| pubmed-article:17023655 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17023655 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:17023655 | lifeskim:mentions | umls-concept:C0577559 | lld:lifeskim |
| pubmed-article:17023655 | lifeskim:mentions | umls-concept:C0037813 | lld:lifeskim |
| pubmed-article:17023655 | lifeskim:mentions | umls-concept:C0439093 | lld:lifeskim |
| pubmed-article:17023655 | lifeskim:mentions | umls-concept:C0439792 | lld:lifeskim |
| pubmed-article:17023655 | pubmed:issue | 5796 | lld:pubmed |
| pubmed-article:17023655 | pubmed:dateCreated | 2006-10-6 | lld:pubmed |
| pubmed-article:17023655 | pubmed:abstractText | For characterization of sequence and posttranslational modifications, molecular and fragment ion mass data from ionizing and dissociating a protein in the mass spectrometer are far more specific than are masses of peptides from the protein's digestion. We extend the approximately 500-residue, approximately 50-kilodalton (kD) dissociation limitation of this top-down methodology by using electrospray additives, heated vaporization, and separate noncovalent and covalent bond dissociation. This process can cleave 287 interresidue bonds in the termini of a 1314-residue (144-kD) protein, specify previously unidentified disulfide bonds between 8 of 27 cysteines in a 1714-residue (200-kD) protein, and correct sequence predictions in two proteins, one with 2153 residues (229 kD). | lld:pubmed |
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| pubmed-article:17023655 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17023655 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17023655 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17023655 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17023655 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:17023655 | pubmed:issn | 1095-9203 | lld:pubmed |
| pubmed-article:17023655 | pubmed:author | pubmed-author:LoaMM | lld:pubmed |
| pubmed-article:17023655 | pubmed:author | pubmed-author:McLaffertyFre... | lld:pubmed |
| pubmed-article:17023655 | pubmed:author | pubmed-author:BreukerKathri... | lld:pubmed |
| pubmed-article:17023655 | pubmed:author | pubmed-author:HanXuemeiX | lld:pubmed |
| pubmed-article:17023655 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17023655 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:17023655 | pubmed:volume | 314 | lld:pubmed |
| pubmed-article:17023655 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17023655 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17023655 | pubmed:pagination | 109-12 | lld:pubmed |
| pubmed-article:17023655 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:17023655 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:17023655 | pubmed:articleTitle | Extending top-down mass spectrometry to proteins with masses greater than 200 kilodaltons. | lld:pubmed |
| pubmed-article:17023655 | pubmed:affiliation | Department of Chemistry and Chemical Biology, Baker Laboratory, Cornell University, Ithaca, NY 14853, USA. | lld:pubmed |
| pubmed-article:17023655 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17023655 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17023655 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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