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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

15 RCH6), a key E3 ubiquitin ligase involved in ER-associated degradation.

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

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

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

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

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

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

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

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

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

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

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

27 ation precludes mutant myocilin clearance by ER-associated degradation.

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

29 ded C1163R C-Proalpha2(I) and targets it for ER-associated degradation.

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

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

32 UBR5 as ubiquitin E3 ligases involved in HC ER-associated degradation.

33 Thus, ACD6 constitutively undergoes ER-associated degradation.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

54 ER-associated degradation clears the secretory pathway o

55 e propose that the microcompartments perform ER-associated degradation, colocalizing the degradation

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

57 2 participates in recruiting p97 ATPase into ER-associated degradation complexes.

58 t include numerous ER protein chaperones and ER associated degradation components.

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

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

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

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

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

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

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

66 hereby inhibiting its endoplasmic reticulum (ER)-associated degradation (ERAD) (Schumacher et al. 201

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

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

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

70 cent studies on E3 of endoplasmic reticulum (ER)-associated degradation (ERAD) in plants have reveale

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

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

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

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

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

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

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 UBIAD1 also inhibits endoplasmic reticulum (ER)-associated degradation (ERAD) of ubiquitinated HMG C

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

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

82 uitin ligase-mediated endoplasmic reticulum (ER)-associated degradation (ERAD) pathway, a cellular pr

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

107 integrated unfold protein response (UPR) and ER-associated degradation (ERAD) are the primary ER qual

108 tegrated unfolded protein response (UPR) and ER-associated degradation (ERAD) are the primary mechani

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

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

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

112 We show that the ER-associated degradation (ERAD) E3 ubiquitin ligase Doa

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

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

115 and proceeds even more vigorously when these ER-associated degradation (ERAD) factors are crippled, s

116 he longevity effects, resulting in increased ER-associated degradation (ERAD) gene expression and deg

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

118 P450 proteolytic turnover occurs via ER-associated degradation (ERAD) involving ubiquitin (Ub

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

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

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

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

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

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

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

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

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

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

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

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

131 ER-associated degradation (ERAD) of glycoproteins depend

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

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

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

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

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

137 uctive replication, in part via promotion of ER-associated degradation (ERAD) of nascent pro-cathepsi

138 ll as an E3 ubiquitin-ligase involved in the ER-associated degradation (ERAD) of not only the tumor m

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

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

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

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

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

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

145 roteasome or to the lysosome/vacuole through ER-associated degradation (ERAD) or ER-phagy.

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

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

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

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

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

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

152 into the ER lumen and are recognized by the ER-associated degradation (ERAD) pathway for removal.

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

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

155 Blocking the ER-associated degradation (ERAD) pathway with a dominant

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

181 RIM25 ameliorates oxidative stress, promotes ER-associated degradation (ERAD), and reduces IRE1 signa

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

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

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

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

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

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

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

189 eotoxicity, i.e. abrogation of HRD1-mediated ER-associated degradation (ERAD), or of the UPR, in part

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

205 cytosol and destroyed by a process known as ER-associated degradation (ERAD).

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

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

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

209 d by the unfolded protein response (UPR) and ER-associated degradation (ERAD).

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

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

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

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

214 losin-containing protein), a major driver of ER-associated degradation (ERAD).

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

230 e endoplasmic reticulum (ER) are degraded by ER-associated degradation (ERAD).

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

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

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

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

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

236 endoplasmic reticulum (ER) proteins undergo ER-associated degradation (ERAD-L): They are retrotransl

237 abundance control by a regulatory branch of ER-associated degradation (ERAD-R) has a role in shaping

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

239 t manipulation of the ER quality control and ER-associated degradation factors to promote mutant prot

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

241 rincipal component of endoplasmic reticulum (ER)-associated degradation-governed NIS proteolysis.

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

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

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

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

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

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

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

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

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

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

252 The ER-associated degradation machinery compensated for dist

253 interface, from where it interacts with the ER-associated degradation machinery, which catalyzes its

254 Through ER-associated degradation, misfolded substrates are targ

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

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

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

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

259 ent protein retention in ER than D923N; more ER-associated degradation of alpha3 (ERAD); larger diffe

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

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

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

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

264 VKORC1v2-enhanced ER-associated degradation of IGF2R and vIL-6 promotion o

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

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

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

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

269 cytosol and targeted for destruction by the ER--associated degradation pathway (ERAD).

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

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

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

273 echanism by which HCMV infection exploits an ER-associated degradation pathway through US11 to disabl

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

275 tion, PINK1 interacts with components of the ER-associated degradation pathway, such as the E3 ligase

276 1 gene, which encodes a key component of the ER-associated degradation pathway, suggesting an alterna

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

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

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

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

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

282 e in the establishment of protein stress and ER associated degradation pathways in Eukarya.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

299 is study, we found that two TQC enzymes, the ER-associated degradation ubiquitin ligase Hrd1 and zinc

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