To fold or not to fold: modulation and consequences of Hsp90 inhibition. - Wikidata - wikimedia - TriplyDB

To fold or not to fold: modulation and consequences of Hsp90 inhibition.

To fold or not to fold: modulation and consequences of Hsp90 inhibition.

http://www.wikidata.org/entity/Q33531705

about

Approaches for defining the Hsp90-dependent proteome.C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances Response of heat shock protein genes of the oriental fruit moth under diapause and thermal stress reveals multiple patterns dependent on the nature of stress exposure Inhibiting heat-shock protein 90 reverses sensory hypoalgesia in diabetic mice.Heat shock protein 90 in Alzheimer's disease 3-Arylcoumarin derivatives manifest anti-proliferative activity through Hsp90 inhibition.Proteomics: a strategy to understand the novel targets in protein misfolding and cancer therapy.Hsp90 C-terminal inhibitors exhibit antimigratory activity by disrupting the Hsp90α/Aha1 complex in PC3-MM2 cells.Engineering an antibiotic to fight cancer: optimization of the novobiocin scaffold to produce anti-proliferative agents.Design, synthesis, and biological evaluation of ring-constrained novobiocin analogues as hsp90 C-terminal inhibitors Molecular chaperone Hsp90 is a therapeutic target for noroviruses Heat shock response and insulin-associated neurodegeneration.Synthesis and evaluation of novologues as C-terminal Hsp90 inhibitors with cytoprotective activity against sensory neuron glucotoxicity.A systematic protocol for the characterization of Hsp90 modulators.Diabetic peripheral neuropathy: should a chaperone accompany our therapeutic approach?Development of Noviomimetics as C-Terminal Hsp90 Inhibitors Promoting Neuronal Tolerance of Diabetic Stress: Modulating Molecular Chaperones.Impaired surface expression and conductance of the KCNQ4 channel lead to sensorineural hearing loss X66, a novel N-terminal heat shock protein 90 inhibitor, exerts antitumor effects without induction of heat shock response The SOCS3-independent expression of IDO2 supports the homeostatic generation of T regulatory cells by human dendritic cells.Heat shock protein 70 is necessary to improve mitochondrial bioenergetics and reverse diabetic sensory neuropathy following KU-32 therapy.Alternate strategies of Hsp90 modulation for the treatment of cancer and other diseases.Gα12 structural determinants of Hsp90 interaction are necessary for serum response element-mediated transcriptional activation.Novel therapeutic strategies in multiple myeloma: role of the heat shock protein inhibitors.Broad action of Hsp90 as a host chaperone required for viral replication.The role of heat shock protein 90 in modulating ischemia-reperfusion injury in the kidney.Barcoding heat shock proteins to human diseases: looking beyond the heat shock response Synthesis and biological evaluation of coumarin replacements of novobiocin as Hsp90 inhibitors.Targeting the heat shock protein 90 dimer with dimeric inhibitors.Anticancer Inhibitors of Hsp90 Function: Beyond the Usual Suspects.Targeting the Diabetic Chaperome to Improve Peripheral Neuropathy.Potent antitumor activity of the novel HSP90 inhibitors AUY922 and HSP990 in neuroendocrine carcinoid cells.Development of a Grp94 inhibitor.Radiosensitizing effect of the novel Hsp90 inhibitor NVP-AUY922 in human tumour cell lines silenced for Hsp90α.Synthesis and biological evaluation of arylated novobiocin analogs as Hsp90 inhibitors.Synthesis and structure-activity relationships of EGCG analogues, a recently identified Hsp90 inhibitor Diverging Novobiocin Anti-Cancer Activity from Neuroprotective Activity through Modification of the Amide Tail.Triazole Containing Novobiocin and Biphenyl Amides as Hsp90 C-Terminal Inhibitors.Heat Shock Proteins in Vascular Diabetic Complications: Review and Future Perspective.Targeting Heat Shock Protein 70 to Ameliorate c-Jun Expression and Improve Demyelinating Neuropathy.

P2860

Q28247643-5E6C1600-A307-4A3D-8825-133C86016F51 Q28271643-EDC63615-EAB8-45C3-A953-EB00596D3D82 Q31087016-B9FBD5C5-5417-412E-BAC6-CEE843A22A55 Q34059530-A6851E8C-AE38-46B2-9A7C-2694CD83130F Q34413279-C49FE429-6274-4EDB-A42D-C6907F2D84A7 Q34547161-352F19B2-CC73-4AA9-9F62-1694330E1596 Q35116243-E6AEF90D-337B-4AAA-BB1C-099DEE5DCE18 Q35121121-98C4A3AE-9EF4-4198-9C84-DC5F2EEBF8A5 Q35188962-A3740189-C219-494A-82C6-CD2E1A2CDFB5 Q35564420-FD3E26A2-3EA5-48D6-A56A-DF3AF8300E76 Q35760516-B16B3664-9397-432F-96B2-E637760FA6BB Q35870561-99FB55AC-1563-4384-B655-C9FFADC065C0 Q36077840-B00586F1-E1D0-4D7F-A7B5-7D811B030DBB Q36201554-A1008AC0-A138-4C8E-A354-62C06B02F862 Q36293649-B6D87DD3-BAFF-42F0-99FC-EB4ACFCC3282 Q36473154-F546AF35-D072-4CDC-857A-CBBCA0D61577 Q37057856-357CC7BB-2EDC-4D3F-87E8-709D09B6583C Q37060221-390BAFCC-E32C-43B8-9E22-61EFB19152B3 Q37301905-244FD375-E22B-4468-973F-DC55B36CB9A1 Q37528354-D6BEC51B-8CFB-487D-A078-67F2DE8A63D8 Q37550709-0C562DDA-F676-4029-81CF-385007ACA987 Q37622446-F4EEFA29-3CD9-4704-A67E-977C6F77A86E Q37663374-AA5EEAB9-9E01-4799-BC5A-DB996A58FF52 Q37813152-91E0DAC7-B9C8-46EA-A84A-088B3CFDF5D5 Q37966479-3895919A-38F0-430D-8FB1-0A210690E958 Q38033199-1387495C-E310-4F7C-873A-78AD5094BD1E Q38203487-53A37F2D-E2F8-4F69-BD35-12463AF7C5CF Q38428349-91869AEB-77D2-4977-BC7E-15FED99D327F Q38604353-D28E3B21-1CCE-465B-A5E7-3E88728DE173 Q38750417-FFFE2372-BE0E-4D91-BA6F-923540E8BDBB Q38869328-BCD91BFA-0882-45F5-B421-A76C52E36D46 Q39084975-0149A0E3-3674-4501-97C3-E67E060113CA Q39340802-DB2CD678-309E-47E2-A0AC-10B7292AD49F Q39375187-3203EB2F-E998-4FDC-8142-02770762A25D Q39455379-752A7965-D6AF-4395-8150-86AE6E84F3A8 Q41873320-5CC9F753-03C6-4ABC-AEC5-AB77C0BA1276 Q42358762-2D28D841-C034-4ECD-A26A-CC9A9F9EE352 Q42945545-94034FE9-F024-44A7-9000-6C7EA6D5A628 Q47294278-04FD3ABC-D4F1-47D1-86DA-E9F19E9D07BC Q47421684-28608022-0690-446A-8568-C7F63BB619BC

P2860

To fold or not to fold: modulation and consequences of Hsp90 inhibition.

http://www.wikidata.org/entity/Q33531705

description

2009 nî lūn-bûn

@nan

2009 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

To fold or not to fold: modulation and consequences of Hsp90 inhibition.

@ast

To fold or not to fold: modulation and consequences of Hsp90 inhibition.

@en

To fold or not to fold: modulation and consequences of Hsp90 inhibition.

@nl

type

label

To fold or not to fold: modulation and consequences of Hsp90 inhibition.

@ast

To fold or not to fold: modulation and consequences of Hsp90 inhibition.

@en

To fold or not to fold: modulation and consequences of Hsp90 inhibition.

@nl

prefLabel

To fold or not to fold: modulation and consequences of Hsp90 inhibition.

@ast

To fold or not to fold: modulation and consequences of Hsp90 inhibition.

@en

To fold or not to fold: modulation and consequences of Hsp90 inhibition.

@nl

P1433

Q33531705-738DAC0B-BF67-4793-A1C9-42CB53C9DCD9

P1476

Q33531705-295AC195-EBCE-4740-BA65-50755596491F

P2093

Q33531705-011E0701-84CB-487B-AB4F-CD534AD17D54

Q33531705-B8FA7172-69A3-4ED1-88B7-65D43FFB2142

P2860

Q33531705-00ED5884-F5AB-4539-A070-50EADE2EAEA4

Q33531705-0227DCA6-0DA6-41BA-8142-D9CC0B68B357

Q33531705-03E0BBAD-127A-46EA-9806-0431C8817B29

Q33531705-043AFCA7-C9BA-4AAF-B7CE-BC311A75BBD5

Q33531705-04B8E8D5-97DC-4C41-8A3E-C1E78F2C2DA2

Q33531705-08CEB951-CC8B-4D97-8631-072DFA353393

Q33531705-09E3C81F-4510-4CDA-9679-231EA1E88565

Q33531705-0B9A4053-DC41-4FA9-BE22-3F10F1425958

Q33531705-0BC6CE96-7259-47B9-B1F0-D6E9C5B40DD8

Q33531705-0CA63ABD-1A1F-4A16-A37F-A6DD65812611

P304

Q33531705-DC6526C6-960C-4B75-94BB-57563D26E21C

P31

Q33531705-30DDDDC7-8532-45ED-8BA1-A9ED1BACE4D0

P356

Q33531705-E2390D35-397F-41D5-BA46-7E04806370B8

P433

Q33531705-63525965-6AA0-4C5F-967E-8B8B7F329DBA

P478

Q33531705-17CA3A8C-7FC0-4022-8553-BF3F6B4CC637

P577

Q33531705-7F9026E9-1B57-4A86-B5F5-3E7963030151

P5875

Q33531705-22387736-25D9-4C7D-8ABC-BB94353DFFCD

P698

Q33531705-D2F90EEF-7204-46F2-936E-DD5DA9E10717

P932

Q33531705-592464CD-D0E2-49B5-8540-03999E17E8CB

P356

P1433

Future Medicinal Chemistry

P1476

To fold or not to fold: modulation and consequences of Hsp90 inhibition.

@en

P2093

Brian S J Blagg

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

Laura B Peterson

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

P2860

Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions.

The Hallmarks of Cancer

The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins

Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40

Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone

Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system

Role of the cochaperone Tpr2 in Hsp90 chaperoning

Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70

The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions.

GrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1

P304

267-283

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

P31

scholarly article

P356

10.4155/FMC.09.17

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

P433

2

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

P478

1

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

P577

2009-05-01T00:00:00Z

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

P5875

41453204

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

P698

20161407

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

P932

2784693

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