| URN | urn:agi-ProtModification:inout-urn:agi-llid:4193:out-urn:agi-llid:7157::negative:ubiquitination |
|---|---|
| References | 100 |
| Connectivity | 2 |
| Effect | negative |
| Mechanism | ubiquitination |
| Original # of References | 122 |
| TextRef | info:pmid/19880522#abs:10 |
|---|---|
| PubYear | 2010 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 19880522:9 |
| Sentence | Pyk2 FERM promoted Mdm2-dependent p53 ubiquitination. |
| CellType | Fibroblasts |
| TextRef | info:pmid/20124408#abs:8 |
|---|---|
| PubYear | 2010 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 20124408:7 |
| Sentence | In addition to reactivating mutant p53, SCH529074 binding inhibits ubiquitination of p53 by HDM2. |
| TextRef | info:pmid/17585950#abs:5 |
|---|---|
| PubYear | 2007 |
| MedlineTA | Math Biosci |
| MedLine Reference | 17585950:4 |
| Sentence | The model predicts existence of the HAUSP-regulated switch from auto- to p53 ubiquitination by Mdm2. |
| TextRef | info:pmid/12860999#abs:2 |
|---|---|
| PubYear | 2003 |
| MedlineTA | Mol Cell Biol |
| MedLine Reference | 12860999:1 |
| Sentence | Mitogenic signals activate p53 by induction of ARF expression, which inhibits p53 ubiquitination by MDM2. |
| TextRef | info:pmid/19756449#abs:3 |
|---|---|
| PubYear | 2009 |
| MedlineTA | J Mol Med |
| MedLine Reference | 19756449:2 |
| Sentence | In the present paper, we demonstrate that Sgk1 activates MDM2-dependent p53 ubiquitylation. |
| Tissue | Serum |
| TextRef | info:pmid/12690203#abs:3 |
|---|---|
| PubYear | 2003 |
| MedlineTA | Science |
| MedLine Reference | 12690203:2 |
| Sentence | In vitro, p300 with MDM2 catalyzed p53 polyubiquitination, whereas MDM2 catalyzed p53 monoubiquitination. |
| TextRef | info:pmid/17500067#abs:3 |
|---|---|
| PubYear | 2007 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 17500067:2 |
| Sentence | In addition to proteasome-mediated degradation, ubiquitination of p53 by Mdm2 acts a key signal for its nuclear export. |
| TextRef | info:pmid/11960383#abs:1 |
|---|---|
| PubYear | 2002 |
| MedlineTA | Oncogene |
| MedLine Reference | 11960383:0 |
| Sentence | Mutation of four lysine residues in the p53 C-terminal domain inhibits MDM2-dependent ubiquitination of p53 and alters its subcellular distribution. |
| TextRef | info:pmid/11707453#abs:2 |
|---|---|
| PubYear | 2002 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 11707453:1 |
| Sentence | Following DNA damage or cellular stress, p53 is phosphorylated within the Mdm2 binding domain on threonine 18 and serine 20. |
| TextRef | info:pmid/16857591#abs:1 |
|---|---|
| PubYear | 2006 |
| MedlineTA | Mol Cell |
| MedLine Reference | 16857591:0 |
| Sentence | The control of p53 ubiquitination by MDM2 provides a model system to define how an E3-ligase functions on a conformationally flexible substrate. |
| TextRef | info:pmid/12407176#abs:1 |
|---|---|
| PubYear | 2002 |
| MedlineTA | Proc Natl Acad Sci U S A |
| MedLine Reference | 12407176:0 |
| Sentence | The oncoprotein hdm2 ubiquitinates p53, resulting in the rapid degradation of p53 through the ubiquitin -proteasome pathway. |
| TextMods | 104: '(Ub)' -> '' |
| TextRef | info:pmid/17237821#abs:5 |
|---|---|
| PubYear | 2007 |
| MedlineTA | Oncogene |
| MedLine Reference | 17237821:4 |
| Sentence | In the present study, we show that TAFII250 stimulates the ubiquitylation and degradation of p53 in a manner that is dependent upon Mdm2 and requires its acidic domain. |
| TextRef | info:pmid/11127820#abs:7 |
|---|---|
| PubYear | 2000 |
| MedlineTA | Oncogene |
| MedLine Reference | 11127820:6 |
| Sentence | In addition, an MDM2-mutant that localized to the cytoplasm was able to ubiquitinate and degrade a p53 mutant which was similarly localized in the cytoplasm. |
| TextRef | info:pmid/12426395#abs:4 |
|---|---|
| PubYear | 2002 |
| MedlineTA | EMBO J |
| MedLine Reference | 12426395:3 |
| Sentence | Ectopic expression of a dominant-negative HDAC1 mutant restores p53 acetylation in the presence of MDM2, whereas wild-type HDAC1 and MDM2 deacetylate p53 synergistically. |
| TextRef | info:pmid/15542844#abs:8 |
|---|---|
| PubYear | 2004 |
| MedlineTA | Mol Cell Biol |
| MedLine Reference | 15542844:7 |
| Sentence | VRK1 phosphorylates human p53 in Thr18 and disrupts p53-Mdm2 interaction in vitro, although a significant decrease in p53 ubiquitination by Mdm2 in vivo was not detected. |
| TextRef | info:pmid/20303977#abs:1 |
|---|---|
| PubYear | 2010 |
| MedlineTA | J Mol Biol |
| MedLine Reference | 20303977:0 |
| Sentence | The multidomain E3 ubiquitin ligase MDM2 catalyzes p53 ubiquitination by a "dual-site" docking mechanism whereby MDM2 binding to at least two distinct peptide motifs on p53 promotes ubiquitination. |
| TextRef | info:pmid/11925449#abs:5 |
|---|---|
| PubYear | 2002 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 11925449:4 |
| Sentence | Mutation of conserved amino acids in the linker at Ser(261) and Leu(264), which bridges the S9-S10 beta-sheets, stimulated p53 activity from reporter templates and increased MDM2-dependent ubiquitination of p53. |
| TextRef | info:pmid/11779115#abs:3 |
|---|---|
| PubYear | 2002 |
| MedlineTA | Anal Biochem |
| MedLine Reference | 11779115:2 |
| Sentence | One mechanism of regulating the amount of p53 in the cell is through the action of the Double Minute 2 protein, DM2 (also known as MDM2), which ubiquitinates p53 and targets it for proteosomal degradation. |
| TextRef | info:pmid/19217357#abs:5 |
|---|---|
| PubYear | 2009 |
| MedlineTA | DNA Repair (Amst) |
| MedLine Reference | 19217357:4 |
| Sentence | In this review we summarize current understanding on p53 ubiquitination by Mdm2 with a particular focus on how the balance between protein levels and other post-translational modifications will direct the p53 response. |
| TextRef | info:pmid/17989425#abs:9 |
|---|---|
| PubYear | 2007 |
| MedlineTA | J Biomol Screen |
| MedLine Reference | 17989425:8 |
| Sentence | The authors describe the development, validation, and execution of a high-throughput screening measuring the ubiquitination of p53 by mdm2, with p53 labeled with europium and the other substrate (Ub-UbcH5b) labeled with a Cy5 on the ubiquitin. |
| TextRef | info:pmid/18333294#abs:8 |
|---|---|
| PubYear | 2008 |
| MedlineTA | Cell Cycle |
| MedLine Reference | 18333294:7 |
| Sentence | We have recently shown that Wip1, also a p53 target gene, dephosphorylates Mdm2 at Ser395 (an ATM target site), resulting in stabilization of Mdm2, enhanced Mdm2-p53 binding, and enhanced ubiquitination of p53 by Mdm2. |
| TextRef | info:pmid/17369817#abs:2 |
|---|---|
| PubYear | 2007 |
| MedlineTA | Nat Cell Biol |
| MedLine Reference | 17369817:1 |
| Sentence | One of the most important regulators of p53 is MDM2, a RING domain E3 ligase that ubiquitinates p53, leading to both proteasomal degradation and relocation of p53 from the nucleus to the cytoplasm. |
| TextRef | info:pmid/19303885#abs:8 |
|---|---|
| PubYear | 2009 |
| MedlineTA | J Mol Biol |
| MedLine Reference | 19303885:7 |
| Sentence | Thus, the results presented here for the first time highlight the role of SMAR1 in masking the active phosphorylation site of p53, enabling the deacetylation of p53 by HDAC1-MDM2 complex, thereby regulating the p53 transcriptional response during stress rescue. |
| TextRef | info:pmid/20657550#abs:1 |
|---|---|
| PubYear | 2010 |
| MedlineTA | EMBO J |
| MedLine Reference | 20657550:0 |
| Sentence | p53 mediates DNA damage-induced cell-cycle arrest, apoptosis, or senescence, and it is controlled by Mdm2, which mainly ubiquitinates p53 in the nucleus and promotes p53 nuclear export and degradation. |
| TextRef | info:pmid/19202598#abs:4 |
|---|---|
| PubYear | 2008 |
| MedlineTA | Ernst Schering Found Symp Proc |
| MedLine Reference | 19202598:3 |
| Sentence | Notably, recent studies indicate that both the stability and the subcellular localization of p53 are tightly regulated by ubiquitination; p53 is mainly ubiquitinated by Mdm2 but other ubiquitin ligases such as ARF-BP1/HectH9/MULE are also involved in p53 regulation in vivo. |
| TextRef | info:pmid/15946545#abs:5 |
|---|---|
| PubYear | 2005 |
| MedlineTA | Zhonghua Zhong Liu Za Zhi |
| MedLine Reference | 15946545:4 |
| Sentence | p53KRKKK-GFP was located in cytoplasm, and was not degraded by either MDM2 or MDM2-nuclear localization signal mutation, but could be ubiquitinated; p53KRKKK-nuclear localization signal-GFP could be brought back to nucleus by SV-40 nuclear localization signal, so could be both degraded and ubiquitinated by either MDM2 or MDM2-nuclear localization signal; Wild type p53 and mutant nuclear localization signal could be ubiquitinated by either wild type MDM2 or mutant nuclear localization signal. |
| TextMods | 83: 'NLS ' -> 'nuclear localization signal ' 158: 'NLS' -> 'nuclear localization signal' 232: 'NLS' -> 'nuclear localization signal' 328: 'NLS' -> 'nuclear localization signal' 382: 'NLS ' -> 'nuclear localization signal ' 468: 'NLS' -> 'nuclear locali... |
| TextRef | info:pmid/9878046#body:47 |
|---|---|
| PubYear | 1999 |
| MedlineTA | EMBO J |
| MedLine Reference | 9878046:1046 |
| Sentence | Ubiquitination of wild-type p53 by Mdm2 . |
| TextRef | info:pmid/16446403#body:115 |
|---|---|
| PubYear | 2006 |
| MedlineTA | Mol Cancer Res |
| MedLine Reference | 16446403:1114 |
| Sentence | MDM2-dependent p53 ubiquitination and degradation assays. |
| TextRef | info:pmid/12586367#title:1 |
|---|---|
| PubYear | 2003 |
| MedLine Reference | 12586367:100 |
| Sentence | Differences in the ubiquitination of p53 by Mdm2 and the HPV protein E6. |
| TextRef | info:pmid/18234968#body:191 |
|---|---|
| PubYear | 2008 |
| MedlineTA | Mol Cancer Res |
| MedLine Reference | 18234968:1190 |
| Sentence | SS18-SSX1-induced p53 ubiquitination is dependent on HDM2. |
| TextRef | info:pmid/15122315#body:193 |
|---|---|
| PubYear | 2004 |
| MedlineTA | Oncogene |
| MedLine Reference | 15122315:1192 |
| Sentence | Thus, only in HIPK2-interfered cells p53 is ubiquitinated by MDM2. |
| TextRef | info:pmid/11807090#body:266 |
|---|---|
| PubYear | 2002 |
| MedlineTA | J Cell Biol |
| MedLine Reference | 11807090:1265 |
| Sentence | MDM2 ubiquitinates itself as well as p53 (Fang et al., 2000). |
| Organ | Fingers |
| TextRef | info:pmid/16023600#body:221 |
|---|---|
| PubYear | 2005 |
| MedlineTA | Cancer Cell |
| MedLine Reference | 16023600:1220 |
| Sentence | Gankyrin enhances the Mdm2-dependent ubiquitylation of p53 . |
| Organ | Fingers |
| TextRef | info:pmid/11486026#body:343 |
|---|---|
| PubYear | 2001 |
| MedlineTA | Mol Cell Biol |
| MedLine Reference | 11486026:1342 |
| Sentence | How does c-Abl impair the ubiquitination of p53 by E6-E6-AP and by Mdm2? |
| TextRef | info:pmid/15577944#body:126 |
|---|---|
| PubYear | 2005 |
| MedlineTA | EMBO J |
| MedLine Reference | 15577944:1125 |
| Sentence | Ubiquitination of p53 by Mdm2 was also negatively regulated by ARF in vivo (data not shown). |
| TextRef | info:pmid/11250899#body:160 |
|---|---|
| PubYear | 2001 |
| MedlineTA | EMBO J |
| MedLine Reference | 11250899:1159 |
| Sentence | Fig. 5. p19ARF reverses the inhibition of p53 acetylation by MDM2. |
| CellLineName | H1299 |
| TextRef | info:pmid/19147532#body:211 |
|---|---|
| PubYear | 2009 |
| MedlineTA | Mol Cancer Res |
| MedLine Reference | 19147532:1210 |
| Sentence | Additional strategies to prevent Mdm2-dependent ubiquitination of p53 have also been explored. |
| TextRef | info:pmid/15021897#body:224 |
|---|---|
| PubYear | 2004 |
| MedlineTA | Oncogene |
| MedLine Reference | 15021897:1223 |
| Sentence | One attractive strategy to inhibit ubiquitination of p53 by Mdm2 is to block their interaction. |
| TextRef | info:pmid/14757841#body:339 |
|---|---|
| PubYear | 2004 |
| MedlineTA | Mol Cancer Res |
| MedLine Reference | 14757841:1338 |
| Sentence | Moreover, ubiquitination of p53 by Mdm2 is not sufficient to catalyze its degradation (99, 100). |
| TextRef | info:pmid/14707282#body:58 |
|---|---|
| PubYear | 2003 |
| MedlineTA | Mol Cancer Res |
| MedLine Reference | 14707282:1057 |
| Sentence | MDM2 functions as the E3 ligase to ubiquitinate p53 at several lysine residues (10, 11). |
| TextRef | info:pmid/14612427#body:152 |
|---|---|
| PubYear | 2003 |
| MedlineTA | Mol Cell Biol |
| MedLine Reference | 14612427:1151 |
| Sentence | HDM2 functions as an E3 ligase to ubiquitinate p53 and promotes p53 degradation (11). |
| TextRef | info:pmid/10626788#body:215 |
|---|---|
| PubYear | 1999 |
| MedlineTA | Cancer Res |
| MedLine Reference | 10626788:1214 |
| Sentence | Thus, p53 phosphorylation may inhibit the efficient ubiquitination of p53 by residual MDM2 protein. |
| TextRef | info:pmid/11313871#body:159 |
|---|---|
| PubYear | 2001 |
| MedlineTA | Oncogene |
| MedLine Reference | 11313871:1158 |
| Sentence | MDM2 possess E3 ligase activity and catalyses its own and p53 ubiquitylation (Fang et al., 2000). |
| TextRef | info:pmid/16107876#body:270 |
|---|---|
| PubYear | 2005 |
| MedlineTA | EMBO J |
| MedLine Reference | 16107876:1269 |
| Sentence | Ubiquitination of p53 by MDM2 is a major mechanism by which p53 level is regulated in the cell. |
| CellLineName | HT 1080 |
| TextRef | info:pmid/15604276#body:228 |
|---|---|
| PubYear | 2004 |
| MedlineTA | Cancer Res |
| MedLine Reference | 15604276:1227 |
| Sentence | Interestingly, the authors observed that E1A stabilizes p53 without interfering p53 ubiquitination by Mdm2 (27) . |
| TextRef | info:pmid/14612423#body:230 |
|---|---|
| PubYear | 2003 |
| MedlineTA | Mol Cell Biol |
| MedLine Reference | 14612423:1229 |
| Sentence | The effects of the LXXLL and PXXP-GFP fusion proteins on MDM2-dependent ubiquitination of p53 were also examined (Fig. 4G). |
| TextRef | info:pmid/12370303#body:236 |
|---|---|
| PubYear | 2002 |
| MedlineTA | Mol Cell Biol |
| MedLine Reference | 12370303:1235 |
| Sentence | This inhibitory effect may not be directly reversed by ARF, since ARF mainly acts by inhibiting p53 ubiquitination by MDM2. |
| TextRef | info:pmid/16636310#body:66 |
|---|---|
| PubYear | 2006 |
| MedlineTA | Exp Biol Med (Maywood) |
| MedLine Reference | 16636310:1065 |
| Sentence | Although Mdm2 catalyzes p53 monoubiquitination (12), the product is not a substrate for proteasome degradation. |
| TextRef | info:pmid/16024788#body:67 |
|---|---|
| PubYear | 2005 |
| MedlineTA | Mol Cell Biol |
| MedLine Reference | 16024788:1066 |
| Sentence | Interestingly, ARF inhibits the ability of MDM2 to ubiquitinate p53 but stimulates MDM2 ubiquitination of MDMX (31). |
| TextRef | info:pmid/12202042#title:1 |
|---|---|
| PubYear | 2002 |
| MedLine Reference | 12202042:100 |
| Sentence | SUMO-1 modification of Mdm2 prevents its self-ubiquitination and increases Mdm2 ability to ubiquitinate p53. |
| TextRef | info:pmid/10892746#title:1 |
|---|---|
| PubYear | 2000 |
| MedLine Reference | 10892746:100 |
| Sentence | SUMO-1 modification of Mdm2 prevents its self-ubiquitination and increases Mdm2 ability to ubiquitinate p53. |
| TextRef | info:pmid/16163388#body:66 |
|---|---|
| PubYear | 2005 |
| MedlineTA | EMBO J |
| MedLine Reference | 16163388:1065 |
| Sentence | ARF inhibits the ability of MDM2 to ubiquitinate p53, but stimulates MDM2 ubiquitination of MDMX (Pan and Chen, 2003). |
| TextRef | info:pmid/11744695#body:141 |
|---|---|
| PubYear | 2002 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 11744695:1140 |
| Sentence | In these conditions, Hdmx did not detectably change the overall pattern of Hdm2-dependent ubiquitination of p53. |
| Organ | Fingers |
| TextRef | info:pmid/17908790#body:230 |
|---|---|
| PubYear | 2007 |
| MedlineTA | Mol Cell Biol |
| MedLine Reference | 17908790:1229 |
| Sentence | Our results so far showed that Mdm2 ubiquitinated mutant p53 less efficiently than wild-type p53 in vitro. |
| CellType | Fibroblasts |
| TextRef | info:pmid/15775960#body:216 |
|---|---|
| PubYear | 2005 |
| MedlineTA | EMBO J |
| MedLine Reference | 15775960:1215 |
| Sentence | In the presence of Mdm2, there is a dramatic increase in the levels of NEDDylated and ubiquitinated p53 (Figure 5). |
| CellLineName | H1299 |
| TextRef | info:pmid/12493762#body:59 |
|---|---|
| PubYear | 2003 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 12493762:1058 |
| Sentence | MDM2 possesses an E3-like ubiquitin ligase activity and thus ubiquitinates p53 (25), leading to its degradation (26, 27). |
| TextRef | info:pmid/11046142#body:193 |
|---|---|
| PubYear | 2000 |
| MedlineTA | Mol Cell Biol |
| MedLine Reference | 11046142:1192 |
| Sentence | Glutathione S-transferase (more ...). p53 C-terminal lysine residues are targets for Mdm2-dependent ubiquitination of p53. |
| TextMods | 0: 'GST ' -> 'Glutathione S-transferase ' |
| TextRef | info:pmid/17098746#body:223 |
|---|---|
| PubYear | 2007 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 17098746:1222 |
| Sentence | Mdm2 ubiquitinates p53 on six C-terminal lysines and targets it to the proteasome for degradation (4, 5). |
| CellLineName | H1299 |
| TextRef | info:pmid/16455486#body:91 |
|---|---|
| PubYear | 2006 |
| MedlineTA | Mol Cell |
| MedLine Reference | 16455486:1090 |
| Sentence | Mdm2 was recently found to differentially catalyze monoubiquitination and polyubiquitination of p53 in a dosage-dependent manner (Li et al., 2003). |
| TextRef | info:pmid/12509446#body:39 |
|---|---|
| PubYear | 2003 |
| MedlineTA | Mol Cell Biol |
| MedLine Reference | 12509446:1038 |
| Sentence | In addition, p90 MDM2 ubiquitinates p53, stimulating its export from the nucleus (8, 50) as well as its degradation (15, 18, 27). |
| TextRef | info:pmid/17015431#body:48 |
|---|---|
| PubYear | 2006 |
| MedlineTA | Genes Dev |
| MedLine Reference | 17015431:1047 |
| Sentence | Furthermore, ubiquitination of p53 by Mdm2 expels p53 from the nucleus, keeping it away from its transcriptional targets. |
| TextRef | info:pmid/15053880#body:66 |
|---|---|
| PubYear | 2004 |
| MedlineTA | Mol Cell |
| MedLine Reference | 15053880:1065 |
| Sentence | DNA Repair [Close]. [You are not entitled to access the full text of this document] p53 ubiquitination by Mdm2: A never ending tail? |
| TextRef | info:pmid/14654783#body:242 |
|---|---|
| PubYear | 2003 |
| MedlineTA | Oncogene |
| MedLine Reference | 14654783:1241 |
| Sentence | In fact, Mdm2-dependent multiple monoubiquitination of p53 is responsible for its nuclear export (Gu et al., 2001; Lohrum et al., 2001). |
| Organ | Fingers |
| TextRef | info:pmid/16805769#body:86 |
|---|---|
| PubYear | 2006 |
| MedlineTA | J Neurochem |
| MedLine Reference | 16805769:1085 |
| Sentence | This degradation is largely regulated by Mdm2, an E3 ubiquitin ligase that binds to and ubiquitinates p53, thus targeting it for degradation. |
| TextRef | info:pmid/12421820#body:107 |
|---|---|
| PubYear | 2002 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 12421820:1106 |
| Sentence | To provide the direct evidence that acetylation of p53 affects its ubiquitination, we set up a reconstitution system for p53 ubiquitination by Mdm2. |
| TextRef | info:pmid/19648273#body:70 |
|---|---|
| PubYear | 2009 |
| MedlineTA | J Immunol |
| MedLine Reference | 19648273:1069 |
| Sentence | Additionally, as an E3 ligase, MDM2 ubiquitinates p53, inducing its nuclear export and proteosomal degradation (21, 22). |
| CellType | B-Lymphocytes |
| Organ | germinal center of lymph node |
| TextRef | info:pmid/15888490#body:137 |
|---|---|
| PubYear | 2005 |
| MedlineTA | Carcinogenesis |
| MedLine Reference | 15888490:1136 |
| Sentence | Ubiquitination of p53 by Mdm2, therefore, appears to have two roles, targeting of p53 to the proteasome for degradation and nuclear export. |
| TextRef | info:pmid/12917636#body:54 |
|---|---|
| PubYear | 2003 |
| MedlineTA | Oncogene |
| MedLine Reference | 12917636:1053 |
| Sentence | Therefore, the C-terminal region of ARF including the nucleolar localization signal is not essential for regulation of p53 ubiquitination by MDM2. |
| TextMods | 54: 'NoLS ' -> 'nucleolar localization signal ' |
| TextRef | info:pmid/12802279#body:42 |
|---|---|
| PubYear | 2003 |
| MedlineTA | Oncogene |
| MedLine Reference | 12802279:1041 |
| Sentence | Under normal conditions, Mdm2, which possesses E3 ubiquitin ligase activity, ubiquitinates and targets nuclear p53 for degradation (Vousden et al., 2000). |
| TextRef | info:pmid/17429071#body:337 |
|---|---|
| PubYear | 2007 |
| MedlineTA | Mol Biol Cell |
| MedLine Reference | 17429071:1336 |
| Sentence | These observations have clearly demonstrated that TGF-β resistance can be uncoupled with the ability of MDM2 to ubiquitinate and degrade p53. |
| Organ | Fingers |
| TextRef | info:pmid/14707283#body:70 |
|---|---|
| PubYear | 2003 |
| MedlineTA | Mol Cancer Res |
| MedLine Reference | 14707283:1069 |
| Sentence | In vitro, p300 with MDM2 catalyzed p53 polyubiquitination, whereas MDM2 alone only catalyzed p53 monoubiquitination. |
| Organ | Fingers |
| TextRef | info:pmid/18483214#body:78 |
|---|---|
| PubYear | 2008 |
| MedlineTA | Genes Dev |
| MedLine Reference | 18483214:1077 |
| Sentence | On the other hand, Mdm2 has been reported to ubiquitinate and degrade tumor-derived mutant forms of p53 (Midgley and Lane 1997; Shimizu et al. 2006). |
| TextRef | info:pmid/17170702#body:134 |
|---|---|
| PubYear | 2007 |
| MedlineTA | EMBO J |
| MedLine Reference | 17170702:1133 |
| Sentence | As a positive control, p53 was ubiquitinated by MDM2 in an in vivo ubiquitination assay (Figure 5C) (Haupt et al, 1997; Kubbutat et al, 1997). [Figure 5]. |
| Organ | Fingers |
| TextRef | info:pmid/18206965#body:120 |
|---|---|
| PubYear | 2008 |
| MedlineTA | Mol Cell |
| MedLine Reference | 18206965:1119 |
| Sentence | We show that FAK inactivates p53 in a kinase-independent manner via the FAK FERM domain acting as a scaffold to enhance Mdm2-dependent p53 ubiquitination. |
| TextRef | info:pmid/11711428#body:37 |
|---|---|
| PubYear | 2001 |
| MedlineTA | Genes Dev |
| MedLine Reference | 11711428:1036 |
| Sentence | The best characterized negative regulator of p53 is Mdm2, which ubiquitinates p53 and targets its proteolytic destruction (Prives 1998;Juven-Gershon and Oren 1999). |
| TextRef | info:pmid/18566590#body:225 |
|---|---|
| PubYear | 2008 |
| MedlineTA | EMBO J |
| MedLine Reference | 18566590:1224 |
| Sentence | Intriguingly, the balance between self- and p53-ubiquitinating activities of MDM2 can be regulated by the combined actions of DAXX and HAUSP (Tang et al, 2006). |
| TextRef | info:pmid/17875722#body:67 |
|---|---|
| PubYear | 2007 |
| MedlineTA | Cancer Res |
| MedLine Reference | 17875722:1066 |
| Sentence | However, MDMX forms heterodimers with MDM2 through COOH-terminal RING domain interactions, which stimulates the ability of MDM2 to ubiquitinate and degrade p53 (10-13). |
| TextRef | info:pmid/11070080#body:224 |
|---|---|
| PubYear | 2000 |
| MedlineTA | Proc Natl Acad Sci U S A |
| MedLine Reference | 11070080:1223 |
| Sentence | By this rationale, inhibition of p300-mediated p53 acetylation by MDM2 would result in more efficient ubiquitination, consequently leading to the degradation of p53. |
| TextRef | info:pmid/12612087#body:234 |
|---|---|
| PubYear | 2003 |
| MedlineTA | Mol Cell Biol |
| MedLine Reference | 12612087:1233 |
| Sentence | MDM2 binds to the N-terminal transactivation domain of p53 with its p53-binding domain, and the RING domain of MDM2 catalyses the ubiquitination of p53 (13). |
| TextRef | info:pmid/11175334#body:144 |
|---|---|
| PubYear | 2000 |
| MedlineTA | Oncogene |
| MedLine Reference | 11175334:1143 |
| Sentence | Mdm-2 may contribute to this process by ubiquitinating p53 in vivo, since Mdm-2 can act as a ubiquitin ligase ES for p53 in vitro (Honda et al., 1997). |
| CellLineName | BV-173 |
| TextRef | info:pmid/12232053#body:161 |
|---|---|
| PubYear | 2002 |
| MedlineTA | Proc Natl Acad Sci U S A |
| MedLine Reference | 12232053:1160 |
| Sentence | The tumor suppressor p53 is a short-lived protein that accumulates after different stress signals that decrease the ability of Mdm-2 to ubiquitinate p53. |
| CellType | thymocytes |
| Organ | Bone Marrow |
| TextRef | info:pmid/19033443#body:261 |
|---|---|
| PubYear | 2009 |
| MedlineTA | J Biol Chem |
| MedLine Reference | 19033443:1260 |
| Sentence | Ubiquitination assays show that although both Mdm2 and MSL2 are able to ubiquitinate wild type p53 (Fig. 8B, lanes 3 and 4), only MSL2 is able to ubiquitinate p53Q22/23S (Fig. 8B, lane 7). |
| TextMods | 159: 'p53QS ' -> 'p53Q22/23S ' |
| TextRef | info:pmid/20348954#body:190 |
|---|---|
| PubYear | 2010 |
| MedlineTA | Oncogene |
| MedLine Reference | 20348954:1189 |
| Sentence | MDM2 is one of the E3 ligases in the ubiquitin-proteasome system and is known to ubiquitinate and degrade p53 tumor suppressor. |
| Tissue | Blood |
| Organ | Gastrointestinal tract |
| TextRef | info:pmid/18172009#body:58 |
|---|---|
| PubYear | 2008 |
| MedlineTA | Mol Cell Biol |
| MedLine Reference | 18172009:1057 |
| Sentence | MDMX forms heterodimers with MDM2 through C-terminal RING domain interactions (40, 47), which stimulates the ability of MDM2 to ubiquitinate and degrade p53 (16, 26). |
| CellType | Fibroblasts |
| Organism | Mus musculus |
| TextRef | info:pmid/16227412#body:159 |
|---|---|
| PubYear | 2005 |
| MedlineTA | Mol Cancer Ther |
| MedLine Reference | 16227412:1158 |
| Sentence | Western blot analysis showed distinctly elevated levels of p53, p53 phosphorylated on Ser15, and MDM2 as early as 3 hours after the initiation of treatment with WMC-79. |
| CellLineName | RKO |
| TextRef | info:pmid/16023592#body:66 |
|---|---|
| PubYear | 2005 |
| MedlineTA | Cancer Cell |
| MedLine Reference | 16023592:1065 |
| Sentence | Compelling data are provided showing that this interaction occurs naturally between endogenous gankyrin and MDM2 and that gankyrin enhances the ability of MDM2 to ubiquitinate p53. |
| TextRef | info:pmid/11593391#body:79 |
|---|---|
| PubYear | 2001 |
| MedlineTA | Oncogene |
| MedLine Reference | 11593391:1078 |
| Sentence | For example, direct modification of p90 MDM2 by the small protein SUMO-1 has been shown to reduce p90 MDM2's ability to ubiquitinate p53 (Buschmann et al., 2000). |
| CellType | Fibroblasts |
| Organism | Homo sapiens |
| TextRef | info:pmid/11331246#body:275 |
|---|---|
| PubYear | 2001 |
| MedlineTA | Cell Growth Differ |
| MedLine Reference | 11331246:1274 |
| Sentence | Reversal of the MDM2-mediated inhibition of p53 acetylation by ARF without a detectable dissociation of the MDM2-p53 complex would be consistent with such a possibility (62) . |
| CellLineName | saos-2 |
| TextRef | info:pmid/11861407#body:274 |
|---|---|
| PubYear | 2002 |
| MedlineTA | Cancer Res |
| MedLine Reference | 11861407:1273 |
| Sentence | Therefore, induction of p53 in cells overexpressing the growth-inhibitory Mdm2 variants is not likely to be attributable to their ability to directly inhibit p53 ubiquitination by full-length Mdm2. |
| TextRef | info:pmid/14707285#body:83 |
|---|---|
| PubYear | 2003 |
| MedlineTA | Mol Cancer Res |
| MedLine Reference | 14707285:1082 |
| Sentence | This is particularly interesting given that ARF blocks the ubiquitination of p53 by MDM2 and is consistent with the idea that SUMO and ubiquitin modifications may be mutually exclusive and/or antagonistic. |
| TextRef | info:pmid/18541670#body:191 |
|---|---|
| PubYear | 2008 |
| MedlineTA | Mol Cell Biol |
| MedLine Reference | 18541670:1190 |
| Sentence | Therefore, the point mutations in the Nbs1 binding domain that inhibited Mdm2-Nbs1 association did not disrupt the interaction of Mdm2 with ARF or the ability of Mdm2 to ubiquitinate p53. |
| TextRef | info:pmid/15933712#body:119 |
|---|---|
| PubYear | 2005 |
| MedlineTA | EMBO J |
| MedLine Reference | 15933712:1118 |
| Sentence | Indeed, the stability of the tumor suppressor is mainly controlled by MDM2, which ubiquitinates p53 at these residues, thereby targeting it for degradation (Michael and Oren, 2003). |
| CellLineName | H1299 |
| TextRef | info:pmid/12832479#body:234 |
|---|---|
| PubYear | 2003 |
| MedlineTA | Mol Cell Biol |
| MedLine Reference | 12832479:1233 |
| Sentence | In summary, our data uncover the central acidic domain of MDM2 as an additional essential contributor, apart from the ring-finger domain, to MDM2-dependent p53 ubiquitination. |
| TextMods | 41: 'AD ' -> 'acidic domain ' 118: 'RFD' -> 'ring-finger domain' |
| Organ | Fingers |
| TextRef | info:pmid/17189186#body:116 |
|---|---|
| PubYear | 2006 |
| MedlineTA | Mol Cell |
| MedLine Reference | 17189186:1115 |
| Sentence | The major sites for p53 ubiquitination by Mdm2 are located at its C terminus, and acetylation of these residues during times of cell stress serves to block protein degradation and stabilize p53. |
| TextRef | info:pmid/15958581#body:264 |
|---|---|
| PubYear | 2005 |
| MedlineTA | Cancer Res |
| MedLine Reference | 15958581:1263 |
| Sentence | B, Western blot analysis for total p53, p53 phosphorylated on Ser15, p21Waf1/Cip1 and MDM2 in MCF-7 cells treated with 0.4 µmol/L aminoflavone for the indicated times.. |
| CellLineName | MCF7 |
| TextRef | info:pmid/17110929#body:54 |
|---|---|
| PubYear | 2006 |
| MedlineTA | EMBO J |
| MedLine Reference | 17110929:1053 |
| Sentence | However, MDMX forms a heterodimer with MDM2 through C-terminal RING domains (Sharp et al, 1999; Tanimura et al, 1999), and stimulates the ability of MDM2 to ubiquitinate and degrade p53 (Gu et al, 2002; Linares et al, 2003). |
| TextRef | info:pmid/10822382#body:146 |
|---|---|
| PubYear | 2000 |
| MedlineTA | Oncogene |
| MedLine Reference | 10822382:1145 |
| Sentence | Peptide 3 blocks Mdm2-dependent p53 ubiquitination in vitro . p14ARF activates p53-dependent transcription and has been reported to block Mdm2-mediated ubiquitination of p53 (Honda and Yasuda, 1999). |
| TextRef | info:pmid/14966292#body:280 |
|---|---|
| PubYear | 2004 |
| MedlineTA | Mol Cell Biol |
| MedLine Reference | 14966292:1279 |
| Sentence | The present model is that ARF stabilizes p53 by targeting MDM2 to the nucleolus and blocking p53 ubiquitination by MDM2 (reviewed in reference 43). |
| CellLineName | M1 |
| CellType | Epithelial Cells |
| Organ | Mammary Gland |
| TextRef | info:pmid/11238917#body:65 |
|---|---|
| PubYear | 2001 |
| MedlineTA | Mol Cell Biol |
| MedLine Reference | 11238917:1064 |
| Sentence | If left unimpeded, mdm2 inhibits p53 function both by binding and by blocking p53's transcriptional activation domain as well as by catalyzing p53's ubiquitination, thus leading to its proteasomal degradation (32). |
| TextRef | info:pmid/15064742#body:28 |
|---|---|
| PubYear | 2004 |
| MedlineTA | Oncogene |
| MedLine Reference | 15064742:1027 |
| Sentence | Although regulation of p53 ubiquitination by MDM2 and other factors has been intensively studied, the exact mechanism by which p53, and polyubiquitinated substrates in general, are recognized by the proteasome, remains unclear. |