Covalent and allosteric inhibitors of the ATPase VCP/p97 induce cancer cell death - Wikidata - awgldk - TriplyDB

Covalent and allosteric inhibitors of the ATPase VCP/p97 induce cancer cell death

Covalent and allosteric inhibitors of the ATPase VCP/p97 induce cancer cell death

http://www.wikidata.org/entity/Q28295447

about

Targeting p97 to Disrupt Protein Homeostasis in Cancer Nuclear assembly as a target for anti-cancer therapies Proteasome-mediated processing of Nrf1 is essential for coordinate induction of all proteasome subunits and p97 Altered cofactor regulation with disease-associated p97/VCP mutations Targeting the AAA ATPase p97 as an Approach to Treat Cancer through Disruption of Protein Homeostasis p97-dependent retrotranslocation and proteolytic processing govern formation of active Nrf1 upon proteasome inhibition Immune-associated proteins with potential inï¿½vivo anti-tumor activities are upregulated in lung cancer cells treated with umbelliprenin: A proteomic approach Suramin inhibits Hsp104 ATPase and disaggregase activity Dendrimer-Based Selective Proteostasis-Inhibition Strategy to Control NSCLC Growth and Progression BOK Is a Non-canonical BCL-2 Family Effector of Apoptosis Regulated by ER-Associated Degradation A non-canonical role of the p97 complex in RIG-I antiviral signaling USP7 is a SUMO deubiquitinase essential for DNA replication Tumorigenic and Immunosuppressive Effects of Endoplasmic Reticulum Stress in Cancer Systematic proteomics of the VCP-UBXD adaptor network identifies a role for UBXN10 in regulating ciliogenesis.VCP/p97 cooperates with YOD1, UBXD1 and PLAA to drive clearance of ruptured lysosomes by autophagy.Cdc48 and a ubiquitin ligase drive disassembly of the CMG helicase at the end of DNA replication Quantitative interaction mapping reveals an extended UBX domain in ASPL that disrupts functional p97 hexamers.Withaferin A Analogs That Target the AAA+ Chaperone p97.Multi-class computational evolution: development, benchmark evaluation and application to RNA-Seq biomarker discovery.A Mighty "Protein Extractor" of the Cell: Structure and Function of the p97/CDC48 ATPase.Degradation of the deubiquitinating enzyme USP33 is mediated by p97 and the ubiquitin ligase HERC2.Specific inhibition of p97/VCP ATPase and kinetic analysis demonstrate interaction between D1 and D2 ATPase domains Functional chromatography reveals three natural products that target the same protein with distinct mechanisms of action.Discovery of Sulfonamidebenzamides as Selective Apoptotic CHOP Pathway Activators of the Unfolded Protein Response.Evaluating p97 inhibitor analogues for their domain selectivity and potency against the p97-p47 complex.Novel VCP modulators mitigate major pathologies of rd10, a mouse model of retinitis pigmentosa.Proteotoxic crisis, the ubiquitin-proteasome system, and cancer therapy.A Fragment-Based Ligand Screen Against Part of a Large Protein Machine: The ND1 Domains of the AAA+ ATPase p97/VCP.Pharmacological targeting of valosin containing protein (VCP) induces DNA damage and selectively kills canine lymphoma cells A ROS-Activatable Agent Elicits Homologous Recombination DNA Repair and Synergizes with Pathway Compounds Designing Irreversible Inhibitors--Worth the Effort?Inhibitors of the AAA+ chaperone p97 Structure-Activity Study of Bioisosteric Trifluoromethyl and Pentafluorosulfanyl Indole Inhibitors of the AAA ATPase p97.The host ubiquitin-dependent segregase VCP/p97 is required for the onset of human cytomegalovirus replication.Chemical Modulation of Endocytic Sorting Augments Adeno-associated Viral Transduction.p97/VCP promotes Cullin-RING-ubiquitin-ligase/proteasome-dependent degradation of IκBα and the preceding liberation of RelA from ubiquitinated IκBα.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.The SMARCA2/4 ATPase Domain Surpasses the Bromodomain as a Drug Target in SWI/SNF-Mutant Cancers: Insights from cDNA Rescue and PFI-3 Inhibitor Studies.Mitochondrial ClpP activity is required for cisplatin resistance in human cells.

P2860

Q26740517-876ACC98-B545-4DC1-BB5F-FE863937699F Q26852806-AEBF3064-5A8F-4FF2-B4BE-7455E9AD024F Q28243388-5B027E35-11AB-4FC5-B93E-989E8F5D200A Q28258936-A1418C1E-EBB3-4514-AA07-631029A5E096 Q28269674-344BB07E-BC4B-402F-8796-6CE8F5FBFCC4 Q28306282-2F5EE7B2-AEC1-414F-899C-300561B8A89C Q28468345-FE429095-3AB8-4898-A130-E7CB47807513 Q28543672-7E4E5A34-B56F-4A94-B986-A0E58185D4C7 Q28552714-EFEC5DB3-1486-4070-8736-D11016040D4B Q28593563-52616336-6992-4D64-B71C-802ABBCCDE4B Q28596603-281CF82B-99FF-4A05-8CB9-0D8F45F2A982 Q28834083-BE5F7217-4AF9-4001-AB34-385ED3E9B4B3 Q29248711-39B0A030-19A6-4FC7-B6BD-5D9E2445CDB0 Q29871526-F7FBAEFC-1E88-4617-B40D-5BB557D48F42 Q30274624-4C296AF2-0913-403A-B1BC-23D020000EC6 Q30663146-1B677525-F8A9-4D47-9379-8B85292B0743 Q30826494-5E5D5AF1-94AF-4A78-BF20-310B9098D83F Q33360763-671685B3-F186-4190-8869-E428D0054B5E Q33601127-D6F5AFFE-3408-4979-ABE5-87545208374C Q33790385-F2A3F215-BF45-4E09-B8D6-10914CEBCE04 Q33888656-E914E311-AC8B-4817-A340-A93C9CF441E4 Q33916854-78D1CA9B-0A0D-4B5C-B4D8-DBB061473966 Q34295600-4382A6D6-0920-46C1-B9F6-014D0D0EF33A Q34701285-975D4522-DEA7-4D72-890C-B25620797084 Q34791483-D06E5E34-6917-4F8B-9D3D-04A206B6BA33 Q35219849-54BAC6DF-5F9F-4CC2-AC0F-738BD8DDC1B1 Q35408665-A227FDDA-F636-4573-8C89-FA83C4EE005C Q35563032-D3E8B1D5-47C1-4D1C-B556-CEC0B2E638FC Q35672293-FA75C1C0-01CA-468F-AF16-1EAD17A9FC85 Q35792527-5F321D8D-A864-413A-8020-75FA9264BB93 Q35848315-67E4AFA0-DB96-4E7D-AB45-9F70857999FA Q36078289-CFE62BBE-39C2-4757-A07B-36EE425A41D5 Q36367307-02F37C78-54B2-4EDE-BCED-5FA83BBA4221 Q36369230-5B95D4E0-4D01-498C-9BDA-B896DEC95EF7 Q36442455-E1670392-8F8F-451B-AF58-C540BC427C77 Q36476873-28598EEC-E75F-43A8-9387-8D86437E2A99 Q36485185-A05CB09C-F590-4093-94FB-6C1A396C66EA Q36579840-CF5980DD-25F0-4055-B1A0-3FC75CA634A8 Q36584337-FBE8FC62-C6D2-4F17-94F7-C9C690019A02 Q36677047-E8229AB2-D105-4759-AA6C-4C362F9A29AA

P2860

Covalent and allosteric inhibitors of the ATPase VCP/p97 induce cancer cell death

http://www.wikidata.org/entity/Q28295447

description

2013 nî lūn-bûn

@nan

2013 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

Covalent and allosteric inhibitors of the ATPase VCP/p97 induce cancer cell death

@ast

Covalent and allosteric inhibitors of the ATPase VCP/p97 induce cancer cell death

@en

Covalent and allosteric inhibitors of the ATPase VCP/p97 induce cancer cell death

@nl

type

label

Covalent and allosteric inhibitors of the ATPase VCP/p97 induce cancer cell death

@ast

Covalent and allosteric inhibitors of the ATPase VCP/p97 induce cancer cell death

@en

Covalent and allosteric inhibitors of the ATPase VCP/p97 induce cancer cell death

@nl

prefLabel

Covalent and allosteric inhibitors of the ATPase VCP/p97 induce cancer cell death

@ast

Covalent and allosteric inhibitors of the ATPase VCP/p97 induce cancer cell death

@en

Covalent and allosteric inhibitors of the ATPase VCP/p97 induce cancer cell death

@nl

P1433

Q28295447-B9077631-0C58-496A-9682-E9E1020EED9C

P1476

Q28295447-AF3D6371-1C92-40E7-97FC-15D7B9BB6318

P2093

Q28295447-0A6FEE79-5459-4B07-8A53-4E9DC9525CAD

Q28295447-1B2054C2-F574-4D9E-B722-FD07165EB20D

Q28295447-1B6AF77B-C290-47C3-851F-F8C375238365

Q28295447-22C00429-1742-411D-813F-0F5CD5D56C8E

Q28295447-265FFEC6-175A-4CCD-80A4-19871DAF9BCE

Q28295447-3255CB08-A32D-44A7-AB39-CC693B05E166

Q28295447-37E4752B-F38E-42FA-AB2C-477157667DAB

Q28295447-5C8D7597-B58A-4526-B3B0-7BB952507442

Q28295447-5EDD510D-3BA5-4317-9937-17BFAB968FC3

Q28295447-72AC619A-8DE9-4FB6-845F-648D52275BCA

P2860

Q28295447-001ABB0C-1116-434C-BF67-5EF7D623DC59

Q28295447-0F69D889-AD26-4A69-82D3-EF54CD2C63F7

Q28295447-178F6A4B-D117-41C3-9ECC-AD028DFBD5EE

Q28295447-1D1D4EFB-AE3A-493B-8488-F5674CE07D29

Q28295447-23DF541F-F338-4296-A90E-E471BA52A771

Q28295447-25C9CB74-D01E-488E-856F-CE2A9FD4238F

Q28295447-2949149A-DE83-4735-99B5-8FBB68199AAB

Q28295447-2D14103E-E2B9-4F1F-857D-8A0B87997D8C

Q28295447-2D1A7771-7BD5-43BC-87A3-7B6767BEE2F4

Q28295447-33D2CF20-7E4A-4E1B-9BFA-6E3B23B0BA8B

P2888

Q28295447-2C2FA538-7F05-4E0A-94C1-D5041EF3EAF1

P304

Q28295447-8AA7DB37-2898-475D-824A-5593219EE208

P31

Q28295447-D733DA92-0C78-4048-A6B0-40D6A86C2ECB

P3181

Q28295447-423318CE-6C1F-4A52-82B2-27CB208ED7F7

P356

Q28295447-1F9C499A-0831-4EE5-9835-943779B33E86

P407

Q28295447-4AC9F753-F74C-4741-9AEC-DCD91CF3218D

P433

Q28295447-1C013A48-312D-46E6-B0AB-7424E118A542

P478

Q28295447-BE3B96ED-A33C-47E1-B70C-05025511E7EE

P50

Q28295447-A56DDEE0-E8BF-4E6F-94FD-0915CD1427B7

Q28295447-AD918324-B585-40B1-9422-CD754F07CB0B

P577

Q28295447-B0951F0D-6309-495F-A3B0-AE83C2F7790E

P698

Q28295447-13144AAD-C09F-4214-AD3D-0A56628C2D34

P921

Q28295447-506A8CEA-2DAC-42E0-82B6-74E9D4AF2A26

P3181

P356

P1433

Nature Chemical Biology

P1476

Covalent and allosteric inhibitors of the ATPase VCP/p97 induce cancer cell death

@en

P2093

Antonella Isacchi

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

Antonella Leone

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

Arturo Galvani

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

Barbara Valsasina

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

Chihunt Wong

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

Christian Orrenius

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

Claudia Perrera

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

Daniela Asa

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

Daniele Donati

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

Dario Ballinari

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

P2860

Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation

UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover

Inhibition of p97-dependent protein degradation by Eeyarestatin I

The crystal structure of murine p97/VCP at 3.6A

Improved structures of full-length p97, an AAA ATPase: implications for mechanisms of nucleotide-dependent conformational change

NMS-P937, a 4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline derivative as potent and selective Polo-like kinase 1 inhibitor

The ATPase activity of purified CDC48p from Saccharomyces cerevisiae shows complex dependence on ATP-, ADP-, and NADH-concentrations and is completely inhibited by NEM.

VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD

AAA+ superfamily ATPases: common structure--diverse function

VCP (p97) regulates NFkappaB signaling pathway, which is important for metastasis of osteosarcoma cell line

P2888

P304

548-556

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

P31

scholarly article

P3181

2627016

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

P356

10.1038/NCHEMBIO.1313

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

P407

P433

9

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

P478

9

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

P50

Daniel J. Anderson

P577

2013-07-28T00:00:00Z

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

P698

23892893

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

P921

allosteric inhibitor