Recognition of D-aspartyl residues in polypeptides by the erythrocyte L-isoaspartyl/D-aspartyl protein methyltransferase. Implications for the repair hypothesis.-Reference-Cited by-同舟云学术

Recognition of D-aspartyl residues in polypeptides by the erythrocyte L-isoaspartyl/D-aspartyl protein methyltransferase. Implications for the repair hypothesis.

Published:1992-03 Issue:9 Volume:267 Page:5985-5995
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Lowenson J.D.,Clarke S

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference67 articles.

1. Deamidation of the asparaginyl-glycyl sequence

2. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation.

3. Role of peptide conformation in the rate and mechanism of deamidation of asparaginyl residues

4. Succinimide Formation from Aspartyl and Asparaginyl Peptides as a Model for the Spontaneous Degradation of Proteins

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