Author

Fred Sablitzky

University of NottinghamORCID 0000-0001-9718-1546Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Research Focus:cell type annotation· 1 Approach:experimental assay· 1 Organism:human· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1

Frequent Co-Authors

Huaitao ChengiD· 2 shared Maha Faisal AlsayeghiD· 1 shared

Activity by Year

2019-2019 · peak 2/yr

Co-Author Collaboration Network

2 top collaborators · 1 mutual co-author link

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2 shared papersMolecular Biology

Huaitao ChengORCID

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2 papers

Recent·Most cited

Molecular BiologybioRxivPreprintFeb 1, 2019

The coiled coil domain of DEF6 facilitates formation of large vesicle-like, cytoplasmic aggregates that trap the P-body marker DCP1 and exhibit prion-like features

Huaitao Cheng, Fred Sablitzky

This paper investigates DEF6's role in forming prion-like aggregates that trap P-body components and alters its localization through phosphorylation-induced conformational changes.

2 citations

human

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Molecular BiologybioRxivPreprintJan 29, 2019

N-terminal 45 amino acids of DEF6 are necessary and sufficient to spontaneously colocalise with DCP1 in P-bodies

Huaitao Cheng, Maha Faisal Alsayegh, Fred Sablitzky

The paper identifies the N-terminal 45 amino acids of DEF6 as necessary and sufficient for its colocalization with DCP1 in P-bodies, challenging the role of the coiled coil domain.

1 citation

proteomicsexperimental assay

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