Protein Sequences from Mastodon and Tyrannosaurus Rex Revealed by Mass Spectrometry

@article{Asara2007ProteinSF,
  title={Protein Sequences from Mastodon and Tyrannosaurus Rex Revealed by Mass Spectrometry},
  author={J. Asara and M. Schweitzer and Lisa M. Freimark and M. Phillips and L. Cantley},
  journal={Science},
  year={2007},
  volume={316},
  pages={280 - 285}
}
Fossilized bones from extinct taxa harbor the potential for obtaining protein or DNA sequences that could reveal evolutionary links to extant species. We used mass spectrometry to obtain protein sequences from bones of a 160,000- to 600,000-year-old extinct mastodon (Mammut americanum) and a 68-million-year-old dinosaur (Tyrannosaurus rex). The presence of T. rex sequences indicates that their peptide bonds were remarkably stable. Mass spectrometry can thus be used to determine unique sequences… Expand
Molecular Phylogenetics of Mastodon and Tyrannosaurus rex
TLDR
The findings suggest that molecular data from long-extinct organisms may have the potential for resolving relationships at critical areas in the vertebrate evolutionary tree that have, so far, been phylogenetically intractable. Expand
Comment on "Protein Sequences from Mastodon and Tyrannosaurus rex Revealed by Mass Spectrometry"
We used authentication tests developed for ancient DNA to evaluate claims by Asara et al. (Reports, 13 April 2007, p. 280) of collagen peptide sequences recovered from mastodon and Tyrannosaurus rexExpand
Response to Comment on "Protein Sequences from Mastodon and Tyrannosaurus rex Revealed by Mass Spectrometry"
Endogenous peptide sequences extracted from a 68-million-year-old Tyrannosaurus rex fossil bone and obtained by mass spectrometry have been shown to be statistically significant based on proteinExpand
Preserved Proteins from Extinct Bison latifrons Identified by Tandem Mass Spectrometry; Hydroxylysine Glycosides are a Common Feature of Ancient Collagen*
TLDR
Bone samples from several vertebrates collected from the Ziegler Reservoir fossil site, in Snowmass Village, Colorado, and processed for proteomics analysis resulted in extensive fibrillar collagen sequence coverage, including the identification of posttranslational modifications of collagen. Expand
Comment on "Protein Sequences from Mastodon and Tyrannosaurus rex Revealed by Mass Spectrometry"
TLDR
It is argued that the reported T. rex peptides may represent statistical artifacts and call for complete data release to enable experimental and computational verification of their findings. Expand
Biomolecular Characterization and Protein Sequences of the Campanian Hadrosaur B. canadensis
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Microstructural and immunological data are consistent with preservation of multiple bone matrix and vessel proteins, and phylogenetic analyses of Brachylophosaurus collagen sequenced by mass spectrometry robustly support the bird-dinosaur clade, consistent with an endogenous source for these collagen peptides. Expand
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The results indicate that collagen I, the main organic component of bone, has been preserved in low concentrations in these tissues and a possible chemical pathway that may contribute to this preservation is proposed. Expand
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