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Ted R. Hupp

Researcher at University of Edinburgh

Publications -  191
Citations -  11038

Ted R. Hupp is an academic researcher from University of Edinburgh. The author has contributed to research in topics: Biology & Cancer. The author has an hindex of 38, co-authored 161 publications receiving 8647 citations. Previous affiliations of Ted R. Hupp include Edinburgh Cancer Research Centre & University of Dundee.

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Journal ArticleDOI

Guidelines for the use and interpretation of assays for monitoring autophagy

Daniel J. Klionsky, +1287 more
- 01 Apr 2012 - 
TL;DR: These guidelines are presented for the selection and interpretation of methods for use by investigators who aim to examine macroautophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
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Pan-cancer analysis of whole genomes

Peter J. Campbell, +1332 more
- 06 Feb 2020 - 
TL;DR: The flagship paper of the ICGC/TCGA Pan-Cancer Analysis of Whole Genomes Consortium describes the generation of the integrative analyses of 2,658 whole-cancer genomes and their matching normal tissues across 38 tumour types, the structures for international data sharing and standardized analyses, and the main scientific findings from across the consortium studies.
Journal Article

The p53 response to ionising radiation in adult and developing murine tissues.

TL;DR: The study of lacZ transgene expression and the occurrence of apoptosis in different tissues that accumulate p53 protein point to a further level of control regulating the nature and degree of the downstream response to elevated levels of p53 in cells.
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Posttranslational Modifications of p53 in Replicative Senescence Overlapping but Distinct from Those Induced by DNA Damage

TL;DR: A direct role for p53 in signaling replicative senescence is supported and is consistent with the generation by telomere erosion of a signal which shares some but not all of the features of DNA double-strand breaks.
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Dual-Site Regulation of MDM2 E3-Ubiquitin Ligase Activity

TL;DR: A model in which the interaction between the p53-BOX-I domain and the N terminus of MDM2 promotes conformational changes inMDM2 that stabilize acid-domain interactions with a ubiquitination signal in the DNA binding domain of the p 53 tetramer is proposed.