C
Curt L. Milliman
Researcher at Washington University in St. Louis
Publications - 6
Citations - 15888
Curt L. Milliman is an academic researcher from Washington University in St. Louis. The author has contributed to research in topics: Apoptosis & Mitochondrion. The author has an hindex of 6, co-authored 6 publications receiving 15626 citations.
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Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programed cell death
TL;DR: Overexpressed Bax accelerates apoptotic death induced by cytokine deprivation in an IL-3-dependent cell line and counters the death repressor activity of B cl-2, suggesting a model in which the ratio of Bcl-2 to Bax determines survival or death following an apoptotic stimulus.
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Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death
TL;DR: It is demonstrated that Bcl-2 is an integral inner mitochondrial membrane protein of relative molecular mass 25,000 (25k) being localized to mitochondria and interfering with programmed cell death independent of promoting cell division.
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Bcl-2 functions in an antioxidant pathway to prevent apoptosis
TL;DR: A model in which Bcl-2 regulates an antioxidant pathway at sites of free radical generation is proposed in which it protected cells from H2O2- and menadione-induced oxidative deaths and suppressed lipid peroxidation completely.
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Caspase cleaved BID targets mitochondria and is required for cytochrome c release, while BCL-XL prevents this release but not tumor necrosis factor-R1/Fas death.
Atan Gross,Xiao Ming Yin,Kun Wang,Michael C. Wei,Jennifer Jockel,Curt L. Milliman,Hediye Erdjument-Bromage,Paul Tempst,Stanley J. Korsmeyer +8 more
TL;DR: While BID appears to be required for the release of cytochrome c in the TNF death pathway, the release is likely not required for cell death, as other aspects of mitochondrial dysfunction still transpired and cells died nonetheless.
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BID: a novel BH3 domain-only death agonist.
TL;DR: This work used interactive cloning to identify Bid, which encodes a novel death agonist that heterodimerizes with either agonists (BAX) or antagonists (BCL-2), and favors a model in which BID represents a death ligand for the membrane-bound receptor BAX.