S
Sally Kornbluth
Researcher at Duke University
Publications - 127
Citations - 12776
Sally Kornbluth is an academic researcher from Duke University. The author has contributed to research in topics: Apoptosis & Xenopus. The author has an hindex of 57, co-authored 127 publications receiving 12234 citations. Previous affiliations of Sally Kornbluth include University of California, San Diego & Rockefeller University.
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The Apoptosome: Physiological, Developmental, and Pathological Modes of Regulation
TL;DR: This review describes knockout and knockin studies of apoptosome components, elegant structural and biochemical experiments, and analyses of the apoptosomes in various cancers and other disease states, all of which have provided new insight into this critical locus of apoptotic control.
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Novel tyrosine kinase identified by phosphotyrosine antibody screening of cDNA libraries.
TL;DR: In an attempt to clone protein tyrosine kinases, antiphosphotyrosine antibodies were used to screen lambda gt11 cDNA expression libraries, and a 2.5-kilobase cDNA encoding a novel tyrosinesine kinase was isolated from a mouse liver cDNA library.
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Nuclear Import of Cdk/Cyclin Complexes: Identification of Distinct Mechanisms for Import of Cdk2/Cyclin E and Cdc2/Cyclin B1
TL;DR: It is found that the nuclear import machinery recognizes these Cdk/cyclin complexes through direct interactions with the cyclin component, and surprisingly, cyclins E and B1 are imported into nuclei via distinct mechanisms.
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The engine driving the ship: metabolic steering of cell proliferation and death.
TL;DR: This work has shown that D-type cyclins, cyclin-dependent kinases, the anaphase-promoting complex, p53, caspase 2 and B cell lymphoma 2 proteins, among others, have been shown to be regulated by metabolic crosstalk.
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Reaper eliminates IAP proteins through stimulated IAP degradation and generalized translational inhibition.
TL;DR: It is reported here that Rpr not only inhibits IAP function, but also greatly decreases IAP abundance, which results from a combination of increased IAP degradation and a previously unrecognized ability of Rpr to repress total protein translation.