Insig.

277 ssette is to mediate entry of COX-2 into the ER-associated degradation system that transports ER prot

278 Genes related to the ER-associated degradation system were not among high-ran

279 In a cell-free reconstituted ER-associated degradation system, P269A CHIP inhibited H

280 that can block entry of ER proteins into the ER-associated degradation system, retards COX-2 degradat

281 the dynamics of Insig in the lipid-activated ER-associated degradation system.

282 ounterpart, undergoes endoplasmic reticulum (ER)-associated degradation that is subject to feedback c

283 ir destabilization by endoplasmic reticulum (ER)-associated degradation; this mechanism has been cons

284 nteraction with Jem1p, an Hsp40 required for ER-associated degradation, was unaffected.