Deamidation and isoaspartate formation in proteins: Unwanted alterations or surreptitious signals?

Cellular and Molecular Life Sciences

Volumn 60, Issue 7, 2003, Pages 1281-1295

  Reissner, K J ^a   Aswad, D W ^b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Deamidation; Isoaspartate; Peptide bond; Protein damage; Protein methylation; Protein L isoaspartyl O methyltransferase; S adenosyl L methionine

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE; HISTONE; ISOASPARTIC ACID; ISOASPARTYL O METHYLTRANSFERASE; METHYLTRANSFERASE; PROTEIN; S ADENOSYLMETHIONINE; UNCLASSIFIED DRUG;

AMINO ACID SYNTHESIS; DEAMINATION; ENZYME ACTIVITY; HUMAN; NONHUMAN; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN METHYLATION; PROTEIN MODIFICATION; PROTEIN STRUCTURE; REGULATORY MECHANISM; REVIEW;

AMIDES; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; BRAIN; ESCHERICHIA COLI; HUMANS; ISOASPARTIC ACID; MALE; MICE; MICE, KNOCKOUT; PROTEIN D-ASPARTATE-L-ISOASPARTATE METHYLTRANSFERASE; PROTEINS; RIBOSOMAL PROTEINS; TESTIS;

EID: 0041367295     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-003-2287-5     Document Type: Review

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