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1 al mutants are recognized for destruction by endoplasmic reticulum-associated degradation.
2 lls and provide new mechanistic insight into endoplasmic reticulum-associated degradation.
3 ed NPC1 proteins, enabling their escape from endoplasmic reticulum-associated degradation.
4 nase ataxin3, which collaborates with p97 in endoplasmic reticulum-associated degradation.
5 TAP and engages the cullin-RING E3 ligase in endoplasmic reticulum-associated degradation.
6 nf145 in proteostasis of the Nox2 complex by endoplasmic reticulum-associated degradation.
7 ling the timing of CYP3A4 ubiquitination and endoplasmic reticulum-associated degradation.
8 sembles membrane E3 ligases that function in endoplasmic reticulum-associated degradation.
9 (Gp78) is a critical E3 ubiquitin ligase in endoplasmic reticulum-associated degradation.
10 by a chaperone-like function that minimizes endoplasmic reticulum-associated degradation.
11 3 ligase and membrane E3 ligases involved in endoplasmic reticulum-associated degradation.
12 gly, this secondary event occurs by cellular endoplasmic reticulum-associated degradation.
13 e biosynthetic pathway, likely by increasing endoplasmic reticulum-associated degradation.
14 gy to the Hrd1 E3 ligase complex involved in endoplasmic reticulum-associated degradation.
15 anscription, RNA processing, DNA damage, and endoplasmic reticulum-associated degradation.
16 CFTR alters the folding pathway resulting in endoplasmic-reticulum-associated degradation.
17 cell-cycle regulation, membrane fusion, and endoplasmic-reticulum-associated degradation, activates
18 st and mammals suggest a co-evolution of the endoplasmic reticulum-associated degradation and DNA rep
19 nding of multisubunit E3 ligases involved in endoplasmic reticulum-associated degradation and fungal
20 anslation, but before assembly, resulting in endoplasmic reticulum-associated degradation and membran
21 al cellular processes such as cell adhesion, endoplasmic reticulum-associated degradation and membran
23 es in different cellular pathways, including endoplasmic reticulum-associated degradation and transcr
25 the alpha1 subunit results in its excessive endoplasmic reticulum-associated degradation at the expe
26 biquitin-selective AAA chaperone involved in endoplasmic reticulum-associated degradation, autophagy
27 nt chaperone that plays an important role in endoplasmic reticulum-associated degradation but whose c
28 Doalpha10) and human TEB4, components of the endoplasmic reticulum-associated degradation C (ERAD-C)
29 t interfere with the entry of COX-2 into the endoplasmic reticulum-associated degradation cascade, it
30 ), plant responses to environmental signals (endoplasmic-reticulum-associated degradation, chloroplas
31 ation that shows architectural similarity to endoplasmic reticulum-associated degradation E3 ligases.
32 Inhibitors of endoplasmic reticulum-associated degradation (eeyarestat
33 st, NH2-terminal mutants escape detection by endoplasmic reticulum-associated degradation entirely, a
34 mutant protein had reduced stability due to endoplasmic reticulum associated degradation (ERAD) and
35 rapidly degraded via the proteasome-mediated endoplasmic reticulum associated degradation (ERAD) path
37 cilitate proteasomal degradation through the endoplasmic reticulum associated degradation (ERAD) syst
38 bc6 and MmUbc7, that have been implicated in endoplasmic reticulum-associated degradation (ERAD) and
42 at the mutant protein is likely targeted for endoplasmic reticulum-associated degradation (ERAD) due
45 , we report that protein quality control via endoplasmic reticulum-associated degradation (ERAD) gove
46 Studies of misfolded protein targeting to endoplasmic reticulum-associated degradation (ERAD) have
47 ked glycoproteins are selectively sorted for endoplasmic reticulum-associated degradation (ERAD) in r
60 se degradation 1 (SEL1L-HRD1) complex of the endoplasmic reticulum-associated degradation (ERAD) mach
61 ed proteins are sent for destruction via the endoplasmic reticulum-associated degradation (ERAD) mach
62 most common mutation, deltaF508, results in endoplasmic reticulum-associated degradation (ERAD) of C
64 son aimed to identify genes required for the endoplasmic reticulum-associated degradation (ERAD) of M
66 native conformation are degraded through the endoplasmic reticulum-associated degradation (ERAD) path
67 , a gene encoding a partner of Cdc48p in the endoplasmic reticulum-associated degradation (ERAD) path
68 otein (BiP) cochaperone and component of the endoplasmic reticulum-associated degradation (ERAD) path
69 teins to degradation pathways, including the endoplasmic reticulum-associated degradation (ERAD) path
70 hat this pathway may share similarity to the endoplasmic reticulum-associated degradation (ERAD) path
72 the TM domain during the natural process of endoplasmic reticulum-associated degradation (ERAD) simi
73 cells with AT3 increases cellular levels of endoplasmic reticulum-associated degradation (ERAD) subs
74 of poly-ubiquitinated proteins, retention of endoplasmic reticulum-associated degradation (ERAD) subs
76 lding- or assembly-defective proteins by the endoplasmic reticulum-associated degradation (ERAD) ubiq
77 e system (UPS) mediated protein degradation, endoplasmic reticulum-associated degradation (ERAD), and
78 degradation) pathway is a conserved route of endoplasmic reticulum-associated degradation (ERAD), by
79 l role in cellular homeostasis by regulating endoplasmic reticulum-associated degradation (ERAD), mit
80 factor mitofusin for degradation through an endoplasmic reticulum-associated degradation (ERAD)-like
81 7/VCP facilitates protein dislocation during endoplasmic reticulum-associated degradation (ERAD).
83 ify and eliminate misfolded proteins through endoplasmic reticulum-associated degradation (ERAD).
84 tion, reduced oxidative damage, and improved endoplasmic reticulum-associated degradation (ERAD).
85 causing mutants are subject to regulation by endoplasmic reticulum-associated degradation (ERAD).
86 membrane domain, was proposed to function in endoplasmic reticulum-associated degradation (ERAD).
87 ukaryotic cells possess a mechanism known as endoplasmic reticulum-associated degradation (ERAD).
88 ase degradation protein 1 (Hrd1) involved in endoplasmic reticulum-associated degradation (ERAD).
89 m, first we find that Kir2.1 is targeted for endoplasmic reticulum-associated degradation (ERAD).
90 in-dependent degradation by a process termed endoplasmic reticulum-associated degradation (ERAD).
93 rom impaired NCC biogenesis through enhanced endoplasmic reticulum-associated degradation (ERAD).
94 Here we report a new function for torsinA in endoplasmic reticulum-associated degradation (ERAD).
95 , a ubiquitin-conjugating enzyme involved in endoplasmic reticulum-associated degradation (ERAD).
96 ysine-11 polyubiquitination is important for endoplasmic reticulum-associated degradation (ERAD).
97 lation of multiple cell processes, including endoplasmic reticulum-associated degradation (ERAD).
98 e proteins are selected and destroyed during endoplasmic reticulum-associated degradation (ERAD).
100 -resident ubiquitin ligases (E3s) to promote endoplasmic reticulum-associated degradation (ERAD).
103 mixed ubiquitin (Ub) chains on substrates of endoplasmic-reticulum-associated degradation (ERAD).
104 ucidate the mechanisms by which glycoprotein endoplasmic reticulum-associated degradation (GERAD) is
106 mportant role of nonlysine ubiquitination in endoplasmic reticulum-associated degradation, immune sig
107 of LD proteome dynamics uncovered a role for endoplasmic reticulum-associated degradation in controll
108 specifically modulating HMGR stability, not endoplasmic reticulum-associated degradation in general.
109 lish that the p97-Ufd1-Npl4 complex mediates endoplasmic reticulum-associated degradation in mammalia
110 hat the CX50fs mutant is rapidly degraded by endoplasmic reticulum-associated degradation in mammalia
111 Notably, MG132 and EerI (proteasomal and endoplasmic reticulum-associated degradation inhibitors,
112 nhibited expression of key components of the endoplasmic reticulum-associated degradation machinery,
113 This effect was neither due to enhanced endoplasmic reticulum-associated degradation nor competi
114 eticulum, it does not become a substrate for endoplasmic reticulum-associated degradation nor does it
115 tabolic defect significantly compromises the endoplasmic reticulum-associated degradation of bri1-9 a
117 alpha1(A322D) expression results from rapid endoplasmic reticulum-associated degradation of the alph
118 ibiting VCP using Eeyarestatin I reduces the endoplasmic reticulum-associated degradation of the alph
119 cretion by ferritins leads to an increase in endoplasmic reticulum-associated degradation of the apol
120 t the plasma membrane possibly by preventing endoplasmic reticulum-associated degradation of the beta
122 mponents of this pathway are involved in the endoplasmic reticulum-associated degradation of the mamm
123 sterol-induced ubiquitination and subsequent endoplasmic reticulum-associated degradation of the rate
124 chaperone and proteasomal components of the endoplasmic reticulum associated degradation pathway in
125 radation of ubiquitin fusion degradation and endoplasmic reticulum-associated degradation pathway rep
127 itin conjugating (E2) enzyme involved in the endoplasmic reticulum-associated degradation pathway, wh
128 e receptors are then rapidly degraded by the endoplasmic reticulum-associated degradation pathway.
129 by the E3 ligase dorfin and degraded via the endoplasmic reticulum-associated degradation pathway.
130 from misfolded glycoproteins as part of the endoplasmic reticulum-associated degradation pathway.
131 nd other chaperones but did not activate the endoplasmic reticulum-associated degradation pathway.
132 gating enzyme, (mam)Ubc7, a component of the endoplasmic reticulum-associated degradation pathway.
133 ion is poorly understood but may involve the endoplasmic reticulum-associated degradation pathway.
134 hrough Xbp1 and downstream activation of the endoplasmic reticulum-associated degradation pathway.
135 calized protein degradation pathway, and the endoplasmic reticulum-associated degradation pathway.
136 E2 enzymes Ubc6 and Ubc7, components of the endoplasmic reticulum-associated degradation pathway.
137 ormer was being degraded, likely through the endoplasmic reticulum-associated degradation pathway.
138 mistargeted and appears to be degraded by an endoplasmic reticulum-associated degradation pathway.
139 V internalization, a post-entry role for the endoplasmic-reticulum-associated degradation pathway in
140 ilitates the degradation of NOX2 through the endoplasmic-reticulum-associated degradation pathway.
141 duction of the unfolded protein response and endoplasmic reticulum-associated degradation pathways ul
142 e endoplasmic reticulum and/or by exploiting endoplasmic-reticulum-associated degradation pathways.
143 s or from misfolded glycoproteins during the endoplasmic reticulum-associated degradation process and
144 oteins related to glutathione metabolism and endoplasmic reticulum-associated degradation process.
145 on pathway for rescue involving a network of endoplasmic reticulum-associated degradation proteins.
146 a greater percentage of the protein escaped endoplasmic-reticulum-associated degradation resulting i
147 pates in the retro-translocation of cellular endoplasmic reticulum-associated degradation substrates
148 hange in the binding of proteins involved in endoplasmic reticulum-associated degradation, such as Hs
149 ody, which was shown in past work to predict endoplasmic reticulum-associated degradation-targeting o
151 mbrane fusion, postmitotic Golgi reassembly, endoplasmic reticulum-associated degradation, ubiquitin-
152 ted whether human-IAPP (h-IAPP) disrupts the endoplasmic reticulum-associated degradation/ubiquitin/p
153 Unlike the classical function of Hrd1 in endoplasmic reticulum-associated degradation, Usp15 is n
155 he three ER stress pathways, the UPR and the endoplasmic reticulum-associated degradation were activa
156 he-27 precursors that were redirected to the endoplasmic reticulum-associated degradation were, howev
157 r fraction of Cx32 is degraded presumably by endoplasmic reticulum-associated degradation, whereas in