ライフサイエンスコーパス: ubiquitin-like protein

1 ine motif (herein called Pup for prokaryotic ubiquitin-like protein).

2 fused at its N terminus to SUMO or any other ubiquitin-like protein.

3 -expressed developmentally downregulated), a ubiquitin-like protein.

4 y is concomitantly induced and modified by a ubiquitin-like protein.

5 l modification in the form of ubiquitin or a ubiquitin-like protein.

6 modification of the TOP1 by SUMO-1/Smt3p, a ubiquitin-like protein.

7 was found to be modified by conjugation to a ubiquitin-like protein.

8 15 is an interferon (IFN)-alpha/beta-induced ubiquitin-like protein.

9 old modifier 1 (UFM1), a recently identified ubiquitin-like protein.

10 tein domains that interact with ubiquitin or ubiquitin-like proteins.

11 ase machinery by conjugation of ubiquitin or ubiquitin-like proteins.

12 ilar to ubiquitin and were henceforth called ubiquitin-like proteins.

13 st steps in the conjugation of ubiquitin and ubiquitin-like proteins.

14 576) within the activating enzymes for other ubiquitin-like proteins.

15 that are predicted or shown to function with ubiquitin-like proteins.

16 d a positively-charged residue in many other ubiquitin-like proteins.

17 /3 chains or SUMO1, but not by several other ubiquitin-like proteins.

18 no acid region present in UBQLN3 and several ubiquitin-like proteins.

19 components, and Dsk2p and Rad23p, a pair of ubiquitin-like proteins.

20 ved domains found in several recently cloned ubiquitin-like proteins.

21 and has facilitated the cloning of numerous ubiquitin-like proteins.

22 y all three members of the sentrin family of ubiquitin-like proteins.

23 fication of RanGAP1 by the sentrin member of ubiquitin-like proteins.

24 covalently modified by the sentrin family of ubiquitin-like proteins.

25 dification by the attachment of ubiquitin or ubiquitin-like proteins.

26 olutionary relative of the progenitor of all ubiquitin-like proteins.

27 Negative regulator of ubiquitin-like protein 1 (NUB1) and its longer isoform N

28 Ubiquitin-like protein 1 was up-regulated over 100 fold

29 Here we report that ubiquitin-like protein 4A (Ubl4A) plays a crucial role i

30 Biological functions of the highly conserved ubiquitin-like protein 5 (UBL5) are not well understood.

31 The ataxin-1 interacting ubiquitin-like protein (A1Up) contains an amino-terminal

32 Here, we have screened most known ubiquitin-like proteins after DNA damage and found that

33 These findings explain how a distinctive ubiquitin-like protein alters the functions of its targe

34 ISG15 is an IFN-inducible ubiquitin-like protein and its expression and conjugatio

35 eins that are modified by the SUMO family of ubiquitin-like proteins and describes how mutation of co

36 1-like DUB prefers ubiquitin substrates over ubiquitin-like proteins and efficiently cleaves polyubiq

37 of GPCR clustering reveals a new function of ubiquitin-like proteins and highlights a cellular requir

38 rse the modification of proteins by a single ubiquitin(-like) protein, and remodel polyubiquitin(-lik

39 Elongin B is a ubiquitin-like protein, and Elongin C is a Skp1-like pro

40 Expression of ISG15 (UCRP), a ubiquitin-like protein, and protein ISGylation are highl

41 f the ubiquitin system, including ubiquitin, ubiquitin-like proteins, and proteins that bind to ubiqu

42 Post-translational modifications by ubiquitin-like proteins are among the most important mec

43 Ubiquitin-like proteins are covalently conjugated to cel

44 However, the functions of these ubiquitin-like proteins are largely unknown.

45 In contrast, archaeal ubiquitin-like proteins are less conserved and not known

46 the autophagy scaffold protein Atg11 and the ubiquitin-like protein Atg8.

47 k cargo to the membrane-bound autophagosomal ubiquitin-like protein Atg8/LC3.

48 to the formation of the autophagosome is the ubiquitin-like protein autophagy-related (Atg)8 (microtu

49 ation requires ATP-coupled activation of the ubiquitin-like protein by members of a superfamily of ev

50 ling cascade, and utilize autophagy-specific ubiquitin-like protein cascades to tether proteins to au

51 uccessful synthesis of ubiquitin conjugates, ubiquitin-like protein conjugates, histone H2A with a C-

52 ontains a domain that interacts with a mouse ubiquitin-like protein conjugating (E2) enzyme, mUBC9.

53 data provide a link between acetylation and ubiquitin-like protein conjugation and define a mechanis

54 erodimeric E1-activating enzyme in the Nedd8 ubiquitin-like protein conjugation pathway.

55 h conserved protein kinase, lipid kinase and ubiquitin-like protein conjugation subnetworks controlli

56 tes in the macroautophagy pathway includes a ubiquitin-like protein conjugation system and a protein

57 he localization of components of two related ubiquitin-like protein conjugation systems, Atg8 and Atg

58 Type I ubiquitin-like proteins constitute a family of protein m

59 cloned the gene and found it encodes a novel ubiquitin-like protein containing an NH2 terminus 36% id

60 ion, we have identified a fragment of UHRF1 (ubiquitin-like protein containing PHD and RING domains 1

61 loss of function of the epigenetic regulator ubiquitin-like protein containing PHD and RING finger do

62 NEDD8, a ubiquitin-like protein, covalently conjugates to cullin

63 ess via the interaction of DSK2 with ATG8, a ubiquitin-like protein directing autophagosome formation

64 The results imply that non-covalent ubiquitin-like protein-E2 complexes are conserved platfo

65 ication scheme can be applied to other small ubiquitin-like proteins, especially those with limited p

66 ISG15 is an IFN-inducible, ubiquitin-like protein expressed after bacterial or vira

67 tin were superior in inducing catalysis, and ubiquitin-like proteins failed to activate phospholipase

68 s the most recently identified member of the ubiquitin-like protein family.

69 a patient with HIVAN, it was found that the ubiquitin-like protein FAT10 is one of the most upregula

70 2, that activates both ubiquitin and another ubiquitin-like protein, FAT10.

71 FUBI belongs to the ubiquitin-like protein group that is capable of forming

72 Modification of CUL1 by the RUB1/NEDD8 ubiquitin-like protein has been proposed to free CUL1 fr

73 The NEDD8/Rub1 class of ubiquitin-like proteins has been implicated in progressi

74 NEDD8, a novel ubiquitin-like protein, has been shown to conjugate to p

75 Recently, a surprising number of ubiquitin-like proteins have been identified that also c

76 Ubiquitin-like proteins have been shown to be covalently

77 The fau gene encodes a ubiquitin-like protein (here called FUBI) fused to the r

78 We identified a ubiquitin-like protein, hPLIC1 (for human homolog 1 of p

79 trated that PML is co-localized with a novel ubiquitin-like protein in the nuclear bodies, which coul

80 Atg8 is a ubiquitin-like protein involved in autophagy in yeast th

81 Apg8 is a ubiquitin-like protein involved in autophagy in yeast.

82 ated protein (GABARAP) comprises a family of ubiquitin-like proteins involved in (macro)autophagy, an

83 The only other known yeast ubiquitin-like protein is encoded by the nucleotide exci

84 Modification by related ubiquitin-like proteins is turning out to have a diverse

85 eria, the C-terminal Gln of Pup (prokaryotic ubiquitin-like protein) is deamidated and isopeptide lin

86 N-stimulated gene 15 (ISG15), an IFN-induced ubiquitin-like protein, is known to have an immunomodula

87 Atg8, a lipid-conjugated ubiquitin-like protein, is required for the formation of

88 The ubiquitin-like protein ISG15 and its conjugation to prot

89 The expression of the ubiquitin-like protein ISG15 and protein modification by

90 Protein modification by the ubiquitin-like protein ISG15 is an interferon (IFN) effe

91 The interferon-inducible ubiquitin-like protein ISG15 is expressed in cells in re

92 Our study revealed that the IFN-induced ubiquitin-like protein ISG15 mimics the IFN effect and i

93 Induction of the 17-kDa ubiquitin-like protein ISG15/UCRP and its subsequent con

94 43 is a protease that specifically removes a ubiquitin-like protein, ISG15, from its targets.

95 -stimulated gene 15 (ISG15), which encodes a ubiquitin-like protein, ISG15.

96 many of which are conserved among the three ubiquitin-like proteins known to undergo parallel ligati

97 g synthesis and lipidation/activation of the ubiquitin-like protein LC3 and formation of autophagic d

98 Upon induction of autophagy, the ubiquitin-like protein LC3 is conjugated to phosphatidyl

99 Such domains are common in ubiquitin and ubiquitin-like protein ligases (E3s), but little was kno

100 tif and also reveal a novel mechanism for E3 ubiquitin-like protein ligases, with the Nup358/RanBP2 E

101 six members of the LC3 and GABARAP family of ubiquitin-like proteins (mATG8s).

102 of other ubiquitin ligases with ubiquitin or ubiquitin-like proteins may likewise have major function

103 Ubiquilin-1 (Ubqln1 or Ubqln), a ubiquitin-like protein, mediates degradation of misfolde

104 The Nedd8 ubiquitin-like protein modification pathway regulates ce

105 Moreover, the variety and function of ubiquitin-like protein modifications in the cell may be

106 on of the design strategy to other polymeric ubiquitin-like protein modifications.

107 , we have investigated the role of the small ubiquitin-like protein modifier (SUMO) in SC formation d

108 d genes (ISGs), including, among others, the ubiquitin-like protein modifier ISG15 and the ubiquitin

109 Previously we showed that the small ubiquitin-like protein modifier SUMO1 interacts with an

110 NEDD8 is a ubiquitin-like protein modifier that is conjugated to ta

111 fier 1 (UFM1) is a small, metazoan-specific, ubiquitin-like protein modifier that is essential for em

112 FAT10 is a ubiquitin-like protein modifier that is induced in verte

113 Ubiquitin-like proteins modify target proteins, altering

114 Covalent modification of cullins by the ubiquitin-like protein NEDD8 (neddylation) regulates pro

115 modification of the cullin subunit with the ubiquitin-like protein Nedd8 (neddylation).

116 odification of their cullin subunit with the ubiquitin-like protein NEDD8 (NEural precursor cell expr

117 Covalent modification of cullins by the ubiquitin-like protein NEDD8 activates cullin ligases th

118 cell extracts depends on the presence of the ubiquitin-like protein Nedd8 and enzymes that catalyze N

119 ultiple cullins and promoted cleavage of the ubiquitin-like protein NEDD8 from Schizosaccharomyces po

120 COP9 signalosome (CSN) cleaves the ubiquitin-like protein Nedd8 from the Cul1 subunit of SC

121 nalosome (CSN) mediates deconjugation of the ubiquitin-like protein Nedd8 from the cullin subunits of

122 the enzymatic activity that deconjugates the ubiquitin-like protein Nedd8 from the SCF Cul1 component

123 The covalent attachment of the ubiquitin-like protein Nedd8 is required for cullin acti

124 Whereas the ubiquitin-like protein NEDD8 is well studied for its rol

125 In eukaryotes, the conjugation of the ubiquitin-like protein NEDD8 onto protein targets is an

126 creases in the relative concentration of the ubiquitin-like protein NEDD8 over ubiquitin lead to acti

127 Covalent attachment of the ubiquitin-like protein NEDD8 to a conserved C-terminal d

128 tes distinctive E3-dependent ligation of the ubiquitin-like protein Nedd8 to Cul1.

129 Conjugation of ubiquitin-like protein Nedd8 to cullins (neddylation) is

130 hat culminates in covalent attachment of the ubiquitin-like protein Nedd8 to cullins.

131 of neddylation, the conjugation of the small ubiquitin-like protein NEDD8 to lysine residues, interru

132 ical processes by covalently conjugating the ubiquitin-like protein NEDD8 to specific targets.

133 regulated by the covalent attachment of the ubiquitin-like protein Nedd8 to the cullin subunit.

134 ly expressed proteins, overexpression of the ubiquitin-like protein NEDD8 was identified in samples f

135 olled by the modification of cullin with the ubiquitin-like protein NEDD8(2-6).

136 NUB1 is a potent down-regulator of the ubiquitin-like protein NEDD8, because it targets NEDD8 t

137 that inhibits CUL3 activity by removing the ubiquitin-like protein NEDD8, cannot interact with CUL3-

138 hange in the subcellular localization of the ubiquitin-like protein NEDD8, which is activated by APP-

139 modification of the Cullin-1 subunit by the ubiquitin-like protein NEDD8.

140 modification of the cullin-1 subunit by the ubiquitin-like protein NEDD8.

141 modification of the cullin-1 subunit by the ubiquitin-like protein NEDD8.

142 bunit of the activating enzyme for the small ubiquitin-like protein NEDD8.

143 (Cifs) into mammalian cells to deamidate the ubiquitin-like protein NEDD8.

144 attention has been given to the role of the ubiquitin-like protein Nedd8.

145 s (CRLs) are regulated by modification of an ubiquitin-like protein, Nedd8 (also known as Rub1) on th

146 uitin ligase (CRL) complexes by removing the ubiquitin-like protein, NEDD8, from their cullin scaffol

147 l1 lysine residue, whose modification by the ubiquitin-like protein, Nedd8, is able to block Cand1-Cu

148 s distantly related to ubiquitin and another ubiquitin-like protein, NEDD8.

149 The recent discovery of three new ubiquitin-like proteins, NEDD8, Sentrin/SUMO, and Apg12,

150 CRLs are activated by the attachment of the ubiquitin-like protein neural precursor cell expressed,

151 UBL3 is a ubiquitin-like protein of unknown function with no conse

152 The SUMO ubiquitin-like proteins play regulatory roles in cell di

153 In a previous report the ubiquitin-like protein Plic-1 was shown to directly inte

154 ct interaction of GABA(A) receptors with the ubiquitin-like protein Plic-1.

155 ave identified an unprecedented role for the ubiquitin-like protein PLIC-2 as a negative regulator of

156 he innate immune response, its activity as a ubiquitin-like protein protease and its activity with re

157 tional modification in which the prokaryotic ubiquitin-like protein Pup is covalently attached to a l

158 The prokaryotic ubiquitin-like protein Pup targets substrates for degrad

159 tion, the covalent attachment of prokaryotic ubiquitin-like protein Pup to lysine side chains of the

160 proteins on lysine residues with prokaryotic ubiquitin-like protein Pup.

161 Prokaryotic ubiquitin-like protein (Pup) is a posttranslational modi

162 Prokaryotic ubiquitin-like protein (Pup) is covalently attached to t

163 Prokaryotic ubiquitin-like protein (Pup) is functionally analogous t

164 Protein degradation via prokaryotic ubiquitin-like protein (Pup) tagging is conserved in bac

165 post-translationally tagged with prokaryotic ubiquitin-like protein (Pup), an intrinsically disordere

166 tituting the recently discovered prokaryotic ubiquitin-like protein (Pup)--proteasome degradation sys

167 The prokaryotic ubiquitin-like protein (Pup)-based proteasomal system in

168 Deamidase of Pup (Dop), the prokaryotic ubiquitin-like protein (Pup)-deconjugating enzyme, is cr

169 nal regulatory mechanisms in the prokaryotic ubiquitin-like protein (Pup)-proteasome system (PPS), th

170 We have identified a prokaryotic ubiquitin-like protein, Pup (Rv2111c), which was specifi

171 The ubiquitin-like protein RELATED TO UBIQUITIN (RUB) is con

172 modification and possible regulation by the ubiquitin-like protein Related to Ubiquitin in vivo.

173 Post-translational modifications with ubiquitin-like proteins require three sequentially actin

174 al modification of the cullin subunit by the ubiquitin-like protein RUB/NEDD8 appears to regulate SCF

175 The ubiquitin-like protein RUB1 is conjugated to target prot

176 bx1 modules also activate conjugation of the ubiquitin-like protein Rub1 to Cdc53 and Cul2 by the ded

177 se transporter (ena1Delta), a putative NEDD8 ubiquitin-like protein (rub1Delta), and a phosphatidylin

178 Ubiquitin-like protein/sentrin-specific proteases (Ulp/S

179 unction of Smt3p, a Saccharomyces cerevisiae ubiquitin-like protein similar to the mammalian protein

180 teins are regulated by modification with the ubiquitin-like protein small ubiquitin-like modifier (SU

181 e recognition sequence for attachment of the ubiquitin-like protein, small ubiquitin-like modifier-1

182 n factors are targets for conjugation to the ubiquitin-like protein Smt3 (also called SUMO).

183 gation and division (tonoplast aquaporin and ubiquitin-like protein SMT3), oxidative stress (glutathi

184 enzymes and readily reversed by a family of ubiquitin-like protein-specific proteases (Ulp) in yeast

185 cation of cellular proteins by ubiquitin and ubiquitin-like proteins, such as small ubiquitin-like mo

186 Modification by the ubiquitin-like protein SUMO affects hundreds of cellular

187 Here, we show that in Drosophila the small ubiquitin-like protein SUMO and the SUMO E3 ligase Su(va

188 valent modification of proteins by the small ubiquitin-like protein SUMO has been implicated in the r

189 Modification of cellular proteins by the ubiquitin-like protein SUMO is essential for nuclear pro

190 Post-translational modification by the ubiquitin-like protein SUMO is often regulated by cellul

191 ination and results in the attachment of the ubiquitin-like protein Sumo onto target proteins.

192 Attachment of the ubiquitin-like protein SUMO to other proteins is an esse

193 The attachment of the ubiquitin-like protein SUMO to target proteins is involv

194 albicans septins are regulated by the small ubiquitin-like protein SUMO was examined in this study b

195 ARgamma, HMGA1, and the SUMO E2 ligase Ubc9 (ubiquitin-like protein SUMO-1 conjugating enzyme).

196 PML) becomes conjugated in vivo to the small ubiquitin-like protein SUMO-1, altering its behavior and

197 In fibroblasts, APA-1 was modified by the ubiquitin-like protein SUMO-1, which increased APA-1 hal

198 ocumented substrate for conjugation with the ubiquitin-like protein SUMO-1.

199 PODs is dependent on modification of PML by ubiquitin-like protein SUMO-1.

200 a 11.5 kDa protein similar to the mammalian ubiquitin-like protein SUMO-1.

201 ion marked by the covalent attachment of the ubiquitin-like protein SUMO-1/SMT3C has been implicated

202 NA-3C in a yeast two-hybrid screen, only the ubiquitin-like proteins SUMO-1 and SUMO-3/hSMT3B map to

203 Here, we show that modification by the small ubiquitin-like protein (SUMO) is required for sister chr

204 ight serve as a modification site by a small ubiquitin-like protein (SUMO).

205 argets cellular proteins to be modified by a ubiquitin-like protein (SUMO).

206 RanGAP1 is covalently modified by the small ubiquitin-like protein, SUMO-1, and we have recently pro

207 , Ubc9 catalyzed the covalent linkage of the ubiquitin-like protein, SUMO-1, to E1.

208 Vertebrate RanGAP1 is conjugated to a small ubiquitin-like protein, SUMO-1.

209 Here, we show that HIPK2 is regulated by a ubiquitin-like protein, SUMO-1.

210 oteins are known to be modified by the small ubiquitin-like protein, SUMO.

211 Paralleling other ubiquitin-like proteins, SUMO proteins are proteolytical

212 porin RanBP2 can act as an E3 enzyme for the ubiquitin-like protein SUMO1.

213 lso is stabilized by derivatization with the ubiquitin-like protein SUMO1.

214 eport the mechanical unfolding properties of ubiquitin-like proteins (SUMO1 and SUMO2) and their comp

215 degree of structural conservation across the ubiquitin-like protein superfamily suggests that the gen

216 SUMO is a member of a ubiquitin-like protein superfamily that is covalently at

217 RNAi of ubl-5, a gene encoding a ubiquitin-like protein, suppresses activation of the UPR

218 shes a framework for investigations of other ubiquitin-like protein systems.

219 proteins that direct the conjugation of two ubiquitin-like protein tags, ATG8 and ATG12, to phosphat

220 NEDD8 is a ubiquitin-like protein that activates cullin-RING E3 ubi

221 SUMO is a small ubiquitin-like protein that becomes covalently conjugate

222 Sentrin is a novel ubiquitin-like protein that can be conjugated to other p

223 SUMO-1 is a small ubiquitin-like protein that can be covalently conjugated

224 ISG15 is a ubiquitin-like protein that conjugates to numerous prote

225 NEDD8 is a ubiquitin-like protein that controls vital biological ev

226 NEDD8 is a ubiquitin-like protein that controls vital biological ev

227 Nedd8 is a ubiquitin-like protein that controls vital biological ev

228 Related to Ubiquitin (RUB)/Nedd8 is a ubiquitin-like protein that covalently attaches to culli

229 he small ubiquitin-like modifier (SUMO) is a ubiquitin-like protein that covalently modifies a large

230 ISG15 is a ubiquitin-like protein that functions in innate immunity

231 ISG15 is an IFN-alpha/beta-induced, ubiquitin-like protein that is conjugated to a wide arra

232 15 is an interferon (IFN)-alpha/beta-induced ubiquitin-like protein that is conjugated to cellular pr

233 ISG15 is an interferon (IFN)-induced ubiquitin-like protein that is conjugated to target prot

234 ISG15 is a ubiquitin-like protein that is induced by interferon and

235 O, or Smt3 in Saccharomyces cerevisiae, is a ubiquitin-like protein that is post-translationally atta

236 FAT10 is a ubiquitin-like protein that is upregulated in renal tubu

237 lated protein 8 (ATG8) is a highly conserved ubiquitin-like protein that modulates autophagy pathways

238 SUMO (also called Sentrin) is a ubiquitin-like protein that plays an important role in r

239 Sentrin is a novel ubiquitin-like protein that protects cells against both

240 f PIC1 shows 52% identity to a S. cerevisiae ubiquitin-like protein that was cloned as a suppressor o

241 tment of targets to LC3/GABARAP, a family of ubiquitin-like proteins that presumably bind to the auto

242 quitin-like domain member 1 protein and NEK, ubiquitin-like proteins that promote proteosomal PC2 deg

243 lin-RING ubiquitin ligases (CRLs) requires a ubiquitin-like protein (that is, Nedd8) modification.

244 similar mechanism to activate their cognate ubiquitin-like proteins, the substrate-assisted inhibiti

245 ymes facilitate conjugation of ubiquitin and ubiquitin-like proteins through adenylation, thioester t

246 enzymes catalyze attachment of ubiquitin and ubiquitin-like proteins to lysine residues directly or t

247 m2 also promotes the conjugation of Nedd8, a ubiquitin-like protein, to p53, inhibiting its transcrip

248 ologous positions in structurally homologous ubiquitin-like proteins; to test sequence specificity, i

249 Ubiquitin-like proteins (ub-lps) are conjugated by a con

250 that mutations in UBQLN2, which encodes the ubiquitin-like protein ubiquilin 2, cause dominantly inh

251 lex containing the proteasome as well as the ubiquitin-like protein ubiquilin-1 (UBQLN1).

252 sponse, modification of the newly identified ubiquitin-like protein ubiquitin-fold modifier 1 and the

253 ing transcription factor DVE-1 and the small ubiquitin-like protein UBL-5, both of which are encoded

254 e C-terminal region of MccB is homologous to ubiquitin-like protein (UBL) activating enzyme (E1) aden

255 enzyme, Atg3, to mediate conjugation of the ubiquitin-like protein (UBL) Atg8 during autophagy.

256 se modifications an E1 enzyme activates each ubiquitin-like protein (Ubl) by adenylation of the Ubl C

257 In ubiquitin-like protein (UBL) cascades, a thioester-linke

258 activate a thioester-linked E2 approximately ubiquitin-like protein (UBL) intermediate and promote UB

259 Among these is ISG15, a ubiquitin-like protein (UBL) that can be covalently atta

260 E1 enzymes initiate ubiquitin-like protein (ubl) transfer cascades by cataly

261 of SUMO(KGG) conjugation alone, as no other ubiquitin-like protein (Ubl) yields this adduct upon Lys

262 ISG15 is an interferon-induced and antiviral ubiquitin-like protein (Ubl).

263 be modulated by ligation to ubiquitin or to ubiquitin-like proteins (Ubl proteins).

264 Ubiquitin-like proteins (Ubl's) are conjugated to target

265 modification of proteins with ubiquitin and ubiquitin-like proteins (Ubl) is vital to many cellular

266 E1 enzymes activate ubiquitin or ubiquitin-like proteins (Ubl) via an adenylate intermedi

267 that interacts with RAD52, RAD51, p53, and a ubiquitin-like protein UBL1.

268 It was previously reported that a ubiquitin-like protein, UBL1, associates with RAD51 in t

269 The autophagic ubiquitin-like protein (ublp) autophagy-related (ATG)12

270 enzymes play a central role in ubiquitin and ubiquitin-like protein (ublp) transfer cascades: the E2

271 Post-translational modification by ubiquitin-like proteins (Ublps) is an essential cellular

272 Ubiquitin-like proteins (UBLs) are conjugated by dynamic

273 Ubiquitin (Ub) and ubiquitin-like proteins (Ubls) are conjugated to their t

274 Ubiquitin and ubiquitin-like proteins (UBLs) are directed to targets b

275 Modification of proteins with ubiquitin or ubiquitin-like proteins (UBLs) by means of an E1-E2-E3 c

276 ability to form analogous adducts with other ubiquitin-like proteins (UBLs) catalyzed by their cognat

277 ational covalent attachment of ubiquitin and ubiquitin-like proteins (ubls) has emerged as a predomin

278 ional covalent modification by ubiquitin and ubiquitin-like proteins (UBLs) is a major eukaryotic mec

279 ic machinery via direct interaction with the ubiquitin-like proteins (UBLs) of the Atg8/LC3/GABARAP f

280 The ubiquitin-like proteins (UBLs) that are part of this fam

281 t Smt3 and its vertebrate homolog SUMO-1 are ubiquitin-like proteins (Ubls) that are reversibly ligat

282 Attachment of ubiquitin (Ub) and ubiquitin-like proteins (Ubls) to cellular proteins regu

283 lysed reactions ligating ubiquitin and other ubiquitin-like proteins (Ubls) to substrates.

284 n-activating enzyme, Uba1, and activates two ubiquitin-like proteins (UBLs), ubiquitin and FAT10.

285 modification is conjugation to ubiquitin and ubiquitin-like proteins (UBLs), which controls an enormo

286 e seminal findings of Ohsumi was on the role ubiquitin-like proteins (UBLs)-Atg5, Atg12, and Atg8-pla

287 t steps in conjugation of ubiquitin (Ub) and ubiquitin-like proteins (Ubls).

288 Hub1/Ubl5 is a member of the family of ubiquitin-like proteins (UBLs).

289 ade that catalyzes lipidation of Atg8-family ubiquitin-like proteins (UBLs).

290 Modification of proteins by the ubiquitin-like protein, UFM1, requires activation of UFM

291 Ubiquitin and ubiquitin-like proteins use unique E1, E2, and E3 enzyme

292 lore the set of proteins modified by a small ubiquitin-like protein, we have developed a proteomic ap

293 tiple components of the immunoproteasome and ubiquitin-like proteins were strongly induced by both IF

294 Ubiquilin 1 (UBQLN1) is a ubiquitin-like protein, which has been shown to play a c

295 IFN-stimulatory gene factor 15 (ISG15) is a ubiquitin-like protein, which is conjugated to many cell

296 directly hinders binding of NEMO to ISG15, a ubiquitin-like protein, which we show targets the modifi

297 FAT10 is a TNF-alpha-inducible ubiquitin-like protein with a putative role in immune re

298 Here, we describe a role for ubiquilin-1, a ubiquitin-like protein with the capacity to interact wit

299 ISG15 is an interferon-stimulated, linear di-ubiquitin-like protein, with anti-viral activity.

300 ISG15 is an interferon-stimulated, ubiquitin-like protein, with anti-viral and anti-bacteri