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).

• Human spermatozoa contain multiple targets for protein S-nitrosylation: an alternative mechanism of the modulation of sperm function by nitric oxide?

  PMID 17683036 · PMC2777308 · Proteomics · 2007 · 7 claims · 5 setups

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  Human sperm proteins undergo S-nitrosylation upon exposure to NO donors, detectable by the biotin switch assay

  percoll-washed fixed pooled excised biotin situ streptavidin-agarose

• Direct in-gel fluorescence detection and cellular imaging of O-GlcNAc-modified proteins.

  PMID 18683930 · PMC2649877 · Journal of the American Chemical Society · 2008 · 7 claims · 5 setups

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  Y289L GalT-mediated transfer of UDP-GalNAz followed by Cu(I)-catalyzed azide-alkyne cycloaddition enables selective, highly sensitive fluorescent/biotin labeling of O-GlcNAc-modified proteins

  α-crystallin forebrain hela chemoenzymatic in-gel nanolc-ms

• Proteomic analysis of ovarian cancer cells reveals dynamic processes of protein secretion and shedding of extra-cellular domains.

  PMID 18560578 · PMC2409963 · PloS one · 2008 · 8 claims · 6 setups

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  Ovarian cancer cells exhibit extensive shedding of extra-cellular domains from cell surface proteins into the extracellular milieu.

  ovcar3 analysis lc-ms cell-surface silac

• Modification-specific proteomics: strategies for characterization of post-translational modifications using enrichment techniques.

  PMID 19743430 · PMC2892724 · Proteomics · 2009 · 8 claims · 8 setups

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  Lack of efficient enrichment procedures for PTM peptides is a major bottleneck in PTM proteomic research

  cytosolic cellular unspecified yeast immunoaffinity azide chemical

• Glycomic analysis: an array of technologies.

  PMID 19728746 · PMC3443568 · ACS chemical biology · 2009 · 8 claims · 8 setups

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  Glycosylation is the most prevalent protein post-translational modification, occurring on at least 50% of all proteins

  sera t-cells serum glycoproteins lectin hydrazide bioorthogonal