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Stephen B. Helliwell

Researcher at Novartis

Publications -  33
Citations -  3504

Stephen B. Helliwell is an academic researcher from Novartis. The author has contributed to research in topics: Saccharomyces cerevisiae & Mutant. The author has an hindex of 20, co-authored 32 publications receiving 3172 citations. Previous affiliations of Stephen B. Helliwell include University of Kent & University of Basel.

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TOR controls translation initiation and early G1 progression in yeast.

TL;DR: In this article, it was shown that the TORs, two related phosphatidylinositol kinase homologues, are part of a novel signaling pathway that activates eIF-4E-dependent protein synthesis and prevent early G1 progression in response to nutrient availability.
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TOR1 and TOR2 are structurally and functionally similar but not identical phosphatidylinositol kinase homologues in yeast.

TL;DR: TOR1 and TOR2 are likely similar but not identical, rapamycin-sensitive PI kinases possibly regulated by phosphorylation, and may be components of a novel signal transduction pathway controlling progression through G1.
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Components of a Ubiquitin Ligase Complex Specify Polyubiquitination and Intracellular Trafficking of the General Amino Acid Permease

TL;DR: It is found that overexpression of Bul1p or Bul2p, two nonessential components of the Rsp5p E3–ubiquitin ligase complex, causes Gap1p to be sorted to the vacuole regardless of nitrogen source.
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Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces cerevisiae.

TL;DR: This work uses the yeast 2 hybrid system to analyze the protein–protein interactions of all 17 soluble class E Vps proteins, as well as proteins thought to be required for the ubiquitination and deubiquitination of cargo proteins at multivesicular bodies, and proposes the formation of a large multimeric complex on the endosome membrane consisting of ESCRTI, ESCRTII, ESC RTIII and other associated proteins.