Isoaspartate in peptides and proteins: formation, significance, and analysis
- 27 December 1999
- journal article
- Published by Elsevier
- Vol. 21 (6) , 1129-1136
- https://doi.org/10.1016/s0731-7085(99)00230-7
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- In vitro aging of calmodulin generates isoaspartate at multiple Asn–Gly and Asp–Gly sites in calcium‐binding domains II, III, and IVProtein Science, 1993
- Spontaneous degradation of polypeptides at aspartyl and asparaginyl residues: Effects of the solvent dielectricProtein Science, 1993
- Structure of the EF corner favors deamidation of asparaginyl residues in hemoglobin: the example of Hb La Roche-sur-Yon [β81 (EF5) Leu → His]Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 1992
- Chemical Stability of Insulin. 1. Hydrolytic Degradation During Storage of Pharmaceutical PreparationsPharmaceutical Research, 1992
- Optimal conditions for the use of protein l-isoaspartyl methyltransferase in assessing the isoaspartate content of peptides and proteinsAnalytical Biochemistry, 1991
- Sequence and structure determinants of the nonenzymatic deamidation of asparagine and glutamine residues in proteinsProtein Engineering, Design and Selection, 1991
- Chemical Pathways of Peptide Degradation. III. Effect of Primary Sequence on the Pathways of Deamidation of Asparaginyl Residues in HexapeptidesPharmaceutical Research, 1990
- Effect of protein conformation on rate of deamidation: Ribonuclease AProteins-Structure Function and Bioinformatics, 1989
- Tertiary Structure Is a Principal Determinant to Protein DeamidationScience, 1988
- Propensity for spontaneous succinimide formation from aspartyl and asparaginyl residues in cellular proteinsInternational Journal of Peptide and Protein Research, 1987