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Tim Van Acker

Researcher at Francis Crick Institute

Publications -  11
Citations -  728

Tim Van Acker is an academic researcher from Francis Crick Institute. The author has contributed to research in topics: Autophagy & Endocytosis. The author has an hindex of 10, co-authored 11 publications receiving 589 citations. Previous affiliations of Tim Van Acker include Ghent University.

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The need for transparency and good practices in the qPCR literature

Stephen A. Bustin, +83 more
- 01 Nov 2013 - 
TL;DR: Two surveys of over 1,700 publications whose authors use quantitative real-time PCR (qPCR) reveal a lack of transparent and comprehensive reporting of essential technical information.
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Bromodomain Protein BRD4 Is a Transcriptional Repressor of Autophagy and Lysosomal Function.

TL;DR: It is reported that the epigenetic reader BRD4 and the methyltransferase G9a repress a TFEB/TFE3/MITF-independent transcriptional program that promotes autophagy and lysosome biogenesis, and is directed independently and also reciprocally to the growth-promoting properties ofBRD4.
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The Small GTPase Arf6: An Overview of Its Mechanisms of Action and of Its Role in Host⁻Pathogen Interactions and Innate Immunity.

TL;DR: The small GTase Arf6 has several important functions in intracellular vesicular trafficking and regulates the recycling of different types of cargo internalized via clathrin-dependent or -independent endocytosis and its role in innate immunity and host–pathogen interactions is reviewed.
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Reconstructing the TIR side of the myddosome: a paradigm for TIR-TIR interactions

TL;DR: In this paper, the authors combine the mammalian two-hybrid system MAPPIT and saturation mutagenesis to complement and extend crystallographic and nuclear magnetic resonance data, and reveal how TIR domains interact.

Reconstructing the TIR side of the Myddosome: a paradigm for TIR-TIR interactions?

TL;DR: The mammalian two-hybrid system MAPPIT and saturation mutagenesis is combined to complement and extend crystallographic and nuclear magnetic resonance data, and how TIR domains interact is revealed, providing a paradigm for the interaction of mammalian T IR domains.