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).
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In vitro and in silico analysis reveals an efficient algorithm to predict the splicing consequences of mutations at the 5' splice sites.
PMID 17726045 · PMC2094079 · Nucleic acids research · 2007 · 8 claims · 6 setups
Two exonic mutations, PINK1 E417G and PARK7 E64D, disrupt binding to U1 snRNA and cause skipping of the mutation-harboring exon
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Rats go genomic.
PMID 16522223 · PMC1431730 · Genome biology · 2006 · 7 claims · 8 setups
A systems biology approach combining genome-wide expression profiling with expression QTL (eQTL) mapping can identify candidate genes underlying complex-disease QTLs
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Biased exon/intron distribution of cryptic and de novo 3' splice sites.
PMID 16141195 · PMC1197134 · Nucleic acids research · 2005 · 7 claims · 5 setups
Cryptic 3'ss (from 3'YAG consensus mutations) are significantly more frequent in exons than in introns
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Prediction and assessment of splicing alterations: implications for clinical testing.
PMID 18951448 · PMC2832470 · Human mutation · 2008 · 8 claims · 5 setups
Bioinformatic prediction alone is insufficient; in vitro analysis is needed to confirm or establish splicing aberrations for clinical variant classification
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A missense mutation (Q279R) in the fumarylacetoacetate hydrolase gene, responsible for hereditary tyrosinemia, acts as a splicing mutation.
PMID 11476670 · PMC35353 · BMC genetics · 2001 · 8 claims · 7 setups
The Q279R missense mutation acts as a splicing mutation in vivo, causing skipping of exon 9 (alone or with exon 8) rather than simply altering the encoded amino acid.
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Proteomic identification of heterogeneous nuclear ribonucleoprotein L as a novel component of SLM/Sam68 Nuclear Bodies.
PMID 19912651 · PMC2784748 · BMC cell biology · 2009 · 7 claims · 7 setups
hnRNP L is a novel Sam68-interacting protein partner identified by proteomics and confirmed by co-immunoprecipitation