Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5 - Wikidata - wikimedia - TriplyDB

Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5

Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5

http://www.wikidata.org/entity/Q28276949

about

The balance between rRNA and ribosomal protein synthesis up- and downregulates the tumour suppressor p53 in mammalian cells Specific domains of nucleolin interact with Hdm2 and antagonize Hdm2-mediated p53 ubiquitination Positive regulation of p53 stability and activity by the deubiquitinating enzyme Otubain 1 HDM2-binding partners: interaction with translation elongation factor EF1alpha.Impaired ribosome biogenesis in Diamond-Blackfan anemia Mitochondrial ribosomal protein L41 suppresses cell growth in association with p53 and p27Kip1.Ribosomal protein S27L is a direct p53 target that regulates apoptosis Mammalian WDR12 is a novel member of the Pes1-Bop1 complex and is required for ribosome biogenesis and cell proliferation Regulation of nucleolar signalling to p53 through NEDDylation of L11 MYBBP1A suppresses breast cancer tumorigenesis by enhancing the p53 dependent anoikis Inhibition of c-Myc activity by ribosomal protein L11 Ribosomal protein S27-like and S27 interplay with p53-MDM2 axis as a target, a substrate and a regulator Nucleophosmin is essential for ribosomal protein L5 nuclear export Ribosomal protein S9 is a novel B23/NPM-binding protein required for normal cell proliferation The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex Mutational analysis reveals a dual role of Mdm2 acidic domain in the regulation of p53 stability A newly identified Pirh2 substrate SCYL1-BP1 can bind to MDM2 and accelerate MDM2 self-ubiquitination Dominant-negative Pes1 mutants inhibit ribosomal RNA processing and cell proliferation via incorporation into the PeBoW-complex Abnormalities of the large ribosomal subunit protein, Rpl35a, in Diamond-Blackfan anemia Aberrant expression of nucleostemin activates p53 and induces cell cycle arrest via inhibition of MDM2 Mdm2 regulates p53 mRNA translation through inhibitory interactions with ribosomal protein L26 Cancer-associated mutations in the MDM2 zinc finger domain disrupt ribosomal protein interaction and attenuate MDM2-induced p53 degradation Regulation of the MDM2-p53 pathway by ribosomal protein L11 involves a post-ubiquitination mechanism The importance of ribosome production, and the 5S RNP-MDM2 pathway, in health and disease Targeted cancer therapy with ribosome biogenesis inhibitors: a real possibility?Progress towards mechanism-based treatment for Diamond-Blackfan anemia Ribosomal proteins as unrevealed caretakers for cellular stress and genomic instability RINGs of good and evil: RING finger ubiquitin ligases at the crossroads of tumour suppression and oncogenesis Deubiquitinating enzyme regulation of the p53 pathway: A lesson from Otub1 Perturbations at the ribosomal genes loci are at the centre of cellular dysfunction and human disease The emerging roles of ribosome biogenesis in craniofacial development Guarding the 'translation apparatus': defective ribosome biogenesis and the p53 signaling pathway Diverse diseases from a ubiquitous process: the ribosomopathy paradox Role of ribosomal protein mutations in tumor development (Review)Regulatory Roles of Rpl22 in Hematopoiesis: An Old Dog with New Tricks Myeloma overexpressed 2 (Myeov2) regulates L11 subnuclear localization through Nedd8 modification A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly 4-thiouridine inhibits rRNA synthesis and causes a nucleolar stress response Ribosomal protein S7 regulates arsenite-induced GADD45α expression by attenuating MDM2-mediated GADD45α ubiquitination and degradation Structure and activity analysis of Inauhzin analogs as novel antitumor compounds that induce p53 and inhibit cell growth

P2860

Q24297086-BCBCDD9C-7022-4D9E-9EAD-90375C88BB6A Q24298079-5EF45A6A-2A96-436B-85A4-238CD90A0636 Q24298615-419BCC9D-FCDB-4587-848E-6476720C5EE2 Q24300548-11115D5E-9CCD-48AE-A735-47B0C04F97CD Q24307762-59DCA1B5-186A-434F-9F2F-5174B91F6F86 Q24307978-113A933D-A487-479B-8128-D4D87708F2F4 Q24308211-0B32C611-152A-4254-B4B0-AB665FB9A9CE Q24310054-00CD4335-AA85-4FF4-8355-021DC49DBEA0 Q24310534-A571468E-39A7-4EE0-B09C-958580DAD5C8 Q24314897-D21A28EF-851C-4A78-85FF-F5CE02982EEC Q24315370-E9C9D587-54D8-4246-A2F6-E8AF837F0D04 Q24318162-2DB38C4B-3D8E-4867-A8EC-FFB5232D4EF1 Q24322766-9846F731-A7A5-4C47-BCC3-7077A11A4E0C Q24322997-5399F5A0-86B4-418B-9067-FF52CB17E28B Q24323508-ABF0BFD0-FBD5-497D-86C4-5B98A5691D72 Q24337178-5CD0A27E-5731-4B79-BC45-0F9A2A189A32 Q24337268-1A728555-A542-45D0-9D4E-CBA5EADDA885 Q24338388-B036A8E8-2396-478F-840C-6368AD027003 Q24642192-6C0C911A-CD7F-44B6-A2E4-325B73761BDD Q24646511-33578B6F-039D-4011-82C8-CACFD208DB85 Q24653892-14EB4112-B36A-4EAE-8BF3-DF11CA474997 Q24673794-0FC0B136-4688-4635-A15B-E19EF06EE3B4 Q24681793-D9A385D7-C423-422D-B116-B64A4EAE692F Q26741340-31D5FE77-F6A4-4A85-A88F-121DE2DC8A50 Q26785508-C5431FB7-FFF4-483B-AEA8-2FBF04277416 Q26823710-E5BB1757-EDBD-4A92-967B-E15EF1DD7798 Q26829490-D725641A-005B-4221-93B5-14A1C98B5CD7 Q26853207-3D82FDED-F7B2-4D41-8ABD-35EE1D7CDA97 Q27003153-753949C2-2C1B-4B97-960E-D4C095EF8D2A Q27005780-5A501009-45CA-4E88-B260-A6E7D4A8CCEA Q27006931-C8014217-19E2-4B1D-8573-644DF8C7AAD5 Q27022918-2EAE06A0-F343-4895-931B-DF639F49A6FD Q27694538-809522FF-8D4E-46DE-B236-2CA59AFF2A55 Q28068265-C9D16779-1A69-4674-8399-B0F771CB1AC7 Q28078535-E923D766-0183-4C4D-AFCC-742470BD11A7 Q28116360-3AED6D45-F281-4493-AAAD-3F663690AAE1 Q28294112-DB9B4B36-4A3E-4EA6-92A3-AACC9DB24AC8 Q28298346-891C192A-69D2-46E8-BCBD-109A9B2702B0 Q28383493-6E2680CF-A908-42FA-9B8A-721B45DBCF95 Q28484540-490DFFEA-2205-4581-B3A4-F44CEDA27B37

P2860

Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5

http://www.wikidata.org/entity/Q28276949

description

2004 nî lūn-bûn

@nan

2004 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2004年の論文

@ja

2004年論文

@yue

2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

name

Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5

@ast

Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5

@en

Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5

@nl

type

label

Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5

@ast

Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5

@en

Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5

@nl

prefLabel

Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5

@ast

Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5

@en

Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5

@nl

P1433

Q28276949-6A6A68A8-C562-4055-AD90-1E41D54C1DC1

P1476

Q28276949-1B1186BD-60CD-4DD5-A1D1-AD4DA252E14E

P2093

Q28276949-39B8F62D-D205-4132-8750-05E0B58FA87A

Q28276949-99F75C10-681B-4BAD-804B-F15E61FF461E

P2860

Q28276949-0BAB4EF2-2C08-462B-880B-A086BC1E8B94

Q28276949-0FBE74D2-2B24-4C88-B263-3317588E5434

Q28276949-1FA3C127-2E38-4C9A-83F8-72B013CBAB14

Q28276949-2542A040-6755-464A-AE82-CBAA1014BBB0

Q28276949-2545CCBE-2963-452A-89AF-D9AB16CBB8E1

Q28276949-42BCA15A-726E-47EE-B010-CEDB3243E597

Q28276949-7F5E2BA2-6C85-43C3-B723-6B659D15CC93

Q28276949-8170F253-7322-47F1-A9A8-2FD7701086B9

Q28276949-823E7DA8-5B0D-4783-9922-E59DFADDD3ED

Q28276949-827C3F73-427A-44EC-A838-1241920039B5

P304

Q28276949-12D57D22-600D-4411-A2C8-BC5AF1681F1C

P31

Q28276949-9EF51A09-8F6A-4F88-A8FE-588B0F5119BD

P3181

Q28276949-02DB99B8-1412-402D-B8D8-FA95EEA939E3

P356

Q28276949-B167DAA4-70BE-48B9-A4AB-017C2397761C

P407

Q28276949-BC711B5F-1757-4908-8758-883A4285F214

P433

Q28276949-E7A2843C-BCB6-4124-9651-79C1997B2BF5

P478

Q28276949-4A165144-D798-49EB-9FDB-023CA4150B6E

P577

Q28276949-90D3F6B9-FC2B-4812-A953-50CF1AF1F091

P5875

Q28276949-D7C2FC35-584F-4C89-BE69-EEC95D844229

P698

Q28276949-CE60CB67-EA88-4D07-A980-310D9EA1C43B

P921

Q28276949-0B2DF8B3-F6C9-4927-9101-B7669AB8C883

P3181

P356

P1433

Journal of Biological Chemistry

P1476

Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5

@en

P2093

Hua Lu

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

Mu-Shui Dai

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

P2860

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

Interaction of the HIV-1 rev cofactor eukaryotic initiation factor 5A with ribosomal protein L5

Mdm2 promotes the rapid degradation of p53

Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53

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

Evidence of p53-dependent cross-talk between ribosome biogenesis and the cell cycle: effects of nucleolar protein Bop1 on G(1)/S transition

Regulation of p53 function and stability by phosphorylation

Ribosomal protein L23 activates p53 by inhibiting MDM2 function in response to ribosomal perturbation but not to translation inhibition

The ribosomal L5 protein is associated with mdm-2 and mdm-2-p53 complexes

Ribosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway

P304

44475-82

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

P31

scholarly article

P3181

894661

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

P356

10.1074/JBC.M403722200

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

P407

P433

43

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

P478

279

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

P577

2004-10-22T00:00:00Z

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

P5875

8401941

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

P698

15308643

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

P921

protein ubiquitination