Mass spectrometric peptide analysis of 2DE-separated mouse spinal cord and rat hippocampus proteins suggests an NGxG motif of importance for in vivo deamidation

Electrophoresis

Volumn 34, Issue 11, 2013, Pages 1610-1618

  Mikkat, Stefan ^a   Kischstein, Timo ^a   Kreutzer, Michael ^a   Glocker, Michael O ^a  

^a ROSTOCK UNIVERSITY MEDICAL CENTER   (Germany)

Author keywords

2DE; Asparagine deamidation; Deamidation motif; MALDI TOF MS; Protein disulfide isomerase

Indexed keywords

AMINO ACIDS; BIOACTIVITY; CHEMICAL REACTIONS; MASS SPECTROMETRY; PEPTIDES; RATS; SULFUR COMPOUNDS;

2DE; ASPARAGINE DEAMIDATION; ASPARAGINYL; DEAMIDATED; DEAMIDATION; DEAMIDATION MOTIF; IN-VIVO; MALDI TOF MS; PROTEIN DISULPHIDE-ISOMERASE;

GELS;

ANAZOLENE SODIUM; ASPARAGINE; ASPARTIC ACID; GLYCINE; ISOASPARTIC ACID; PROTEIN DISULFIDE ISOMERASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; TROPOMODULIN;

ANIMAL TISSUE; ARTICLE; DEAMINATION; FEMALE; HIPPOCAMPUS; IN VIVO STUDY; MALE; MASS SPECTROMETRY; MOUSE; NONHUMAN; PEPTIDE ANALYSIS; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PROCESSING; PROTEIN TERTIARY STRUCTURE; RAT; SPINAL CORD; TWO DIMENSIONAL ELECTROPHORESIS;

EID: 84878641681     PISSN: 01730835     EISSN: 15222683     Source Type: Journal    
DOI: 10.1002/elps.201200682     Document Type: Article

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