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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Mutations in the focal adhesion targeting region of deleted in liver cancer-1 attenuate their expression and function.
PMID 18829524 · PMC2597479 · Cancer research · 2008 · 8 claims · 6 setups
The DLC-1 fragment spanning residues 201-500 is sufficient for focal adhesion targeting (FAT region)
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Proteomics identification of nuclear Ran GTPase as an inhibitor of human VRK1 and VRK2 (vaccinia-related kinase) activities.
PMID 18617507 · PMC2577208 · Molecular & cellular proteomics : MCP · 2008 · 8 claims · 8 setups
Nuclear Ran GTPase was identified by mass spectrometry as a novel interacting partner of VRK1 and VRK2B
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A new paradigm for MAPK: structural interactions of hERK1 with mitochondria in HeLa cells.
PMID 19847302 · PMC2760858 · PloS one · 2009 · 8 claims · 8 setups
hERK1 translocates to the mitochondria of HeLa cells upon a proliferative stimulus
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Proteomic screen defines the hepatocyte nuclear factor 1alpha-binding partners and identifies HMGB1 as a new cofactor of HNF1alpha.
PMID 18160415 · PMC2275099 · Nucleic acids research · 2008 · 8 claims · 8 setups
HMGB1 is a novel HNF1α-interacting protein identified via a co-IP-MS screening strategy
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Enthoprotin: a novel clathrin-associated protein identified through subcellular proteomics.
PMID 12213833 · PMC2173151 · The Journal of cell biology · 2002 · 8 claims · 8 setups
Subcellular proteomics of purified CCVs identifies enthoprotin (encoded by KIAA0171), a novel ENTH domain-containing protein not previously detected at the protein level.
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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
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Has reproduction
PID1 regulates insulin-dependent glucose uptake by controlling intracellular sorting of GLUT4-storage vesicles.
PMID 30904610 · PMC6624118 · Biochimica et biophysica acta. Molecular basis of disease · 2019 · 8 claims · 8 setups
PID1 serves as an insulin-regulated retention adaptor protein controlling co-translocation of LRP1 and GLUT4 to the adipocyte plasma membrane