Glycosylation analysis of two cysteine proteinase inhibitors from Atlantic salmon skin: di-O-acetylated sialic acids are the major sialic acid species on N-glycans

• Other Authors: Professor Nicolle H Packer (isManagedBy)
• Format: Other/Unknown Material
• Language: unknown
• Published: Macquarie University
• Subjects: O-linked; Analytical Biochemistry; BIOLOGICAL SCIENCES; BIOCHEMISTRY AND CELL BIOLOGY; Bioinformatics; Carbohydrate Sequence; The Portal; Atlantic salmon
• Online Access: https://researchdata.ands.org.au/glycosylation-analysis-cysteine-n-glycans/18438; http://glycosuitedb.expasy.org/glycosuite/results?selected+results.x=31&selected+results.y=9&results_index=reference&index_order=PUB_YEAR____AUTHORS____TITLE____JOURNAL____VOLUME____PAGES&index=2001____Ylonen,+Kalkkinen,+Saarinen,+Bogwald,+Helin____Glycosylation+analysis+of+two+cysteine+proteinase+inhibitors+from+Atlantic+salmon+skin%3A+di-O-acetylated+sialic+acids+are+the+major+sialic+acid+species+on+N-glycans; http://www.ncbi.nlm.nih.gov/pubmed/11447131; http://www.isb-sib.ch

GlycoSuiteDB is a curated database of carbohydrate (glycan) structures sourced from published material. This entry corresponds to a catologue of structures reported in the publication - Glycosylation analysis of two cysteine proteinase inhibitors from Atlantic salmon skin: di-O-acetylated sialic acids are the major sialic acid species on N-glycans The results obtained in the context of research activities will be immediately made available to the scientific community through the portal, taking due precautions for protecting the potential for exploiting the results and will be be disseminated and exploited at the other research initiatives in the network as soon as feasible.