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Biochemical modifications phosphorylation

Recent advances in mass spectrometry (MS) technology have provided researchers with an unparalleled ability to identify the types and patterns of secondary biochemical modifications found on proteins in living cells. Matrix-assisted laser desorption/ionization-MS (MALDI-MS) analyses have shown, for example, that HMGA proteins in vivo are simultaneously subject to complex patterns of phosphorylation, acetylation and methylation and that, within the same cell type, different isoforms of these proteins can exhibit quite different modification patterns [33]. Furthermore, these in vivo modifications have been demonstrated to markedly alter the binding affinity of HMGA proteins for both DNA and chromatin substrates in vitro [33]. Nevertheless, due to their number and complexity, it has been difficult to determine the actual biological function(s) played by these biochemical modifications in living cells. [Pg.161]

Many of radioactive isotopes are very useful for the following biochemical processes (Table 6.1). The radioactive label is introduced into macromolecules, especially proteins, either during biosynthesis, e.g., during translation in the presence of S-methionine, or enzymatically, e.g., by use of P-labeled ATP during protein phosphorylation by protein kinases, or chemically by modification of amino acid side chains. Examples for reagents used in chemical radiolabeling of proteins are given in Table 6.2. [Pg.181]

The analytical problem becomes more complicated when complex proteins, glyco-or lipoproteins are a cause of allergenic response. As most of allergens are proteins, which are subject to different posttranslational modifications, of which glycosylation and phosphorylation are the most common ones, conventional biochemical methods used in research on glyco- and lipoproteins comprise the most suitable analytical techniques for description of these allergens. [Pg.89]

Gow AJ, Duran D, Malcolm S, Ischiropoulos H (1996) Effects of peroxynitrite-induced protein modifications on tyrosine phosphorylation and degradation. FEES Lett 385 63-66 Grune T, Merker K, Sandig G, Davies KJ (2003) Selective degradation of oxidatively modified protein substrates by the proteasome. Biochem Biophys Res Commun 305 709-718 Halliwell B (2002) Hypothesis proteasomal dysfunction a primary event in neurogeneration that leads to nitrative and oxidative stress and subsequent cell death. Ann N Y Acad Sci 962 182-194... [Pg.601]

Tau pathology corresponds to the intraneuronal aggregation of microtubule-associated tau proteins into abnormal filaments. Paired hehcal filaments (PHF) are the most characteristic cytoskeletal alterations affecting numerous neurons in AD. Using a combined immunocytochemical and biochemical approach (Iqbal et al., 1989) demonshated for the first time that the microtubule-associated protein tau, a normal brain cytoskeletal protein, is a component of the PHF. The authors also indicated for the first time that posttranslational modification of tau such as phosphorylation might occur which would allow it to assemble either alone or together... [Pg.650]

Shakoori AR. Phosphorylation and glycosylation interplay Protein modifications at hydroxy amino acids and prediction of signaling functions of the human beta(3) integrin family. J. Cell Biochem. 2006 99 706-718. 41. [Pg.320]

Pu MY, Akhand AA, Kato M, Koike T, Elamaguchi M, Suzuki El, Nakashima I Mercuric chloride mediates a protein sulfhydryl modification-based pathway of signal transduction for activating Src kinase which is independent of the phosphorylation/de-phosphorylation of a carboxyl terminal tyrosine. J Cell Biochem 1996 63 104-14. [Pg.148]


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See also in sourсe #XX -- [ Pg.157 , Pg.161 ]




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Biochemical modifications

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