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1 lls and provide new mechanistic insight into endoplasmic reticulum-associated degradation.
2 nf145 in proteostasis of the Nox2 complex by endoplasmic reticulum-associated degradation.
3 nase ataxin3, which collaborates with p97 in endoplasmic reticulum-associated degradation.
4 ling the timing of CYP3A4 ubiquitination and endoplasmic reticulum-associated degradation.
5 sembles membrane E3 ligases that function in endoplasmic reticulum-associated degradation.
6 (Gp78) is a critical E3 ubiquitin ligase in endoplasmic reticulum-associated degradation.
7 by a chaperone-like function that minimizes endoplasmic reticulum-associated degradation.
8 3 ligase and membrane E3 ligases involved in endoplasmic reticulum-associated degradation.
9 gly, this secondary event occurs by cellular endoplasmic reticulum-associated degradation.
10 e biosynthetic pathway, likely by increasing endoplasmic reticulum-associated degradation.
11 gy to the Hrd1 E3 ligase complex involved in endoplasmic reticulum-associated degradation.
12 anscription, RNA processing, DNA damage, and endoplasmic reticulum-associated degradation.
13 al mutants are recognized for destruction by endoplasmic reticulum-associated degradation.
14 CFTR alters the folding pathway resulting in endoplasmic-reticulum-associated degradation.
15 cell-cycle regulation, membrane fusion, and endoplasmic-reticulum-associated degradation, activates
16 st and mammals suggest a co-evolution of the endoplasmic reticulum-associated degradation and DNA rep
17 nding of multisubunit E3 ligases involved in endoplasmic reticulum-associated degradation and fungal
18 anslation, but before assembly, resulting in endoplasmic reticulum-associated degradation and membran
19 es in different cellular pathways, including endoplasmic reticulum-associated degradation and transcr
21 the alpha1 subunit results in its excessive endoplasmic reticulum-associated degradation at the expe
22 biquitin-selective AAA chaperone involved in endoplasmic reticulum-associated degradation, autophagy
23 nt chaperone that plays an important role in endoplasmic reticulum-associated degradation but whose c
24 Doalpha10) and human TEB4, components of the endoplasmic reticulum-associated degradation C (ERAD-C)
25 t interfere with the entry of COX-2 into the endoplasmic reticulum-associated degradation cascade, it
26 ation that shows architectural similarity to endoplasmic reticulum-associated degradation E3 ligases.
27 st, NH2-terminal mutants escape detection by endoplasmic reticulum-associated degradation entirely, a
28 mutant protein had reduced stability due to endoplasmic reticulum associated degradation (ERAD) and
29 rapidly degraded via the proteasome-mediated endoplasmic reticulum associated degradation (ERAD) path
30 bc6 and MmUbc7, that have been implicated in endoplasmic reticulum-associated degradation (ERAD) and
33 at the mutant protein is likely targeted for endoplasmic reticulum-associated degradation (ERAD) due
36 Studies of misfolded protein targeting to endoplasmic reticulum-associated degradation (ERAD) have
43 ed proteins are sent for destruction via the endoplasmic reticulum-associated degradation (ERAD) mach
44 most common mutation, deltaF508, results in endoplasmic reticulum-associated degradation (ERAD) of C
45 son aimed to identify genes required for the endoplasmic reticulum-associated degradation (ERAD) of M
46 otein (BiP) cochaperone and component of the endoplasmic reticulum-associated degradation (ERAD) path
48 native conformation are degraded through the endoplasmic reticulum-associated degradation (ERAD) path
49 hat this pathway may share similarity to the endoplasmic reticulum-associated degradation (ERAD) path
50 the TM domain during the natural process of endoplasmic reticulum-associated degradation (ERAD) simi
51 cells with AT3 increases cellular levels of endoplasmic reticulum-associated degradation (ERAD) subs
52 of poly-ubiquitinated proteins, retention of endoplasmic reticulum-associated degradation (ERAD) subs
54 lding- or assembly-defective proteins by the endoplasmic reticulum-associated degradation (ERAD) ubiq
55 e system (UPS) mediated protein degradation, endoplasmic reticulum-associated degradation (ERAD), and
56 degradation) pathway is a conserved route of endoplasmic reticulum-associated degradation (ERAD), by
57 factor mitofusin for degradation through an endoplasmic reticulum-associated degradation (ERAD)-like
58 causing mutants are subject to regulation by endoplasmic reticulum-associated degradation (ERAD).
59 7/VCP facilitates protein dislocation during endoplasmic reticulum-associated degradation (ERAD).
61 ify and eliminate misfolded proteins through endoplasmic reticulum-associated degradation (ERAD).
62 membrane domain, was proposed to function in endoplasmic reticulum-associated degradation (ERAD).
63 ukaryotic cells possess a mechanism known as endoplasmic reticulum-associated degradation (ERAD).
64 ase degradation protein 1 (Hrd1) involved in endoplasmic reticulum-associated degradation (ERAD).
65 m, first we find that Kir2.1 is targeted for endoplasmic reticulum-associated degradation (ERAD).
66 in-dependent degradation by a process termed endoplasmic reticulum-associated degradation (ERAD).
69 rom impaired NCC biogenesis through enhanced endoplasmic reticulum-associated degradation (ERAD).
70 Here we report a new function for torsinA in endoplasmic reticulum-associated degradation (ERAD).
71 , a ubiquitin-conjugating enzyme involved in endoplasmic reticulum-associated degradation (ERAD).
72 ysine-11 polyubiquitination is important for endoplasmic reticulum-associated degradation (ERAD).
73 lation of multiple cell processes, including endoplasmic reticulum-associated degradation (ERAD).
74 e proteins are selected and destroyed during endoplasmic reticulum-associated degradation (ERAD).
76 -resident ubiquitin ligases (E3s) to promote endoplasmic reticulum-associated degradation (ERAD).
79 ucidate the mechanisms by which glycoprotein endoplasmic reticulum-associated degradation (GERAD) is
81 of LD proteome dynamics uncovered a role for endoplasmic reticulum-associated degradation in controll
82 specifically modulating HMGR stability, not endoplasmic reticulum-associated degradation in general.
83 lish that the p97-Ufd1-Npl4 complex mediates endoplasmic reticulum-associated degradation in mammalia
84 hat the CX50fs mutant is rapidly degraded by endoplasmic reticulum-associated degradation in mammalia
85 Notably, MG132 and EerI (proteasomal and endoplasmic reticulum-associated degradation inhibitors,
87 eticulum, it does not become a substrate for endoplasmic reticulum-associated degradation nor does it
88 tabolic defect significantly compromises the endoplasmic reticulum-associated degradation of bri1-9 a
90 ibiting VCP using Eeyarestatin I reduces the endoplasmic reticulum-associated degradation of the alph
91 alpha1(A322D) expression results from rapid endoplasmic reticulum-associated degradation of the alph
92 cretion by ferritins leads to an increase in endoplasmic reticulum-associated degradation of the apol
93 t the plasma membrane possibly by preventing endoplasmic reticulum-associated degradation of the beta
95 mponents of this pathway are involved in the endoplasmic reticulum-associated degradation of the mamm
96 sterol-induced ubiquitination and subsequent endoplasmic reticulum-associated degradation of the rate
97 chaperone and proteasomal components of the endoplasmic reticulum associated degradation pathway in
98 radation of ubiquitin fusion degradation and endoplasmic reticulum-associated degradation pathway rep
99 itin conjugating (E2) enzyme involved in the endoplasmic reticulum-associated degradation pathway, wh
100 nd other chaperones but did not activate the endoplasmic reticulum-associated degradation pathway.
101 gating enzyme, (mam)Ubc7, a component of the endoplasmic reticulum-associated degradation pathway.
102 ion is poorly understood but may involve the endoplasmic reticulum-associated degradation pathway.
103 calized protein degradation pathway, and the endoplasmic reticulum-associated degradation pathway.
104 E2 enzymes Ubc6 and Ubc7, components of the endoplasmic reticulum-associated degradation pathway.
105 hrough Xbp1 and downstream activation of the endoplasmic reticulum-associated degradation pathway.
106 ormer was being degraded, likely through the endoplasmic reticulum-associated degradation pathway.
107 mistargeted and appears to be degraded by an endoplasmic reticulum-associated degradation pathway.
108 by the E3 ligase dorfin and degraded via the endoplasmic reticulum-associated degradation pathway.
109 from misfolded glycoproteins as part of the endoplasmic reticulum-associated degradation pathway.
110 V internalization, a post-entry role for the endoplasmic-reticulum-associated degradation pathway in
111 ilitates the degradation of NOX2 through the endoplasmic-reticulum-associated degradation pathway.
112 duction of the unfolded protein response and endoplasmic reticulum-associated degradation pathways ul
113 e endoplasmic reticulum and/or by exploiting endoplasmic-reticulum-associated degradation pathways.
114 s or from misfolded glycoproteins during the endoplasmic reticulum-associated degradation process and
115 on pathway for rescue involving a network of endoplasmic reticulum-associated degradation proteins.
116 a greater percentage of the protein escaped endoplasmic-reticulum-associated degradation resulting i
117 pates in the retro-translocation of cellular endoplasmic reticulum-associated degradation substrates
118 hange in the binding of proteins involved in endoplasmic reticulum-associated degradation, such as Hs
120 mbrane fusion, postmitotic Golgi reassembly, endoplasmic reticulum-associated degradation, ubiquitin-
121 ted whether human-IAPP (h-IAPP) disrupts the endoplasmic reticulum-associated degradation/ubiquitin/p
123 he three ER stress pathways, the UPR and the endoplasmic reticulum-associated degradation were activa
124 he-27 precursors that were redirected to the endoplasmic reticulum-associated degradation were, howev
125 r fraction of Cx32 is degraded presumably by endoplasmic reticulum-associated degradation, whereas in
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