Antimyeloma Effects of the Heat Shock Protein 70 Molecular Chaperone Inhibitor MAL3-101 - Wikidata - awgldk - TriplyDB

Antimyeloma Effects of the Heat Shock Protein 70 Molecular Chaperone Inhibitor MAL3-101

Antimyeloma Effects of the Heat Shock Protein 70 Molecular Chaperone Inhibitor MAL3-101

http://www.wikidata.org/entity/Q35251058

about

DangER: protein ovERload. Targeting protein degradation to treat myeloma The human HSP70 family of chaperones: where do we stand?Novel therapeutic strategies for multiple myeloma Contributions of academic laboratories to the discovery and development of chemical biology tools Combined chemical-genetic approach identifies cytosolic HSP70 dependence in rhabdomyosarcoma Heat shock protein responses to aging and proteotoxicity in the olfactory bulb.Identification of an allosteric small-molecule inhibitor selective for the inducible form of heat shock protein 70.The HSP70 modulator MAL3-101 inhibits Merkel cell carcinoma.Heat shock protein defenses in the neocortex and allocortex of the telencephalon.Chalazia Development in Multiple Myeloma: A New Complication Associated with Bortezomib Therapy.Chemical induction of Hsp70 reduces α-synuclein aggregation in neuroglioma cells.Dihydropyrimidinones and -thiones with improved activity against human polyomavirus family members Paradoxical resistance of multiple myeloma to proteasome inhibitors by decreased levels of 19S proteasomal subunits.Heat shock protein 70 regulates Tcl1 expression in leukemia and lymphomas.Chemical Tools to Investigate Mechanisms Associated with HSP90 and HSP70 in Disease.The HSP70 family and cancer Hsp70 protein complexes as drug targets.Heat shock proteins 27, 40, and 70 as combinational and dual therapeutic cancer targets.Opportunities and challenges for molecular chaperone modulation to treat protein-conformational brain diseases Heat shock proteins in multiple myeloma Heat shock protein 70 - the next chaperone to target in the treatment of human acute myelogenous leukemia?Hsp70 in cancer: back to the future.When Cancer Fights Back: Multiple Myeloma, Proteasome Inhibition, and the Heat-Shock Response.Heat shock protein 70 inhibitors. 1. 2,5'-thiodipyrimidine and 5-(phenylthio)pyrimidine acrylamides as irreversible binders to an allosteric site on heat shock protein 70 Efficacy of the HSP70 inhibitor PET-16 in multiple myeloma.MARCKS and HSP70 interactions regulate mucin secretion by human airway epithelial cells in vitro.The PI3K/Akt signaling pathway regulates the expression of Hsp70, which critically contributes to Hsp90-chaperone function and tumor cell survival in multiple myeloma.Targeting Heat Shock Proteins in Cancer: A Promising Therapeutic Approach HSPB1 deficiency sensitizes melanoma cells to hyperthermia induced cell death.Fluorescent-Linked Enzyme Chemoproteomic Strategy (FLECS) for Identifying HSP70 Inhibitors.N-Acetyl-l-Cysteine Protects Astrocytes against Proteotoxicity without Recourse to Glutathione.Proteasome and heat shock protein 70 (HSP70) inhibitors as therapeutic alternative in multiple myeloma.Cancer cell responses to Hsp70 inhibitor JG-98: Comparison with Hsp90 inhibitors and finding synergistic drug combinations.Dual targeting of HSP70 does not induce the heat shock response and synergistically reduces cell viability in muscle invasive bladder cancer

P2860

Q26825417-05024905-9A37-4205-BBAA-BB0125C7EDF8 Q28071416-82DDCCFF-9604-4B13-86A4-E3131C0C6533 Q28081590-5DEFD6DA-9DDC-47FC-ADBC-EAD1A5A19A84 Q28389188-CE9FB3E9-7F26-4348-9834-F38A16AB09A8 Q28830095-717936D7-915B-4FF8-9C5A-8AD5C6A126B6 Q30382422-10414D54-32F4-4064-8179-D3803C25E652 Q34747269-73A0CFB8-BBAA-4E06-BB6A-DF3655B9024E Q35138259-AB2A0DEE-16BF-445B-9D96-3E841C93EFBA Q35561538-4B4305C7-E471-4CDD-A6DD-D7DC2D66424C Q35868965-5B5FF482-5EB4-4F35-90BC-47C99C2FA067 Q35939982-6F3FAD6F-76F7-4331-AF61-F39AC1FC6130 Q36131702-555CAA87-D167-449A-8CC3-7AC6BFE488AB Q36150369-8CB13D53-A3A3-46DF-A231-B7F934CFE081 Q36529496-8026812C-81D4-43C7-8FEA-02E55FC62AAA Q36655158-52D60666-288E-4E10-BC87-20587C8E4F92 Q36895403-55A7D82B-2E9F-451E-8499-903A6EFE1152 Q38037745-FEC2D87D-2EA2-4565-A145-A7A6D53AC682 Q38085897-8FAFE60A-F14B-48B2-B550-C045E9D5CFAF Q38093796-5E547B0F-E49E-4520-9B22-3F4B855943BD Q38199919-DB17C01C-FFD3-4B97-859A-8FB8B0BB621A Q38222563-D4FBDDE3-5812-4137-A389-DD9FC2F46FD5 Q38263003-6F8F1402-9609-4A8A-B703-6DC869CAF2DA Q38503345-45E347D8-D6A2-49F8-B51A-5C05B6569359 Q38705756-DD8FF569-CC26-4BB0-A1F1-54AFABD4FB1B Q38852874-B4773797-4D83-4D42-B81F-F40483324EAE Q39837785-01C9D0E7-616A-4891-82CD-8D268124E56A Q41470772-F203236C-84CE-4A04-808C-A6FB9E0079B0 Q41660505-0AB16950-457F-418A-926A-7E77F06EEFEA Q41989169-53894E38-6A16-4868-83BF-E78F713EFE21 Q47362668-A28B631E-BCEE-4096-B9BD-C5CE33A1B9C9 Q47919698-5402CE6D-60D8-4B1D-A7F6-97966BDC6A2F Q49569621-909B83A6-3F59-4051-B289-E15D793EDFB4 Q50354200-E9359101-9D54-4DD9-9C62-533203E907AC Q58704620-6D2743E7-BEB7-4BF3-B7E8-AD6BC486DA3C

P2860

Antimyeloma Effects of the Heat Shock Protein 70 Molecular Chaperone Inhibitor MAL3-101

http://www.wikidata.org/entity/Q35251058

description

2011 nî lūn-bûn

@nan

2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի սեպտեմբերին 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

Antimyeloma Effects of the Heat Shock Protein 70 Molecular Chaperone Inhibitor MAL3-101

@ast

Antimyeloma Effects of the Heat Shock Protein 70 Molecular Chaperone Inhibitor MAL3-101

@en

type

label

Antimyeloma Effects of the Heat Shock Protein 70 Molecular Chaperone Inhibitor MAL3-101

@ast

Antimyeloma Effects of the Heat Shock Protein 70 Molecular Chaperone Inhibitor MAL3-101

@en

prefLabel

Antimyeloma Effects of the Heat Shock Protein 70 Molecular Chaperone Inhibitor MAL3-101

@ast

Antimyeloma Effects of the Heat Shock Protein 70 Molecular Chaperone Inhibitor MAL3-101

@en

P1433

Q35251058-C0EBD37E-B699-48D9-BC4F-EFAE508CCD27

P1476

Q35251058-E9B47B3C-363F-4313-956B-7CE3C9F453F2

P2093

Q35251058-08F90204-5391-4675-BC9C-F6DABF5972D6

Q35251058-2AFE464D-5FAA-48B5-8496-A505296694E1

Q35251058-77539B11-648B-4A0E-9834-EEDE8BDAF364

Q35251058-7E2D1EE2-2D57-42CA-9BFF-1519B295C70D

Q35251058-8AE3CC35-2335-414B-8899-CDAFA1CE2F4A

Q35251058-C7FAA13C-4915-4493-AD82-798015198B79

Q35251058-D5BD4BA8-095F-419B-8ABF-055F7811396F

Q35251058-F7EF484B-381C-43AE-98EA-2C078E51D869

Q35251058-FE7BBDA4-D54E-47D7-8565-B328EF678D18

P2860

Q35251058-012E5AAA-137E-4D8F-80B6-727BA9DAFC1B

Q35251058-04044027-0580-41AF-A558-E977A8C69780

Q35251058-06CEBCEA-4151-410D-A7A7-B062AEF2B504

Q35251058-082D8ADC-8321-4EC8-86D0-040FD84CE4FE

Q35251058-0A596537-AC04-4E23-9DD1-C45C1F8A5D37

Q35251058-0B8A5D82-3C86-4B53-BAB6-D9CF3502BFE3

Q35251058-0CAE359E-27EA-497A-827C-80A93B96C4A4

Q35251058-0F5D1B97-D87C-4D40-B9B5-CCFF333D1CEB

Q35251058-1AB2A581-FD06-4D0B-9742-E94A2C2833CA

Q35251058-1B13D4DE-476F-4061-88BA-3DE95C129DD2

P304

Q35251058-3100CF3C-4D80-498F-9500-49C457CE23FE

P31

Q35251058-9A1FF35D-FD7C-4F92-93E3-161E17E19A81

P356

Q35251058-19DA5944-709C-410D-B28F-AF218CC01237

P478

Q35251058-3063343F-4223-48B4-BF05-F95DCD238BA6

P50

Q35251058-0F25C7B6-2A96-42B0-9C64-9460F6F983BA

Q35251058-4DD58FB0-712C-4C96-9640-CE58B5972464

P577

Q35251058-64D74257-547A-441C-9CFE-A871B2C09B17

P5875

Q35251058-735D11D6-D5C8-4927-9DC6-205457C09778

P698

Q35251058-7A293ED1-FFC6-4582-9205-57A9374F87DB

P921

Q35251058-61C3B32B-A6C2-42EC-BD7A-57655E4F6E20

P932

Q35251058-CFC46AF2-1B76-4E9D-B0BB-AE3D63C35A20

P356

P1433

Journal of oncology

P1476

Antimyeloma Effects of the Heat Shock Protein 70 Molecular Chaperone Inhibitor MAL3-101

@en

P2093

Craig M Scott

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

Danielle Joseph

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

Jeffrey L Brodsky

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

Jeremy D Coplan

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

Marc J Braunstein

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

Olcay Batuman

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

Sadeaqua S Scott

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

Shannon Behrman

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

William Chrico

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

P2860

One step at a time: endoplasmic reticulum-associated degradation

Proteasome inhibitors disrupt the unfolded protein response in myeloma cells

The mammalian unfolded protein response

Progressively impaired proteasomal capacity during terminal plasma cell differentiation.

Endothelial progenitor cells display clonal restriction in multiple myeloma.

Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response

Lenalidomide, bortezomib, and dexamethasone combination therapy in patients with newly diagnosed multiple myeloma.

Interleukin-1 is essential for systemic inflammatory bone loss.

Binding of a small molecule at a protein-protein interface regulates the chaperone activity of hsp70-hsp40.

Heat shock protein 70 (hsp70) as an emerging drug target.

P304

232037

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

P31

scholarly article

P356

10.1155/2011/232037

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

P478

2011

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

P50

P577

2011-09-29T00:00:00Z

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

P5875

51697081

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

P698

21977030

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

P921

molecular chaperones

P932

3184436

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