Regulation of anti-apoptotic BCL2-proteins by non-canonical interactions: the next step forward or two steps back? - Wikidata - awgldk - TriplyDB

Regulation of anti-apoptotic BCL2-proteins by non-canonical interactions: the next step forward or two steps back?

Regulation of anti-apoptotic BCL2-proteins by non-canonical interactions: the next step forward or two steps back?

http://www.wikidata.org/entity/Q37928566

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Upregulation of miR-150* and miR-630 induces apoptosis in pancreatic cancer cells by targeting IGF-1R.BAK activation is necessary and sufficient to drive ceramide synthase-dependent ceramide accumulation following inhibition of BCL2-like proteins.Structural biology of the Bcl-2 family and its mimicry by viral proteins Protect and serve: Bcl-2 proteins as guardians and rulers of cancer cell survival.Multipolar functions of BCL-2 proteins link energetics to apoptosis The Bcl-2 family: structures, interactions and targets for drug discovery.Regulation of ceramide channel formation and disassembly: Insights on the initiation of apoptosis.PI3K-Akt Signal Transduction Molecules Maybe Involved in Downregulation of Erythroblasts Apoptosis and Perifosine Increased Its Apoptosis in Chronic Mountain Sickness.

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P2860

Regulation of anti-apoptotic BCL2-proteins by non-canonical interactions: the next step forward or two steps back?

http://www.wikidata.org/entity/Q37928566

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artikel ilmiah

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Regulation of anti-apoptotic B ...... tep forward or two steps back?

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Regulation of anti-apoptotic B ...... tep forward or two steps back?

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Regulation of anti-apoptotic B ...... tep forward or two steps back?

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Regulation of anti-apoptotic B ...... tep forward or two steps back?

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prefLabel

Regulation of anti-apoptotic B ...... tep forward or two steps back?

@en

Regulation of anti-apoptotic B ...... tep forward or two steps back?

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Journal of Cellular Biochemistry

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Regulation of anti-apoptotic B ...... tep forward or two steps back?

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Levi J Beverly

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P2860

BAR: An apoptosis regulator at the intersection of caspases and Bcl-2 family proteins

Aven, a novel inhibitor of caspase activation, binds Bcl-xL and Apaf-1

A novel protein, RTN-XS, interacts with both Bcl-XL and Bcl-2 on endoplasmic reticulum and reduces their anti-apoptotic activity

The association of Aiolos transcription factor and Bcl-xL is involved in the control of apoptosis

p53 has a direct apoptogenic role at the mitochondria

Bcl-2 and Bcl-XL regulate proinflammatory caspase-1 activation by interaction with NALP1

HSpin1, a transmembrane protein interacting with Bcl-2/Bcl-xL, induces a caspase-independent autophagic cell death

Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis

Mechanisms of apoptosis sensitivity and resistance to the BH3 mimetic ABT-737 in acute myeloid leukemia

p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulum

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3-12

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scholarly article

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10.1002/JCB.23335

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1

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113

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2012-01-01T00:00:00Z

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51625609

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21898539

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apoptotic process