Targeting the AAA ATPase p97 as an Approach to Treat Cancer through Disruption of Protein Homeostasis - Wikidata - awgldk - TriplyDB

Targeting the AAA ATPase p97 as an Approach to Treat Cancer through Disruption of Protein Homeostasis

Targeting the AAA ATPase p97 as an Approach to Treat Cancer through Disruption of Protein Homeostasis

http://www.wikidata.org/entity/Q28269674

about

Targeting p97 to Disrupt Protein Homeostasis in Cancer Ring of Change: CDC48/p97 Drives Protein Dynamics at Chromatin UBXD Proteins: A Family of Proteins with Diverse Functions in Cancer Structural Details of Ufd1 Binding to p97 and Their Functional Implications in ER-Associated Degradation Potent, Reversible, and Specific Chemical Inhibitors of Eukaryotic Ribosome Biogenesis Quantitative interaction mapping reveals an extended UBX domain in ASPL that disrupts functional p97 hexamers.p97/VCP promotes degradation of CRBN substrate glutamine synthetase and neosubstrates.Current status and perspectives of patient-derived xenograft models in cancer research.Selective inhibition of p97 by chlorinated analogues of dehydrocurvularin A Mighty "Protein Extractor" of the Cell: Structure and Function of the p97/CDC48 ATPase.CRISPulator: a discrete simulation tool for pooled genetic screens Inadequate fine-tuning of protein synthesis and failure of amino acid homeostasis following inhibition of the ATPase VCP/p97 Allosteric Indole Amide Inhibitors of p97: Identification of a Novel Probe of the Ubiquitin Pathway.Structure and function of the AAA+ ATPase p97/Cdc48p.p97 Composition Changes Caused by Allosteric Inhibition Are Suppressed by an On-Target Mechanism that Increases the Enzyme's ATPase Activity.A Dynamic molecular basis for malfunction in disease mutants of p97/VCP.Lipid disequilibrium disrupts ER proteostasis by impairing ERAD substrate glycan trimming and dislocation.Opportunistic intruders: how viruses orchestrate ER functions to infect cells.A Proteomic Analysis of the Malignant Mesothelioma Secretome Using iTRAQ.Ubiquitin- and ATP-dependent unfoldase activity of P97/VCP•NPLOC4•UFD1L is enhanced by a mutation that causes multisystem proteinopathy.Sec61 blockade by mycolactone inhibits antigen cross-presentation independently of endosome-to-cytosol export.p97 Negatively Regulates NRF2 by Extracting Ubiquitylated NRF2 from the KEAP1-CUL3 E3 Complex.Valosin-containing Protein is a Target of 5'-l Fuligocandin B and Enhances TRAIL Resistance in Cancer Cells.Proteome complexity and the forces that drive proteome imbalance.Chlorinated Dehydrocurvularins and Alterperylenepoxide A from Alternaria sp. AST0039, a Fungal Endophyte of Astragalus lentiginosus.Ubiquitin recognition by the proteasome.Targeting VCP enhances anticancer activity of oncolytic virus M1 in hepatocellular carcinoma.Valosin-containing protein (VCP)-Adaptor Interactions are Exceptionally Dynamic and Subject to Differential Modulation by a VCP Inhibitor.The AAA+ ATPase p97, a cellular multitool.Valosin-Containing Protein/p97 as a Novel Therapeutic Target in Acute Lymphoblastic Leukemia.Hepatic cytochromes P450: structural degrons and barcodes, posttranslational modifications and cellular adapters in the ERAD-endgame.VCP inhibitors induce endoplasmic reticulum stress, cause cell cycle arrest, trigger caspase-mediated cell death and synergistically kill ovarian cancer cells in combination with Salubrinal.Combined CRISPRi/a-Based Chemical Genetic Screens Reveal that Rigosertib Is a Microtubule-Destabilizing Agent.Using the Ubiquitin-modified Proteome to Monitor Distinct and Spatially Restricted Protein Homeostasis Dysfunction.Capzimin is a potent and specific inhibitor of proteasome isopeptidase Rpn11.Characterization of protein complexes of the endoplasmic reticulum-associated degradation E3 ubiquitin ligase Hrd1.Targeting protein quality control pathways in breast cancer.Alcohol-abuse drug disulfiram targets cancer via p97 segregase adaptor NPL4.CRISPRi and CRISPRa Screens in Mammalian Cells for Precision Biology and Medicine.Elucidating drug targets and mechanisms of action by genetic screens in mammalian cells.

P2860

Q26740517-858D7600-672D-4ED8-A350-520E4D63BDDF Q26747328-24652219-BA3D-4149-B8D3-69DA03FB4D70 Q28069036-8D1BFEEC-AE3E-4586-8B56-8C10EC4563D8 Q28554390-93DFB06F-CF64-4FEB-B73C-D5847AB01788 Q28820989-41DA4753-7293-4542-8418-FF3A881298B2 Q30826494-B92BEC3D-A7EB-4B48-A1EF-6BFD820D62DB Q33556826-7C99344C-70CE-4ADD-8883-622E1C9FE726 Q33667686-763036CE-FE1E-44D3-9865-9FCA823D87D4 Q33785301-E79A62B8-7712-4EB1-BF64-5059446FFEB2 Q33790385-3308925B-BFA5-4AEB-98CB-83C9BD300005 Q33922903-ADB193D9-B1C0-4764-AE70-4E00146C78D5 Q36485185-DAE27F14-5EE9-4F97-870C-55B5A585B65E Q36579840-C48F8C3C-3484-4C5A-AC98-A5B612E4B2D8 Q36767612-104A6FDE-A92F-402A-9BEA-13F7FDEDC86C Q36827995-E199D17F-6C7D-47E0-B3CE-2DB6A67C84B8 Q37404484-3CFAB65C-51B1-405A-9F66-200F8AB71716 Q37583253-4A19BF2A-837B-4216-8E48-2721CBC078B3 Q37610842-77AC3CED-ED04-4D64-ABAF-B8E0FC9002C8 Q37724883-420D3B16-4CB7-4DD6-8ADF-F0FE36820F0A Q38682988-F6ECB545-23B4-424B-BDFA-895B5C2CAAE4 Q38692382-7445BF7B-F243-4B58-A708-81318DDA06F8 Q38719829-1FC53427-D7B9-43F6-A6A8-8403F3C2C0C5 Q38723897-A34709F5-A361-4F6B-8B07-9DDE4FABCC39 Q38954697-2C50A93C-5D7F-46C5-8D6D-51A6115FF77C Q38989927-993D54E2-2A73-4A0E-B919-17366EB623CB Q39077452-18892005-633A-471A-8A39-6FB244740EB5 Q40072916-4B352C41-4D38-430B-B40B-9C0285A8AB03 Q41028234-DA221089-3D9E-4C19-97FC-330E841C04CE Q41438223-E2961859-2FA8-44A2-AFE3-013C24C31F47 Q41563447-B5B2BC89-6CF1-498E-A5CF-E8D23F806310 Q41666716-7B272121-9A2E-46A8-81D1-ED58D9BD30FC Q41895056-8BC9AE71-23DE-4F3D-B296-EECCC9C236DB Q42377052-E6E911B6-A773-4F6A-A702-CD1E0B9CF028 Q42380194-8AEA1C2B-2FAE-4939-AC54-C24257AE1D10 Q42791381-83E63814-A21D-4F50-9977-6138FE2E8C2E Q45974018-1AEB152A-9663-4E2E-A16A-A1855CC7DC4B Q46087491-EBEA45B0-1185-4768-9FA1-941DDFA219E3 Q46185130-75707D88-DCEC-47DA-9E19-32261F9E1E44 Q46190066-AF06A71F-FE62-4F48-8E1F-40716C333413 Q46347911-B9A19082-94AB-45C0-95EE-8958606386B9

P2860

Targeting the AAA ATPase p97 as an Approach to Treat Cancer through Disruption of Protein Homeostasis

http://www.wikidata.org/entity/Q28269674

description

2015 nî lūn-bûn

@nan

2015 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի նոյեմբերին 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 AAA ATPase p97 a ...... ruption of Protein Homeostasis

@ast

Targeting the AAA ATPase p97 a ...... ruption of Protein Homeostasis

@en

Targeting the AAA ATPase p97 a ...... ruption of Protein Homeostasis

@nl

type

label

Targeting the AAA ATPase p97 a ...... ruption of Protein Homeostasis

@ast

Targeting the AAA ATPase p97 a ...... ruption of Protein Homeostasis

@en

Targeting the AAA ATPase p97 a ...... ruption of Protein Homeostasis

@nl

prefLabel

Targeting the AAA ATPase p97 a ...... ruption of Protein Homeostasis

@ast

Targeting the AAA ATPase p97 a ...... ruption of Protein Homeostasis

@en

Targeting the AAA ATPase p97 a ...... ruption of Protein Homeostasis

@nl

P1433

Q28269674-6057845D-176F-40FA-93B1-81C327BFCE2B

P1476

Q28269674-87495B51-FB96-4709-88AB-AE5F774BD2C2

P2093

Q28269674-02936ED5-C182-4D3B-A7F1-EA20AB27B0F6

Q28269674-0408C370-235C-446F-9246-D33965770C13

Q28269674-092C4A1A-1D10-4153-979E-880BEE3DBC78

Q28269674-17C6F329-149C-42CE-B331-3513C393C7CE

Q28269674-1B30DFEB-B156-422F-8DB8-5B8E6BA78363

Q28269674-1F124682-95AB-4C1D-B0D9-3F5425C80F64

Q28269674-21F0F894-19DE-4441-BED7-47613096761D

Q28269674-41E85694-C932-4991-BF14-DB5A7DB39A83

Q28269674-54FBE868-6B49-4BD3-ABA6-04E819D5DC66

Q28269674-6938F601-9396-4B4B-8790-DF7C8DA16E0C

P2860

Q28269674-020AA208-1B84-42F2-840B-AA8FEDA927A2

Q28269674-02E64A67-72E0-48BC-A785-1A02778BA026

Q28269674-1186EAAE-CDF3-4918-A177-D63446AB0C73

Q28269674-1773E02B-5FD8-4C45-B5ED-00B89108013E

Q28269674-195B422A-D3FA-493A-B0F7-866C4AB1EB68

Q28269674-1B113B1B-06C0-489E-91D9-8996C9425B63

Q28269674-22A51C1B-C3C7-462F-BD94-5F2B82280886

Q28269674-245012DC-5FAA-4A79-835D-F5AC5FC7EC88

Q28269674-2B120EBA-25F4-4DEE-BA3A-5318CB34ADE6

Q28269674-2BD56971-25D7-43F7-AB35-9BB7B9CCB142

P304

Q28269674-A078EDD3-7877-40D6-82F5-37CE7EFD3496

P31

Q28269674-922D3479-D698-43F7-BC9F-54BD98421949

P3181

Q28269674-544BC46F-2034-4DD0-9D6F-24E90033F7C3

P356

Q28269674-0296296B-8A98-4E8D-9B17-62ED6C973E3B

P407

Q28269674-A50212B7-3B58-461D-AA68-ADD4640DCEF4

P433

Q28269674-FA2E641E-A276-4F5B-8FE9-021073C4291A

P478

Q28269674-CB85EB3C-D2CB-4522-9799-80BD19DB38A1

P50

Q28269674-20DE00D8-D98B-4750-A139-CBFCA9A9EA56

P577

Q28269674-6CEF26B1-C506-4F54-A9F3-187008EBCF8C

P5875

Q28269674-9FB095D5-1017-4C1F-80CC-E55C239555A3

P698

Q28269674-4F78E438-EAE7-4CB4-AF4C-117166AC77B9

P921

Q28269674-F7047DA9-CF70-4767-B749-FB3994728E2A

P932

Q28269674-6463B7B7-A5B8-4A2D-ACB6-5089D1597AC8

P3181

P356

J.CCELL.2015.10.002

P1433

P1476

Targeting the AAA ATPase p97 a ...... ruption of Protein Homeostasis

@en

P2093

Antonett Madriaga

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

Bing Yao

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

Blake T Aftab

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

Brajesh Kumar

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

Daniel J Anderson

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

David Wustrow

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

Eduardo Valle

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

F Michael Yakes

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

Ferdie Soriano

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

Han-Jie Zhou

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

P2860

Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation

Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase

ER stress-induced cell death mechanisms

The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol.

AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation.

ATPase activity of p97-valosin-containing protein (VCP). D2 mediates the major enzyme activity, and D1 contributes to the heat-induced activity

Central pore residues mediate the p97/VCP activity required for ERAD

Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system

Expanding into new markets--VCP/p97 in endocytosis and autophagy

Structure-activity relationship study reveals ML240 and ML241 as potent and selective inhibitors of p97 ATPase

P304

653-65

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

P31

scholarly article

P3181

1891448

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

P356

10.1016/J.CCELL.2015.10.002

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

P407

P433

5

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

P478

28

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

P50

Jonathan Weissman

P577

2015-11-09T00:00:00Z

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

P5875

283583088

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

P698

26555175

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

P921

P932

4941640

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