A modified HSP70 inhibitor shows broad activity as an anticancer agent. - Wikidata - wikimedia - TriplyDB

A modified HSP70 inhibitor shows broad activity as an anticancer agent.

A modified HSP70 inhibitor shows broad activity as an anticancer agent.

http://www.wikidata.org/entity/Q30537961

about

Crystal structure of the stress-inducible human heat shock protein 70 substrate-binding domain in complex with peptide substrate The G protein α chaperone Ric-8 as a potential therapeutic target Functional analysis of Hsp70 inhibitors The human HSP70 family of chaperones: where do we stand?Structural basis for the inhibition of HSP70 and DnaK chaperones by small-molecule targeting of a C-terminal allosteric pocket Protein expression profile of HT-29 human colon cancer cells after treatment with a cytotoxic daunorubicin-GnRH-III derivative bioconjugate Evaluating melanoma drug response and therapeutic escape with quantitative proteomics Protein chaperones: a composition of matter review (2008 - 2013).Heat shock factor 1 confers resistance to Hsp90 inhibitors through p62/SQSTM1 expression and promotion of autophagic flux Hsp72 is targeted to the mitotic spindle by Nek6 to promote K-fiber assembly and mitotic progression.Quantitative proteomics of the yeast Hsp70/Hsp90 interactomes during DNA damage reveal chaperone-dependent regulation of ribonucleotide reductase.Hsc70 chaperone activity underlies Trio GEF function in axon growth and guidance induced by netrin-1.Mutations in the Yeast Hsp70, Ssa1, at P417 Alter ATP Cycling, Interdomain Coupling, and Specific Chaperone Functions.Chemical Tools to Investigate Mechanisms Associated with HSP90 and HSP70 in Disease.The HSP70 family and cancer HSP70 inhibition by 2-phenylethynesulfonamide induces lysosomal cathepsin D release and immunogenic cell death in primary effusion lymphoma.HSP70 Inhibition Limits FAK-Dependent Invasion and Enhances the Response to Melanoma Treatment with BRAF Inhibitors.Heat shock proteins regulate activation-induced proteasomal degradation of the mature phosphorylated form of protein kinase C.Comparison of the activity of three different HSP70 inhibitors on apoptosis, cell cycle arrest, autophagy inhibition, and HSP90 inhibition.Heat shock protein 70 - the next chaperone to target in the treatment of human acute myelogenous leukemia?Hsp70 in cancer: back to the future.Targeting Hsp70: A possible therapy for cancer.Inhibition of stress-inducible HSP70 impairs mitochondrial proteostasis and function.Targeting Allosteric Control Mechanisms in Heat Shock Protein 70 (Hsp70).Restoring Anticancer Immune Response by Targeting Tumor-Derived Exosomes With a HSP70 Peptide Aptamer.Efficacy of the HSP70 inhibitor PET-16 in multiple myeloma.Exogenously delivered heat shock protein 70 displaces its endogenous analogue and sensitizes cancer cells to lymphocytes-mediated cytotoxicity.Pifithrin-μ, an inhibitor of heat-shock protein 70, can increase the antitumor effects of hyperthermia against human prostate cancer cells.Targeting Heat Shock Proteins in Cancer: A Promising Therapeutic Approach Etoposide induces cell death via mitochondrial-dependent actions of p53.Analogs of the Allosteric Heat Shock Protein 70 (Hsp70) Inhibitor, MKT-077, as Anti-Cancer Agents.Lipid bodies containing oxidatively truncated lipids block antigen cross-presentation by dendritic cells in cancer.Hsp70: A Cancer Target Inside and Outside the Cell.N-Acetyl-l-Cysteine Protects Astrocytes against Proteotoxicity without Recourse to Glutathione.Domain Mapping of Heat Shock Protein 70 Reveals That Glutamic Acid 446 and Arginine 447 Are Critical for Regulating Superoxide Dismutase 2 Function.The Hsp70 inhibitor 2-phenylethynesulfonamide inhibits replication and carcinogenicity of Epstein-Barr virus by inhibiting the molecular chaperone function of Hsp70

P2860

Q21090602-8205B4CB-3237-4E8D-A4B1-6B0C90D0E830 Q26824363-B8905005-E883-430A-B0BC-12020B1A3993 Q27680671-BC32628E-0020-4DDF-B4E4-B20AED1C03BB Q28071416-AD109330-2161-47CC-8D6C-11C9A73E0B75 Q28246523-EAA94E1D-71D1-4D95-B544-BCC1593E74CC Q28537657-D130C57F-F55E-47EC-B383-F2A16A1DEDE2 Q33850665-84126965-6600-4827-98BD-9AA45E99CC69 Q34013266-9EDF2EE2-4B7B-45E9-A463-4D4B03102D60 Q35057071-CC9ED2F6-00D3-4621-A1F8-1A73DB5E42FF Q35594561-F1261421-CFC2-4CE6-8817-1FA6A7C4AC8B Q35799982-AD670AF0-6C8E-4998-BE81-2AB6385CF65D Q36014654-045B8F4A-A9B7-4EEE-BAC5-503BE2807135 Q36058976-6B451444-D4FA-42F1-9BB8-EAC2629EBF4E Q36655158-7BC7625C-4D4D-4360-92F3-E1B43EBE3100 Q36895403-A17B9AF7-2251-4F4C-86F4-2147C1ABE7E7 Q37062084-CF5C9AE1-9DA6-4EBB-AFC7-EBD539D67A6D Q37082577-3733981C-7DE1-4096-A3AA-E00DA0E5E3A4 Q37189447-DD553B06-9502-45C3-9AB1-54221682BEDE Q37591467-E5AABD4E-55BF-4598-9E92-BC6371E83BA0 Q38222563-E3AC8006-DA4B-424C-9A62-70574F641C03 Q38263003-65C7081B-B255-4B0F-91EB-89E186DF6B9E Q38742944-CBE352BC-C466-4FA4-8622-436EE4A13817 Q38796931-F2AE21BF-5842-4180-9827-41234514E643 Q38806853-4E2E9048-EF89-458F-9E06-78ADF6F4CE0C Q38817373-39100710-B9F1-4A94-97BE-763BE22B7389 Q38852874-0E905AC6-AA7F-41A5-AB56-A8BDA9FF81FF Q38998531-194E0D75-A1B8-4DCE-AA97-ECDAB18593DC Q39062053-D4B2FB5A-81C5-4BF7-8A49-D563B028A8AF Q41660505-A5376FAA-10B8-4621-BB25-C909C47E7CD8 Q41850633-760C8252-B613-4DCA-BEA7-78659438A7B1 Q42552152-F869F435-5949-40BD-8CDB-1CE9113474CD Q47113436-1668255A-F0E5-4B40-AD70-75EF5DD87379 Q47362469-6913DC1E-D825-42E6-B4C5-8642BFAA5933 Q47919698-E6CABF74-3729-48CB-9553-D7892382E6A2 Q49814595-BC9C28DE-2469-4D97-85D3-29AB7F25CDA1 Q56476012-1B82C32E-BFAA-497A-87CC-7D59D7B7E703

P2860

A modified HSP70 inhibitor shows broad activity as an anticancer agent.

http://www.wikidata.org/entity/Q30537961

description

2013 nî lūn-bûn

@nan

2013 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի հունվարին 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

A modified HSP70 inhibitor shows broad activity as an anticancer agent.

@ast

A modified HSP70 inhibitor shows broad activity as an anticancer agent.

@en

type

label

A modified HSP70 inhibitor shows broad activity as an anticancer agent.

@ast

A modified HSP70 inhibitor shows broad activity as an anticancer agent.

@en

prefLabel

A modified HSP70 inhibitor shows broad activity as an anticancer agent.

@ast

A modified HSP70 inhibitor shows broad activity as an anticancer agent.

@en

P1433

Q30537961-D8A8D9F3-BEB1-4641-93D3-5BA414EC90A2

P1476

Q30537961-CCE0A8E9-EF13-406C-A514-39B2FFF33E70

P2093

Q30537961-126CCD0A-8E7C-4007-B637-B35BA14B2043

Q30537961-1FB208A5-C9DE-4C4B-96F9-8EA553E96DF9

Q30537961-45A0A128-25BD-426B-B63C-9326FD0AA622

Q30537961-5EF258E2-7A4A-4DB2-8F42-727747C42C05

Q30537961-A9AF57B2-13B1-4C04-BAFA-0EC54C19859F

Q30537961-BDEB8274-BF28-4083-8212-1B07CEF9BDC6

Q30537961-E5A5F71C-CF64-474D-AAB5-6C954266B5E1

Q30537961-F13210FA-C50B-4536-A607-6DC1AF7D1567

Q30537961-F25702FC-EECD-4AF5-AD37-2E1F45B3EAB2

P2860

Q30537961-1D22AB92-A7DE-47EA-B647-A6C67A92A5FE

Q30537961-1D5C1881-430C-4C7D-AE7B-CE86395EEECA

Q30537961-1E7DBF00-46A9-468B-81B9-2B2C4E4FB710

Q30537961-21BECF5A-5F29-484E-B91F-5BA03D29178B

Q30537961-26729E1A-4583-4F60-9DD1-715E7A77EE80

Q30537961-4515858B-CE44-4682-90EB-CF29472C6F58

Q30537961-45E535AA-9629-4FF1-ACDB-BF0EC62BA7C1

Q30537961-46E0DD14-AD28-4C40-84EC-7B4373C14634

Q30537961-515CC3E7-7129-455B-A0C7-D3DE83B2BD7F

Q30537961-54CFAB3B-9814-4DD6-BB4C-7EC1B6ACD92F

P304

Q30537961-6CC9B322-9E64-4C3B-BB3E-70A58371C9AB

P31

Q30537961-CC3976D2-8819-42CF-B0A6-65581D3C68DC

P356

Q30537961-3B2C396A-2479-4D44-B36C-CF88C2EDA846

P433

Q30537961-F68969EF-63D7-47FE-BC24-63AB89776412

P478

Q30537961-192C5574-515F-4350-9846-50B89CA56870

P50

Q30537961-C1A4EBF8-85DE-4F15-8DCF-5E89FB77E5C9

Q30537961-D38A480A-C8A5-4EF9-AAC1-677FB98EDA2D

Q30537961-F539ACE3-75AE-45CB-B61D-F5123532BD2F

P577

Q30537961-4A14FA38-0BA4-4BFB-BF42-713F79E024FF

P698

Q30537961-1F022D60-4E26-43CE-8350-49B1A985F57C

P932

Q30537961-F0BA9AD6-3042-4529-BA56-1C27F8C0E28E

P356

1541-7786.MCR-12-0547-T

P1433

Molecular Cancer Research

P1476

A modified HSP70 inhibitor shows broad activity as an anticancer agent.

@en

P2093

Donna L George

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

Gao Zhang

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

Gregor M Balaburski

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

Jessie Villanueva

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

Julia I-Ju Leu

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

Mark D Andrake

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

Maureen E Murphy

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

Neil Beeharry

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

Seth Hayik

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

P2860

Hallmarks of Cancer: The Next Generation

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

Inhibition of macroautophagy triggers apoptosis

SCWRL and MolIDE: computer programs for side-chain conformation prediction and homology modeling

Two different mitotic checkpoint inhibitors of the anaphase-promoting complex/cyclosome antagonize the action of the activator Cdc20

Checkpoint inhibition of the APC/C in HeLa cells is mediated by a complex of BUBR1, BUB3, CDC20, and MAD2

Adenosine-derived inhibitors of 78 kDa glucose regulated protein (Grp78) ATPase: insights into isoform selectivity

UCSF Chimera--a visualization system for exploratory research and analysis

Rhodacyanine derivative selectively targets cancer cells and overcomes tamoxifen resistance

Genomic instability and enhanced radiosensitivity in Hsp70.1- and Hsp70.3-deficient mice

P304

219-229

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

P31

scholarly article

P356

10.1158/1541-7786.MCR-12-0547-T

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

P433

3

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

P478

11

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

P50

Meenhard Herlyn

Roland Dunbrack

P577

2013-01-09T00:00:00Z

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

P698

23303345

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

P932

3606282

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