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- Backofen, Rolf, et al.
(författare)
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Requirements and specification of bioinformatics use cases
- 2005
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Rapport (övrigt vetenskapligt/konstnärligt)abstract
- This deliverable specifies use cases based on bioinformatics research carried out by members ofA2. The use cases involve the use of rules to reason over ontologies and pathways (Dresden,Edinburgh, Paris, Linköping) and rules to specify workflows to integrate bioinformatics data (Lisbon, Skövde, Jena, Bucharest). The use cases are designed as a reference point to foster the take up of A2 use cases by I-work packages. Most notably, many of the use cases specify the need for querying and reactivity with languages like Xcerpt (I4), Erus (I5) and Prova (I5). The use cases range from basic research applications to fully deployed software with an international user base.
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| 4. |
- Backofen, Rolf, et al.
(författare)
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Usage of bioinformatics tools and identification of information sources
- 2005
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Rapport (övrigt vetenskapligt/konstnärligt)abstract
- Bioinformatics is an important application area for semantic web technologies as much of the data is online and accessible in XML format, as some sites already support web services, and as ontologies are widely used to annotate data. In this deliverable, we give a survey over 18 of the most important bioinformatics resources and discuss their availability and accessibility, which are two of the main criteria for these resources to act as bases for later demonstrators.
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| 6. |
- Bergström Lind, Sara, et al.
(författare)
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Immunoaffinity Enrichments Followed by Mass Spectrometric Detection for Studying Global Protein Tyrosine Phosphorylation
- 2008
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Ingår i: Journal of Proteome Research. - : American Chemical Society (ACS). - 1535-3893 .- 1535-3907. ; 7:7, s. 2897-2910
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Tidskriftsartikel (refereegranskat)abstract
- Phosphorylation of protein tyrosine residues regulates important cell functions and is, when dysregulated, often crucially involved in oncogenesis. It is therefore important to develop and evaluate methods for identifying and studying tyrosine phosphorylated (P-Tyr) proteins. P-Tyr proteins are present at very low concentrations within cells, requiring highly selective enrichment methods to be detected. In this study, we applied immunoaffinity as enrichment step for P-Tyr proteins. Five selected anti-phosphotyrosine antibodies (monoclonal antibodies 4G10, PY100, PYKD1, 13F9 and one polyclonal antiserum) were evaluated with respect to their capability to enrich P-Tyr proteins from cell extracts of the K562 leukemia cell line. The enrichment resulted in the detection of a group of proteins that potentially were tyrosine-phosphorylated (putative P-Tyr proteins). High accuracy identification of actual P-Tyr sites were performed using a highly selective and sensitive liquid chromatography Fourier transform mass spectrometer (LC-FTMS) setup with complementary collision activated dissociation (CAD) and electron capture dissociation (ECD) fragmentations. 4G10 and PY100 antibodies recognized the greatest number of putative P-Tyr proteins in initial screening experiments and were therefore further evaluated and compared in immunoaffinity enrichment of both P-Tyr proteins and peptides. Using the 4G10 antibody for enrichment of proteins, we identified 459 putative P-Tyr proteins by MS. Out of these proteins, 12 were directly verified as P-Tyr proteins by MS analysis of the actual site. Using the PY100 antibody for enrichment of peptides, we detected 67 P-Tyr peptides (sites) and 89 putative P-Tyr proteins. Generally, enrichment at the peptide level made it difficult to reliably determine the identity of the proteins. In contrast, protein identification following immunoaffinity enrichment at the protein level gave greater sequence coverage and thus a higher confidence in the protein identification. By combining all available information, 40 proteins were identified as true P-Tyr proteins from the K562 cell line. In conclusion, this study showed that a combination of immunoaffinity enrichment using multiple antibodies of both intact and digested proteins in parallel experiments is required for best possible coverage of all possible P-Tyr proteins in a sample.
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