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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Genomic analysis of a heterogeneous Mendelian phenotype: multiple novel alleles for inherited hearing loss in the Palestinian population.
PMID 16460646 · PMC3525152 · Human genomics · 2006 · 8 claims · 8 setups
GJB2 (connexin 26) mutations account for hearing loss in only 17 of 156 families (11%), a smaller fraction than reported in other populations.
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Identification of ERGIC-53 as an intracellular transport receptor of alpha1-antitrypsin.
PMID 18283111 · PMC2265576 · The Journal of cell biology · 2008 · 8 claims · 6 setups
α1-antitrypsin is a novel ERGIC-53 cargo protein identified via a YFP protein-fragment complementation assay (PCA) cDNA library screen
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Human Lsg1 defines a family of essential GTPases that correlates with the evolution of compartmentalization.
PMID 16209721 · PMC1262696 · BMC biology · 2005 · 8 claims · 9 setups
hLsg1 is the human orthologue of yeast Lsg1p and defines a family of circularly permuted GTPases named YRG (YlqF Related GTPases)
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Mutations in TRPV4 cause Charcot-Marie-Tooth disease type 2C.
PMID 20037586 · PMC2812627 · Nature genetics · 2010 · 8 claims · 8 setups
Heterozygous missense mutations in TRPV4 (c.805C>T/R269C and c.806G>A/R269H) cause CMT2C
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Has reproduction · 63
Transcriptomics, regulatory syntax, and enhancer identification in mesoderm-induced ESCs at single-cell resolution.
PMID 35977485 · PMC9644345 · Cell reports · 2022 · 8 claims · 8 setups
Bmp4 treatment instructs ESCs to downregulate pluripotency genes and upregulate genes associated with formative pluripotency and fate specification
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Regulation of P2X2 receptors by the neuronal calcium sensor VILIP1.
PMID 18922787 · PMC3523710 · Science signaling · 2008 · 8 claims · 8 setups
VILIP1 was identified via a proteomic (GST pull-down) approach as a protein interacting with the P2X2 receptor C-terminal tail