Author

D. C. David

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Cell Biology· 3

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Organism:C. elegans· 2 Research Focus:cell type annotation· 2 Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:development & morphogenesis· 1 Research Focus:differential expression· 1 Approach:genetic perturbation / CRISPR· 1

Frequent Co-Authors

M. C. Lechler· 2 shared R. Jung· 2 shared A. A. Hyman· 1 shared A. C. Murthy· 1 shared A. D. Stephens· 1 shared A. Hermann· 1 shared A. J. Baldwin· 1 shared A. M. de Jesus Domingues· 1 shared

Activity by Year

2018-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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2 shared papersCell Biology

M. C. Lechler

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3 papers

Recent·Most cited

Small molecule modulation of a redox-sensitive stress granule protein dissolves stress granules with beneficial outcomes for familial amyotrophic lateral sclerosis models

H. Uechi, S. Sridharan, J. Nijssen, J. Bilstein, J. M. Iglesias-Artola, S. Kishigami, V. Casablancas-Antras, I. Poser, E. J. Martinez, E. Boczek, M. Wagner, N. Tomschke, A. M. de Jesus Domingues, A. Pal, T. Doeleman, , R. J. Wheeler

The paper identifies lipoamide as a small molecule that dissolves stress granules and improves outcomes in ALS models by modulating redox-sensitive proteins.

bioRxiv · Jan 5, 2024 · PreprintCell Biology

Tissue-specific safety mechanism results in opposite protein aggregation patterns during aging

R. Jung, M. C. Lechler, C. Rödelsperger, W. Röseler, R. J. Sommer, D. C. David

The paper identifies a tissue-specific safety mechanism, SAPA, that suppresses age-dependent protein aggregation in C. elegans pharyngeal muscles but not body-wall muscles.

bioRxiv · Dec 4, 2020 · PreprintCell Biology

Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in C. elegans

C. Huang, S. Wagner-Valladolid, A. D. Stephens, R. Jung, C. Poudel, T. Sinnige, M. C. Lechler, N. Schlörit, R. F. Laine, C. H. Michel, M. M. Vendruscolo, C. F. Kaminski, G. S. Kaminski Schierle, D. C. David

This study shows that age-dependent protein aggregation in C. elegans forms amyloid-like structures and accelerates tissue functional decline, suggesting a role for protein aggregation in aging.

bioRxiv · Sep 14, 2018Cell Biology