Quantitative assessment of the preferences for the amino acid residues flanking archaeal N-linked glycosylation sites

Glycobiology

Volumn 21, Issue 5, 2011, Pages 575-583

  Igura, Mayumi ^a   Kohda, Daisuke ^a  

^a KYUSHU UNIVERSITY   (Japan)

Author keywords

archaea; enzyme kinetics; N linked protein glycosylation; oligosaccharyltransferase; peptide library

Indexed keywords

AMINO ACID; ASPARAGINE; OLIGOSACCHARYLTRANSFERASE; PEPTIDE LIBRARY; PROLINE; RECOMBINANT GLYCOPROTEIN GP 120; SERINE; THREONINE; TRANSFERASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARCHAEBACTERIUM; ARTICLE; BACTERIAL CELL; EUBACTERIUM; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN GLYCOSYLATION; PROTEIN VARIANT; PYROCOCCUS FURIOSUS; QUANTITATIVE ANALYSIS; THERMOSTABILITY;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; GLYCOSYLATION; HEXOSYLTRANSFERASES; KINETICS; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; OLIGOPEPTIDES; PEPTIDES; PROTEIN PROCESSING, POST-TRANSLATIONAL; PYROCOCCUS FURIOSUS; SUBSTRATE SPECIFICITY;

ARCHAEA; BACTERIA (MICROORGANISMS); PYROCOCCUS FURIOSUS;

EID: 79953880285     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwq196     Document Type: Article

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