Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/16442
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dc.contributor.authorSoliman, Caroline-
dc.contributor.authorYuriev, Elizabeth-
dc.contributor.authorRamsland, Paul A-
dc.date2016-11-04-
dc.date.accessioned2016-11-23T01:06:40Z-
dc.date.available2016-11-23T01:06:40Z-
dc.date.issued2017-06-
dc.identifier.citationCurrent Opinion in Structural Biology 2017; 44: 1-8en_US
dc.identifier.urihttps://ahro.austin.org.au/austinjspui/handle/1/16442-
dc.description.abstractCarbohydrate-binding antibodies and carbohydrate-based vaccines are being actively pursued as targeted immunotherapies for a broad range of cancers. Recognition of tumor-associated carbohydrates (glycans) by antibodies is predominantly towards terminal epitopes on glycoproteins and glycolipids on the surface of cancer cells. Crystallography along with complementary experimental and computational methods have been extensively used to dissect antibody recognition of glycan epitopes commonly found in cancer. We provide an overview of the structural biology of antibody recognition of tumor-associated glycans and propose potential rearrangements of these targets in the membrane that could dictate the complex biological activities of these antibodies against cancer cells.en_US
dc.titleAntibody recognition of aberrant glycosylation on the surface of cancer cellsen_US
dc.typeJournal Articleen_US
dc.identifier.journaltitleCurrent Opinion in Structural Biologyen_US
dc.identifier.affiliationSchool of Science, RMIT University, Bundoora, Victoria, Australiaen_US
dc.identifier.affiliationMedicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, Victoria, Australiaen_US
dc.identifier.affiliationDepartment of Immunology, Monash University, Alfred Medical Research and Education Precinct, Melbourne, Victoria, Australiaen_US
dc.identifier.affiliationDepartment of Surgery, Austin Health, The University of Melbourne, Heidelberg, Victoria, Australiaen_US
dc.identifier.affiliationCentre for Biomedical Research, Burnet Institute, Melbourne, Victoria, Australiaen_US
dc.identifier.pubmedurihttps://pubmed.ncbi.nlm.nih.gov/27821276en_US
dc.identifier.doi10.1016/j.sbi.2016.10.009en_US
dc.type.contentTexten_US
dc.type.austinJournal Articleen_US
local.name.researcherRamsland, Paul A
item.fulltextNo Fulltext-
item.grantfulltextnone-
item.openairetypeJournal Article-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
crisitem.author.deptSurgery (University of Melbourne)-
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