Prideapplication/xmlftp://ftp.pride.ebi.ac.uk/pride/data/archive/2009/07/PRD000074/PRIDE_Exp_Complete_Ac_8633.xml.gzftp://ftp.pride.ebi.ac.uk/pride/data/archive/2009/07/PRD000074/PRIDE_Exp_Complete_Ac_9284.xml.gzftp://ftp.pride.ebi.ac.uk/pride/data/archive/2009/07/PRD000074/PRIDE_Exp_Complete_Ac_9285.xml.gzftp://ftp.pride.ebi.ac.uk/pride/data/archive/2009/07/PRD000074/PRIDE_Exp_Complete_Ac_9284.pride.mgf.gzftp://ftp.pride.ebi.ac.uk/pride/data/archive/2009/07/PRD000074/PRIDE_Exp_Complete_Ac_9285.pride.mgf.gzftp://ftp.pride.ebi.ac.uk/pride/data/archive/2009/07/PRD000074/PRIDE_Exp_Complete_Ac_8633.pride.mgf.gzprimaryOK200002850John AsaraMass SpectrometryBottom-up proteomicsSequest/Mascot Server 2.2Sequest and Mascot 2.2Not availablehttp://www.ebi.ac.uk/pride/archive/projects/PRD000074Not availablePrideNot availableNot availableNot availableProteomicsLTQ Orbitrapinstrument modelLTQDinosauriaTyrannosaurus Rex (tyrant Lizard King)PRIDE17823333 Asara JM, Garavelli JS, Slatter DA, Schweitzer MH, Freimark LM, Phillips M, Cantley LC; Interpreting sequences from mastodon and T. rex., Science, 2007 Sep 7, 317, 5843, 1324-5, 10.1126/science.317.5843.132417431179 Schweitzer MH, Suo Z, Avci R, Asara JM, Allen MA, Arce FT, Horner JR; Analyses of soft tissue from Tyrannosaurus rex suggest the presence of protein., Science, 2007 Apr 13, 316, 5822, 277-80, 10.1126/science.113870917431180 Asara JM, Schweitzer MH, Freimark LM, Phillips M, Cantley LC; Protein sequences from mastodon and Tyrannosaurus rex revealed by mass spectrometry., Science, 2007 Apr 13, 316, 5822, 280-5, 10.1126/science.113761418436782 Organ CL, Schweitzer MH, Zheng W, Freimark LM, Cantley LC, Asara JM; Molecular phylogenetics of mastodon and Tyrannosaurus rex., Science, 2008 Apr 25, 320, 5875, 499, 10.1126/science.1154284jasara@bidmc.harvard.eduSignal TransductionAnalyses of soft tissue from Tyrannosaurus rex suggest the presence of protein.Molecular phylogenetics of mastodon and Tyrannosaurus rex.Protein sequences from mastodon and Tyrannosaurus rex revealed by mass spectrometry.Interpreting sequences from mastodon and T. rex.Asara John M JM, Schweitzer Mary H MH, Freimark Lisa M LM, Phillips Matthew M, Cantley Lewis C LCSchweitzer Mary Higby MH, Suo Zhiyong Z, Avci Recep R, Asara John M JM, Allen Mark A MA, Arce Fernando Teran FT, Horner John R JROrgan Chris L CL, Schweitzer Mary H MH, Zheng Wenxia W, Freimark Lisa M LM, Cantley Lewis C LC, Asara John M JMAsara John M JM, Garavelli John S JS, Slatter David A DA, Schweitzer Mary H MH, Freimark Lisa M LM, Phillips Matthew M, Cantley Lewis C LCFossilized 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.We performed multiple analyses of Tyrannosaurus rex (specimen MOR 1125) fibrous cortical and medullary tissues remaining after demineralization. The results indicate that collagen I, the main organic component of bone, has been preserved in low concentrations in these tissues. The findings were independently confirmed by mass spectrometry. We propose a possible chemical pathway that may contribute to this preservation. The presence of endogenous protein in dinosaur bone may validate hypotheses about evolutionary relationships, rates, and patterns of molecular change and degradation, as well as the chemical stability of molecules over time.We report a molecular phylogeny for a nonavian dinosaur, extending our knowledge of trait evolution within nonavian dinosaurs into the macromolecular level of biological organization. Fragments of collagen alpha1(I) and alpha2(I) proteins extracted from fossil bones of Tyrannosaurus rex and Mammut americanum (mastodon) were analyzed with a variety of phylogenetic methods. Despite missing sequence data, the mastodon groups with elephant and the T. rex groups with birds, consistent with predictions based on genetic and morphological data for mastodon and on morphological data for T. rex. Our 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.Not Available, Unavailable.portion of tissue, count in organism, protein polypeptide chains, native protein, natural protein, polypeptide chain, Protein., SOFT, protein complex, tissue portion, Tissue, number, simple tissue, PIX2, quantitative, proteins, protein, protein aggregate, WDR51A, protein-containing complex, presence, presence or absence in organismNot Available, Unavailable.Not Available, Unavailable.Rex, DNS, (Deoxyribonucleotide)n, protein complex, DNAn+1, number, protein, Double-Stranded, Spectrum Analyses, protein-containing complex, dinosaur, Spectrum Analysis, presence, Peptide, Deoxyribonucleic acids, Mdu, CG11121, (Deoxyribonucleotide)n+m, Spectroscopy, polypeptide, peptide, Polypeptides, protein polypeptide chains, count in organism, old, native protein, ClvPrd, peptido, natural protein, polypeptide chain, Deoxyribonucleic Acid, DmelCG11121, mda, Protein, reducing end xylose-releasing exo-oligoxylanase activity, Mass, bones, Analysis, ds-DNA, protein aggregate, desoxyribose nucleic acid, Mass Spectrum Analyses, ami, Mass Spectroscopy, Mass Spectrum Analysis, Mass Spectrum, thymus nucleic acid, somda, peptides, Analyses, med, Spectrometry, dinosaurs, study., Double Stranded, Dinosaur, proteins, Deoxyribonucleic acid, SO, bone, ds DNA, Desoxyribonukleinsaeure, beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranose reducing-end xylanase activity, Peptid, peptidos, Double-Stranded DNA, (Deoxyribonucleotide)m, species, Polypeptide, DNA, deoxyribonucleic acids, quantitative, DNAn, bone organ, So, Drl, presence or absence in organismFossil.285trueAncient fossil sequencing - Interpreting sequences from mastodon and TNot 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