Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells. - Wikidata - wikimedia - TriplyDB

Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells.

Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells.

http://www.wikidata.org/entity/Q40310345

about

The RBCC gene RFP2 (Leu5) encodes a novel transmembrane E3 ubiquitin ligase involved in ERAD Noxa/Bcl-2 protein interactions contribute to bortezomib resistance in human lymphoid cells Blockade of XBP1 splicing by inhibition of IRE1α is a promising therapeutic option in multiple myeloma The antitumor natural compound falcarindiol promotes cancer cell death by inducing endoplasmic reticulum stress Novel strategies to target the ubiquitin proteasome system in multiple myeloma Lipid metabolic reprogramming in cancer cells Endoplasmic reticulum stress-mediated pathways to both apoptosis and autophagy: Significance for melanoma treatment Oncogenes strike a balance between cellular growth and homeostasis New molecular targets in mantle cell lymphoma DangER: protein ovERload. Targeting protein degradation to treat myeloma Advances in the understanding of mechanisms and therapeutic use of bortezomib Xenobiotic perturbation of ER stress and the unfolded protein response Small molecules in the treatment of systemic lupus erythematosus Treatment options and strategies for antibody mediated rejection after renal transplantation Evolving Paradigms in the Management of Multiple Myeloma: Novel Agents and Targeted Therapies The ubiquitin/proteasome system mediates entry and endosomal trafficking of Kaposi's sarcoma-associated herpesvirus in endothelial cells A clinical update on the role of carfilzomib in the treatment of relapsed or refractory multiple myeloma Touch and go: nuclear proteolysis in the regulation of metabolic genes and cancer The Role of Panobinostat Plus Bortezomib and Dexamethasone in Treating Relapsed or Relapsed and Refractory Multiple Myeloma: A European Perspective Clinical use of proteasome inhibitors in the treatment of multiple myeloma Novel therapeutic strategies for multiple myeloma Mechanism of Action of Bortezomib and the New Proteasome Inhibitors on Myeloma Cells and the Bone Microenvironment: Impact on Myeloma-Induced Alterations of Bone Remodeling Trial Watch: Proteasomal inhibitors for anticancer therapy Tumor progression and the different faces of the PERK kinase Glycogen synthase kinase 3 regulates expression of nuclear factor-erythroid-2 related transcription factor-1 (Nrf1) and inhibits pro-survival function of Nrf1 Nuclear factor-erythroid 2-related factor 1 regulates expression of proteasome genes in hepatocytes and protects against endoplasmic reticulum stress and steatosis in mice The ERAD inhibitor Eeyarestatin I is a bifunctional compound with a membrane-binding domain and a p97/VCP inhibitory group Reversible inhibitor of p97, DBeQ, impairs both ubiquitin-dependent and autophagic protein clearance pathways ERAD inhibitors integrate ER stress with an epigenetic mechanism to activate BH3-only protein NOXA in cancer cells PERK Integrates Oncogenic Signaling and Cell Survival During Cancer Development Synergistic apoptosis induction in leukemic cells by the phosphatase inhibitor salubrinal and proteasome inhibitors Secretion of novel SEL1L endogenous variants is promoted by ER stress/UPR via endosomes and shed vesicles in human cancer cells The involvement of SMILE/TMTC3 in endoplasmic reticulum stress response Compound C prevents the unfolded protein response during glucose deprivation through a mechanism independent of AMPK and BMP signaling Production of Infectious Dengue Virus in Aedes aegypti Is Dependent on the Ubiquitin Proteasome Pathway Proteasome Inhibition Suppresses Dengue Virus Egress in Antibody Dependent Infection Proteasome inhibition is partially effective in attenuating pre-existing immunity against recombinant adeno-associated viral vectors Tumorigenic and Immunosuppressive Effects of Endoplasmic Reticulum Stress in Cancer Proteasome inhibition reverses hedgehog inhibitor and taxane resistance in ovarian cancer.Targeting the UPS as therapy in multiple myeloma.

P2860

Q24297892-990B946F-71FD-4088-AB44-44584C2C3D8E Q24298561-AC09BF18-62EA-4655-9634-1DAF9713C27D Q24598483-D93461F7-0E59-4344-8EEE-F85D1562090F Q24606479-EDE6160E-97AC-43B0-A2DE-C0EEB5CEB3FA Q26773246-F31B9313-BAF6-4EEF-9BE1-1F21153C3290 Q26774859-0336F490-AC1D-4200-BB53-6A7F7DC512D7 Q26776032-C9652970-EA1F-42DE-8546-4CC3AE589094 Q26798085-8B1FB964-E842-4A39-A110-C18297CB7265 Q26821766-2DFF82DD-6AD3-42BF-9E0E-77D1B1B51C41 Q26825417-1440CCF1-E4EF-41F9-B8E4-3BAF34B46C2B Q26849940-D697EB8B-00F9-448B-95E8-20B07309CA2A Q26998690-E0DC00D4-B0F2-434A-AAA6-5B4C418D5E89 Q27010090-18E9A928-6A61-48BC-BD2B-0AD56D18B5E4 Q27021397-40B8BBD3-A5FB-4081-8BCA-D1FD986F850F Q27026478-F9DD62FB-F0E2-464A-9E73-45059F5F0113 Q27345534-9203D0CC-D923-45B4-88B2-D3C795FF3B8A Q28067148-5B20AB42-F9E0-45FD-8288-87573F90739B Q28068146-0F3F8CE7-96AF-4F1A-8E4A-7D4BB1B29B31 Q28069789-24C88F5E-9B00-4B21-8F48-27D406650EE8 Q28080999-83A61412-1C5C-4122-BF48-599F08338432 Q28081590-5547C3C3-576C-41C9-919C-D87BAD920346 Q28082335-8208006C-84ED-496C-9ABF-AECB921BFC56 Q28082910-C1FE8C55-808D-47D2-8C1D-EF7761E57E67 Q28087036-5CC62DCB-055A-44A9-BE89-024C90DDACA7 Q28289761-977B30E5-B0FC-4B17-BFAF-9E1B7E2E4E84 Q28291312-D0C17ED7-80EC-4248-93C9-DDBBA133FA53 Q28299691-4CD9BE89-9AD6-42AC-B183-9BF9DA4E0DD5 Q28306744-65D11527-6B03-4636-BB87-65DEF12EA6AA Q28307506-F593E46F-A77C-4318-8A1F-79126FD470FE Q28397172-7B702163-C92B-4912-921B-F7D8E10F0E17 Q28474489-32E0D028-3858-4121-AF27-2DE59BD57D9E Q28477193-C03C1BB9-7242-4B89-AE3B-ED5DD64C32F8 Q28478144-8CD3D09D-0D4F-43B9-8E20-F53B0D9E655A Q28483959-E8AAB91A-F703-4A9F-9884-473BCDB72556 Q28550947-3B65300A-2105-49A8-8260-D81C3C79FB46 Q28550953-79F1D07E-8B7C-40B9-A70F-B8616009F8DB Q28730577-BB370AF3-E8BB-4C58-AD60-869A7349FA9B Q29248711-EE1EED26-921C-41D9-AD07-75C85A101E7B Q30410019-B5E2483C-8D40-4E71-80BD-B62A7B5BDB65 Q33384287-A6398382-3986-46D5-AB83-8842DE1982F8

P2860

Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells.

http://www.wikidata.org/entity/Q40310345

description

2006 nî lūn-bûn

@nan

2006年の論文

@ja

2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

2006年论文

@zh

2006年论文

@zh-cn

name

Proteasome inhibitors induce a ...... nse in multiple myeloma cells.

@en

type

label

Proteasome inhibitors induce a ...... nse in multiple myeloma cells.

@en

prefLabel

Proteasome inhibitors induce a ...... nse in multiple myeloma cells.

@en

P1433

Q40310345-00F59658-9939-4CCF-A0D8-124E01C250C2

P1476

Q40310345-BF06593E-5411-48E8-A5A4-6180345215BC

P2093

Q40310345-4B892085-0738-4C76-8809-37B6C961D94E

Q40310345-60701C70-D840-498F-ACF6-4C4329CC7823

Q40310345-78D85044-4E71-4208-AEB2-B9C799E38140

Q40310345-CA6A24CD-B7FD-41F7-8BC4-5204BF280D3E

Q40310345-D2B3578B-D074-4037-83EC-FD7400508872

Q40310345-D8D4B7A3-5E64-4E86-9630-15B5D80DCEBA

P2860

Q40310345-016B8D99-CE22-4FAF-BF9F-E0A50805A0C4

Q40310345-101C006C-C799-4F68-A341-5DCF38FC1248

Q40310345-123DD96A-AC95-411F-BCAD-225598744936

Q40310345-12E940C4-0857-4A98-A66F-765E713E645E

Q40310345-18FC18A1-9F74-4A3F-9FEF-6F57F9A39E46

Q40310345-1A360050-9E4B-4BD3-A309-36FD893A657A

Q40310345-1CD1491D-1D9A-4C70-A1E9-737EC5B2A806

Q40310345-1D3E4634-6DD5-4DBB-BDA3-B78F77D2BC07

Q40310345-21B67035-9064-494B-98C9-E6AB2DB8809E

Q40310345-23A91CA6-2241-4E49-83E2-C02988C7F84F

P304

Q40310345-ED029135-D939-4FA1-8E8D-8AA360C2E0BB

P31

Q40310345-B0014B56-2619-4679-9308-7B04246420CC

P356

Q40310345-E03CBF72-B365-4426-9BA3-7CFCBE68ACEB

P407

Q40310345-33CDC5B9-47CC-46FF-A18A-C03482A1AECD

P433

Q40310345-5C37DE8C-A61C-4270-AE2F-2D436F03ECEE

P478

Q40310345-66B0B0F6-8890-4043-B28B-DF73E8C36AE8

P577

Q40310345-3B3E30E1-6079-45D8-ABBF-65571A8F81CC

P5875

Q40310345-F21B1DC7-55FC-4E50-97A2-BCDAE68EF777

P698

Q40310345-8B5BFE72-05FB-453A-8735-05C04C5C9B84

P932

Q40310345-4797CB32-F297-4C85-ADCB-F7F2B1E3B91D

P356

BLOOD-2005-08-3531

P1433

P1476

Proteasome inhibitors induce a ...... nse in multiple myeloma cells.

@en

P2093

Delia M Gutman

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

Esther A Obeng

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

Kelvin P Lee

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

Lawrence H Boise

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

Louise M Carlson

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

William J Harrington

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

P2860

Plasma cell differentiation requires the transcription factor XBP-1

Heat shock protein 90 modulates the unfolded protein response by stabilizing IRE1alpha.

Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control

Caspase-mediated cleavage of eukaryotic translation initiation factor subunit 2alpha

Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response

IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response

Phosphorylation of initiation factor 2 alpha by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast.

Cutting edge: proteasome involvement in the degradation of unassembled Ig light chains

Perk is essential for translational regulation and cell survival during the unfolded protein response

PERK mediates cell-cycle exit during the mammalian unfolded protein response

P304

4907-4916

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

P31

scholarly article

P356

10.1182/BLOOD-2005-08-3531

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

P407

P433

12

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

P478

107

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

P577

2006-02-28T00:00:00Z

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

P5875

7269587

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

P698

16507771

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

P932

1895817

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