Degradation of phosphorylated p53 by viral protein-ECS E3 ligase complex. - Wikidata - awgldk - TriplyDB

Degradation of phosphorylated p53 by viral protein-ECS E3 ligase complex.

Degradation of phosphorylated p53 by viral protein-ECS E3 ligase complex.

http://www.wikidata.org/entity/Q33489621

about

Rotavirus-encoded nonstructural protein 1 modulates cellular apoptotic machinery by targeting tumor suppressor protein p53 The structure and regulation of Cullin 2 based E3 ubiquitin ligases and their biological functions The role of cullin 5-containing ubiquitin ligases Microbial Regulation of p53 Tumor Suppressor Cullin family proteins and tumorigenesis: genetic association and molecular mechanisms Noise cancellation: viral fine tuning of the cellular environment for its own genome replication.Arsenic trioxide inhibits EBV reactivation and promotes cell death in EBV-positive lymphoma cells.Adenovirus 12 E4orf6 inhibits ATR activation by promoting TOPBP1 degradation The Epstein-Barr virus BZLF1 protein inhibits tumor necrosis factor receptor 1 expression through effects on cellular C/EBP proteins Making sense of ubiquitin ligases that regulate p53.A ubiquitin-specific protease possesses a decisive role for adenovirus replication and oncogene-mediated transformation.Cullin E3 ligases and their rewiring by viral factors The Role of Elongin BC-Containing Ubiquitin Ligases.The α2 helix in the DNA ligase IV BRCT-1 domain is required for targeted degradation of ligase IV during adenovirus infection.An Epstein-Barr Virus (EBV) mutant with enhanced BZLF1 expression causes lymphomas with abortive lytic EBV infection in a humanized mouse model.Release of severe acute respiratory syndrome coronavirus nuclear import block enhances host transcription in human lung cells.Phosphorylation drives an apoptotic protein to activate antiapoptotic genes: paradigm of influenza A matrix 1 protein function.p53 Is a Host Cell Regulator during Herpes Simplex Encephalitis.p53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PLpro via E3 ubiquitin ligase RCHY1 CUL2 overexpression driven by CUL2/E2F1/miR-424 regulatory loop promotes HPV16 E7 induced cervical carcinogenesis.Interference with p53 functions in human viral infections, a target for novel antiviral strategies?Genome guardian p53 and viral infections.Switching of EBV cycles between latent and lytic states.The Ying-Yang of the virus-host interaction: control of the DNA damage response.The Putative Role of Viruses, Bacteria, and Chronic Fungal Biotoxin Exposure in the Genesis of Intractable Fatigue Accompanied by Cognitive and Physical Disability.Modulation of p53 during bacterial infections.Analysis of the Cullin binding sites of the E4orf6 proteins of human adenovirus E3 ubiquitin ligases.Epstein-Barr virus: more than 50 years old and still providing surprises.p53 and Sp1 cooperate to regulate the expression of Epstein-Barr viral Zta protein.Viral oncoprotein LMP1 disrupts p53-induced cell cycle arrest and apoptosis through modulating K63-linked ubiquitination of p53.The role of oxidative stress in EBV lytic reactivation, radioresistance and the potential preventive and therapeutic implications.miRNA expression profiling of Epstein-Barr virus-associated NKTL cell lines by Illumina deep sequencing.Small molecule perturbation of the CAND1-Cullin1-ubiquitin cycle stabilizes p53 and triggers Epstein-Barr virus reactivation.Cullin-RING E3 Ubiquitin Ligases: Bridges to Destruction.Latency-Associated Nuclear Antigen E3 Ubiquitin Ligase Activity Impacts Gammaherpesvirus-Driven Germinal Center B Cell Proliferation.Roles of miR-138 and ISG15 in oral squamous cell carcinoma.Sequence analysis of EBV immediate-early gene BZLF1 and BRLF1 in lymphomas.Epstein-Barr Virus Hijacks DNA Damage Response Transducers to Orchestrate Its Life Cycle.Proteasomal degradation of the metabotropic glutamate receptor 1α is mediated by Homer-3 via the proteasomal S8 ATPase: Signal transduction and synaptic transmission.Antitumor effects of duvelisib on Epstein-Barr virus-associated lymphoma cells.

P2860

Q24338301-DFE4ACF4-76FA-4B43-AB9B-58CF117AF1C7 Q26746044-7B19BFBC-42BA-4F70-8595-E0CDAF631780 Q26749274-0262FE18-500F-4340-99BC-48A850ED5C56 Q26785743-DE388DBB-C65F-4EC4-A659-BF7525F2E5F4 Q26822657-95394F02-9EFF-4C77-941A-F9AA759437F2 Q33780955-74FA7006-3E09-4E9E-96FD-AE0730D1FDE2 Q33823359-F631733B-B179-4E91-898F-4D2D24D4F147 Q33982295-DA53500E-3E2F-4347-8D4C-3266AA9DB50B Q34291099-C6237984-9A36-4DEA-93CF-CBC490A9C775 Q34503497-37639395-39D0-4E4B-91F2-A34CD78D196B Q34649757-ADF3D35A-0984-4A44-A6CF-10C5066B702F Q34785767-CA6E0653-82D8-4236-97E7-FC2A965FBB64 Q35971082-CA293F1D-8709-44B5-A781-F8C4AC4EF22E Q36057815-E94EEF8A-55B7-4F5E-95E9-1DBA306EAEDD Q36171933-82D056E0-126C-4869-BB6D-6D995757E906 Q36759684-F3C5C7C4-FF71-4C24-A136-764CA44962CB Q36850385-5308D354-60B1-4D83-A625-AB551820CC9F Q37093496-C5FFB561-E526-4B3A-9495-7617F029A0E9 Q37258617-F3E21E25-3661-40B4-86DA-02388236AD69 Q37327810-530C339C-97D5-499B-B63E-9115794D0F02 Q37897197-1CB5473C-3204-47E8-8AC5-03E219B850B8 Q38068825-2FD63A57-87E0-4E36-97D2-E32B3FC5EDC7 Q38171455-8AECA1FE-850F-4EFD-A315-796BCBA3FB39 Q38356270-AA350622-49E2-4C2F-BD13-A04C7C16182F Q38529622-72F20D22-29F5-4ABB-9F4F-BE4C0F5D93CD Q38628212-CDC6083B-6B5C-4CD9-A2B6-51EA889CB794 Q38854475-0F34987C-BA17-43F5-8CCF-16C15C7F4261 Q38968588-216F9437-05C5-44F1-89FD-4CCC4693B071 Q39328814-03789406-1246-41EE-A43F-5950EDE6A681 Q39333947-077082C6-550F-4E94-AC0C-7ACFE5D39C12 Q39344275-2015BB57-C0D2-4D7A-BF36-ADE1D9AFF92C Q39882004-DEB39392-4D74-461F-8757-C0F580859CA9 Q40120026-CBE757C6-3E80-4B5C-98B7-C8260450242C Q40303257-B83B0C0B-1400-405D-B3CF-76148D5A7735 Q40698869-DF6F35D3-028C-4920-B4C2-AFEE75D74133 Q41672604-7F933CD4-E56B-4C32-B58D-FC8EFF303293 Q42232463-1DCD8260-9821-4484-841B-9BB338B8D216 Q45324762-20540E8C-9C64-4575-AA2C-B92637C42582 Q48578100-40E7954E-C2AB-4587-84A3-834C99A16B45 Q52664561-FEAA89EA-8F23-43DC-A524-253C5CB21833

P2860

Degradation of phosphorylated p53 by viral protein-ECS E3 ligase complex.

http://www.wikidata.org/entity/Q33489621

description

2009 nî lūn-bûn

@nan

2009 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Degradation of phosphorylated p53 by viral protein-ECS E3 ligase complex.

@ast

Degradation of phosphorylated p53 by viral protein-ECS E3 ligase complex.

@en

type

label

Degradation of phosphorylated p53 by viral protein-ECS E3 ligase complex.

@ast

Degradation of phosphorylated p53 by viral protein-ECS E3 ligase complex.

@en

prefLabel

Degradation of phosphorylated p53 by viral protein-ECS E3 ligase complex.

@ast

Degradation of phosphorylated p53 by viral protein-ECS E3 ligase complex.

@en

P1433

Q33489621-A4CFDAEB-820B-4B59-8517-AB543F9BB932

P1476

Q33489621-63B237CA-F145-4BF2-928C-A8242537EE88

P2093

Q33489621-6C35E034-88BD-4A60-89FD-FB6004F5C3EF

Q33489621-6E7DCCD0-5C53-4E3C-AC23-21CE10A5599B

Q33489621-7B1B012D-0C9F-4926-87AD-741A453D4BC8

Q33489621-997E5784-3B6A-4DA9-A747-43FA6B606486

Q33489621-A4336579-3675-490F-B6AA-25D970C8FC47

Q33489621-B43A1523-C266-4571-8857-5D9DD25B952D

Q33489621-D1F87C50-1617-44E5-83CC-2D78A4696B6C

Q33489621-D491F82C-1502-4173-9F41-6308E4B8B952

Q33489621-FD78288B-C1D7-46DC-8917-B2FDC6352B2A

P2860

Q33489621-0AEA4653-2ED6-413C-BFD0-63CF6C88A9A2

Q33489621-0CADA234-C3E8-4413-B24A-A8413D0A72BA

Q33489621-0F18523E-6177-4A9E-B4EB-22B21A5DA5CB

Q33489621-13E44DF9-D9E8-4351-99B0-AD1296F7C76F

Q33489621-15A2A8A6-6948-46F7-ACEB-7161918EEAEC

Q33489621-1A141FE0-B6EC-40CB-B4C6-BBA67A6DA30D

Q33489621-1A52DF77-8B38-4AE7-8B5D-B508AD5A2067

Q33489621-1ED78B23-6F25-4847-82BB-8CF1683C791C

Q33489621-2A5CF6C2-8695-4733-8632-BBB28633A7CF

Q33489621-3081B04B-EEA4-48BE-889F-5BF9E057D65D

P304

Q33489621-80542C6E-2C12-4F7A-9AE2-F7C77A12899F

P31

Q33489621-72F36D27-A99E-4E87-9531-2DE36766CFC0

P356

Q33489621-54D832CB-E020-4843-ACFF-C3E607717D75

P433

Q33489621-2A994EB7-DD49-4319-B7EF-F1CBEA3407AA

P478

Q33489621-4D9D2624-7B1F-4909-9298-DA38BF98C707

P50

Q33489621-3A104AE8-EF7C-4A6B-B506-67E98FDDA220

P577

Q33489621-D8B7FCC5-A2A7-4D07-AE11-13371A4E1EF7

P5875

Q33489621-7D3EFD01-B4A7-47E8-9014-5193EF415EC2

P698

Q33489621-CD12F870-3116-4F5D-835B-DEAFB6F680B9

P921

Q33489621-87D5DF53-A469-475D-8F1C-AF9E291F1D9B

P932

Q33489621-ACBAD70E-8CE6-4D99-923C-150447E65589

P356

JOURNAL.PPAT.1000530

P1433

P1476

Degradation of phosphorylated p53 by viral protein-ECS E3 ligase complex.

@en

P2093

Ayumi Kudoh

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

Hiroki Isomura

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

Noriko Shirata

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

Sanae Nakayama

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

Satoko Iwahori

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

Takayuki Murata

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

Takumi Kamura

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

Tatsuya Tsurumi

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

Yukihiro Nishiyama

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

P2860

Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex

Identification of redox/repair protein Ref-1 as a potent activator of p53

The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53

CARPs are ubiquitin ligases that promote MDM2-independent p53 and phospho-p53ser20 degradation

VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases

Activation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex

Mechanisms underlying ubiquitination

The ubiquitin system

Surfing the p53 network

Function and regulation of cullin-RING ubiquitin ligases

P304

e1000530

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

P31

scholarly article

P356

10.1371/JOURNAL.PPAT.1000530

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

P433

7

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

P478

5

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

P50

P577

2009-07-31T00:00:00Z

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

P5875

26711688

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

P698

19649319

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

P921

phosphorylation

P932

2712087

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