The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex (Q28141249)

5

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author name string

D C Huang

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L A O'Reilly

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S M King

The Bcl-2 protein family: arbiters of cell survival

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publication date

March 1999

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language of work or name

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3

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issue

3

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page(s)

287-96

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cites work

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Dimerization of the Highly Conserved Light Chain Shared by Dynein and Myosin V

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Interaction of CED-4 with CED-3 and CED-9: a molecular framework for cell death

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The C. elegans Protein EGL-1 Is Required for Programmed Cell Death and Interacts with the Bcl-2–like Protein CED-9

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Akt Phosphorylation of BAD Couples Survival Signals to the Cell-Intrinsic Death Machinery

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A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD

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Death cycle and Swiss army knives

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C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2.

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Kinesin and Dynein Superfamily Proteins and the Mechanism of Organelle Transport

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Bcl-2, Bcl-XL and adenovirus protein E1B19kD are functionally equivalent in their ability to inhibit cell death.

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Brain cytoplasmic and flagellar outer arm dyneins share a highly conserved Mr 8,000 light chain

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Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis

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Bid, a Bcl2 Interacting Protein, Mediates Cytochrome c Release from Mitochondria in Response to Activation of Cell Surface Death Receptors

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Membrane Oligomerization and Cleavage Activates the Caspase-8 (FLICE/MACHα1) Death Signal

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Bim: a novel member of the Bcl-2 family that promotes apoptosis

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Rapid hybridoma screening method for the identification of monoclonal antibodies to low-abundance cytoplasmic proteins

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Developing Caenorhabditis elegans neurons may contain both cell-death protective and killer activities

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Bcl-2 and Fas/APO-1 regulate distinct pathways to lymphocyte apoptosis

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BID: a novel BH3 domain-only death agonist

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Interaction and regulation of subcellular localization of CED-4 by CED-9

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Essential Role of CED-4 Oligomerization in CED-3 Activation and Apoptosis

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Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)

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Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3

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