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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Conservation, variability and the modeling of active protein kinases.
PMID 17912359 · PMC1989141 · PloS one · 2007 · 7 claims · 5 setups
A novel sequence-order independent (fold-independent) structural alignment algorithm was developed that maximizes side-chain similarity to produce a consensus kinase structure.
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Disruption of the EGFR E884-R958 ion pair conserved in the human kinome differentially alters signaling and inhibitor sensitivity.
PMID 19015641 · PMC2633425 · Oncogene · 2009 · 8 claims · 8 setups
E884K works in concert with L858R in-cis, in a dominant fashion, to differentially alter EGFR downstream signaling and inhibitor sensitivity in an inhibitor-specific manner
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Structural insights into the inhibited states of the Mer receptor tyrosine kinase.
PMID 19028587 · PMC2686088 · Journal of structural biology · 2009 · 8 claims · 8 setups
Nucleotide-bound (ADP and ANP/AMP-PNP) Mer kinase domain adopts an autoinhibited DFG-Asp-in/αC-Glu-out conformation with an activation-loop residue inserted into the active site
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Hierarchical modeling of activation mechanisms in the ABL and EGFR kinase domains: thermodynamic and mechanistic catalysts of kinase activation by cancer mutations.
PMID 19714203 · PMC2722018 · PLoS computational biology · 2009 · 8 claims · 8 setups
Cancer mutations in ABL and EGFR activate kinases via a common multi-stage mechanism involving hydrophobic spine assembly, formation of a Src-like intermediate structure, and cooperative breakage/formation of characteristic salt bridges
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Prediction of specificity-determining residues for small-molecule kinase inhibitors.
PMID 19032760 · PMC2655090 · BMC bioinformatics · 2008 · 8 claims · 5 setups
S-Filter is a novel method combining sequence and structural information (within PFAAT) to predict specificity-determining residues and selectivity profiles for small-molecule kinase inhibitors
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Sequence and structure signatures of cancer mutation hotspots in protein kinases.
PMID 19834613 · PMC2759519 · PloS one · 2009 · 8 claims · 6 setups
Developed CKMD (Composite Kinase Mutation Database), an integrated bioinformatics resource mapping genetic variation in protein kinase genes to sequence, structural, and functional data