The kinase inhibitor sorafenib induces cell death through a process involving induction of endoplasmic reticulum stress. - Wikidata - wikimedia - TriplyDB

The kinase inhibitor sorafenib induces cell death through a process involving induction of endoplasmic reticulum stress.

The kinase inhibitor sorafenib induces cell death through a process involving induction of endoplasmic reticulum stress.

http://www.wikidata.org/entity/Q35950143

about

Modulation of Autophagy by Sorafenib: Effects on Treatment Response Targeting the Bcl-2 family for cancer therapy Xenobiotic perturbation of ER stress and the unfolded protein response Targeting Mcl-1 for the therapy of cancer Compound C prevents the unfolded protein response during glucose deprivation through a mechanism independent of AMPK and BMP signaling Mcl-1 downregulation by pro-inflammatory cytokines and palmitate is an early event contributing to β-cell apoptosis Reduced immunosuppressive properties of axitinib in comparison with other tyrosine kinase inhibitors.Inositol-requiring enzyme 1alpha is a key regulator of angiogenesis and invasion in malignant glioma Phase II study of sorafenib in patients with relapsed or refractory lymphoma.Histone deacetylase inhibitors activate NF-kappaB in human leukemia cells through an ATM/NEMO-related pathway Pharmacological inhibition of cystine-glutamate exchange induces endoplasmic reticulum stress and ferroptosis A genome-wide RNA interference screen reveals an essential CREB3L2-ATF5-MCL1 survival pathway in malignant glioma with therapeutic implications.Bcl-2 antagonists interact synergistically with bortezomib in DLBCL cells in association with JNK activation and induction of ER stress.Sorafenib activates CD95 and promotes autophagy and cell death via Src family kinases in gastrointestinal tumor cells.Sorafenib: complexities of Raf-dependent and Raf-independent signaling are now unveiled.Sorafenib/regorafenib and lapatinib interact to kill CNS tumor cells.Stat5 regulates cellular iron uptake of erythroid cells via IRP-2 and TfR-1.Melanoma differentiation associated gene-7/interleukin-24 potently induces apoptosis in human myeloid leukemia cells through a process regulated by endoplasmic reticulum stress.Dinaciclib (SCH727965) inhibits the unfolded protein response through a CDK1- and 5-dependent mechanism A novel proteasome inhibitor acting in mitochondrial dysfunction, ER stress and ROS production.In vitro and in vivo interactions between the HDAC6 inhibitor ricolinostat (ACY1215) and the irreversible proteasome inhibitor carfilzomib in non-Hodgkin lymphoma cells Sorafenib synergizes with metformin in NSCLC through AMPK pathway activation.Inhibition of MEK/ERK1/2 sensitizes lymphoma cells to sorafenib-induced apoptosis Mechanism by which Mcl-1 regulates cancer-specific apoptosis triggered by mda-7/IL-24, an IL-10-related cytokine Identification of known drugs targeting the endoplasmic reticulum stress response.Gefitinib and Erlotinib Lead to Phosphorylation of Eukaryotic Initiation Factor 2 Alpha Independent of Epidermal Growth Factor Receptor in A549 Cells FADD cleavage by NK cell granzyme M enhances its self-association to facilitate procaspase-8 recruitment for auto-processing leading to caspase cascade Inhibition of Bcl-2 antiapoptotic members by obatoclax potently enhances sorafenib-induced apoptosis in human myeloid leukemia cells through a Bim-dependent process Suppression of PP2A is critical for protection of melanoma cells upon endoplasmic reticulum stress.Lapatinib and obatoclax kill breast cancer cells through reactive oxygen species-dependent endoplasmic reticulum stress.A combination of sorafenib and nilotinib reduces the growth of castrate-resistant prostate cancer.Autophagy-dependent EIF2AK3 activation compromises ursolic acid-induced apoptosis through upregulation of MCL1 in MCF-7 human breast cancer cells.A SPRY2 mutation leading to MAPK/ERK pathway inhibition is associated with an autosomal dominant form of IgA nephropathy Nexavar/Stivarga and viagra interact to kill tumor cells.GRP78/Dna K Is a Target for Nexavar/Stivarga/Votrient in the Treatment of Human Malignancies, Viral Infections and Bacterial Diseases.Artemisinin-derived dimer ART-838 potently inhibited human acute leukemias, persisted in vivo, and synergized with antileukemic drugs.Vorinostat and sorafenib synergistically kill tumor cells via FLIP suppression and CD95 activation.Vemurafenib potently induces endoplasmic reticulum stress-mediated apoptosis in BRAFV600E melanoma cells.p21(Cip1) protects against oxidative stress by suppressing ER-dependent activation of mitochondrial death pathways.The Bruton tyrosine kinase (BTK) inhibitor PCI-32765 synergistically increases proteasome inhibitor activity in diffuse large-B cell lymphoma (DLBCL) and mantle cell lymphoma (MCL) cells sensitive or resistant to bortezomib.

P2860

Q26745320-5F3504D4-CEFA-4534-A7C2-9DFB83380B09 Q26866936-7FD83A43-A86C-41C0-8876-A78291E5D1E7 Q26998690-3E374655-620C-47B1-9167-E0079ADA3AF4 Q27011870-2CBC6835-24B7-4C54-B930-9B807FA08169 Q28483959-B6965BAA-AF58-40CA-8F54-E1AC94494DE4 Q28571868-4301131D-EDE9-4943-A319-99C9EA37301B Q30317831-2E650BA5-D0C4-4592-8D69-F363F04525AB Q30496396-DA787EDA-5014-4753-896E-47356F7AA226 Q33401136-871B8FCF-4645-48D4-ADC0-ECAD5AD82458 Q33744417-B6013727-112C-41A8-B2EA-9800087F6C02 Q33745283-BD01D3C3-C537-4B98-AC77-CEB02A7442FE Q33900952-E5E890D0-45DF-4F9F-A350-C0D234EC0C22 Q33989217-D9CFF289-F3D7-42BD-8C5C-02B524F57EA5 Q34104350-D0253FC6-21EC-4D2B-A099-11B40350A547 Q34241371-DC321B7D-8973-4C36-8D06-2F82C780A4D8 Q34276149-3BD3E7C5-26F7-4456-AA3F-68D6F70228C6 Q34293299-663BA6B7-4875-45FE-9016-5AAD97D6BBB2 Q34359570-BCF6CA77-6565-4FF2-B9EF-24B2ED3B7E3D Q34393767-A4757A16-FA71-4AE9-89FF-CC0A2572C54C Q34414191-E060C4B2-1549-4D0B-8D8C-9ABB7858E42A Q35007061-B4CD172F-8400-41E9-A200-46EFB5863FCC Q35035126-8175BDEE-687E-4019-BE16-0E9EF277A912 Q35147986-5B99870A-361E-45C1-BBB9-C15913F63DAF Q35209685-30F98BD8-249D-41F3-B5F4-94B763AADE29 Q35618325-C8058DC2-4B4C-4D8D-BBEB-7F01570D2FBD Q35750388-AA9B7488-8BEE-42CD-ACF4-D32AD271E2BD Q35840521-541004AB-1446-41E9-8CD6-CF94B32B463E Q36057887-60C1430F-1BFE-4707-90F4-06CFD711768C Q36072016-53BBD3C7-C8EC-4F5F-B6AC-44CAD1B08E9E Q36412836-CD726145-88D6-4233-9546-3158A0C3F6E8 Q36462972-FD92EC2F-920D-4839-B5A6-4E472C6245F6 Q36556245-25D7EDDF-2720-4B7F-B1B1-CA914FFA19C4 Q36695721-96353A23-2693-4827-A232-C0D87C469395 Q36808335-49B1F2BF-EB09-4C12-8A8D-9724BBF5AF39 Q36830763-32C6B8D1-D313-446B-A1CE-6B2F9822494D Q36916456-8C94FEDB-ABAA-4B7B-8EAA-97F4BC6946EC Q36922674-0C5B379A-4CA0-4FAE-995F-F26A899EFD67 Q36974839-9A41E879-5124-46CB-A455-B81A588D75AE Q37074474-3A3338A1-D50D-45EA-9F25-C712C72036A7 Q37084564-0A2276E5-7C2F-4BEF-A9E3-18EDBD276ECA

P2860

The kinase inhibitor sorafenib induces cell death through a process involving induction of endoplasmic reticulum stress.

http://www.wikidata.org/entity/Q35950143

description

2007 nî lūn-bûn

@nan

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

2007年论文

@zh

2007年论文

@zh-cn

name

The kinase inhibitor sorafenib ...... endoplasmic reticulum stress.

@ast

The kinase inhibitor sorafenib ...... endoplasmic reticulum stress.

@en

type

label

The kinase inhibitor sorafenib ...... endoplasmic reticulum stress.

@ast

The kinase inhibitor sorafenib ...... endoplasmic reticulum stress.

@en

prefLabel

The kinase inhibitor sorafenib ...... endoplasmic reticulum stress.

@ast

The kinase inhibitor sorafenib ...... endoplasmic reticulum stress.

@en

P1433

Q35950143-8DD42806-1EC3-4E06-90B9-F3DD199231A1

P1476

Q35950143-86F8797D-B08F-4891-9E9F-AF68695D40B2

P2093

Q35950143-4920F7D0-1767-47B3-86DF-237B570CB57D

Q35950143-6E9E96A5-5B9B-41C0-AF50-9C4AC6D4C332

Q35950143-76D586FF-4E8E-4144-B4C1-A40DBB60FE85

Q35950143-87E60135-9325-400F-A48E-E7E91B092235

Q35950143-8B94C0CA-8E62-4E5D-BBEE-E96C9EDFCAAF

Q35950143-BEF40DAA-515B-4DD9-BCB9-97DD9BC5A2A2

P2860

Q35950143-04BE7C99-DD14-41E0-9BA9-27AAA8351E8D

Q35950143-0D2B0035-7C12-4211-8D65-CF0242864A4E

Q35950143-0EC9BEB2-D833-4C12-A660-E7EAF070F4D6

Q35950143-1290081F-6662-4AE9-AF65-A75D491BD321

Q35950143-130EEBA2-4332-4CE6-BF0E-C61B00A603D6

Q35950143-1859F013-E52D-45C8-B7EC-5691445029B9

Q35950143-19039312-6CA9-469E-9966-623FB732D530

Q35950143-19C11ED5-8F31-4D09-BEF1-1A97845352F5

Q35950143-1BB10E11-DC44-454A-B199-7549E244337A

Q35950143-1EE7F84E-BBC0-4C2B-8699-E6710671E931

P304

Q35950143-3085B959-56BA-4167-8F36-4E26352A053F

P31

Q35950143-4EB7681B-FECD-4859-A98A-A0BC9E10B3A9

P356

Q35950143-3DA0E5AD-0F18-4989-8700-BB277DD48B10

P407

Q35950143-7B1AF7A0-4E2E-4A17-826B-3754F0BE88D5

P433

Q35950143-13F3AA8F-7B56-4C31-965D-592AEBA31640

P478

Q35950143-F968EA86-0E4C-4614-BAE9-458EF1CFE025

P50

Q35950143-51428C33-F676-4B16-A011-85082CA6DFFE

P577

Q35950143-0A534477-6E0D-49D9-B7A4-D437B0FC7DC8

P698

Q35950143-8B0A731D-2A2D-497D-ACCB-148872375C27

P921

Q35950143-5BC2FE3C-4060-4120-98E2-880C76FA9642

P932

Q35950143-C996F752-0110-4E33-A81F-6023BA80A85C

P356

P1433

Molecular and Cellular Biology

P1476

The kinase inhibitor sorafenib ...... endoplasmic reticulum stress.

@en

P2093

Eric Maynard Davis

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

Joseph Reza Habibi

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

Mohamed Rahmani

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

Steven Grant

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

Timothy Ryan Crabtree

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

Tri K Nguyen

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

P2860

XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor

ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats

De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling

Proapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1alpha

Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death

Endoplasmic reticulum stress: cell life and death decisions.

Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2alpha.

MCL1, a gene expressed in programmed myeloid cell differentiation, has sequence similarity to BCL2

Mutations of the BRAF gene in human cancer

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

P304

5499-5513

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

P31

scholarly article

P356

10.1128/MCB.01080-06

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

P407

P433

15

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

P478

27

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

P50

P577

2007-06-04T00:00:00Z

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

P698

17548474

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

P921

endoplasmic reticulum

P932

1952105

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