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Posttranslational Modifications of Protein

Walsh, C. 2005. Posttranslational Modification of Proteins. Roberts Company Publishers. [Pg.35]

Larsen, M.R., Trelle, M.B., Thingholm, T.E., and lensen, O.N. 2006. Analysis of posttranslational modifications of proteins by tandem mass spectrometry. BioTechniques 40, 790-798. [Pg.203]

Zhou Z. and Menard H.A. (2002), Autoantigenic posttranslational modifications of proteins does it apply to rheumatoid arthritis , Curr. Opin. Rheumatol. 14,250-253. [Pg.274]

The most common posttranslational modifications, discussed in the following sections, include phosphorylation, sulfation, disulfide formation, N-methylation, O-methylation, S-methylation, N-acetylation, hydroxylation, glycosylation, ADP-ribosylation, prenylation, biotinylation, lipoylation, and phosphopan-tetheine tethering. Many of the posttranslational modifications are proven to be cross talks. Other modifications exist in a smaller extent and include oxidation of methionine, C-methylation, ubiquitylation, carboxylation, and amidation. These topics will not be covered in this chapter which is meant to focus primarily on the recent literature (2005-08). For a more complete coverage of all posttranslational modifications and earlier literature (up to 2005), the reader is referred to Professor Christopher T. Walsh s book Posttranslational Modification of Proteins Expanding Nature s Inventory ... [Pg.433]

We would like to acknowledge the work on posttranslational modification of proteins of those not cited in this chapter either due to the scope of the chapter or our ignorance. We thank Dr. Oleg V. Tsodikov for critical reading of the manuscript and help in the preparation of Figures 2, 6, and 9. SGT would also like to thank Professors John C. Vederas and Christopher T. Walsh for their invaluable support and mentorship. [Pg.463]

C. T. Walsh, Posttranslational Modification of Proteins Expanding Nature s Inventory, Isted. Roberts and Company Publishers Englewood, CO, 2005. [Pg.465]

Carr SA, Annan RS, Huddleston MJ. Mapping posttranslational modifications of proteins by MS-based selective detection Application to phosphoproteomics. In Burlingame AL, ed.. Mass Spectrometry Modified Proteins and Glycoconjugates, Vol. 405, New York Academic Press, 2005, 82-115. [Pg.229]

Pantothenic acid (vitamin B5) is both present in many nutrientcients and it is also produced by intestinal bacteria. Deficiency is therefore thought to be unlikely. Its active form, 4-phosphopantetheine, is an element of both coenzyme-A and acyl-carrier protein and thus participates in fatty acid synthesis and in the posttranslational modification of proteins. Acetylcoenzyme-A is important for the synthesis of the neurotransmitter acetylcholine. [Pg.474]

Results of cell biological, biochemical, and immunological research of the past decades have revealed that glycosylation is a very common posttranslational modification of proteins in eukaryotic cells [1]. The carbohydrate portions of glycoproteins obviously play important roles in the organized distribution of these macromolecules within the cells and... [Pg.265]


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See also in sourсe #XX -- [ Pg.402 , Pg.521 , Pg.522 ]

See also in sourсe #XX -- [ Pg.402 , Pg.521 , Pg.522 ]

See also in sourсe #XX -- [ Pg.402 , Pg.521 , Pg.522 ]

See also in sourсe #XX -- [ Pg.183 , Pg.203 , Pg.204 , Pg.225 , Pg.546 , Pg.547 ]




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