SAHA shows preferential cytotoxicity in mutant p53 cancer cells by destabilizing mutant p53 through inhibition of the HDAC6-Hsp90 chaperone axis. - Wikidata - wikimedia - TriplyDB

SAHA shows preferential cytotoxicity in mutant p53 cancer cells by destabilizing mutant p53 through inhibition of the HDAC6-Hsp90 chaperone axis.

SAHA shows preferential cytotoxicity in mutant p53 cancer cells by destabilizing mutant p53 through inhibition of the HDAC6-Hsp90 chaperone axis.

http://www.wikidata.org/entity/Q35207366

about

Chemical Variations on the p53 Reactivation Theme Mutant p53: One, No One, and One Hundred Thousand Regulation of Mutant p53 Protein Expression Targeting Oncogenic Mutant p53 for Cancer Therapy The Contrived Mutant p53 Oncogene - Beyond Loss of Functions Tumor suppressor p53 and its gain-of-function mutants in cancer The rebel angel: mutant p53 as the driving oncogene in breast cancer.UDP glucuronosyltransferase 1A expression levels determine the response of colorectal cancer cells to the heat shock protein 90 inhibitor ganetespib.Molecular Characterization of Epithelial Ovarian Cancer: Implications for Diagnosis and Treatment Arsenic trioxide reactivates proteasome-dependent degradation of mutant p53 protein in cancer cells in part via enhanced expression of Pirh2 E3 ligase NET silencing by let-7i in postural tachycardia syndrome.Phase I study of pazopanib and vorinostat: a therapeutic approach for inhibiting mutant p53-mediated angiogenesis and facilitating mutant p53 degradation.Histone deacetylases and cancer.Histone deacetylase inhibitors facilitate dihydroartemisinin-induced apoptosis in liver cancer in vitro and in vivo.Inhibition of DNA methyltransferase activity and expression by treatment with the pan-deacetylase inhibitor panobinostat in hepatocellular carcinoma cell lines.Mutant p53 - Heat Shock Response Oncogenic Cooperation: A New Mechanism of Cancer Cell Survival.Recent progress in targeting cancer.Novel oral histone deacetylase inhibitor, MPT0E028, displays potent growth-inhibitory activity against human B-cell lymphoma in vitro and in vivo.Hsp90 inhibitors and drug resistance in cancer: the potential benefits of combination therapies of Hsp90 inhibitors and other anti-cancer drugs Improving survival by exploiting tumour dependence on stabilized mutant p53 for treatment The Therapeutic Potential of AN-7, a Novel Histone Deacetylase Inhibitor, for Treatment of Mycosis Fungoides/Sezary Syndrome Alone or with Doxorubicin Histone deacetylase inhibitors suppress mutant p53 transcription via histone deacetylase 8.BAG2 promotes tumorigenesis through enhancing mutant p53 protein levels and function.Small-Molecule NSC59984 Restores p53 Pathway Signaling and Antitumor Effects against Colorectal Cancer via p73 Activation and Degradation of Mutant p53.Mutant p53: one name, many proteins.Antitumor activity of vorinostat-incorporated nanoparticles against human cholangiocarcinoma cells A unique histone deacetylase inhibitor alters microRNA expression and signal transduction in chemoresistant ovarian cancer cells Defining the role of histone deacetylases in the inhibition of mammary carcinogenesis by dietary energy restriction (DER): effects of suberoylanilide hydroxamic acid (SAHA) and DER in a rat model.Preclinical activity of combined HDAC and KDM1A inhibition in glioblastoma.It Takes 15 to Tango: Making Sense of the Many Ubiquitin Ligases of p53.Repositioning antipsychotic chlorpromazine for treating colorectal cancer by inhibiting sirtuin 1 Sensitization of multidrug-resistant human cancer cells to Hsp90 inhibitors by down-regulation of SIRT1.p63 the guardian of human reproduction.TAp73 protein stability is controlled by histone deacetylase 1 via regulation of Hsp90 chaperone function.Mutant p53 Amplifies Epidermal Growth Factor Receptor Family Signaling to Promote Mammary Tumorigenesis.Proteomic profiling identifies the inorganic pyrophosphatase (PPA1) protein as a potential biomarker of metastasis in laryngeal squamous cell carcinoma.Chaperone-mediated autophagy degrades mutant p53.Ribophorin II regulates breast tumor initiation and metastasis through the functional suppression of GSK3β.The consequence of oncomorphic TP53 mutations in ovarian cancer.Histone deacetylase regulation of ATM-mediated DNA damage signaling.

P2860

Q26749008-C87E41E3-9662-41E7-834B-5EE158556F0B Q26770576-C1A05957-8F56-49C4-995A-493133E78C0E Q26770579-E36D9B5E-34D7-4585-A35D-41B7479E982B Q26770856-61ABA7C9-F3B3-425D-A913-38FB4E4342C9 Q26772237-DCFDC77F-2013-4FF3-A5E1-5613C5CA3672 Q27000754-C5A866EC-7629-4928-8369-33D4BD7302CD Q27686765-1EBBEFE0-FA7A-4C6A-88B0-18CD269A8818 Q27853065-258D8BA5-6C1C-4C31-83E2-DA64F823663F Q28066904-5F0EB272-E35D-4EF5-A7D3-ECEA38E5CEEF Q28541801-2B87AA30-8216-4B49-B51D-4E3DDADD6371 Q33168474-E0877516-D5C1-4748-89B0-164ACE2D53DC Q33420276-D8F03AEE-43A2-4466-96F6-57B8D014C56A Q34298745-AB788B8A-F1CC-4FB6-84BD-30CF7F18FA36 Q34326588-E72E35DE-EE42-4F1A-8DB9-56BC9C026B50 Q34401887-02F5002F-2BDF-4A6B-B1C7-8EA02043C750 Q35522196-078E94AE-E572-4F53-8C84-E9BA508CA1BC Q35740782-9F14E77F-504E-45D1-B62A-0A08C1BC2783 Q35741591-E6316086-A630-4B10-BF6F-2D57A5F94A75 Q35823157-8C6CBC5B-D70B-4915-9676-40B1CD90D5AE Q35862613-72324010-DD0E-4B4D-85F0-ED58A86F1FFD Q35890561-5A1C78FE-7E20-4F3D-9394-BE47120974EB Q36019774-4BCA833C-87FC-4373-8E58-C7D66F0A85F2 Q36032139-5B40DF57-B21B-4EE2-A871-F230EDFED596 Q36070528-7F99648A-1273-4ECD-9E90-F9E593BB3664 Q36070574-40B626D4-0993-4EE6-AE91-1F2B62D4B237 Q36094595-EAD80A48-A5D1-42D7-AF12-2DA1153DE36B Q36129967-0CC52C0F-B524-4B5E-B849-E89D17F1472B Q36257402-B10AE30C-8641-48CD-82E2-E68864148C82 Q36288249-57715624-9823-497A-A703-20879C469839 Q36387588-E1648C97-B53C-4ED0-B99E-48E6B1831692 Q36413835-DDEA36E2-801E-4E41-B9C2-D79347BBA502 Q36546609-6891BB1C-5C64-45EB-B71D-10596B0A561F Q36581663-01D4F585-865B-4075-8B91-64A522DD7FC4 Q36685194-6D1F0C1F-5572-451B-8B36-C246B32D6445 Q36775403-FDDC82F1-091A-4DC8-B171-DAAA65415EF6 Q36924057-040F31BB-A414-4AC1-80E0-90C4D8F3B4C5 Q37098172-F664C227-85A8-4696-A2F1-F3A9157EEA36 Q37105454-6838416E-2B5B-4CA3-B506-4D1657BCF5D9 Q37225303-28CC015D-F9D2-4DE0-B2C9-1D9A99ED0079 Q37291739-2BD30593-B0E8-4414-92BE-BCDFA5BAE9CA

P2860

SAHA shows preferential cytotoxicity in mutant p53 cancer cells by destabilizing mutant p53 through inhibition of the HDAC6-Hsp90 chaperone axis.

http://www.wikidata.org/entity/Q35207366

description

2011 nî lūn-bûn

@nan

2011 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

SAHA shows preferential cytoto ...... he HDAC6-Hsp90 chaperone axis.

@ast

SAHA shows preferential cytoto ...... he HDAC6-Hsp90 chaperone axis.

@en

type

label

SAHA shows preferential cytoto ...... he HDAC6-Hsp90 chaperone axis.

@ast

SAHA shows preferential cytoto ...... he HDAC6-Hsp90 chaperone axis.

@en

prefLabel

SAHA shows preferential cytoto ...... he HDAC6-Hsp90 chaperone axis.

@ast

SAHA shows preferential cytoto ...... he HDAC6-Hsp90 chaperone axis.

@en

P1433

Q35207366-FC7B2279-8E61-4940-A087-4A26ECDFAE0C

P1476

Q35207366-BE870EA1-D09D-49E2-8018-AA0FF3DAFF10

P2093

Q35207366-11080C15-878B-454D-8E64-22492D8B30FC

Q35207366-1AD0CF84-D40B-4082-B4EA-03E90D5C280F

Q35207366-D2B6C5F2-3FAD-408B-BDF1-CF8401D7CFCE

P2860

Q35207366-011CE3CB-7D87-4E82-9B07-4DA8EBD71B67

Q35207366-020774AE-566C-4B2A-B7F2-81E2A2A74F69

Q35207366-048D6CEF-E769-46AA-B003-6471EF644E3E

Q35207366-1D9EC86B-A492-4F8B-9E28-76B7DA0AE09D

Q35207366-1EF37BE7-EE62-48B5-AB3C-02CFAB73398D

Q35207366-21B7A4AD-A43F-4BCF-BFC1-E48484F355BF

Q35207366-2FEC5000-4424-48A9-A330-427F77BEE56B

Q35207366-371CAF0B-1AB5-4DAF-B2C5-A2ACF2D6BDA0

Q35207366-39656933-608A-4110-9833-08282D642CE6

Q35207366-3C08B909-9A9D-400F-B429-5781D7E5103E

P2888

Q35207366-5EF166A6-ED2D-4152-967F-45139BF75E68

P304

Q35207366-14C8009E-BEFA-432D-94E4-EB5438E24306

P31

Q35207366-6C5572CF-9485-4F83-8A7C-88E0DC5C0715

P356

Q35207366-0C404BE6-3805-44E3-93BE-6B45C210495D

P433

Q35207366-872E6DB0-49FF-44DB-9F83-E75B11855FE3

P478

Q35207366-9601340C-E675-45E6-9F32-0CE266CEBD6A

P577

Q35207366-FCE2220E-73D5-41CA-8F47-F7B8CBB5C9B8

P5875

Q35207366-FB6B080E-C11F-49E5-AE45-5CF3258EFADE

P6179

Q35207366-AD53565C-FB42-4658-B686-19FCC67035F9

P698

Q35207366-880F8481-EBBD-4395-8A08-2D05189DD15C

P921

Q35207366-3388A62C-B584-4F64-8252-5622CC749524

Q35207366-44F675D4-B215-4165-A8FB-3959782BE9F6

P932

Q35207366-46E425F5-0891-42AD-BF21-A402406A98AF

P356

P1433

Cell Death & Differentiation

P1476

SAHA shows preferential cytoto ...... he HDAC6-Hsp90 chaperone axis.

@en

P2093

D Li

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

N D Marchenko

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

U M Moll

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

P2860

HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor

A Mutant-p53/Smad complex opposes p63 to empower TGFbeta-induced metastasis

Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53.

Sulforaphane destabilizes the androgen receptor in prostate cancer cells by inactivating histone deacetylase 6

The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent

Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer

Anticancer activities of histone deacetylase inhibitors

HSP90 and the chaperoning of cancer

The role of mutant p53 in human cancer.

Endogenous retrovirus drives hitherto unknown proapoptotic p63 isoforms in the male germ line of humans and great apes

P2888

P304

1904-1913

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

P31

scholarly article

P356

10.1038/CDD.2011.71

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

P433

12

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

P478

18

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

P577

2011-06-03T00:00:00Z

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

P5875

51187680

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

P6179

1045446987

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

P698

21637290

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

P921

molecular chaperones

P932

3170683

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