An Enriched Look at Tyrosine Phosphorylation  

Oleh:

Conrads, Thomas P. ; Veenstra, Timothy D.

Jenis: Article from Journal - ilmiah internasional
Dalam koleksi: Nature Biotechnology: The Science and Business of Biotechnology vol. 23 no. 1 (Jan. 2005), page 36-37.
Topik: IMMUNE SYSTEM; tyrosine; phosphorylation

Ketersediaan

Perpustakaan Pusat (Semanggi) Nomor Panggil: NN9.2 Non-tandon: 1 (dapat dipinjam: 0) Tandon: tidak ada

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Isi artikel

Immunoaffinity isolation enables the identification of posphotyrosine peptide on a global level. Although phosphorylated tyrosyl residues represent only 0.05% of the phosphoamino acids within a cell, they are indispensable in many signal transduction cascades. Abnormalities in tyrosine phosphorylation are directly responsible for the pathogenesis of numerous inherited and acquired human diseases, ranging from cancer to immune deficiencies. Unfortunately, existing proteomics tecniques for detecting proteins containing phosphotyrosiner continue to leave these proteins underepresented. In this issue, rush et al address this deficiency wit a sample preparation technique specific for the enrichment of phosphotyrosine containing peptides.

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