ライフサイエンスコーパス: DUB

1 DUB activity was necessary for inflammasome association

2 DUB inhibitors, especially the inhibitors of proteasomal

3 DUB profiling identified 28 DUBs that cleave DIX-ubiquit

4 DUBs directly recognize existing conformations, but may

5 DUBs present specificity toward different ubiquitin chai

6 DUBs used in UbiCRest can be obtained commercially; howe

7 DUBs were, moreover, found to be associated with several

8 Approximately 100 DUBs are encoded in the human genome and are involved in

9 DUB profiling identified 28 DUBs that cleave DIX-ubiquitin conjugates, half of which

10 profiling 11 compounds against a panel of 32 DUBs.

11 We tagged 66 DUBs with green fluorescent protein and systematically s

12 To explore how the BRCA1-A DUB activity contributes to its function at DNA double s

13 la pneumophila SidE effector family harbor a DUB module important for ubiquitin dynamics on the bacte

14 oronavirus papain-like protease (PLpro) is a DUB that cleaves ISG15, a two-domain Ub-like protein, an

15 and protein analysis show that Rpn11/POH1, a DUB enzyme upstream of 20S proteasome, is more highly ex

16 ves a putative nuclease (CinB) rather than a DUB.

17 observations raise the question of whether a DUB can control the fate of a nonubiquitinated ERAD subs

18 dy reveals an unexpected paradigm in which a DUB prevents undesired ubiquitination to sharpen substra

19 changes conformational dynamics and affects DUB activity.

20 believe the field of drug discovery against DUBs is still in its infancy, but advances in assay deve

21 chemical probes to study the effect of AMSH DUB activity on cell surface receptor degradation.

22 ergy transfer (FRET)-based add-and-read AMSH DUB assay in a 384-well format.

23 at inhibits its interaction with ASXL1/2 and DUB activity and deregulates cell proliferation.

24 ric inhibitors of the ubiquitin E1-E2-E3 and DUB enzymatic cascade developed over the past decade wit

25 The HAT and DUB modules are in close proximity, and the DUB module m

26 -dependent control of a ubiquitin ligase and DUB at mammalian CNS synapses.

27 ave been pursued in the search for lead anti-DUB compounds.

28 as necessary for inflammasome association as DUB inhibition also impaired ASC oligomerization and cas

29 Successful capture of the TRIM-25-associated DUB, ubiquitin specific protease 15, demonstrated the ve

30 y, we probed the role of the ERAD-associated DUB, YOD1, during retro-translocation of the nonubiquiti

31 ntly, we identify USP13 as a gp78-associated DUB that eliminates ubiquitin conjugates from Ubl4A to m

32 nction and that JosD1, a membrane-associated DUB whose activity is regulated by ubiquitination, helps

33 via targeting the 19S proteasome-associated DUBs (UCHL5 and USP14), without effecting on the 20S pro

34 ione inhibits both 19S proteasome-associated DUBs and 20S proteasome activity with a mechanism distin

35 ct the contribution of proteasome-associated DUBs and the complexity of the degradation process.

36 Unlike the ATXN7L3 DUB complex, a USP22-ATXN7L3B-ENY2 complex cannot deubiq

37 Bacterial DUBs have been discovered, but little is known about the

38 XL2 cancer-associated mutations disrupt BAP1 DUB activity.

39 is study investigates the importance of BAP1 DUB activity and the interactions with FoxK2 and HCF-1 i

40 target genes, and this effect requires BAP1 DUB activity but not interaction with HCF-1.

41 Both DUB activity and PIP sequence are conserved in the membe

42 Both DUBs are capable of deubiquitinating Ede1 in vitro.

43 Inactivating BRCC36 DUB attenuated BRCA1-A functions at DSBs and led to unre

44 ur findings uncover a pivotal role of BRCC36 DUB in limiting DSB processing and repair and illustrate

45 a new regulatory mechanism underlying BRCC36 DUB activity, subcellular localization, and biological f

46 transcription factors, induction of IDOL by DUB inhibition is LXR-independent and occurs in Lxralpha

47 In addition, cleavage of the K48 linkage by DUB is faster if this linkage is at the distal end.

48 ariant of ubiquitin (HA-Ub-VME), we captured DUBs that are differentially recruited to the cytosol on

49 used pharmacological inhibition of cellular DUB activity.

50 derable functional redundancy among cellular DUBs that restrict ubiquitin-dependent protein assembly

51 seudo DUB allosterically activates a cognate DUB partner and implicates super dimerization as a new r

52 identical substrates than their constituent DUBs by roughly 2 orders of magnitude.

53 These results establish M40-containing DUB complexes as novel HSC regulators of HSC expansion,

54 be defined, but the mechanisms that control DUB activity in vivo are understood poorly.

55 Our findings reveal that a cytosolic DUB exerts a negative function during retro-translocatio

56 regulators of Ub signaling, but a dedicated DUB for Met1 linkages has not been identified.

57 ed in cancer, functions as a deubiquitinase (DUB) for histone H2A.

58 acetyltransferase (HAT) and deubiquitinase (DUB) activities.

59 nesis, while loss of the H2B deubiquitinase (DUB) activity does not.

60 gly, an MHV68 mutant lacking deubiquitinase (DUB) activity, embedded within the large tegument protei

61 Inhibition of deubiquitinase (DUB) activity is a promising strategy for cancer therapy

62 derivatives block proteasome deubiquitinase (DUB) activity and have been developed and tested in the

63 The deubiquitinase (DUB) and tumor suppressor BAP1 catalyzes ubiquitin remov

64 t in ATXN7, a subunit of the deubiquitinase (DUB) module (DUBm) in the SAGA complex.

65 The deubiquitinase (DUB) Ubp10 is thought to promote heterochromatic silenci

66 We identified the deubiquitinase (DUB) Ubp7 as a late-arriving endocytic protein.

67 the UPS involves targeting deubiquitinases (DUB).

68 Deubiquitinases (DUBs) are a new class of drug targets, although the phys

69 Deubiquitinases (DUBs) are key regulators of Ub signaling, but a dedicate

70 Deubiquitinases (DUBs) are proteases that regulate various cellular proce

71 Deubiquitinases (DUBs) play an important role in regulating the ubiquitin

72 Deubiquitinases (DUBs) remove ubiquitin conjugates from diverse substrate

73 Deubiquitinases (DUBs) reverse ubiquitin signals with equally high sophis

74 domain (UBD), 10 out of 12 deubiquitinases (DUBs), including USP8, USP15 and USP30, are impaired in

75 oteasome peptidases and 19S deubiquitinases (DUBs) are becoming attractive targets of cancer therapy.

76 There are approximately 90 deubiquitinases (DUBs) encoded in the human genome, of which 79 are predi

77 iquitin-binding domains and deubiquitinases (DUBs) select pre-existing conformations.

78 ubiquitin ligases (E3s) and deubiquitinases (DUBs), enzymes with opposing activities, can both promot

79 family of enzymes known as deubiquitinases (DUBs).

80 a class of enzymes known as deubiquitinases (DUBs).

81 s implicate ERAD-associated deubiquitinases (DUBs) as positive and negative regulators during ERAD, r

82 f two proteasome-associated deubiquitinases (DUBs), Rpn11 and Ubp6, and explored their impact on over

83 ssed to a similar extent by deubiquitinases (DUBs) as that of a native Nepsilon-Gly-L-Lys isopeptide

84 uitin chains is mediated by deubiquitinases (DUBs).

85 ing through its reversal by deubiquitinases (DUBs).

86 In eukaryotes, deubiquitinases (DUBs) remove ubiquitin conjugates from diverse substrate

87 ovarian tumor (OTU) family deubiquitinases (DUBs) exist in humans, and most members regulate cell-si

88 omponents, particularly key deubiquitinases (DUBs) of the ubiquitin-specific protease (USP) class.

89 rate, and susceptibility to deubiquitinases (DUBs) affect processing of different substrates by prote

90 n be antagonized by various deubiquitinases (DUBs) including the CYLD tumour suppressor that attenuat

91 , as are a variety of viral deubiquitinases (DUBs).

92 By screening a deubiquitinating (DUB) enzyme small interfering RNA (siRNA) library, we id

93 onjugating, E3 ligase, and deubiquitinating (DUB) enzymes offers an ideal platform for modulating act

94 vestigated whether the EBV deubiquitinating (DUB) enzyme encoded by BPLF1 targets ubiquitinated PCNA

95 of an Lnk-associated Lys63 deubiquitinating (DUB) complex, attenuates HSC expansion.

96 in subcomplex known as the deubiquitinating (DUB) module.

97 tone acetylation (HAT) and deubiquitination (DUB).

98 ction of Ataxin-3 (ATXN3), a deubiquitylase (DUB) involved in Machado-Joseph Disease (MJD), remains e

99 n but is endowed with K63-Ub deubiquitylase (DUB) activity.

100 Deubiquitylases (DUBs) are key regulators of the ubiquitin system which c

101 ng cancer cells to identify deubiquitylases (DUBs) that have an impact on PI3K signaling by regulatin

102 examined whether targeting deubiquitylating (DUB) enzymes upstream of 20S proteasome overcomes protea

103 es that encode an ovarian tumor (OTU) domain DUB known as papain-like protease 2 (PLP2).

104 Instead, depletion of each DUB increases expression of both the PTEN transcript and

105 Occupancy of either DUB by a ubiquitin conjugate leads to ATPase stimulation

106 und that both forms of ATXN7 greatly enhance DUB activity but that ATXN7-92Q NT is largely insoluble

107 ently shown to be a deubiquitinating enzyme (DUB) and to possess deISGylating activity, as previously

108 th understanding of deubiquitinating enzyme (DUB) catalysis, particularly the mode of ubiquitin bindi

109 a Zn(2+)-dependent deubiquitinating enzyme (DUB) that hydrolyzes lysine-63-linked ubiquitin chains a

110 STAM3 (AMSH3) is a deubiquitinating enzyme (DUB) that interacts with endosomal complex required for

111 ate that USP25 is a deubiquitinating enzyme (DUB) that negatively regulates IL-17-triggered signaling

112 d activation of the deubiquitinating enzyme (DUB) USP8.

113 and the specialized deubiquitinating enzyme (DUB), ataxin-3, participate in initiating, regulating, a

114 have identified the deubiquitinating enzyme (DUB), ubiquitin-specific protease 7 (USP7), as a novel r

115 udied; however, the deubiquitinating enzyme (DUB), which regulates TRAF2 stability, has not been iden

116 , we identified the deubiquitination enzyme (DUB) USP20 as a pivotal regulator of ATR-related DDR pat

117 ow that a Wolbachia deubiquitylating enzyme (DUB) induces CI.

118 mains unclear which deubiquitylating enzyme (DUB) removes H2AK13,15ub.

119 itination, yet few deubiquitinating enzymes (DUB) have been implicated.

120 ffectively inhibit deubiquitinating enzymes (DUB), including the enzymes USP9x and UCH37, which are a

121 t can be reversed by deubiquitinase enzymes (DUBs) that remove ubiquitin moieties from the protein th

122 inating as well as deubiquitinating enzymes (DUBs) can regulate these processes by modifying the ubiq

123 Deubiquitinating enzymes (DUBs) have emerged as key players in the maintenance of

124 is modification by deubiquitinating enzymes (DUBs) impacts genome maintenance in vivo is largely unkn

125 f linkage-specific deubiquitinating enzymes (DUBs) in parallel reactions, followed by gel-based analy

126 To search for the deubiquitinating enzymes (DUBs) involved in the antiviral activity of IFN, we used

127 ional diversity of deubiquitinating enzymes (DUBs) is not well understood.

128 Deubiquitinating enzymes (DUBs) recognize and cleave linkage-specific polyubiquiti

129 Deubiquitinating enzymes (DUBs) regulate various cellular processes ranging from p

130 Deubiquitinating enzymes (DUBs) remove ubiquitin (Ub) from Ub-conjugated substrate

131 f viruses encoding deubiquitinating enzymes (DUBs) suggests they remove ubiquitin to evade ubiquitin-

132 The deubiquitinating enzymes (DUBs) that function in the nervous system are beginning

133 s regulated by the deubiquitinating enzymes (DUBs) Ubp2 and Ubp15.

134 r homologous human deubiquitinating enzymes (DUBs), and no significant cytotoxicity in Vero E6 and HE

135 ing superfamily of deubiquitinating enzymes (DUBs), which is capable of inhibiting ISG15 production a

136 Deubiquitinating enzymes (DUBs), which reverse the process of ubiquitination, are

137 to 26 S-associated deubiquitinating enzymes (DUBs): in yeast to Ubp6, which is essential for the ATPa

138 Deubiquitylating enzymes (DUBs) remove ubiquitin (Ub) from various cellular protei

139 pproach to uncover deubiquitylating enzymes (DUBs) that participate during TCR signaling in primary m

140 Here we show that deubiquitylating enzymes (DUBs) USP14 and UCHL5 are more highly expressed in MM ce

141 opposed by several deubiquitylating enzymes (DUBs), including OTUB1 and USP3.

142 ent on activity of deubiquitylating enzymes (DUBs).

143 ugh the action of de-ubiquitylating enzymes (DUBs).

144 lytic turnover, is imperative for exploiting DUBs for therapeutic intervention.

145 any of three members of the Josephin family DUBs: ataxin 3 (ATXN3), ataxin 3-like (ATXN3L) and Josep

146 Found in all eukaryotes, MINDY-family DUBs are highly selective at cleaving K48-linked polyUb,

147 hough the physiological function of only few DUBs has been characterized.

148 verall, to our knowledge, USP13 is the first DUB identified to modulate STAT1 and play a role in the

149 lysosomal degradation of the LDLR following DUB inhibition.

150 roteins, ATXN7L3 and ENY2, are necessary for DUB activity toward histone H2Bub1 and other substrates.

151 heterodimers (super dimers) was required for DUB activity and interaction with targeting proteins SHM

152 These data reveal the requirement for DUB activity in a key reaction of the innate immune resp

153 gn and preparation of a FRET-based assay for DUBs based on the application of our recent chemical met

154 Our results uncover a novel function for DUBs in the endocytic pathway by which Ubp2 and Ubp15 po

155 rategy for rational design of inhibitors for DUBs and other UPS proteins.

156 ase 3 (USP3; Usp3Delta/Delta), a histone H2A DUB which negatively regulates ubiquitin-dependent DDR s

157 Moreover, USP44 but not other H2A DUBs was recruited to RNF168-generated ubiquitylation pr

158 Here we characterized an H2A-DUB targeted mouse line Mysm1(tm1a/tm1a) and demonstrate

159 (PRC1) and H2A-deubiquitinating enzymes (H2A-DUBs).

160 The roles of H2A-DUBs in mammalian development, stem cells, and hematopoi

161 e observations led us to discover two H2Bub1 DUBs, USP27X and USP51, which function independently of

162 A interference screening to identify a human DUB, ubiquitin-specific protease (USP) 13, whose express

163 re, we reveal a previously unannotated human DUB, OTULIN (also known as FAM105B), which is exquisitel

164 By analysing 42 human DUBs against all diubiquitin topoisomers we provide an e

165 idually overexpressing the majority of human DUBs on RNF8/RNF168-mediated 53BP1 retention at DSB site

166 iew, we discuss the recent findings on human DUBs that participate in genome maintenance, with a focu

167 Here we reveal USP48 as the first identified DUB to deubiquitinate and stabilize TRAF2 in epithelial

168 a framework to tackle lingering questions in DUB biology.

169 e it into eggs, and a catalytically inactive DUB does not induce sterility.

170 The CI-inducing DUB, CidB, cleaves ubiquitin from substrates and is enco

171 nism between the silencing machinery and its DUB partner allows erasure of active PTMs and the de nov

172 subunit that confers the BRCA1-A complex its DUB activity.

173 in fold with no homology to any of the known DUBs.

174 ation, PL(pro) variants specifically lacking DUB activity were no longer able to do so.

175 Here we show that many DUBs of the USP and UCH subfamilies can be reversibly in

176 s of the OTU and JAB/MPN/Mov34 metalloenzyme DUB families and highlight that all USPs tested display

177 (STAM) (AMSH) is a conserved metalloprotease DUB in eukaryotes.

178 IC50 value of the nonspecific small molecule DUB inhibitor N-ethylmaleimide was 16.2+/-3.2 muM and ca

179 activity based probes and assays to monitor DUB activities in vitro and in cellular contexts.

180 he role of USP19 in ERAD and suggest a novel DUB regulation that involves chaperone association and m

181 (motif interacting with Ub-containing novel DUB family).

182 we provide an extensive characterization of DUB activity and specificity.

183 e evasion, but the selective inactivation of DUB activity also opens unique possibilities for develop

184 eport here that small molecule inhibitors of DUB activity inhibit inflammasome activation.

185 protein cleavage was intact, but the loss of DUB activity strikingly enhanced innate immune signaling

186 hese findings establish a novel mechanism of DUB regulation that may be integrated with other redox-d

187 We further discuss the many mechanisms of DUB regulation with a focus on those that modulate catal

188 e and highlight the therapeutic potential of DUB inhibitors for chronic auto-inflammatory diseases.

189 yed to assess the potency and specificity of DUB inhibitors by profiling 11 compounds against a panel

190 168 pathway and illustrate the usefulness of DUB overexpression screens for identification of antagon

191 ct ubiquitylated proteins from the action of DUBs and the proteasome in crude cell extracts.

192 icate that the regulation of the activity of DUBs is important for homeostasis and is achieved by mul

193 uitin conjugates to study various aspects of DUBs such as their specificities and structures.

194 in-specific proteases (USP) are one class of DUBs that have drawn special attention as cancer targets

195 The MJD family of DUBs consists of four cysteine proteases that share a ca

196 ectively, our results reveal a new family of DUBs that may have specialized roles in regulating prote

197 e we report the discovery of a new family of DUBs, which we have named MINDY (motif interacting with

198 cal entities for the selective inhibition of DUBs based on these tools are also highlighted with sele

199 Inhibition of DUBs blocked the processing and release of IL-1beta in b

200 hat the isothiocyanate-induced inhibition of DUBs may also explain how isothiocyanates affect inflamm

201 Short term (2 h) inhibition of DUBs resulted in accumulation of high molecular weight u

202 uncovers a novel class of dual inhibitors of DUBs and proteasome and suggests a potential clinical st

203 Through screening a panel of DUBs, we identified USP20 as critical for replication st

204 Concurrent with the revelation of DUBs as potential therapeutic targets are publications o

205 he ubiquitin system and studying the role of DUBs in health and disease.

206 Studying the role of DUBs in health and diseases has been a major goal for ma

207 ome maintenance, with a focus on the role of DUBs in the modulation of DNA repair and DNA damage sign

208 Consistent with the role of DUBs in transcriptional regulation, we identified a 70-b

209 e points to the important regulatory role of DUBs, the molecular basis of their regulation is still n

210 ogical significance of the ubiquitination of DUBs to their functions in vivo is unclear.

211 The effects of ATXN7-poly(Q) on DUB activity are not known.

212 One DUB whose function has been proposed to include monoubiq

213 USP19, the only DUB containing a carboxyl-terminal transmembrane domain,

214 iverse roles of deubiquitinating enzymes, or DUBs, in determining the fate of specific proteins conti

215 Correspondingly, the ORF64 DUB active site mutant virus exhibited impaired ability

216 n melanoma 2 pathways, and lack of the ORF64 DUB was associated with impaired delivery of viral DNA t

217 resents a new subclass of zinc-dependent OTU DUBs.

218 b-binding sites on the OTU domain enable OTU DUBs to distinguish linkage types.

219 analysis and five crystal structures of OTU DUBs with or without Ub substrates reveal four mechanism

220 Several OTU DUBs were reported to be ubiquitin (Ub) chain linkage sp

221 Ub chain restriction analysis, in which OTU DUBs are used as restriction enzymes to reveal linkage t

222 otein substrates involved in these pathways, DUBs provide an untapped means of modulating many import

223 Our findings not only establish PLP2 DUB activity as a critical factor in arteriviral innate

224 ns at the N-terminal border of the nsp2 PLP2-DUB domain.

225 we show that FOXK2 binds to the SIN3A and PR-DUB complexes.

226 nt of the polycomb deubiquitylase complex PR-DUB to sites of DNA damage.

227 w the polycomb repressive-deubiquitinase (PR-DUB) complex controls substrate selection specificity, w

228 the Polycomb repressive deubiquitination (PR-DUB) complex.

229 an important functional role for ASXL3 in PR-DUB mediated deubiquitination.

230 ancestry for BAP1 and Uch37 regulators in PR-DUB, INO80 chromatin remodelling and proteosome complexe

231 The PR-DUB complex contains the important tumour suppressor pro

232 ed a strategy to selectively disable PL(pro) DUB activity, we were able to specifically examine the e

233 n effective inhibitor of the 19S proteasomal DUBs and suggests a potentially new strategy for cancer

234 rs, especially the inhibitors of proteasomal DUBs are becoming a research hotspot in targeted cancer

235 VLX1570 is an inhibitor of proteasome DUB activity currently in clinical trials for relapsed m

236 explored their impact on overall proteasome DUB activity.

237 ide an explanation of how an inactive pseudo DUB allosterically activates a cognate DUB partner and i

238 domain protein BRCC36 associates with pseudo DUB MPN(-) proteins KIAA0157 or Abraxas, which are essen

239 details for generating a toolkit of purified DUBs and for profiling their linkage preferences in vitr

240 mutate this surface to significantly reduce DUB activity without affecting polyprotein cleavage.

241 how that Arabidopsis AMSH1, an AMSH3-related DUB, interacts with the ESCRT-III subunit vacuolar prote

242 r results establish that two closely related DUBs differ markedly in activity and function and that J

243 ulated in yeast by CidB alone; this requires DUB activity but is rescued by coexpressed CidA.

244 at ATXN7L3B regulates H2Bub1 levels and SAGA DUB activity through competition for ENY2 binding.

245 Several DUBs have been implicated in various diseases and are at

246 ystal structure of the Ubp8/Sgf11/Sus1/Sgf73 DUB module bound to a ubiquitinated nucleosome reveals t

247 Thus, USP7 directly serves as a specific DUB for Poleta.

248 The development of specific DUB inhibitors, together with inhibitors of BoNT/A prote

249 there is an urgent need to identify specific DUBs associated with therapeutically relevant targets of

250 ) via targeting both 19S proteasome-specific DUBs and 20S proteolytic peptidases with a mechanism dis

251 strategy toward identifying target-specific DUBs.

252 cal data provide the rationale for targeting DUB enzyme Rpn11 upstream of 20S proteasome to enhance c

253 P15 in MM disease models validates targeting DUBs in the ubiquitin proteasomal cascade to overcome pr

254 ptualize the many layers of specificity that DUBs encompass to control the ubiquitin code and discuss

255 The DUB AMSH (associated molecule with the SH3 domain of STA

256 The family is named after the DUB ATXN3, which causes the neurodegenerative disease Ma

257 DUB modules are in close proximity, and the DUB module modestly stimulates HAT function.

258 sequencing) analysis revealed that both the DUB and HAT modules bind most SAGA target genes even tho

259 The ability to decouple the DUB activity of PL(pro) from its role in viral polyprote

260 enocysteine-based strategies to generate the DUB probe dehydroalanine (Dha).

261 However, the DUB module regulates a subset of genes in early embryoge

262 Here we identified the DUB USP15 as a crucial negative regulator of T cell acti

263 These findings directly implicate the DUB function of PL(pro), and not its proteolytic activit

264 itin binding and the individual steps in the DUB catalytic turnover, is imperative for exploiting DUB

265 These results show that USP51 is the DUB for H2AK13,15ub and regulates DNA damage response.

266 Here, we report that ubiquitination of the DUB ataxin-3 at lysine residue 117, which markedly enhan

267 USP22 is the catalytic subunit of the DUB module, but two adaptor proteins, ATXN7L3 and ENY2,

268 enes in early embryogenesis, and loss of the DUB subunits causes defects in embryogenesis.

269 In this study, we report the DUB USP9X is an important regulator of the core kinases

270 ugh many of these targets do not require the DUB module for expression.

271 form a complex with USP-46 and stimulate the DUB to deubiquitinate and stabilize GLR-1 in vivo.

272 ereas EDE1 deletion partially suppressed the DUB deletion phenotype.

273 Furthermore, we found that the DUB module can bind to chromatin and regulate transcript

274 We find that the DUB module deubiquitinates H2B both in the context of th

275 Our results suggest that the DUB module has functions within SAGA and independent fun

276 a ubiquitinated nucleosome reveals that the DUB module primarily contacts H2A/H2B, with an arginine

277 We found previously that the DUB USP-46 deubiquitinates the Caenorhabditis elegans gl

278 The DUBs comprise a relatively small group of proteins, most

279 Deletion of the DUBs Ubp2 and Ubp7 resulted in elongation of endocytic c

280 library to develop inhibitors targeting the DUBs USP7 and USP10, which are involved in regulating le

281 These DUBs thus have the potential to promote Dvl polymerizati

282 Individual depletion of these DUBs only mildly enhanced accumulation of ubiquitin conj

283 el and potent inhibitor able to inhibit this DUB in time-dependent manner with k(inact) = 0.065 min(-

284 red for the neuroprotective function of this DUB in Drosophila.

285 or maintaining proper protein levels of this DUB.

286 milar to its human counterpart and that this DUB is necessary during fly development.

287 biquitination in HSC signaling, and point to DUB-specific inhibitors as reagents to expand stem cell

288 sive element, which mediates the response to DUB inhibition.

289 this isopeptide replacement is resistant to DUBs and to shaving by proteasome.

290 Intriguingly, we found that the K63-Ub DUB activity, although dispensable for maintaining the i

291 We find that Sir2/4 stimulates Ubp10 DUB activity on nucleosomes, likely through a combinatio

292 how that USP51, a previously uncharacterized DUB, deubiquitylates H2AK13,15ub and regulates DNA damag

293 , ultimately resulting in increases in USP48 DUB activity.

294 er dissect the role(s) of PL(pro) as a viral DUB during MERS-CoV infection.

295 ubiquitinated by cellular USP1, by the viral DUB can disrupt repair of DNA damage by compromising rec

296 ensitive and fast assay to quantify in vitro DUB enzyme activity using matrix-assisted laser desorpti

297 ubiquitin code and discuss examples in which DUB specificity has been understood at the molecular lev

298 y to oxidative inhibition is associated with DUB activation wherein the active site cysteine is conve

299 ctively, and can be used in combination with DUBs to generate K29- and K33-linked chains for biochemi

300 rrogation of these branched derivatives with DUBs reveals that the relative orientation of the two Ub