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1 in upon ubiquitin transfer to a substrate or ubiquitin chain.
2 adation by the 26S proteasome by attaching a ubiquitin chain.
3 hort-lived proteins that are labeled with an ubiquitin chain.
4 d that AMSH1 specifically cleaves K63-linked ubiquitin chains.
5 trameric, and longer Lys48- and Lys63-linked ubiquitin chains.
6 uitin chains but does not bind Lys-48-linked ubiquitin chains.
7 enzyme that removes Lys63- or linear-linked ubiquitin chains.
8 n 21 (TRIM21) and are positive for lysine-48 ubiquitin chains.
9 ppaB activation through its interaction with ubiquitin chains.
10 the E3 ligase HOIP, which synthesizes linear ubiquitin chains.
11 cleaves ubiquitinated proteins and releases ubiquitin chains.
12 In vitro, only JosD2 can cleave ubiquitin chains.
13 dification specifically by lysine(63)-linked ubiquitin chains.
14 low affinity receptor for long lysine-linked ubiquitin chains.
15 , controls NF-kappaB signaling by binding to ubiquitin chains.
16 ge complex consisting of four RIG-I and four ubiquitin chains.
17 h cells expressing NEMO that binds to linear ubiquitin chains.
18 domain of NEMO and linear (Met-1-linked) di-ubiquitin chains.
19 in intraneuronal inclusions often containing ubiquitin chains.
20 n (residues 120-133) and attaches K63-linked ubiquitin chains.
21 preference for proteins that carry multiple ubiquitin chains.
22 the U4 snRNP, with nonproteolytic K63-linked ubiquitin chains.
23 monoubiquitin, it can also be modified with ubiquitin chains.
24 DAT is mainly conjugated with Lys(63)-linked ubiquitin chains.
25 ghly adaptive and cooperative toward binding ubiquitin chains.
26 of the canonical proteolytic signal, Lys-48 ubiquitin chains.
27 lysine 48 (K48)- and lysine 63 (K63)-linked ubiquitin chains.
28 N-terminal alpha-amino group to build linear ubiquitin chains.
29 n types of homotypic chains as well as mixed ubiquitin chains.
30 quitin ligase (Ufd4p), resulting in branched ubiquitin chains.
31 ivated Uch37 cannot disassemble hRpn13-bound ubiquitin chains.
32 targets Ku80 that is modified by K48-linked ubiquitin chains.
33 inding activates CYLD-mediated hydrolysis of ubiquitin chains.
34 age toward the distal isopeptide bond in tri-ubiquitin chains.
35 ed to the formation of an array of polymeric ubiquitin chains.
36 protein degradation-associated Lys-48-linked ubiquitin-chains.
38 , in the presence of STAM, the length of the ubiquitin chains affects the apparent cleavage rate.
39 y an E2 enzyme, UBE2S/E2-EPF, that elongates ubiquitin chains after the substrates are pre-ubiquitina
42 tion of ubiquitin aldehyde, which mimics the ubiquitin chain and binds to 26 S-associated deubiquitin
43 n monomers or attachment of a preformed poly-ubiquitin chain and requiring either a single pair of ub
44 tions as a high affinity receptor for linear ubiquitin chains and a low affinity receptor for long ly
45 ld complex sequentially cleaved Lys63-linked ubiquitin chains and catalyzed Lys48-linked ubiquitinati
46 he conformational ensembles of the above tri-ubiquitin chains and chains possessing the same linkages
48 s an E3 ligase complex that generates linear ubiquitin chains and is important for tumour necrosis fa
49 in Lewy bodies is largely due to K63-linked ubiquitin chains and markedly reduced in the substantia
51 nd substrates for modification with branched ubiquitin chains and points to an important role of thes
52 less is understood about the other types of ubiquitin chains and proteasome-independent functions.
53 ex), which catalyzes the formation of linear ubiquitin chains and regulates immune and apoptopic sign
54 atalyzed the formation of Lys63 (K63)-linked ubiquitin chains and stimulated the transcription factor
55 quitin homeostasis with accumulation of free ubiquitin chains and ubiquitinated substrates in the leo
56 ative conjugation signals (monoubiquitin and ubiquitin chains) and interactions with ubiquitin-bindin
57 onoubiquitin and Lys(48)- and Lys(63)-linked ubiquitin chains), and that wild-type and mutant RNF170
64 with OPTN and the ability of OPTN to bind to ubiquitin chains are essential for TBK1 recruitment and
67 ably, the attached Lys-48- and Lys-63-linked ubiquitin chains are homogeneous and are segregated to s
69 a cells determines that the levels of Lys-63 ubiquitin chains are insensitive to short-time proteasom
72 hains to tankyrase 1, while in G1 phase such ubiquitin chains are removed by BRISC, an ABRO1/BRCC36-c
74 1 is therefore important to ensure that poly-ubiquitin chains are removed only from committed substra
76 ults underscore the importance of K11-linked ubiquitin chains as critical regulators of mitotic prote
77 nzyme (DUB) that hydrolyzes lysine-63-linked ubiquitin chains as part of distinct macromolecular comp
80 inked multi-monoubiquitination on K29-linked ubiquitin chains assembled by the ubiquitin ligase (Ufd4
83 modulate the interaction between the linear ubiquitin chain assembly complex (LUBAC) and the deubiqu
84 1, MALT1, and the HOIP subunit of the linear ubiquitin chain assembly complex (LUBAC) but not the HOI
86 w a catalytic-independent role of the linear ubiquitin chain assembly complex (LUBAC) in lymphocyte a
89 linked polyubiquitin (Met1-Ub) by the linear ubiquitin chain assembly complex (LUBAC) is an important
94 PIN (Sharpin(cpdm) mice), a member of linear ubiquitin chain assembly complex (LUBAC), develop severe
96 These chains are generated by the linear ubiquitin chain assembly complex (LUBAC), the only known
97 ng HOIL-1 and HOIP, components of the linear ubiquitin chain assembly complex (LUBAC), which has a pi
99 deficient in K63 ubiquitin chains or linear ubiquitin chain assembly complex (LUBAC)-mediated linear
102 urther reveal that cFLIPLrequires the linear ubiquitin chain assembly complex and the kinase TAK1 for
105 is the catalytic component of LUBAC (linear ubiquitin chain assembly complex), a multisubunit E3 lig
106 biquitin ligase complex called LUBAC (linear ubiquitin chain assembly complex), which catalyzes the f
108 s showed that HOIL-1, a member of the linear ubiquitin chain assembly complex, contributes to activat
110 nder native conditions to date is the linear ubiquitin chain assembly complex, of which the catalytic
111 y SHARPIN as a third component of the linear ubiquitin chain assembly complex, recruited to the CD40
112 protein Sharpin is a component of the linear ubiquitin chain assembly complex, which regulates NF-kap
116 inus of the proximal Ub, which allows, after ubiquitin chain assembly, the introduction of various re
117 ons point out that two parameters accelerate ubiquitin chain assembly: the increasing number of CUE b
118 g protein), a component of the LUBAC (linear ubiquitin chain-assembly complex), regulates inflammatio
122 36 regulates the abundance of Lys(63)-linked ubiquitin chains at chromatin and that one of its substr
124 nstrate the facile conjugation to K48-linked ubiquitin chains, bearing up to four ubiquitins, through
126 nt phosphorylation on S473 and S513 promotes ubiquitin chain binding in vitro as well as TBK1 activat
130 at spartin, via the UBR, binds Lys-63-linked ubiquitin chains but does not bind Lys-48-linked ubiquit
131 d that its C-terminal UBA domain can bind to ubiquitin chains but that the Dsc2 UBA domain is not ess
132 bute equally to the high-affinity binding of ubiquitin chains, but in their absence, ubiquitin conjug
133 separate IP(3)R subunits, and Lys-48-linked ubiquitin chains, but not Lys-63-linked chains, are requ
134 y targeting protein-protein interactions, or ubiquitin chains, but the details of the inhibition mech
135 me E1 by PYR-41 or blocking the formation of ubiquitin chains by over-expressing the lysine to argini
137 ent of U4 snRNP, is modified with K63-linked ubiquitin chains by the PRP19 complex and deubiquitinate
138 ignal than shorter chains, and (3) the tetra-ubiquitin chain can be degraded with the substrate.
140 uitin to substrates modified with K29-linked ubiquitin chains, can the substrates be escorted to the
141 nd that, although the kcat of Lys(63)-linked ubiquitin chain cleavage was comparable for di- and tri-
143 et al. describe how viral RNA and unanchored ubiquitin chains conspire to promote activation of RIG-I
144 main of STAM and required that the substrate ubiquitin chain contain homogenous Lys(63)-linkages.
145 We investigated this idea by engineering di-ubiquitin chains containing differential proximal and di
146 on is a posttranslational modification where ubiquitin chains containing isopeptide bonds linking one
148 cificities of these proteins for K48- or K63-ubiquitin chains determine whether a ubiquitinated prote
152 In eukaryotes, the covalent attachment of ubiquitin chains directs substrates to the proteasome fo
153 ond UBL-binding site ( T2: ) that assists in ubiquitin chain disassembly, by binding the UBL of deubi
157 he generation of K29 chains in vitro using a ubiquitin chain-editing complex consisting of the HECT E
158 r, APC engages and activates its specialized ubiquitin chain-elongating E2 UBE2S in ways that differ
161 ng of the UEV domain to Rim8 interferes with ubiquitin chain elongation and directs Rim8 monoubiquiti
162 E4 enzymes that are specifically involved in ubiquitin chain elongation but whose roles in proteolysi
163 Ubiquitination of a subset of proteins by ubiquitin chain elongation factors (E4), represented by
164 by multiple LUBAC components, whereas linear ubiquitin chain elongation is realized by a specific int
167 he canonical function of Poh1, which removes ubiquitin chains en bloc from proteasomal substrates pri
169 ically, beta-catenin modified with lysine-11 ubiquitin chain extension efficiently activates a lympho
170 NCL ubiquitinates beta-catenin with atypical ubiquitin chain extension known to have nonproteolytic f
175 Our data also confirm that Vif could induce ubiquitin chain formation on lysine residues intersperse
176 t compounds as inhibitors of the proteasome, ubiquitin chain formation or perception, CRL activity, o
177 that monomeric E2s promote linkage-specific ubiquitin chain formation through substrate-assisted cat
178 stabilises RACO-1 by facilitating K63-linked ubiquitin chain formation, and enables RACO-1 dimerisati
179 t1 (CBM) complex and removes the TCR-induced ubiquitin chain from Bcl10, which facilitates the associ
180 ly of enzymes cleaves mono-ubiquitin or poly-ubiquitin chains from a target protein through different
181 ysis provides evidence that CYLD removes K48 ubiquitin chains from p53 indirectly by cleaving K63 lin
182 eferentially removes non-canonical K6-linked ubiquitin chains from parkin, a process required for the
184 USP38 specifically cleaves K33-linked poly-ubiquitin chains from TBK1 at Lys670, and it allows for
185 (DUBA), which selectively cleaves K63-linked ubiquitin chains from TRAF3, was up-regulated in the abs
189 e USP2 enzyme, which was found to cleave the ubiquitin chain in a similar manner to unanchored ones.
191 l-length NEMO binds preferentially to linear ubiquitin chains in competition with lysine-linked ubiqu
193 Quantitative mass spectrometric analysis of ubiquitin chains in HeLa cells determines that the level
195 but interfacing barriers to promote loss of ubiquitin chains in the IRIF core, which is required for
197 inhibits its ability to serve as a donor for ubiquitin chain initiation or elongation, but can be res
198 have been reported for the assembly of poly-ubiquitin chains, involving either stepwise transfer of
199 AK1 to TNFR1, suggesting that the K63-linked ubiquitin chain is not capable of recruiting IKK in vivo
202 l modification of cell-cycle regulators with ubiquitin chains is essential for eukaryotic cell divisi
203 known about how the progressive assembly of ubiquitin chains is managed by the responsible enzymes.
207 nd non-covalent interactions with K63-linked ubiquitin chains (K63-Ubn) were shown to occur in its si
208 rticular route of degradation likely include ubiquitin chain length and linkage type, which may favor
210 y)ubiquitin and found that, depending on the ubiquitin chain length, the orientation of the resulting
211 ing in the recruitment of IKK and the linear ubiquitin chain ligase LUBAC, which is essential for IKK
213 qualitative method that yields insights into ubiquitin chain linkage types and architecture within ho
214 ts suggest that Ufd2p functions by switching ubiquitin chain linkages to allow the degradation of pro
215 review recent studies of ubiquitin ligases, ubiquitin chain linkages, and ubiquitin binding proteins
216 RNAPII, an Elc1/Cul3 complex then produces a ubiquitin chain linked via lysine 48, which can trigger
219 ative ubiquitin chains such as linear or K11 ubiquitin chains may also play a role in certain pathway
220 ineered to bind exclusively to Lys-63-linked ubiquitin chains mediated partial NF-kappaB activation c
221 e Keap1 was polyubiquitinated with lysine-63-ubiquitin chains, modifications known to increase their
222 This study suggests that USP14 removes the ubiquitin chain of I-kappaB, therefore inducing I-kappaB
225 tin chains in competition with lysine-linked ubiquitin chains of defined length, including long Lys-6
227 oreover, OTUD1 cleaves Lysine 33-linked poly-ubiquitin chains of SMAD7 Lysine 220, which exposes the
231 strongly suggest that removal of K63-linked ubiquitin chains on alpha-synuclein by Usp8 is a critica
232 Ls activate the RBR enzyme ARIH1 to initiate ubiquitin chains on CRL substrates, thereby marking an u
233 ause its recruitment signal, K63-linked poly-ubiquitin chains on histones, is actively destroyed by t
235 through noncovalent interactions between the ubiquitin chains on Mdm2 and the ubiquitin binding domai
236 adaptor phosphorylation with the assembly of ubiquitin chains on mitochondria to facilitate efficient
238 te the ubiquitin ligase parkin, which builds ubiquitin chains on mitochondrial outer membrane protein
242 ese structures, using cells deficient in K63 ubiquitin chains or linear ubiquitin chain assembly comp
243 ytic ubiquitin signaling mediated by Lys(63) ubiquitin chains plays a critical role in multiple pathw
247 resses 26S proteasome remodeling, unanchored ubiquitin chain production, and aggresome clearance.
252 of the proteasome can be regulated by rapid ubiquitin chain removal, which resolves substrates based
256 the dynamic appendage of different types of ubiquitin chains represents a versatile, three-dimension
259 We also show that, in the presence of K63 ubiquitin chains, RIG-I catalyzes the conversion of MAVS
261 cent research suggests that some alternative ubiquitin chains such as linear or K11 ubiquitin chains
262 host-derived glycans and K48- and K63-linked ubiquitin chains, suffices to restrict bacterial prolife
263 ential modifier efficiently binds K11-linked ubiquitin chains, suggesting that this ubiquitin linkage
264 l degradation, the presence of Lys-63-linked ubiquitin chains suggests that ubiquitination of IP(3)Rs
265 Proteins to be degraded are conjugated to ubiquitin chains that act as recognition signals for the
266 degradation by the 26 S proteasome using the ubiquitin chains that mark most substrates for degradati
267 partners, in addition to removing K63-linked ubiquitin chains that serve as a docking platform for do
268 ubiquitin ligases responsible for catalysing ubiquitin chains that surround intracellular bacteria ar
269 mitotic regulators by assembling K11-linked ubiquitin chains, the formation of which is initiated by
270 ant interacted with Vif and were modified by ubiquitin chains, the latter remained more resistant to
271 gulates I-kappaB degradation by removing its ubiquitin chain, thus promoting the deubiquitinated I-ka
272 new chemical approaches to covalently attach ubiquitin chains to a protein substrate through its Cys
274 ulatively involved both direct attachment of ubiquitin chains to DMalpha and a functional tyrosine-ba
276 ike TNF, IL-1 requires K63-linked and linear ubiquitin chains to recruit NEMO into higher-order compl
277 ponsive E3 ligase RNF8 conjugates K63-linked ubiquitin chains to tankyrase 1, while in G1 phase such
278 ligase-1 (HOIL-1L) and conjugate K48-linked ubiquitin chains to the catalytic RING-between-RING doma
280 DUBs present specificity toward different ubiquitin chain topologies and are crucial for recycling
283 the connectivity between subunits, different ubiquitin chain types trigger distinct outputs, as seen
284 own enzyme complex capable of forming linear ubiquitin chains under native conditions to date is the
287 by producing unanchored lysine (K)63-linked ubiquitin chains via the proteasomal deubiquitinating en
288 PC is modified predominantly with K63-linked ubiquitin chains when it is bound to Axin in unstimulate
290 ms2, thereby stimulating formation of Lys-63 ubiquitin chains, whereas the related RNF168 RING domain
291 njugating enzyme to a substrate or a growing ubiquitin chain, which is mediated by E3 ubiquitin ligas
293 SHARPIN conjugated with Lys63 (K63)-linked ubiquitin chains, which led to inhibition of the associa
295 e of individual components, including linear ubiquitin chains-which allows for the remarkable versati
297 ly compared proteasomal processing of Lys-63 ubiquitin chains with that of the canonical proteolytic
298 ion depends on the interaction of K29-linked ubiquitin chains with two N-terminal loops of Ufd2p.
299 ave implications on the ease of synthesis of ubiquitin chains with varying lengths and types for stru
300 s also suggested roles for mixed or branched ubiquitin chains, yet without a method to monitor endoge
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