Experiments

Searchable full-text extractions: founding hypothesis, core claims, experimental setups, key results and statistics — pulled out of each paper as structure. Search a cell line, an assay or an entity (e.g. HUH7) and find every paper that worked with it. This corpus stands on its own: most entries carry no reproduction assessment (yet).

• RNA interference in functional genomics and medicine.

  PMID 12808314 · PMC3055057 · Journal of Korean medical science · 2003 · 8 claims · 7 setups

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  RNAi is sequence-specific gene silencing induced by double-stranded RNA and is mediated by ~22-nt siRNAs generated from long dsRNA by the RNase III enzyme Dicer.

  caenorhabditis drosophila mammalian postnatal dsrna biochemical synthetic

• Structural proteomics of the SARS coronavirus: a model response to emerging infectious diseases.

  PMID 17680348 · PMC7088133 · Journal of structural and functional genomics · 2007 · 8 claims · 8 setups

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  Structures of 16 SARS-CoV proteins or functional domains have been determined, and 8 of these have novel folds

  sars-cov x-ray gst emsa

• A combined approach exploring gene function based on worm-human orthology.

  PMID 15877817 · PMC1112593 · BMC genomics · 2005 · 8 claims · 6 setups

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  Strict phylogenetic criteria (concordant Neighbor Joining and Maximum Parsimony tree topology) can select single most-likely human orthologs for C. elegans genes despite the large phylogenetic distance between worm and human sequences.

  sapiens elegans hela phylogenetic rnai gfp

• From single cells to whole organisms.

  PMID 16420683 · PMC1414103 · Genome biology · 2005 · 8 claims · 8 setups

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  The genetic-interaction map in S. cerevisiae is roughly four times as complex as the protein-protein interaction map, and genetic interactions do not overlap with physical interactions but instead predict functional neighborhoods

  saccharomyces caenorhabditis mammalian cylindromatosis automated interference rnai

• Nucleotide oligomerization domain-2 interacts with 2'-5'-oligoadenylate synthetase type 2 and enhances RNase-L function in THP-1 cells.

  PMID 19853919 · PMC2787966 · Molecular immunology · 2009 · 7 claims · 6 setups

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  OAS2 is identified as a novel NOD2-binding partner in THP-1 cells by tandem affinity purification and mass spectrometry

  thp-1 hek293 tandem co-immunoprecipitation oas2