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1 g in aggregate clearance in the absence of a small ubiquitin-like modifier.
3 The BRD, PHD, and ZZ domains interact with small ubiquitin-like modifier 1 (SUMO-1) and Ubc9, and f
6 how that nonvisual arrestins are modified by small ubiquitin-like modifier 1 (SUMO-1) upon activation
7 quitin, it conjugates a ubiquitin homologue, small ubiquitin-like modifier 1 (SUMO-1), also known as
8 nal modification by the ubiquitin homologue, small ubiquitin-like modifier 1 (SUMO-1), has been estab
9 ed that Ubc9, an E2-like enzyme specific for small ubiquitin-like modifier 1 (Sumo-1), is required fo
14 or attachment of the ubiquitin-like protein, small ubiquitin-like modifier-1 (SUMO-1), and the conser
15 we demonstrated that GATA4 is sumoylated by small ubiquitin-like modifier-1 (SUMO-1), which resulted
18 We demonstrate that CBS is modified by the small ubiquitin-like modifier-1 protein (SUMO-I) under b
19 ents with COS-7 cells using PIAS and SUMO-1 (small ubiquitin-like modifier-1) expression vectors.
24 s of full-length histone H2B modified by the small ubiquitin-like modifier-3 (SUMO-3) protein further
26 Reversible modification of proteins by SUMO (small ubiquitin-like modifier) affects a large number of
27 fect of AR SUMOylation (where SUMO indicates small ubiquitin-like modifier) by mutating conserved lys
29 In some cases, the transcription factor is a small ubiquitin-like modifier conjugated directly, thus
30 abrata We identified the enzymes involved in small ubiquitin-like modifier conjugation and show that
33 posttranslational modification by the SUMO (small ubiquitin-like modifier) conjugation pathway is es
35 slation is accompanied by an increase in the small ubiquitin-like modifier-dependent nuclear localiza
36 nt in the cytoplasm and at S phase undergoes small ubiquitin-like modifier-dependent translocation to
38 e of Ubc8 among known ubiquitin E2s, nor the small ubiquitin-like modifier E2 Ubc9 supports protein I
39 n experiments suggest that PIAS3 acts as the small ubiquitin-like modifier E3 ligase for FOXP2 sumoyl
40 s levels of the deSUMOylating (where SUMO is small ubiquitin-like modifier) enzyme SENP1, leading to
41 critical E2-binding surface on the E1 of the small ubiquitin-like modifier has unusually high populat
42 is associated with its conjugation by SUMOs (small ubiquitin-like modifiers) in response to the topo
45 nase C zeta and it's binding to the E3 SUMO (small ubiquitin-like modifier) ligase PIASy (protein inh
46 bers are ubiquitin-protein isopeptide ligase-small ubiquitin-like modifier ligases for diverse transc
47 inhibitor of activated STAT) family of SUMO (small ubiquitin-like modifier) ligases has been implicat
48 tors of Activated STAT 1) and PIAS3 E3 SUMO (small ubiquitin-like modifier)-ligases, at two conserved
49 alate development is beginning to emerge for small ubiquitin-like modifier modification, a widely use
50 argest groups of proteins regulated by SUMO (small ubiquitin-like modifier) modification, and their s
53 riguingly, SUMOylation (where SUMO indicates small ubiquitin-like modifier) of AR inhibits its transc
54 plex, a newly identified player in the SUMO (small ubiquitin-like modifier) pathway, led to increased
55 Post-translational modification by SUMO (small ubiquitin-like modifier) plays important but still
56 all of which are involved in conjugating the small ubiquitin-like modifier polypeptide, SUMO-1, to it
58 c post-translational modification in which a small ubiquitin-like modifier protein (SUMO) is attached
59 ional modification of target proteins by the small ubiquitin-like modifier protein (SUMO) regulates m
61 ggesting that binding of Ubc9 and subsequent small ubiquitin-like modifier protein 1 (SUMO-1) modific
62 lating enzyme CgUlp2 leads to highly reduced small ubiquitin-like modifier protein levels, and impair
63 f the Snf1 catalytic subunt of SNF1 with the small ubiquitin-like modifier protein SUMO, catalyzed by
64 man histone H4 N-terminal tail region by the small ubiquitin-like modifier protein, SUMO-3, is associ
67 tly and reversibly on lysine residues by the small ubiquitin-like modifier proteins termed SUMOs.
68 slational modification of proteins by SUMOs (small ubiquitin-like modifier proteins; SUMOylation).
70 ctive RNA polymerase I transcription and the small ubiquitin-like modifier-specific protease SENP3.
71 hird post-translational modification, by the small ubiquitin like modifier SUMO, is part of the same
72 udy, we have discovered a novel role for the small ubiquitin-like modifier SUMO in the regulation of
77 zed by immunofluorescence with antibodies to small ubiquitin-like modifier (SUMO) 1 localized to nucl
80 tification by mass spectrometry of a site of small ubiquitin-like modifier (SUMO) adduction, Lys-679
81 Dynamic modification of proteins with the small ubiquitin-like modifier (SUMO) affects the stabili
82 4 ICD is posttranslationally modified by the small ubiquitin-like modifier (SUMO) and functionally in
83 .7 was enhanced by conjugation of CRMP2 with small ubiquitin-like modifier (SUMO) and further control
84 neering studies on the interplay between the small ubiquitin-like modifier (SUMO) and influenza A vir
86 of TDG mutants defective for sumoylation and Small Ubiquitin-like Modifier (SUMO) binding and by alte
97 we report that SHMT1 is ubiquitinated at the small ubiquitin-like modifier (SUMO) consensus motif and
98 e show that lysine residues within conserved small ubiquitin-like modifier (SUMO) consensus sites in
99 sin response mediator protein 2 (CRMP2) by a small ubiquitin-like modifier (SUMO) could affect NaV tr
101 study, we found that the SAE2 subunit of the small ubiquitin-like modifier (SUMO) E1 is autoSUMOylate
102 Hsp27 interacted physically with Ubc9, the small ubiquitin-like modifier (SUMO) E2 conjugating enzy
103 tin proteasome system, and expression of the small ubiquitin-like modifier (SUMO) E2 enzyme UBC9 impr
104 evidence establishes that AtSIZ1 is a plant small ubiquitin-like modifier (SUMO) E3 ligase and is a
106 tion factor IIIA (TFIIIA) interacts with the small ubiquitin-like modifier (SUMO) E3 ligase PIAS2b an
107 ligase, we find that TIF1gamma operates as a small ubiquitin-like modifier (SUMO) E3 ligase that prom
108 re, we show that PIAS1, which functions as a small ubiquitin-like modifier (SUMO) E3 ligase, associat
112 , but not C/EBP beta-2, is conjugated to the small ubiquitin-like modifier (SUMO) family members, SUM
113 tional modification in which a member of the small ubiquitin-like modifier (SUMO) family of proteins
114 l to the recognition site for members of the small ubiquitin-like modifier (SUMO) family of ubiquitin
115 oylation involves activation and transfer of small ubiquitin-like modifier (SUMO) from the thioester
116 st-translational modification of proteins by Small Ubiquitin-like Modifier (SUMO) has been reported t
118 osttranslational modification of proteins by small ubiquitin-like modifier (SUMO) has received much a
119 s for the post-translational modification of small ubiquitin-like modifier (SUMO) in regulating the r
120 Here we report that BRCA1 is modified by small ubiquitin-like modifier (SUMO) in response to geno
123 ere we demonstrate that conjugation with the small ubiquitin-like modifier (SUMO) is a novel PTM requ
131 osttranslational modification of proteins by small ubiquitin-like modifier (SUMO) is required for sur
133 slational modification of ZBP-89 by multiple small ubiquitin-like modifier (SUMO) isoforms occurs at
134 single-strand binding protein POT-1, and the small ubiquitin-like modifier (SUMO) ligase GEI-17.
135 nction except for Nse2/Mms21, which is an E3 small ubiquitin-like modifier (SUMO) ligase important fo
137 ultiple subunits and identify SIZ1 as the E3 Small Ubiquitin-like Modifier (SUMO) ligase responsible
138 tein inhibitor of activated STAT1 (PIAS1), a small ubiquitin-like modifier (SUMO) ligase that regulat
139 hat the yeast proline isomerase Fpr3 and the small ubiquitin-like modifier (SUMO) ligase Zip3 ensure
140 transcription) RING domain characteristic of small ubiquitin-like modifier (SUMO) ligases, two struct
143 UBC9 and was a substrate for UBC9-catalyzed small ubiquitin-like modifier (SUMO) modification in vit
144 ey mechanism by which this occurs is through small ubiquitin-like modifier (SUMO) modification of Maf
145 We recently described a critical role for a small ubiquitin-like modifier (SUMO) modification of NF-
151 We show here that BLM is a substrate for small ubiquitin-like modifier (SUMO) modification, with
152 lation of NRL in vivo and in vitro, with two small ubiquitin-like modifier (SUMO) molecules attached
154 dified in vitro and in cultured cells by the Small ubiquitin-like modifier (SUMO) on two independent
155 Here, we show that hypoxia activates the Small Ubiquitin-like Modifier (SUMO) pathway in rat cere
157 mber of the E3 ligase family involved in the small ubiquitin-like modifier (SUMO) pathway, we show fu
161 osttranslational modification of proteins by small ubiquitin-like modifier (SUMO) plays essential rol
164 ing evolution, the enzyme Ubc9 activates the small ubiquitin-like modifier (SUMO) prior to its covale
165 ve analyzed the mitotic function of SENP6, a small ubiquitin-like modifier (SUMO) protease that disas
170 eins both as targets for modification by the small ubiquitin-like modifier (SUMO) protein and as cata
172 this process, an extremely limited number of small ubiquitin-like modifier (SUMO) protein ligases (E3
173 a proportion of DELLAs is conjugated to the Small Ubiquitin-like Modifier (SUMO) protein, the extent
174 cation pathway catalyzing the conjugation of small ubiquitin-like modifier (SUMO) proteins (SUMO1, SU
178 t posttranslational modification of Kv1.5 by small ubiquitin-like modifier (SUMO) proteins modulates
181 ovalent modification of cellular proteins by small ubiquitin-like modifier (SUMO) proteins, regulates
186 karyotes, the conjugation of proteins to the small ubiquitin-like modifier (SUMO) regulates numerous
187 Structural studies of the E1 for the Ubl small ubiquitin-like modifier (SUMO) revealed a single a
188 of this particular antiviral response is the small ubiquitin-like modifier (SUMO) signaling pathway.
191 ols has allowed elucidation and study of the small ubiquitin-like modifier (SUMO) system in this unic
193 jugating enzyme that transfers the activated small ubiquitin-like modifier (SUMO) to protein substrat
196 how that MEL-18 is able to interact with the small ubiquitin-like modifier (SUMO) ubiquitin carrier p
198 When a transcription factor is modified by small ubiquitin-like modifier (SUMO), this usually repre
199 sites of post-translational modification by small ubiquitin-like modifier (SUMO), we have examined w
201 global hyposumoylation and redistribution of small ubiquitin-like modifier (SUMO)-1 conjugates into d
202 n this study, we determined the occupancy of Small Ubiquitin-like MOdifier (SUMO)-1 on chromatin in H
203 t of Htt (Httex1p) can be modified either by small ubiquitin-like modifier (SUMO)-1 or by ubiquitin o
210 ntification of Ubc9 and PIASy, the E2 and E3 small ubiquitin-like modifier (SUMO)-conjugating enzymes
212 nts a class of ubiquitin ligases that target Small Ubiquitin-like Modifier (SUMO)-modified proteins f
213 on, we used de-SUMOylation enzyme of sentrin/Small Ubiquitin-like MOdifier (SUMO)-specific protease 2
215 s, both of which are implicated in ubiquitin/small ubiquitin-like modifier (SUMO)-targeted protein de
217 we demonstrate that RNF4, a highly conserved small ubiquitin-like modifier (SUMO)-targeted ubiquitin
223 undergoes PML-dependent hyper-sumoylation by small ubiquitin-like modifier (SUMO)2/3 but not SUMO1, u
225 nhibitory and transrepressor activities to a small ubiquitin-like modifier (SUMO-1) protein consensus
228 ting macrophages, some IRF8 is conjugated to small ubiquitin-like modifiers (SUMO) 2/3 through the ly
230 ough post-translational modifications by the small ubiquitin-like modifiers (SUMO) are known to be im
231 lved the crystal structure of the E2 for the small ubiquitin-like modifiers (SUMO) in complex with an
235 nslational modification of substrates by the small ubiquitin-like modifier, SUMO, regulates diverse b
237 e we analyzed the modification of PKR by the small ubiquitin-like modifiers SUMO1 and SUMO2 and evalu
238 show that FXR is covalently modified by the small ubiquitin-like modifier (Sumo1), an important regu
241 , whether human septins could be modified by small ubiquitin-like modifiers (SUMOs) and what roles th
246 sttranslational modifications of proteins by small ubiquitin-like modifiers (SUMOs) regulate protein
247 sites and conjugates these proteins with the small ubiquitin-like modifiers (SUMOs) through its SUMO
251 We have previously described a role for the small ubiquitin-like modifier type 1 (SUMO-1) as a regul
252 orm-alpha (HSP90-SUMO1, where SUMO indicates small ubiquitin-like modifier), while no reactivity with
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