Literature DB >> 17431180

Protein sequences from mastodon and Tyrannosaurus rex revealed by mass spectrometry.

John M Asara1, Mary H Schweitzer, Lisa M Freimark, Matthew Phillips, Lewis C Cantley.   

Abstract

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 from ancient organisms from peptide fragmentation patterns, a valuable tool to study the evolution and adaptation of ancient taxa from which genomic sequences are unlikely to be obtained.

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Year:  2007        PMID: 17431180     DOI: 10.1126/science.1137614

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  64 in total

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Journal:  Proc Biol Sci       Date:  2008-10-07       Impact factor: 5.349

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8.  Infrared mapping resolves soft tissue preservation in 50 million year-old reptile skin.

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9.  A role for iron and oxygen chemistry in preserving soft tissues, cells and molecules from deep time.

Authors:  Mary H Schweitzer; Wenxia Zheng; Timothy P Cleland; Mark B Goodwin; Elizabeth Boatman; Elizabeth Theil; Matthew A Marcus; Sirine C Fakra
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10.  Reanalysis of Tyrannosaurus rex Mass Spectra.

Authors:  Marshall Bern; Brett S Phinney; David Goldberg
Journal:  J Proteome Res       Date:  2009-09       Impact factor: 4.466

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