Mdm2-mediated NEDD8 modification of TAp73 regulates its transactivation function. - Wikidata - awgldk - TriplyDB

Mdm2-mediated NEDD8 modification of TAp73 regulates its transactivation function.

Mdm2-mediated NEDD8 modification of TAp73 regulates its transactivation function.

http://www.wikidata.org/entity/Q45345758

about

The NEDD8 modification pathway in plants TRIM40 promotes neddylation of IKKγ and is downregulated in gastrointestinal cancers Ribosomal proteins are targets for the NEDD8 pathway E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification NEDD8 acts as a 'molecular switch' defining the functional selectivity of VHL Inhibition of NEDD8-conjugation pathway by novel molecules: potential approaches to anticancer therapy E2-binding surface on Uba3 β-grasp domain undergoes a conformational transition p73 as a pharmaceutical target for cancer therapy Eukaryotic translation elongation factor 1-alpha 1 inhibits p53 and p73 dependent apoptosis and chemotherapy sensitivity TP63 and TP73 in cancer, an unresolved "family" puzzle of complexity, redundancy and hierarchy.Protein neddylation: beyond cullin-RING ligases.Targeting cullin-RING ligases for cancer treatment: rationales, advances and therapeutic implications.The NEDD8 Conjugation Pathway and Its Relevance in Cancer Biology and Therapy.p53 Family and Cellular Stress Responses in Cancer.Targeting Neddylation pathways to inactivate cullin-RING ligases for anticancer therapy Nedd8 regulates inflammasome-dependent caspase-1 activation.Neddylation and deneddylation in cardiac biology Regulation of p73 activity by post-translational modifications.Oncolytic targeting of renal cell carcinoma via encephalomyocarditis virus NEDD8 Ultimate Buster 1 Long (NUB1L) Protein Suppresses Atypical Neddylation and Promotes the Proteasomal Degradation of Misfolded Proteins.Recognition and cleavage of related to ubiquitin 1 (Rub1) and Rub1-ubiquitin chains by components of the ubiquitin-proteasome system Function and regulation of protein neddylation. 'Protein modifications: beyond the usual suspects' review series Regulatory feedback loop between TP73 and TRIM32.Molecular basis of the interactions between the p73 N terminus and p300: effects on transactivation and modulation by phosphorylation.Insights from mouse models into human retinoblastoma p53-family proteins and their regulators: hubs and spokes in tumor suppression.Targeting protein neddylation: a novel therapeutic strategy for the treatment of cancer.CRL Ubiquitin Ligases and DNA Damage Response.Mdm2 and MdmX as Regulators of Gene Expression The TP73 complex network: ready for clinical translation in cancer?A balancing act: orchestrating amino-truncated and full-length p73 variants as decisive factors in cancer progression.Effects of the NEDD8-activating enzyme inhibitor MLN4924 on lytic reactivation of Kaposi's sarcoma-associated herpesvirus NEDDylation controls the target specificity of E2F1 and apoptosis induction.NEDDylation regulates E2F-1-dependent transcription NUB1, an interferon-inducible protein, mediates anti-proliferative actions and apoptosis in renal cell carcinoma cells through cell-cycle regulation.Suppression of hypoxia-inducible factor 2alpha restores p53 activity via Hdm2 and reverses chemoresistance of renal carcinoma cells.Chemotherapy induces NEDP1-mediated destabilization of MDM2.TIP60 represses transcriptional activity of p73beta via an MDM2-bridged ternary complex.Changes in the ratio of free NEDD8 to ubiquitin triggers NEDDylation by ubiquitin enzymes.A linker strategy for trans-FRET assay to determine activation intermediate of NEDDylation cascade.

P2860

Q21129204-95274E3F-81C3-4D05-AF26-D6876BDFF40E Q24299200-C12252CE-A94B-4422-9128-B210165E41C6 Q24313502-C40B5162-99C6-4A4E-A1C7-12071D0019AD Q24316067-4E72FB77-DDE3-4684-B18F-2E4708158FAE Q24321579-0A560602-6A0A-4FEF-B61D-88301643B414 Q27003218-234F89CB-4562-47D7-8958-FC3A1F8C9A51 Q27681811-0CB33493-C8B3-4E9F-B082-D4901B00DB22 Q28611414-A562F30F-58E4-4324-A86B-C591CA054B7D Q31121002-2445F140-E9E4-48DD-A5A7-35F157F72B7A Q33358710-1E7D2B22-6766-4FD1-AEE3-4BE27B921CA1 Q34042816-55C7B869-B101-40CD-AC04-AAEED591609C Q34043821-BBEB0047-B46B-4220-AC09-9D6E3822B7B8 Q34202686-448D60DF-EA0D-476F-8C60-AAE85BF29576 Q34377287-AA3A0517-25EA-40ED-82DF-264F53AA1148 Q34563129-AEF63C89-AD7C-4075-B4E0-45CEEEC65A6B Q34846646-2BABCDFF-9DA3-4558-B6F7-7E0FF04A6D39 Q34987403-EF2F7AE8-000E-48AF-AA1C-EDC581332311 Q35865249-99BCAEE5-3E28-4CA8-AC70-8CB553C9A248 Q36039304-AAFFDC01-F216-4294-A6E0-BABF40DF2AF2 Q36092993-ACB29668-CCD1-4F67-9043-4B287786170C Q36455731-2F2B3494-5A06-491D-B2A7-53A118AF53CE Q36946992-F26C07A7-6A5F-44C9-9EC7-FCF0431873EC Q37062004-F1354F4D-C3B0-4990-9CDF-2007D2A42F8D Q37117547-733E5B0F-5AF4-415D-B053-968F91FC8B9E Q37167727-490C53BB-8F35-4789-B4CA-766C5A5E14B7 Q37727778-316E5904-9A82-417E-BF0D-24B95C55DE8F Q37827165-EE63C765-E5D5-415F-BE2E-81391A4D5779 Q38015388-2C417419-6341-4E3D-A852-E980865C8C91 Q38059700-4CBB3903-1453-42E3-81F9-AFD21AC44E98 Q38126476-BF29EF6A-9EE6-4CA3-A7B0-6E2D8B1EA5DC Q38266299-08F79C36-3719-4D1B-B439-3A642899DD53 Q39152964-57F1DD2C-B2D2-4299-BB70-1A6288D3FC08 Q39273538-F4273903-E71C-4D1B-9B90-C5E8AF092F21 Q39307613-BFCF9556-42D0-444A-A561-9535FB61CB0F Q39440633-0E99BF8E-0260-4EBF-9BFA-DDB6721B76FF Q39773550-ACD707B2-44F1-4358-BF3E-934A759B14BE Q39794548-6EE3A6F8-60E1-4107-9901-140A8B56B59E Q39979226-C71D1F3B-8F40-4BC1-A735-1EFC7218A16E Q41141041-1373262B-4EF5-4755-88CF-F5AE60E2EA5E Q44598512-D45B6291-E0E4-45D3-BA40-5BAA2D88B582

P2860

Mdm2-mediated NEDD8 modification of TAp73 regulates its transactivation function.

http://www.wikidata.org/entity/Q45345758

description

2006 nî lūn-bûn

@nan

2006年の論文

@ja

2006年学术文章

@wuu

2006年学术文章

@zh

2006年学术文章

@zh-cn

2006年学术文章

@zh-hans

2006年学术文章

@zh-my

2006年学术文章

@zh-sg

2006年學術文章

@yue

2006年學術文章

@zh-hant

name

Mdm2-mediated NEDD8 modification of TAp73 regulates its transactivation function.

@en

Mdm2-mediated NEDD8 modification of TAp73 regulates its transactivation function.

@nl

type

label

Mdm2-mediated NEDD8 modification of TAp73 regulates its transactivation function.

@en

Mdm2-mediated NEDD8 modification of TAp73 regulates its transactivation function.

@nl

prefLabel

Mdm2-mediated NEDD8 modification of TAp73 regulates its transactivation function.

@en

Mdm2-mediated NEDD8 modification of TAp73 regulates its transactivation function.

@nl

P1433

Q45345758-F62601E7-B797-484B-9506-8D2AF75CA296

P1476

Q45345758-B3B27DF4-01A4-4E26-862E-60119E7369C4

P2093

Q45345758-4A318B17-4470-4070-A64D-2F50301BAC02

Q45345758-7FDBB4BA-902D-40F8-8778-228CBC0D90FF

Q45345758-86775238-9A0A-4276-96FA-134328FEA455

Q45345758-99E6AB3E-1052-4559-89FF-3307866B9F0D

Q45345758-CACB8615-091E-4388-A7FE-AEEB66B4295E

P2860

Q45345758-024B9E88-4946-408D-A3D7-D6D38E6C6927

Q45345758-11A6EB20-46DC-40E3-9C44-1A9050D6D8F9

Q45345758-19A2232C-701B-495D-87A3-D38B6349FCC5

Q45345758-1B0B97AB-5371-4F61-90AC-0F59415004E6

Q45345758-26E0920C-7BF6-45F0-9595-BBA6D7372D07

Q45345758-27F2C31D-6FDB-4B88-832C-27C4BB6CFBD1

Q45345758-27F9544D-0D22-40EC-B9F7-ACAA902A19A5

Q45345758-327DBC0A-EE05-4880-987F-924F8F82D7A9

Q45345758-32B1E43F-31DC-43C9-A09B-7D460D1B2106

Q45345758-3550E959-D6EE-4AB4-9553-434BBC279CAE

P304

Q45345758-45EF8369-FF6C-40FE-8DFD-D819ED52C79D

P31

Q45345758-C345B53C-5B98-446C-90C9-57EFA9E0FF74

P356

Q45345758-45E12885-F21E-40DE-B414-6A27EB153482

P407

Q45345758-7D87AA30-E5EB-43ED-BA95-452DF62B3F9B

P433

Q45345758-83825837-2CE0-4793-AE23-0B20E1FEEB12

P478

Q45345758-1A400704-6AA1-48CD-A2EF-77568F07C9D1

P577

Q45345758-B0E26A8E-B285-437E-9334-96E6F5AB8B16

P698

Q45345758-AC4AD655-8DB0-4198-B7F8-688A50A41358

P356

P1433

Journal of Biological Chemistry

P1476

Mdm2-mediated NEDD8 modification of TAp73 regulates its transactivation function.

@en

P2093

Alvaro Blanch

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

Dan C C Lin

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

Ian R Watson

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

Meredith S Irwin

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

Michael Ohh

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

P2860

The tyrosine kinase c-Abl regulates p73 in apoptotic response to cisplatin-induced DNA damage

p73 is regulated by tyrosine kinase c-Abl in the apoptotic response to DNA damage

MDM2 and MDMX bind and stabilize the p53-related protein p73

The ubiquitin-protein ligase Itch regulates p73 stability

Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain

Mdm2 promotes the rapid degradation of p53

Characterization of NEDD8, a developmentally down-regulated ubiquitin-like protein

Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53

MDM2 suppresses p73 function without promoting p73 degradation

PIAS-1 is a checkpoint regulator which affects exit from G1 and G2 by sumoylation of p73

P304

34096-34103

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

P31

scholarly article

P356

10.1074/JBC.M603654200

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

P407

P433

45

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

P478

281

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

P577

2006-09-14T00:00:00Z

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

P698

16980297

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