Targeting the ubiquitin pathway for cancer treatment - Wikidata - wikimedia - TriplyDB

Targeting the ubiquitin pathway for cancer treatment

Targeting the ubiquitin pathway for cancer treatment

http://www.wikidata.org/entity/Q26866185

about

Protease inhibition as new therapeutic strategy for GI diseases Hepatocellular carcinoma mouse models: Hepatitis B virus-associated hepatocarcinogenesis and haploinsufficient tumor suppressor genes A cascading activity-based probe sequentially targets E1-E2-E3 ubiquitin enzymes Dysregulation of ubiquitin ligases in cancer Inhibition of SCF ubiquitin ligases by engineered ubiquitin variants that target the Cul1 binding site on the Skp1-F-box interface.Anti-infective Activity of 2-Cyano-3-Acrylamide Inhibitors with Improved Drug-Like Properties against Two Intracellular Pathogens.Protein expression changes induced in a malignant melanoma cell line by the curcumin analogue compound D6.A dominant-negative F-box deleted mutant of E3 ubiquitin ligase, β-TrCP1/FWD1, markedly reduces myeloma cell growth and survival in mice.Small molecule therapeutics targeting F-box proteins in cancer.Efficacy of bortezomib in sarcomas with high levels of MAP17 (PDZK1IP1).Inhibitors of Deubiquitinating Enzymes Block HIV-1 Replication and Augment the Presentation of Gag-Derived MHC-I Epitopes.Hydrophobic Patch of Ubiquitin is Important for its Optimal Activation by Ubiquitin Activating Enzyme E1.Design Principles Involving Protein Disorder Facilitate Specific Substrate Selection and Degradation by the Ubiquitin-Proteasome System.ASB7 regulates spindle dynamics and genome integrity by targeting DDA3 for proteasomal degradation.Cooperative oncogenic effect and cell signaling crosstalk of co‑occurring HER2 and mutant PIK3CA in mammary epithelial cells.Integrative analysis of genomic and epigenomic regulation of the transcriptome in liver cancer.E3 ubiquitin ligases in cancer and implications for therapies.Ubiquitin ligase SPSB4 diminishes cell repulsive responses mediated by EphB2.Dysregulated expression of SKP2 and its role in hematological malignancies.Pirh2 mediates the sensitivity of myeloma cells to bortezomib via canonical NF-κB signaling pathway.NEDD4 promotes cell growth and motility in hepatocellular carcinoma.Ubiquitin-Dependent Regulation of the Mammalian Hippo Pathway: Therapeutic Implications for Cancer.Gastric Cancer Cell Lines Have Different -Regulated Expression Patterns but Share a Common Core of Altered Genes

P2860

Q26747722-1DBE633D-EC56-40BD-96EF-CBDD03C75A5A Q26772317-33EF0C4B-77CD-401E-866E-049B29D9E66C Q27704870-FBCF0DF9-C0EA-4BCB-9947-6137BE0EE6E4 Q28086796-F389E775-01F4-4F47-BA9C-7D159CE3FE77 Q35956904-4B7C6E6A-BF9B-4905-96FC-6B728BE7B1CD Q36006797-787599BE-3183-4464-904C-B12D83C48F4A Q36021520-9A68E76A-8EF9-4FDE-84E5-384ABAD1A6F9 Q36356398-8C840B46-2F17-425D-865B-59E4199A80B6 Q36600976-0C383E6C-F790-4C2B-A1CA-16D8334920D8 Q37687113-54F665F9-9F54-408A-8583-76CC0357238F Q38626145-6030993C-BEB1-4548-B04F-E0A3B2984B97 Q38689249-0908D94B-14C3-40C6-9879-B4BA91A4D9E3 Q38724758-B007BDA1-70D8-449E-BF80-ABFDF14E03A3 Q39327025-9D1A5830-2D50-4399-B5DA-1D20EC894751 Q41389205-9E9159DD-B98E-4DB9-8218-840B3CA84E60 Q42019561-3F2D5D3C-06F2-49AB-9EDF-9094EC2CEEF1 Q47636038-1DE32988-B7CF-4622-A9D5-F8734E861FE6 Q47771134-21738F96-2692-4FFB-9B5A-DBE044F92D5C Q47967824-0803C3D7-DF15-4A6D-A1BE-2A949DE3C337 Q50020971-B36C403B-EA8A-4589-81FA-71A1B306250B Q52685727-91F8AD82-AE3A-4F57-A4B1-8F3E4A8AB115 Q54973587-1BD6496F-D9E9-4AE5-98C7-BC5ADBFCD43A Q58551710-FD164101-E9E7-4B1C-BBE1-09456E78F498

P2860

Targeting the ubiquitin pathway for cancer treatment

http://www.wikidata.org/entity/Q26866185

description

2015 nî lūn-bûn

@nan

2015 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

name

Targeting the ubiquitin pathway for cancer treatment

@ast

Targeting the ubiquitin pathway for cancer treatment

@en

Targeting the ubiquitin pathway for cancer treatment

@nl

type

label

Targeting the ubiquitin pathway for cancer treatment

@ast

Targeting the ubiquitin pathway for cancer treatment

@en

Targeting the ubiquitin pathway for cancer treatment

@nl

prefLabel

Targeting the ubiquitin pathway for cancer treatment

@ast

Targeting the ubiquitin pathway for cancer treatment

@en

Targeting the ubiquitin pathway for cancer treatment

@nl

P1433

Q26866185-5F1C7117-6E22-435C-8502-8CCF698B7A9B

P1476

Q26866185-884C4595-146E-434D-9EA7-1FC195C2693A

P2093

Q26866185-2B883914-4761-4EF2-A6A5-DBDE4E2DE5C3

Q26866185-313D47EA-DF0D-40A1-ABAB-A6C3F7D2A635

Q26866185-6756DB21-7D16-476C-B98B-13061884871C

Q26866185-B3D7F005-7B18-4D6A-A924-FBF503F90A48

Q26866185-D3EF9AAC-00C1-4043-840D-45D18CD4C1A2

Q26866185-D4CDB30A-CC30-4BA2-A9B8-4C58462E3784

Q26866185-FE6F48CA-016B-4F5F-93C9-6DB8BFF27F12

P2860

Q26866185-01325FE0-D88B-4C58-84B1-5F693E1389DC

Q26866185-051B03BB-DA70-4903-AEFC-6E2660F8C498

Q26866185-06C718E1-71C6-4FC8-8CCC-99BD6927C3A1

Q26866185-0768300B-1603-4E65-B952-DDE30E00C241

Q26866185-0C449F42-60E1-449A-9016-9EC2B9654282

Q26866185-0CCF4519-CA9D-47CB-BAF3-2CB1C3117C45

Q26866185-0CFC0F87-6A70-4C53-BFC0-120D39C7567F

Q26866185-0E1B2AA8-2F84-41E1-8EB2-8548E1400E92

Q26866185-0E390B8D-9A77-4E74-8F55-3DB7BB839266

Q26866185-0FEBCFCB-0026-49CE-8315-0949E3862FBC

P304

Q26866185-C2CFC13E-9284-4EA5-9BA4-24A96EA4C1F9

P31

Q26866185-EB85C92D-F9ED-414D-9881-CC07D65C0F8A

P3181

Q26866185-C6302166-163E-4BA9-BA4D-512085B3BF27

P356

Q26866185-3FFADD90-A87B-4EB6-9999-CEA8564C7BB5

P407

Q26866185-167557DB-77E8-4839-94FC-8460BB162199

P433

Q26866185-EEA56C47-92E1-46FA-9CD3-6A27A18A9CF2

P478

Q26866185-FED9DD1B-421E-414C-A690-54DB1CC9DB53

P577

Q26866185-02BC822A-8EFB-4AB9-839C-914CA0F31F35

P698

Q26866185-963D71B1-1932-414B-989F-9B9C76D48870

P932

Q26866185-8725E531-AE5F-40A4-9906-E1F8F12F1EF1

P3181

P356

J.BBCAN.2014.11.005

P1433

Biochimica et Biophysica Acta

P1476

Targeting the ubiquitin pathway for cancer treatment

@en

P2093

Jia Liu

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

Qiong Wu

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

Shavali Shaik

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

Wenyi Wei

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

Xiangpeng Dai

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

Xiuxia Zhou

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

Zhiwei Wang

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

P2860

Acetylation-dependent regulation of Skp2 function

NEDD4-1 is a proto-oncogenic ubiquitin ligase for PTEN

Phosphorylation by casein kinase I promotes the turnover of the Mdm2 oncoprotein via the SCF(beta-TRCP) ubiquitin ligase

FOXO4 transcriptional activity is regulated by monoubiquitination and USP7/HAUSP

Pharmacologic inhibition of the anaphase-promoting complex induces a spindle checkpoint-dependent mitotic arrest in the absence of spindle damage

Prophase destruction of Emi1 by the SCF(betaTrCP/Slimb) ubiquitin ligase activates the anaphase promoting complex to allow progression beyond prometaphase

Pharmacological inactivation of Skp2 SCF ubiquitin ligase restricts cancer stem cell traits and cancer progression

Site-specific Lys-63-linked tumor necrosis factor receptor-associated factor 6 auto-ubiquitination is a critical determinant of I kappa B kinase activation

Grb10 prevents Nedd4-mediated vascular endothelial growth factor receptor-2 degradation

M-phase kinases induce phospho-dependent ubiquitination of somatic Wee1 by SCFbeta-TrCP

P304

50-60

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

P31

scholarly article

P3181

2348201

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

P356

10.1016/J.BBCAN.2014.11.005

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

P407

P433

1

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

P478

1855

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

P577

2015-01-01T00:00:00Z

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

P698

25481052

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

P932

4312704

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