Molecular mechanisms of caspase regulation during apoptosis - Wikidata - awgldk - TriplyDB

Molecular mechanisms of caspase regulation during apoptosis

Molecular mechanisms of caspase regulation during apoptosis

http://www.wikidata.org/entity/Q29617861

about

Protective effects and potential mechanisms of Pien Tze Huang on cerebral chronic ischemia and hypertensive stroke TNF-alpha mediates eosinophil cationic protein-induced apoptosis in BEAS-2B cells The phosphorylation-dependent regulation of mitochondrial proteins in stress responses HLA-DR alpha 2 mediates negative signalling via binding to Tirc7 leading to anti-inflammatory and apoptotic effects in lymphocytes in vitro and in vivo Notch inhibits apoptosis by direct interference with XIAP ubiquitination and degradation Integrin-linked kinase interacts with caspase-9 and -8 in an adhesion-dependent manner for promoting radiation-induced apoptosis in human leukemia cells Dissection of a signaling pathway by which pathogen-associated molecular patterns recruit the JNK and p38 MAPKs and trigger cytokine release DJ-1 inhibits TRAIL-induced apoptosis by blocking pro-caspase-8 recruitment to FADD The holo-apoptosome: activation of procaspase-9 and interactions with caspase-3 Up-regulation of the proapoptotic caspase 2 splicing isoform by a candidate tumor suppressor, RBM5 Blastocystis ratti induces contact-independent apoptosis, F-actin rearrangement, and barrier function disruption in IEC-6 cells Crystal structure of RAIDD death domain implicates potential mechanism of PIDDosome assembly Ripped to death Crystallization and preliminary X-ray crystallographic studies of the oligomeric death-domain complex between PIDD and RAIDD Genomic analysis of the immune gene repertoire of amphioxus reveals extraordinary innate complexity and diversity The developmentally active and stress-inducible noncoding hsromega gene is a novel regulator of apoptosis in Drosophila Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis Caspase 3 attenuates XIAP (X-linked inhibitor of apoptosis protein)-mediated inhibition of caspase 9 Human inhibitor of apoptosis proteins: why XIAP is the black sheep of the family Targeted cell killing by reconstituted caspases Engineering a dimeric caspase-9: a re-evaluation of the induced proximity model for caspase activation Suppressors of Cytokine Signaling in Sickness and in Health of Pancreatic β-Cells Targeted Nanotheranostics for Future Personalized Medicine: Recent Progress in Cancer Therapy Crosstalk between Autophagy and Apoptosis: Potential and Emerging Therapeutic Targets for Cardiac Diseases Onto better TRAILs for cancer treatment Molecular mechanisms of etoposide Pathophysiological role of different tubular epithelial cell death modes in acute kidney injury Inhibitor of apoptosis (IAP) proteins-modulators of cell death and inflammation Cell phones and male infertility: a review of recent innovations in technology and consequences Cell death and DAMPs in acute pancreatitis Regulation of cell death by transfer RNA Helical assembly in the death domain (DD) superfamily Caspases uncouple p27(Kip1) from cell cycle regulated degradation and abolish its ability to stimulate cell migration and invasion Transcriptome wide analyses reveal a sustained cellular stress response in the gill tissue of Trematomus bernacchii after acclimation to multiple stressors.An Engineered Split Intein for Photoactivated Protein Trans-Splicing High throughput ratio imaging to profile caspase activity: potential application in multiparameter high content apoptosis analysis and drug screening Contribution of caspase(s) to the cell cycle regulation at mitotic phase Caspase 3-Dependent Cell Death of Neurons Contributes to the Pathogenesis of West Nile Virus Encephalitis Death Domain Assembly Mechanism Revealed by Crystal Structure of the Oligomeric PIDDosome Core Complex Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein

P2860

Q21203063-5FC4425C-59C4-4A08-9333-D128CD4FE1BE Q21284187-A5472D33-D5DF-4FB5-AE63-A070BA7F6481 Q21285141-80CD5361-694D-4070-B546-7466A095D003 Q21562298-B5EF0670-155D-4F44-AEEE-48E0E8843FC4 Q24298097-1020AB9F-836F-45FC-968C-49A2DE64EE62 Q24300849-DE440219-904B-44DE-9B16-4B101D27B40E Q24312954-451B09BD-603D-4C0A-8EB3-BE5F262C446E Q24316876-83D90B06-2FE2-4396-ACE7-062803AF3357 Q24320222-5A8C38DD-12A3-469C-8172-3266AA65FE0D Q24321236-F8350736-CE9D-45F2-A483-F0665539F689 Q24549436-3916E81A-14EC-4785-B4F1-CB0722D859BE Q24610262-07784A97-4634-4836-BD38-A2D25867D212 Q24632980-D2C89B35-2B26-42FF-A471-3B552C2F0440 Q24642060-3DAF6333-A91F-4E16-A75A-BCA2F5201D74 Q24650676-1C64F444-B91A-43E5-90A8-CEEB0ED1C8DE Q24654990-459648AA-73A0-4B49-BCB8-9CDFADB2FB14 Q24655066-2417568D-E850-4141-9D22-A8CF89AF0914 Q24669658-7F77CADB-0EC3-4874-855D-5052E8C14ECF Q24670396-E5E638CE-5294-425B-B781-0BD7477259C5 Q24671860-A4C4C36F-D95D-4C51-898B-A007F851A6E3 Q24798064-80FA2FA4-BC0B-43DE-ABC9-3A35C094DF50 Q26744658-A4AAEB70-DAAC-4A13-88C5-EF48E951F08D Q26744832-963403D9-2A93-4A7A-BC1E-C6BC1835092E Q26767369-A8A2D152-002F-49DB-BD3F-058D60583598 Q26768160-78784C9D-3281-480F-B418-AD278CC69CE2 Q26776299-9AB83B15-8C5D-4202-A087-748824A0FF74 Q26785893-663E6F16-9C64-41E2-B56A-A0E141DC3DD3 Q26824586-08EDD7C5-966C-4D0A-B429-FAE9E154099F Q26830309-C94AD801-51D1-4E25-B41C-6802EB31735E Q26994999-46EF0B31-1917-427B-B7B7-1884DBD28EA7 Q27003645-47CCE3CC-14EB-4650-ABD0-04D207EA3445 Q27025156-BC6C742D-8D90-4AE6-A892-C03A9366349B Q27309926-CC945259-4FAA-49D1-ADC3-5CC75188F09B Q27316714-CD1691F3-2432-48A7-9070-DE0B0B3A26A4 Q27323039-600ED33C-7D78-4092-A8DC-A134C8D1FE51 Q27339765-01D79294-87FC-4533-92F5-0C4D55E799DB Q27348581-FB751F37-AF26-40A5-95D1-0AC9BD2EE97F Q27478369-A74700EE-C5F8-4E52-89FB-A25AD4CF17FD Q27643768-8FBBB3BE-3072-4650-A43A-5E165D8FDB80 Q27643981-61F19371-5902-4C59-9FFB-75162931AEE1

P2860

Molecular mechanisms of caspase regulation during apoptosis

http://www.wikidata.org/entity/Q29617861

description

2004 nî lūn-bûn

@nan

2004 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2004年の論文

@ja

2004年論文

@yue

2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

name

Molecular mechanisms of caspase regulation during apoptosis

@ast

Molecular mechanisms of caspase regulation during apoptosis

@en

type

label

Molecular mechanisms of caspase regulation during apoptosis

@ast

Molecular mechanisms of caspase regulation during apoptosis

@en

prefLabel

Molecular mechanisms of caspase regulation during apoptosis

@ast

Molecular mechanisms of caspase regulation during apoptosis

@en

P1433

Q29617861-51D78FF2-2425-4C30-A946-D473AD7D82DF

P1476

Q29617861-B78D6084-549A-435C-9B21-7A27D349638C

P2093

Q29617861-1835D945-DD48-4C76-A27F-09570378081E

Q29617861-7E03D317-9A0F-40CF-8C36-68BA8CE7BF61

P2860

Q29617861-006AF584-F829-4890-80FE-A4AB687B1B3C

Q29617861-030D292B-90B8-4F78-AF24-17F578964D0B

Q29617861-062D91B3-A617-42D1-A909-0AEB2BE48F8B

Q29617861-09F4DE41-291B-4A65-BA07-971DF1CA5C3E

Q29617861-0E47759C-6442-4620-B08F-82DDAA4408D8

Q29617861-169F0793-266B-422A-9B2E-19A03A130138

Q29617861-16EF7D37-888C-41EF-8B65-D0EF5D00C742

Q29617861-1B077ED8-B6FD-4EC9-8194-49B34298D301

Q29617861-1C36A351-87B8-4B94-8AA5-A1EE33ACA1CE

Q29617861-1D5666C9-CDD6-4349-B228-285BF9DF297C

P2888

Q29617861-F60C4CCD-71EF-475A-8DDA-D363F90C6D73

P304

Q29617861-65BC9D2B-4870-4DCA-9564-8711A8D52F07

P31

Q29617861-8D5AAD15-A1C5-44F9-B8B1-ADFDBFFFA9EF

P3181

Q29617861-038A6D75-96EB-4316-B257-2D663014E8C5

P356

Q29617861-7178D60C-B043-4BFB-B055-39C398E9E052

P407

Q29617861-B7EA5593-757A-4DBD-9FFE-1827D0623D4D

P433

Q29617861-7D40E116-B973-47A8-A9BF-69F7EC5B0F8F

P478

Q29617861-2504E1A1-464E-4451-BD7C-CF46727D7FB0

P577

Q29617861-3DDA0A56-6537-4E90-B604-BA9CBE5486AE

P5875

Q29617861-A1074096-F2AA-419B-AE94-DDBD755E91DA

P6179

Q29617861-DA1156BE-B244-42C8-9289-5DAF63ECE0B8

P698

Q29617861-819A131D-3D1A-4F3B-B9DE-2D4EDA1FA414

P3181

P356

P1433

Nature Reviews Molecular Cell Biology

P1476

Molecular mechanisms of caspase regulation during apoptosis

@en

P2093

Riedl SJ

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

Shi Y

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

P2860

An APAF-1.cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9

Inherited human Caspase 10 mutations underlie defective lymphocyte and dendritic cell apoptosis in autoimmune lymphoproliferative syndrome type II

The Hallmarks of Cancer

Livin, a novel inhibitor of apoptosis protein family member

Structure of a serpin-protease complex shows inhibition by deformation

ML-IAP, a novel inhibitor of apoptosis that is preferentially expressed in human melanomas

A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death

The serine protease Omi/HtrA2 regulates apoptosis by binding XIAP through a reaper-like motif

HtrA2 promotes cell death through its serine protease activity and its ability to antagonize inhibitor of apoptosis proteins

Mechanism of XIAP-mediated inhibition of caspase-9

P2888

P304

897-907

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

P31

scholarly article

P3181

472017

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

P356

10.1038/NRM1496

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

P407

P433

11

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

P478

5

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

P577

2004-11-01T00:00:00Z

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

P5875

8199336

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

P6179

1002939646

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

P698

15520809

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