Heat shock protein 90 controls HIV-1 reactivation from latency. - Wikidata - wikimedia - TriplyDB

Heat shock protein 90 controls HIV-1 reactivation from latency.

Heat shock protein 90 controls HIV-1 reactivation from latency.

http://www.wikidata.org/entity/Q37711958

about

Understanding HIV latency: the road to an HIV cure Selective targeting of the stress chaperome as a therapeutic strategy The heat shock protein 90 of Toxoplasma gondii is essential for invasion of host cells and tachyzoite growth Proteomic analysis of host brain components that bind to infectious particles in Creutzfeldt-Jakob disease.Stable Phenotypic Changes of the Host T Cells Are Essential to the Long-Term Stability of Latent HIV-1 Infection.Molecular chaperone Hsp90 is a therapeutic target for noroviruses Identification of Genes Whose Expression Profile Is Associated with Non-Progression towards AIDS Using eQTLs.Identification of matrine as a promising novel drug for hepatic steatosis and glucose intolerance with HSP72 as an upstream target The mTOR Complex Controls HIV Latency.HSP70 binding protein 1 (HspBP1) suppresses HIV-1 replication by inhibiting NF-κB mediated activation of viral gene expression.Inhibition of Heat Shock Protein 90 Prevents HIV Rebound Heat Shock Factor 1 Mediates Latent HIV Reactivation.Inhibition of HIV-1 reactivation by a telomerase-derived peptide in a HSP90-dependent manner.Strategies to target non-T-cell HIV reservoirs Activation of HIV-1 expression in latently infected CD4+ T cells by the small molecule PKC412.Hsp90 inhibitor reduces porcine circovirus 2 replication in the porcine monocytic line 3D4/31.Transcription Factor NF-κB: An Update on Intervention Strategies.HSP90: a promising broad-spectrum antiviral drug target.Microwave & magnetic proteomics of macrophages from patients with HIV-associated cognitive impairment.Heat Shock Protein 90 Facilitates Latent HIV Reactivation through Maintaining the Function of Positive Transcriptional Elongation Factor b (p-TEFb) under Proteasome Inhibition.Cellular fatty acid synthase is required for late stages of HIV-1 replication.Elucidating the in vivo interactome of HIV-1 RNA by hybridization capture and mass spectrometry.Class 1-selective histone deacetylase inhibitors enhance HIV latency reversal while preserving the activity of HDAC isoforms necessary for maximal HIV gene expression.The Glial Cell-Derived Neurotrophic Factor (GDNF)-responsive Phosphoprotein Landscape Identifies Raptor Phosphorylation Required for Spermatogonial Progenitor Cell Proliferation.Cyclin-dependent kinase 7 (CDK7)-mediated phosphorylation of the CDK9 activation loop promotes P-TEFb assembly with Tat and proviral HIV reactivation.Adapting to stress - chaperome networks in cancer.

P2860

Q28085296-F626C714-17F7-429C-BB7A-01EA67DC969A Q28248791-CA26551B-481B-4BB0-8DDF-2AECBA1057AB Q30544077-2225A78F-86CF-44D5-9235-D7B06E4D82DC Q34474526-783743F9-215F-4E0F-AB95-1AA821D2B245 Q35745365-77DE9741-4AED-4FA7-9831-20143CB302F1 Q35760516-B5EA9D7C-7FB2-4363-8D42-9F5B9F3BF5E3 Q35773031-3F5AB3F7-F6BF-4372-9B83-A2D77D2B6554 Q36016417-C2C53153-9177-4BB8-AE1A-6E7226EF6313 Q36225471-E61B73B7-8701-4A5C-A3C3-B09E65A92A35 Q36627905-EFE03725-DE77-409F-BDBE-B4F0FD467E8E Q36876244-49A3DB87-3EA1-4A62-BDF0-F0EA332DAAA0 Q36910965-D3AEDE19-51B2-4C34-BC9B-96C67D46C140 Q37057289-84A12AEE-F9C1-40F5-9332-ED01DEB2A890 Q37099969-A6B5DEB2-DCD5-4C14-89C9-EC89CC345FC8 Q37356604-72AD7A13-CD12-4D92-A431-0F82F6804701 Q38750354-5318CCDA-EC96-46D3-AE2F-EC5253E4D8BC Q38802627-0D431C12-77CB-48B6-B0DC-65166D5CFAAA Q40093256-DB679980-9C6F-4DCB-8114-10264702EA88 Q40107495-ADDE1FFA-4853-4619-A8E3-3007C9321E77 Q40473076-AD9278FD-EE22-4E60-BD64-B393FE61ECA7 Q41927731-01D2398C-476E-448B-8858-52D86775CF0D Q47094347-5E66B9C2-17B5-4F5A-B2D4-213680BB55B9 Q47234362-21F7F50C-5AB7-4FF5-8E33-31220F208947 Q48276432-0101FF23-A624-489D-B923-E70AE53BB115 Q54216878-45A1374C-3210-4306-B5EB-BB7A0F975C3B Q54425017-0213E30E-8159-4344-B41D-97B03F6F826C

P2860

Heat shock protein 90 controls HIV-1 reactivation from latency.

http://www.wikidata.org/entity/Q37711958

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 31 March 2014

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Heat shock protein 90 controls HIV-1 reactivation from latency.

@en

Heat shock protein 90 controls HIV-1 reactivation from latency.

@nl

type

label

Heat shock protein 90 controls HIV-1 reactivation from latency.

@en

Heat shock protein 90 controls HIV-1 reactivation from latency.

@nl

prefLabel

Heat shock protein 90 controls HIV-1 reactivation from latency.

@en

Heat shock protein 90 controls HIV-1 reactivation from latency.

@nl

P1433

Q37711958-FDBDEADE-63A4-4E8B-82FF-2EC2D099D474

P1476

Q37711958-29E00862-E557-403C-B956-CAE6DCE14A70

P2093

Q37711958-09185157-8E0C-4B13-A2C3-07BCAFCE815C

Q37711958-168EF60C-0805-4AD6-9FF2-B3D012EE7AED

Q37711958-18F2BCFA-2ADC-4F1E-B1A7-C7058A2BE0A5

Q37711958-24D6B99B-418E-404C-A52A-15AC761DA2A3

Q37711958-25967C80-0BAB-45DF-9C9D-3F24ECA66466

Q37711958-298AF9F6-B9A6-4C4D-B947-427048FE4671

Q37711958-67B87763-3B12-4CD9-BD3C-F09CC4D3986B

Q37711958-A74BDE00-BA8B-43EE-B940-7210613D8995

P2860

Q37711958-026583E6-4CA5-4980-8632-3ACBAF17C6A7

Q37711958-0AB0B025-5B54-48CC-BFDE-8AF4B9060A4C

Q37711958-0DFF509E-3B8A-4894-8383-CC6681312193

Q37711958-0F6FD592-1456-4334-9310-385938229718

Q37711958-13295915-F538-4825-BE15-6976BAC24210

Q37711958-17692E1E-8AA2-4F46-82E8-D797D49FD5B7

Q37711958-185CB152-3578-4B64-B3B2-DA8E9DA6AF01

Q37711958-1F018B0A-1D36-4320-9851-08D9A50F91E7

Q37711958-346DFFFE-C2A1-4886-997E-72A8D2F328D4

Q37711958-3573C877-D6E4-4D05-9BA0-794962428B78

P304

Q37711958-BA9C9730-96EA-4F8C-9A5E-7AAA9B78B2FF

P31

Q37711958-27C95F0C-4BF7-4A6B-B1AB-7BDD0D8F0E45

P356

Q37711958-E374F64A-15E7-4747-9784-AAC8F4014542

P407

Q37711958-D1539613-80F7-4DF7-B489-0FE4B4B470AD

P433

Q37711958-05BA201B-3726-4132-8ABB-4E4BD4033F08

P478

Q37711958-3F98EC67-5558-44EE-A7B2-705FC2976960

P50

Q37711958-17C228D5-7A2E-4A99-A56E-0ABF27020DC7

Q37711958-377CCC85-CD56-4475-AB77-8AE00ECB7214

Q37711958-DC339015-F625-4236-9BD3-E3836F3FE184

P577

Q37711958-A8A43C9A-6516-4744-B60C-F6516CA176DD

P698

Q37711958-3442254D-A47D-480C-B09D-77177FBFE808

P921

Q37711958-5498A422-234A-46A1-86DD-F0A6B54BD43F

P932

Q37711958-95FBDA8E-B53E-43C5-80FE-2B7DDBB5CE23

P356

PNAS.1320178111

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Heat shock protein 90 controls HIV-1 reactivation from latency.

@en

P2093

Aksana A Labokha

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

Alessandro Marcello

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

Alexander Zhyvoloup

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

Gianmarco Corazza

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

Ian Anderson

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

Jun Siong Low

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

Michael Weinberger

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

Russell A Kitson

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

P2860

IKK-1 and IKK-2: cytokine-activated IkappaB kinases essential for NF-kappaB activation

Phosphorylation of human I kappa B-alpha on serines 32 and 36 controls I kappa B-alpha proteolysis and NF-kappa B activation in response to diverse stimuli

The rising challenge of non-AIDS-defining cancers in HIV-infected patients

4,5-diarylisoxazole Hsp90 chaperone inhibitors: potential therapeutic agents for the treatment of cancer

Synthesis of 19-substituted geldanamycins with altered conformations and their binding to heat shock protein Hsp90

Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent

Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

Requirement for a kinase-specific chaperone pathway in the production of a Cdk9/cyclin T1 heterodimer responsible for P-TEFb-mediated tat stimulation of HIV-1 transcription

TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90

The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones

P304

E1528-37

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

P31

scholarly article

P356

10.1073/PNAS.1320178111

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

P407

P433

15

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

P478

111

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

P50

Christopher J. Moody

Ariberto Fassati

P577

2014-03-31T00:00:00Z

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

P698

24706778

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

P921

P932

3992654

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