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Deamidation of asparaginyl residues

Y. Nabuchi, E. Fujiwara, H. Kuboniwa, Y. Asoh, H. Ushio, The Stability and Degradation Pathway of Recombinant Human Parathyroid Hormone Deamidation of Asparaginyl Residue and Peptide Bond Cleavage at Aspartyl and Asparaginyl Residues , Pharm. Res. 1997, 14, 1685-1690. [Pg.374]

A. Artigues, H. Farrant, V. Schirch, Cytosolic Serine Hydroxymethyltransferase. Deamidation of Asparaginyl Residues and Degradation in Xenopus laevis Oocytes , J. Biol. Chem. 1993, 268, 13784-13790. [Pg.374]

K. Patel, R. T. Borchardt, Deamidation of Asparaginyl Residues in Proteins A Potential Pathway for Chemical Degradation of Proteins in Lyophihzed Dosage Form , J. Parent. Sci. Technol. 1990,44, 300-301. [Pg.376]

Patel K, Borchardt RT. Chemical pathways of peptide degradation. III. Effect of primary sequence on the pathways of deamidation of asparaginyl residues in hexapeptides. Pharm Res 1990 7(8) 787-793. [Pg.304]

J. H. McKerrow and A. B. Robinson. Deamidation of asparaginyl residues as a hazard in experimental protein and peptide procedures. Anal. Biochem., 42, 565-8 (1971)... [Pg.461]

Nabuchi Y, Fujiwara E, Kuboniwa H, et al. (1997). The stability and degradation pathway of recombinant human parathyroid hormone Deamidation of asparaginyl residue and peptide bond cleavage at aspartyl and asparaginyl residues. Pharm. Res. 14 1685-1690. [Pg.404]

H. T. Wright, Nonenzymatic Deamidation of Asparaginyl and Glutaminyl Residues in Proteins , Crit. Rev. Biochem. Mol. Biol. 1991, 26, 1-52. [Pg.375]

Robinson NE, Robinson AB. Molecular Clocks. In Deamidation of Asparaginyl and Glutaminyl Residues in Peptides and Proteins. Cave Junction, Oregon Althouse Press, 2004. [Pg.305]

A. B. Robinson, C. J. Rudd, Deamidation of Glutaminyl and Asparaginyl Residues in Peptides and Proteins , Curr. Topics Cell. Regul. 1974, 8, 247-295. [Pg.374]

K. Patel, R. T. Borchardt, Chemical Pathways of Peptide Degradation. II. Kinetics of Deamidation of an Asparaginyl Residue in a Model Hexapeptide , Pharm. Res. 1990, 7, 703-711. [Pg.375]

C. Goolcharran, L. L. Stauffer, J. L. Cleland, R. T. Borchardt, The Effects of a Histidine Residue on the C-Terminal Side of an Asparaginyl Residue on the Rate of Deamidation Using Model Pentapeptides , J. Pharm. Sci. 2000, 89, 818-825. [Pg.375]

Nonenzymatic Deamidation of Glutaminyl and Asparaginyl Residues in Protein 387... [Pg.383]

Robinson, A.B. Rudd, C.J. Deamidation of glutaminyl and asparaginyl residues in peptides and proteins. In Current Topics in Cellular Regulations Horecker, B.L., Stadman, E.R., Eds. Academic Press New York, 1974 Vol. 8, 247-295. [Pg.298]

Recent experiments indicate that the lifetime of a protein in vivo may be a function of the rate of deamidation of its glutaminyl and asparaginyl residues (258,259). The authors do not argue for a specific enzyme system for deamidation. Rather, they suggest that the proteins slowly undergo deamidation nonenzymatically with a half-time of approxi-... [Pg.147]


See other pages where Deamidation of asparaginyl residues is mentioned: [Pg.84]    [Pg.341]    [Pg.84]    [Pg.94]    [Pg.21]    [Pg.84]    [Pg.341]    [Pg.84]    [Pg.94]    [Pg.21]    [Pg.852]    [Pg.852]    [Pg.387]    [Pg.98]    [Pg.378]    [Pg.349]    [Pg.173]    [Pg.189]    [Pg.461]    [Pg.98]    [Pg.476]    [Pg.388]   
See also in sourсe #XX -- [ Pg.84 ]

See also in sourсe #XX -- [ Pg.84 ]

See also in sourсe #XX -- [ Pg.84 ]

See also in sourсe #XX -- [ Pg.84 ]




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