MDM2 promotes p21waf1/cip1 proteasomal turnover independently of ubiquitylation. - Wikidata - wikimedia - TriplyDB

MDM2 promotes p21waf1/cip1 proteasomal turnover independently of ubiquitylation.

MDM2 promotes p21waf1/cip1 proteasomal turnover independently of ubiquitylation.

http://www.wikidata.org/entity/Q40323831

about

Mdm2 is involved in the ubiquitination and degradation of G-protein-coupled receptor kinase 2 14-3-3gamma binds to MDMX that is phosphorylated by UV-activated Chk1, resulting in p53 activation Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2-adrenergic receptor hSSB1 binds and protects p21 from ubiquitin-mediated degradation and positively correlates with p21 in human hepatocellular carcinomas Differential regulation of p53 and p21 by MKRN1 E3 ligase controls cell cycle arrest and apoptosis Ribosomal protein L23 activates p53 by inhibiting MDM2 function in response to ribosomal perturbation but not to translation inhibition N-Terminal ubiquitination of extracellular signal-regulated kinase 3 and p21 directs their degradation by the proteasome Proteasomal Turnover of Hepatitis C Virus Core Protein Is Regulated by Two Distinct Mechanisms: a Ubiquitin-Dependent Mechanism and a Ubiquitin-Independent but PA28 -Dependent Mechanism Examination of the expanding pathways for the regulation of p21 expression and activity.Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5 A novel, non-apoptotic role for Scythe/BAT3: a functional switch between the pro- and anti-proliferative roles of p21 during the cell cycle Aciculatin induces p53-dependent apoptosis via MDM2 depletion in human cancer cells in vitro and in vivo The intrinsically disordered N-terminal domain of thymidylate synthase targets the enzyme to the ubiquitin-independent proteasomal degradation pathway Rapamycin inhibits IGF-1-mediated up-regulation of MDM2 and sensitizes cancer cells to chemotherapy A regulatory mechanism involving TBP-1/Tat-Binding Protein 1 and Akt/PKB in the control of cell proliferation.Quantitative proteome analysis of the 20S proteasome of apoptotic Jurkat T cells.14-3-3Tau regulates ubiquitin-independent proteasomal degradation of p21, a novel mechanism of p21 downregulation in breast cancer.Hepatitis C virus NS2 protein is phosphorylated by the protein kinase CK2 and targeted for degradation to the proteasome.MDM2 promotes proteasomal degradation of p21Waf1 via a conformation change.Regulation of p53-MDMX interaction by casein kinase 1 alpha.MDM2 mediates ubiquitination and degradation of activating transcription factor 3 Regulating the 20S proteasome ubiquitin-independent degradation pathway.14-3-3Gamma inhibition of MDMX-mediated p21 turnover independent of p53.Cooperative actions of p21WAF1 and p53 induce Slug protein degradation and suppress cell invasion U-box-type ubiquitin E4 ligase, UFD2a attenuates cisplatin mediated degradation of DeltaNp63alpha.Lysine-independent turnover of cyclin G1 can be stabilized by B'alpha subunits of protein phosphatase 2A.Inhibition of p53 DNA binding function by the MDM2 protein acidic domain.Increased protein stability of CDKN1C causes a gain-of-function phenotype in patients with IMAGe syndrome Screening E3 substrates using a live phage display library A p53-independent role of Mdm2 in estrogen-mediated activation of breast cancer cell proliferation Aging mice have increased chromosome instability that is exacerbated by elevated Mdm2 expression Stress-induced alternative splice forms of MDM2 and MDMX modulate the p53-pathway in distinct ways Ubiquitin-independent proteasomal degradation during oncogenic viral infections.MDM2-mediated degradation of p14ARF: a novel mechanism to control ARF levels in cancer cells.The RING finger domain of MDM2 is essential for MDM2-mediated TGF-beta resistance.Mdm2 is required for inhibition of Cdk2 activity by p21, thereby contributing to p53-dependent cell cycle arrest Ubiquitylation and proteasomal degradation of the p21(Cip1), p27(Kip1) and p57(Kip2) CDK inhibitors Ubiquitin- and MDM2 E3 ligase-independent proteasomal turnover of nucleostemin in response to GTP depletion Ubiquitin ligases in malignant lymphoma.Differential regulation of p21 (waf1) protein half-life by DNA damage and Nutlin-3 in p53 wild-type tumors and its therapeutic implications.

P2860

Q24305064-90ABBDDE-C092-4799-A194-14F8314D5CE6 Q24306380-3BAFF58D-5AFC-4119-A2DF-4CC5BBD36476 Q24320318-66CFD5E9-2385-4E9F-B858-9C51D2695005 Q24337430-2AA860AA-A118-48F4-9909-020DF8E5C9D0 Q24338676-FED35786-AD08-426B-B2FF-E6A13FBFCAAE Q24562892-55602D13-8EED-4965-94F8-D1002D4C1ACE Q24563960-04FE527E-0B9D-4A14-92BD-397A8494A2F5 Q27487945-2E485AB5-E389-4C40-B000-A0C841F857E0 Q27692024-25110EA5-7F8F-4A16-BF3F-5C19B854B4BE Q28276949-0FBE74D2-2B24-4C88-B263-3317588E5434 Q28385780-39DF9DA4-9740-419F-99EC-B73CD436ABA2 Q28482222-C929CEDE-D0C7-4B85-89A5-DD36183CA099 Q28749496-9E5D83D0-EBCA-404A-B7F7-F3AE6210C490 Q30419679-8B1BA9C3-08AC-44FB-AA0F-435A28178D5F Q31032249-842B69E0-D7DE-46F6-9785-37070D829AC5 Q33549232-2A155478-6FFC-405B-A211-FBF7406A5DDC Q33705055-5249ED88-A5A1-416E-A7C3-3278FF3A99FC Q33835218-5110ABC5-3EC8-4F0B-8C7A-D8B937F65A1D Q33897779-79F9E599-528B-404E-AE85-610D22E83B80 Q33925248-C2698651-AB75-4FCD-B9CC-F130E8C1DD0C Q34094359-E9BB7DBF-9446-41EC-9F02-CEFACF0844ED Q34318192-1807CFAB-3A7D-4430-BC42-5810BC910DCC Q34568342-431AD894-BCA7-4D6E-A0B1-91BF6D0C616F Q34621458-D265B0E4-D840-4C1F-BFDC-F82980F07975 Q34775706-764A9783-E007-464B-B86F-76EC051EE5BD Q34871504-4E279E56-C2F0-445C-B925-ABCB387BADA1 Q34963324-82D01CDF-5601-447D-A315-54006FAF77D9 Q35009947-C84213CE-5CA1-43AE-80BA-C486A2C6E6FD Q35017038-1FC1CAFA-9576-48A9-A875-05C73634C686 Q35029505-39F2F3B6-525E-4341-9703-E2FD930A6726 Q35179539-B12A0FAB-2C3A-4797-AF29-312E211C4394 Q35221809-DCDE5A17-6453-4158-993E-E70447B7B81E Q35354212-83BF411E-D1CE-49C8-BFDF-F7AC0B55759B Q35568951-BBB82B9C-8716-4041-A04E-49775DBEF392 Q35810677-7B9B463F-7BEE-43EF-A470-C27A7C8445D0 Q35857003-26122CF1-04F7-4AF1-A312-E5427FD636DA Q35871417-DABCC653-1086-4021-A39D-FDAF187E2DB7 Q35880075-F3C1406F-BC9F-4D2C-BCFE-A39B3FEB0689 Q35883781-10069D07-2159-461C-B4E1-38AF24779051 Q36289902-5F10C727-B6E7-487C-8EBB-E302210F2ECB

P2860

MDM2 promotes p21waf1/cip1 proteasomal turnover independently of ubiquitylation.

http://www.wikidata.org/entity/Q40323831

description

2003 nî lūn-bûn

@nan

2003年の論文

@ja

2003年論文

@yue

2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

@wuu

2003年论文

@zh

2003年论文

@zh-cn

name

MDM2 promotes p21waf1/cip1 proteasomal turnover independently of ubiquitylation.

@en

type

label

MDM2 promotes p21waf1/cip1 proteasomal turnover independently of ubiquitylation.

@en

prefLabel

MDM2 promotes p21waf1/cip1 proteasomal turnover independently of ubiquitylation.

@en

P1433

Q40323831-5ACFFA3A-AD98-4F51-8A2C-FA2BFBC2B9EA

P1476

Q40323831-B003D2E8-51FC-4750-93E9-D7CD8DA1D500

P2093

Q40323831-2C92477A-BD82-4FBD-B700-31377ABB4E87

Q40323831-6E60E34F-5506-49D7-B4D6-2236AC2B02DC

Q40323831-B55A412D-2A15-4ED4-A28B-846E88A4DBCC

Q40323831-BD811D24-F6AC-4ADA-8E7E-FE569C28B383

Q40323831-D0A6D71C-4188-4F29-A33F-BAE8A041B362

P2860

Q40323831-01A3CB85-61C0-4CB0-9E26-FE8F30F13363

Q40323831-0C1CE83D-FDED-4FF8-812F-4606F9681AA4

Q40323831-0E665FAA-6F74-41C4-AAA5-F742A71AC672

Q40323831-231E1512-51D2-4EDE-9C54-B69D0163BBB7

Q40323831-2FD0CD3F-E6EE-4789-AE81-A1200F674EB9

Q40323831-31AE4CCB-44A3-4DA7-9F3A-F866B15263F6

Q40323831-3D8D85E5-1C3E-4E46-94BF-C7173E4478A4

Q40323831-441D82A1-B5B3-4FE8-ACFF-3AE0FCD92718

Q40323831-4812E84D-7479-4E9F-9986-5EFD31524CD0

Q40323831-49D3CAA2-2FF3-44E5-8A6E-5454609EF6E9

P304

Q40323831-BA5BC28D-F48C-4438-A0D1-C1DB8481E93E

P31

Q40323831-EFC37D6E-BEC9-4B64-82CD-71B43E11F61E

P356

Q40323831-E299B24A-EEB6-426D-9576-472D5B8F718E

P407

Q40323831-B74F160F-BFCD-4FE7-B142-76A1C9148604

P433

Q40323831-87909AC4-8C16-4E5C-BC62-D3A09D4BCBED

P478

Q40323831-D39ECD38-64EC-4C46-B34C-3C39B33E88AD

P577

Q40323831-5BFFE892-E10A-4969-A2F7-37EFC25AC01A

P5875

Q40323831-A3E77E74-B869-4922-A645-4347C9ECB9CC

P698

Q40323831-35B404F3-D5B8-4D43-8688-F4DEDB2AA19C

P921

Q40323831-352AA77F-562E-4CFA-AD2C-73D204A89E2B

P932

Q40323831-A30CF5CA-EDCC-4251-BEBD-EA0C00FEE1EF

P356

P1433

The EMBO Journal

P1476

MDM2 promotes p21waf1/cip1 proteasomal turnover independently of ubiquitylation.

@en

P2093

Hua Lu

http://www.w3.org/2001/XMLSchema#string

Hunjoo Lee

http://www.w3.org/2001/XMLSchema#string

Mu-Shui Dai

http://www.w3.org/2001/XMLSchema#string

Shelya X Zeng

http://www.w3.org/2001/XMLSchema#string

Yetao Jin

http://www.w3.org/2001/XMLSchema#string

P2860

Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53

Mdm4 (Mdmx) regulates p53-induced growth arrest and neuronal cell death during early embryonic mouse development.

Activation of the ATM kinase by ionizing radiation and phosphorylation of p53

The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases

ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways

Mdm2 promotes the rapid degradation of p53

Interaction between the retinoblastoma protein and the oncoprotein MDM2

Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53

SSRP1 functions as a co-activator of the transcriptional activator p63

A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 alpha-subunit of the 20S proteasome

P304

6365-6377

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1093/EMBOJ/CDG600

http://www.w3.org/2001/XMLSchema#string

P407

P433

23

http://www.w3.org/2001/XMLSchema#string

P478

22

http://www.w3.org/2001/XMLSchema#string

P577

2003-12-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

6739444

http://www.w3.org/2001/XMLSchema#string

P698

14633995

http://www.w3.org/2001/XMLSchema#string

P921

P932

291841

http://www.w3.org/2001/XMLSchema#string