Selective inactivation of a Fas-associated death domain protein (FADD)-dependent apoptosis and autophagy pathway in immortal epithelial cells. - Wikidata - awgldk - TriplyDB

Selective inactivation of a Fas-associated death domain protein (FADD)-dependent apoptosis and autophagy pathway in immortal epithelial cells.

Selective inactivation of a Fas-associated death domain protein (FADD)-dependent apoptosis and autophagy pathway in immortal epithelial cells.

http://www.wikidata.org/entity/Q33913756

about

FADD and caspase-8 control the outcome of autophagic signaling in proliferating T cells Autophagy, a process within reperfusion injury: an update FLIP and the death effector domain family Nanomaterials and autophagy: new insights in cancer treatment Autophagic and tumour suppressor activity of a novel Beclin1-binding protein UVRAG Autophagy in cell death: an innocent convict?Beclin-1-mediated Autophagy Protects Against Cadmium-activated Apoptosis via the Fas/FasL Pathway in Primary Rat Proximal Tubular Cell Culture.MDA-7/IL-24-induced cell killing in malignant renal carcinoma cells occurs by a ceramide/CD95/PERK-dependent mechanism.Fas-associated death domain (FADD) is a negative regulator of T-cell receptor-mediated necroptosis.Crosstalk between apoptosis and autophagy: molecular mechanisms and therapeutic strategies in cancer.Anticancer effects of imperatorin isolated from Angelica dahurica: induction of apoptosis in HepG2 cells through both death-receptor- and mitochondria-mediated pathways.The complex interplay between autophagy, apoptosis, and necrotic signals promotes T-cell homeostasis.Regulation of autophagy by sphingosine kinase 1 and its role in cell survival during nutrient starvation.TNF-alpha induces macroautophagy and regulates MHC class II expression in human skeletal muscle cells.Immune evasion by Kaposi's sarcoma-associated herpesvirus.Intertwined pathways of programmed cell death in immunity.Cleavage of p53-vimentin complex enhances tumor necrosis factor-related apoptosis-inducing ligand-mediated apoptosis of rheumatoid arthritis synovial fibroblasts Autophagy as a therapeutic target in cancer.Oncolytic vesicular stomatitis virus induces apoptosis via signaling through PKR, Fas, and Daxx.Modulation of Immune System by Kaposi's Sarcoma-Associated Herpesvirus: Lessons from Viral Evasion Strategies.TRIP-Br1 oncoprotein inhibits autophagy, apoptosis, and necroptosis under nutrient/serum-deprived condition.Effector caspase Dcp-1 and IAP protein Bruce regulate starvation-induced autophagy during Drosophila melanogaster oogenesis.Inhibition of hepatocyte autophagy increases tumor necrosis factor-dependent liver injury by promoting caspase-8 activation Apoptosis and autophagy: regulatory connections between two supposedly different processes.TNFalpha and reactive oxygen species in necrotic cell death.Mechanisms of lysosomal proteases participating in cerebral ischemia-induced neuronal death.Autophagy in CD4+ T-cell immunity and tolerance.A role for interleukin-1 alpha in the 1,25 dihydroxyvitamin D3 response in mammary epithelial cells.Interconnections between apoptotic, autophagic and necrotic pathways: implications for cancer therapy development.Autophagy-mediated antigen processing in CD4(+) T cell tolerance and immunity.Autophagy and Crohn's disease: at the crossroads of infection, inflammation, immunity, and cancer.Autophagy and cancer.Fas-associated death domain protein and adenosine partnership: fad in RA.The crosstalk between autophagy and apoptosis: where does this lead?Role of autophagy and its significance in cellular homeostasis.A novel anti-human DR5 monoclonal antibody with tumoricidal activity induces caspase-dependent and caspase-independent cell death.Estradiol inhibits osteoblast apoptosis via promotion of autophagy through the ER-ERK-mTOR pathway.Autophagic degradation of active caspase-8: a crosstalk mechanism between autophagy and apoptosis.Inhibition of ERK attenuates autophagy and potentiates tumour necrosis factor-alpha-induced cell death in MCF-7 cells Autophagy is a regulator of TRAIL-induced apoptosis in NSCLC A549 cells

P2860

Q24646372-CD52EDE2-DFC5-464E-AF7A-A31EB29C27E4 Q28086932-8B2A618A-4035-44E9-9474-658F1F008E46 Q28297969-E312F046-8CD1-4EF9-852D-A325700FAB3D Q28386642-818A86DC-89D5-4CBE-9FBD-FAEC591DF757 Q29615716-9C763FA9-4F13-4E8E-B70D-A245453859B9 Q29617604-2EEC649D-9300-4282-B16A-B69E0E828CFC Q33681263-DB899881-0B0C-4989-9226-DCC3553F1F37 Q33926871-8242AF64-970A-481E-91A0-338083EBA135 Q34059345-BAF773F7-5637-41C8-8256-DA64CA503E53 Q34102626-B813C333-F7E4-4E28-A893-A537B09520D0 Q34108042-207C391B-63F6-407F-BBB4-3BC2F17717D2 Q34252212-D4320B17-F4A2-4B6A-8BDF-37DD662910FA Q34484983-DFB12071-F89E-4BD0-B4A0-86B8EE78DBFF Q34537114-465F562B-E623-4996-A193-A49AAD00D4E4 Q34795543-2747627A-47D7-4451-871C-59EFD8D436E4 Q35108580-0DF1A479-46EA-4777-8444-EBE760716419 Q35221776-E43867E6-9424-4B64-B4BE-E24DB2486BBC Q35591562-9E44F957-1938-4C6E-B06D-441ADF538325 Q35784861-59F0450E-8A81-4071-8B1E-6788892ED432 Q35801076-8FD72C9E-9C25-4C9B-91C6-AE0E8B1643A9 Q36557212-759427E9-4500-4D20-84A5-4C3B16732777 Q36890091-D93D297B-FDAE-4133-AACE-F59FB2595F6D Q36920805-C9947923-C35B-4263-BE57-1A3E96CC0511 Q36996255-C2078A83-7655-461F-9146-5C701183EB41 Q37095205-51BE1003-5193-4502-89DD-F5B9F4DE22CA Q37120227-2517C85A-90E3-4304-8FBB-942052AC4F14 Q37219526-B0B57BFF-F81E-407B-90F7-0EC5BCFB0142 Q37288401-2C60DB7C-7582-49E6-B8E2-E604D7FBC99F Q37295309-BA06D017-010E-4B65-A65C-9C749C355B24 Q37675250-BB973196-12DE-4991-81C9-2C9C6BBDD12D Q37764367-24CA2C40-11BA-4267-A3C1-04AAFF732A9A Q37967998-45F7881B-3A1D-40AB-B15A-7E76E48726EB Q37976645-CA59C337-E130-4DC9-92FC-25B65225491E Q37982296-D45F9676-1253-41E9-906B-D740DCB42A03 Q38205378-70523412-3801-45DD-B808-833024889F0E Q38319762-AB9A3D2D-A06C-4119-A871-3F0ED9617BDC Q39142962-4138EBFB-6506-48F9-B8EF-2D322DFCDC5D Q39665408-8C39162F-6F57-4681-ADE4-B02FB690D623 Q40014283-F78F66EF-A79E-4C57-88E5-1026D3B99A07 Q41435998-F290207F-6FA5-43D5-817A-D54D0C92A7B6

P2860

Selective inactivation of a Fas-associated death domain protein (FADD)-dependent apoptosis and autophagy pathway in immortal epithelial cells.

http://www.wikidata.org/entity/Q33913756

description

2005 nî lūn-bûn

@nan

2005 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2005年の論文

@ja

2005年論文

@yue

2005年論文

@zh-hant

2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

@zh-tw

2005年论文

@wuu

name

Selective inactivation of a Fa ...... in immortal epithelial cells.

@ast

Selective inactivation of a Fa ...... in immortal epithelial cells.

@en

type

label

Selective inactivation of a Fa ...... in immortal epithelial cells.

@ast

Selective inactivation of a Fa ...... in immortal epithelial cells.

@en

prefLabel

Selective inactivation of a Fa ...... in immortal epithelial cells.

@ast

Selective inactivation of a Fa ...... in immortal epithelial cells.

@en

P1433

Q33913756-FC84C5AE-B2DA-4FB0-B511-81E3145A7ED3

P1476

Q33913756-5C8B2645-69B3-4C56-ACCE-5E0EA86B5373

P2093

Q33913756-2ACE19E4-1FDB-4AF8-BC19-277A93288E3E

Q33913756-42F81124-2A12-4956-962E-E83067701C32

Q33913756-7D13DC8D-72DC-40BE-B434-F01A74F13104

Q33913756-87DFF4B5-BE14-4742-84CB-A3F8F086CB40

Q33913756-90291E61-A8A1-4239-82F9-4A19A5B00EA8

Q33913756-BA0E7FCA-5538-4786-8B5A-292A45047C06

Q33913756-D5F27331-77D0-4FE4-AB41-6E5004579B42

Q33913756-E63D3A3D-B4A0-4C7D-B67D-1B5F97D43DCC

P2860

Q33913756-00738B6C-CF5C-4ABB-A2F3-996560F5CC4B

Q33913756-03735621-F67F-45CC-A121-97316403B5AF

Q33913756-0456731C-E56C-491A-80ED-253E14D6E3EA

Q33913756-169816D2-4A72-443E-8071-DFF264EF175A

Q33913756-202AD644-4582-42DA-B8C1-2EC7943FA82C

Q33913756-2761A26F-DDC9-4C7D-93EC-1C29B7BE46DD

Q33913756-2CDDE69A-0657-4D06-A75D-D8206B854B55

Q33913756-45F400DC-BB0A-43D0-A145-1872B5D1F439

Q33913756-56FC0B60-A652-4E3B-A930-2BF7E7AF522F

Q33913756-575824EB-5103-4047-A3A8-7C1BB0C4A1E0

P304

Q33913756-57E99C65-B207-47E4-B4CE-8CA54037C08E

P31

Q33913756-B87DAF9D-AF6C-4BA9-9EB5-BFC4D2CCAA2E

P356

Q33913756-AB7ECF07-79D0-4FE4-87D6-6E03F4E9B0E9

P433

Q33913756-BB8CC354-50BB-4FF4-A75B-3642902DCCFA

P478

Q33913756-94D3314C-CFA6-48F3-8D23-F8B03F5A4107

P577

Q33913756-ECC7F2EC-8914-44AC-BDE2-9D628912676D

P698

Q33913756-FA40DC1A-2154-4AA4-AD48-EDCE1D2DE02F

P921

Q33913756-D444D034-3B44-497A-8293-C44209859B75

P932

Q33913756-2DE20741-6FB4-4994-A539-A3D11C343CB1

P356

MBC.E04-10-0906

P1433

Molecular Biology of the Cell

P1476

Selective inactivation of a Fa ...... in immortal epithelial cells.

@en

P2093

Andrew Thorburn

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

Anuradha Rao

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

Franklin Moore

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

Jacqueline Thorburn

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

Ken W Grant

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

Lance R Thomas

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

Scott D Cramer

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

Wendy W Barclay

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

P2860

The Hallmarks of Cancer

Beclin 1, an autophagy gene essential for early embryonic development, is a haploinsufficient tumor suppressor

LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing

Promotion of tumorigenesis by heterozygous disruption of the beclin 1 autophagy gene

DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death

Induction of autophagy and inhibition of tumorigenesis by beclin 1

Mechanisms of caspase activation

Proliferation, cell cycle and apoptosis in cancer

c-MYC: more than just a matter of life and death

A unified model for apical caspase activation

P304

1189-1199

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

P31

scholarly article

P356

10.1091/MBC.E04-10-0906

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

P433

3

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

P478

16

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

P577

2005-01-05T00:00:00Z

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

P698

15635090

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

P921

P932

551484

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