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Clive A. Slaughter

Researcher at St. Jude Children's Research Hospital

Publications -  133
Citations -  21547

Clive A. Slaughter is an academic researcher from St. Jude Children's Research Hospital. The author has contributed to research in topics: Peptide sequence & Protein subunit. The author has an hindex of 64, co-authored 132 publications receiving 20947 citations. Previous affiliations of Clive A. Slaughter include Howard Hughes Medical Institute & University of Texas Southwestern Medical Center.

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

TL;DR: The purification of a cytosolic protein that induces cytochrome c release from mitochondria in response to caspase-8, the apical caspases activated by cell surface death receptors such as Fas and TNF is reported.
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Activation of the IκB Kinase Complex by TRAF6 Requires a Dimeric Ubiquitin-Conjugating Enzyme Complex and a Unique Polyubiquitin Chain

TL;DR: It is found that TRAF6, a RING domain protein, functions together with Ubc13/Uev1A to catalyze the synthesis of unique polyubiquitin chains linked through lysine-63 (K63) of ubiquitin.
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DFF, a Heterodimeric Protein That Functions Downstream of Caspase-3 to Trigger DNA Fragmentation during Apoptosis

TL;DR: In this article, the authors identified and purified from HeLa cytosol a protein that induces DNA fragmentation in coincubated nuclei after it is activated by caspase-3.
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Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix

TL;DR: The hypothesis that the dramatic reduction in the 156K DAG in Duchenne muscular dystrophy leads to a loss of a linkage between the sarcolemma and extra-cellular matrix and that this may render muscle fibres more susceptible to necrosis is supported.
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Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin

TL;DR: The discovery of a brain protein of relative molecular mass 67,000 (67K) which binds stably to syntaxin suggests that Munc-18 is a previously unidentified essential component of the synaptic vesicle fusion protein complex.