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Approaches for systematic proteome exploration
KTH, School of Biotechnology (BIO), Molecular Biotechnology.ORCID iD: 0000-0002-9282-0174
KTH, School of Biotechnology (BIO), Proteomics.ORCID iD: 0000-0003-0605-8417
2007 (English)In: Biomolecular Engineering, ISSN 1389-0344, E-ISSN 1878-559X, Vol. 24, no 2, 155-168 p.Article, review/survey (Refereed) Published
Abstract [en]

With the completion of the human genome project (HUGO) during recent years, gene function, protein abundance and expression patterns in tissues and cell types have emerged as central areas for the scientific community. A mapped human proteome will extend the value of the genome sequence and large-scale efforts aiming at elucidating protein localization, abundance and function are invaluable for biomarker and drug discovery. This research area, termed proteomics, is more demanding than any genome sequencing effort and to perform this on a wide scale is a highly diverse task. Therefore, the proteornics field employs a range of methods to examine different aspects of proteomics including protein localization, protein-protein interactions, posttranslational modifications and alteration of protein composition (e.g. differential expression) in tissues and body fluids. Here, some of the most commonly used methods, including chromatographic separations together with mass spectrometry and a number of affinity proteomics concepts are discussed and exemplified.

Place, publisher, year, edition, pages
2007. Vol. 24, no 2, 155-168 p.
Keyword [en]
proteomics, protein atlas, protein array, protein localization, mass spectrometry, protein quantification, resonance mass-spectrometry, capillary liquid-chromatography, bacterial receptor domain, antibody-based proteomics, human plasma proteome, large-scale analysis, human serum samples, saccharomyces-cerevisiae, gene-expression, subcellular-localization
URN: urn:nbn:se:kth:diva-16720DOI: 10.1016/j.bioeng.2007.01.001ISI: 000247422300001ScopusID: 2-s2.0-34248508844OAI: diva2:334763
QC 20100525Available from: 2010-08-05 Created: 2010-08-05Bibliographically approved

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