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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Has reproduction · 85
Predicting the pathogenicity of missense variants using features derived from AlphaFold2.
PMID 37084271 · PMC10203375 · Bioinformatics (Oxford, England) · 2023 · 6 claims · 8 setups
AlphaFold2-derived structural features (solvent accessibility, amino acid network features, physicochemical environment, pLDDT) can be used to train a random forest classifier (AlphScore) that distinguishes proxy-benign from proxy-pathogenic missense variants.
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Prediction of catalytic residues using Support Vector Machine with selected protein sequence and structural properties.
PMID 16790052 · PMC1534064 · BMC bioinformatics · 2006 · 8 claims · 7 setups
The Sequential Minimal Optimization (SMO) SVM algorithm was the best-performing classifier among 26 WEKA classifiers for predicting catalytic residues
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Structural evolution of the protein kinase-like superfamily.
PMID 16244704 · PMC1261164 · PLoS computational biology · 2005 · 8 claims · 5 setups
All kinases in the superfamily share a 'universal core' domain consisting only of the regions required for ATP binding and the phosphotransfer reaction.
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MODBASE, a database of annotated comparative protein structure models and associated resources.
PMID 18948282 · PMC2686492 · Nucleic acids research · 2009 · 8 claims · 8 setups
MODBASE contains 5,152,695 reliable comparative protein structure models for 1,593,209 unique protein sequences.
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Natural history of S-adenosylmethionine-binding proteins.
PMID 16225687 · PMC1282579 · BMC structural biology · 2005 · 8 claims · 6 setups
The last universal common ancestor (LUCA) of cellular life had between 10 and 20 SAM-binding proteins from at least 5 fold classes
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Coverage of whole proteome by structural genomics observed through protein homology modeling database.
PMID 17146617 · PMC1769342 · Journal of structural and functional genomics · 2006 · 8 claims · 7 setups
FAMSBASE, a homology-modeling database of whole-genome ORFs, currently covers about 50% of predicted ORFs (368,724 of 734,193) across 276 genomes with modeled 3D structures.
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Genome bioinformatic analysis of nonsynonymous SNPs.
PMID 17708757 · PMC1978506 · BMC bioinformatics · 2007 · 8 claims · 8 setups
Structure- and sequence-based prediction tools can generally distinguish disease-causing mutations from neutral ones
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nsSNPAnalyzer: identifying disease-associated nonsynonymous single nucleotide polymorphisms.
PMID 15980516 · PMC1160133 · Nucleic acids research · 2005 · 6 claims · 4 setups
nsSNPAnalyzer is a web server that predicts whether a query nsSNP is disease-associated or functionally neutral using a Random Forest classifier combining structural and evolutionary information
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A systematic comparative and structural analysis of protein phosphorylation sites based on the mtcPTM database.
PMID 17521420 · PMC1929158 · Genome biology · 2007 · 7 claims · 6 setups
mtcPTM is a hierarchically organized database of human and mouse phosphosites that preserves experimental context, enabling comparison of phosphorylation patterns across conditions
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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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Predicting deleterious nsSNPs: an analysis of sequence and structural attributes.
PMID 16630345 · PMC1489951 · BMC bioinformatics · 2006 · 8 claims · 7 setups
Sequence conservation (PSIC score difference) at the nsSNP position is the single most useful attribute for predicting deleterious vs neutral status.
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Nitrosothiol reactivity profiling identifies S-nitrosylated proteins with unexpected stability.
PMID 19101475 · PMC2628636 · Chemistry & biology · 2008 · 8 claims · 7 setups
Most protein nitrosothiols are rapidly denitrosylated by physiological GSH, but a small subset show markedly reduced GSH reactivity and remain stably S-nitrosylated