Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/12677
Full metadata record
DC FieldValueLanguage
dc.contributor.authorDingjan, Tamiren
dc.contributor.authorSpendlove, Ianen
dc.contributor.authorDurrant, Lindy Gen
dc.contributor.authorScott, Andrew Men
dc.contributor.authorYuriev, Elizabethen
dc.contributor.authorRamsland, Paul Aen
dc.date.accessioned2015-05-16T02:24:18Z-
dc.date.available2015-05-16T02:24:18Z-
dc.date.issued2015-03-07en
dc.identifier.citationMolecular Immunology 2015; 67(2 Pt A): 75-88en
dc.identifier.govdoc25757815en
dc.identifier.otherPUBMEDen
dc.identifier.urihttps://ahro.austin.org.au/austinjspui/handle/1/12677en
dc.description.abstractMonoclonal antibodies represent the most successful class of biopharmaceuticals for the treatment of cancer. Mechanisms of action of therapeutic antibodies are very diverse and reflect their ability to engage in antibody-dependent effector mechanisms, internalize to deliver cytotoxic payloads, and display direct effects on cells by lysis or by modulating the biological pathways of their target antigens. Importantly, one of the universal changes in cancer is glycosylation and carbohydrate-binding antibodies can be produced to selectively recognize tumor cells over normal tissues. A promising group of cell surface antibody targets consists of carbohydrates presented as glycolipids or glycoproteins. In this review, we outline the basic principles of antibody-based targeting of carbohydrate antigens in cancer. We also present a detailed structural view of antibody recognition and the conformational properties of a series of related tissue-blood group (Lewis) carbohydrates that are being pursued as potential targets of cancer immunotherapy.en
dc.language.isoenen
dc.subject.otherAntibody tumor targetingen
dc.subject.otherBlood group carbohydratesen
dc.subject.otherCancer immunotherapyen
dc.subject.otherCarbohydrate conformationsen
dc.subject.otherCarbohydrate recognitionen
dc.subject.otherProtein–carbohydrate interactionsen
dc.titleStructural biology of antibody recognition of carbohydrate epitopes and potential uses for targeted cancer immunotherapies.en
dc.typeJournal Articleen
dc.identifier.journaltitleMolecular immunologyen
dc.identifier.affiliationTumour Targeting Laboratory, Olivia Newton-John Cancer Research Institute, Melbourne, Victoria, Australiaen
dc.identifier.affiliationFaculty of Medicine, University of Melbourne, Melbourne, Victoria, Australiaen
dc.identifier.affiliationCentre for Biomedical Research, Burnet Institute, Melbourne, VIC 3004, Australiaen
dc.identifier.affiliationDepartment of Immunology, Monash University, Alfred Medical Research and Education Precinct, Melbourne, VIC 3004, Australiaen
dc.identifier.affiliationDepartment of Surgery Austin Health, University of Melbourne, Heidelberg, VIC 3084, Australiaen
dc.identifier.affiliationSchool of Cancer Medicine, La Trobe University, Melbourne, Victoria, Australiaen
dc.identifier.affiliationSchool of Biomedical Sciences, CHIRI Biosciences, Curtin University, Perth, WA 6845, Australiaen
dc.identifier.affiliationMonash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC 3052, Australiaen
dc.identifier.affiliationAcademic Department of Clinical Oncology, Division of Cancer and Stem cells, University of Nottingham, City Hospital, Nottingham NG5 1PB, United Kingdom.en
dc.identifier.doi10.1016/j.molimm.2015.02.028en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/25757815en
dc.type.austinJournal Articleen
local.name.researcherRamsland, Paul A
item.grantfulltextnone-
item.cerifentitytypePublications-
item.openairetypeJournal Article-
item.fulltextNo Fulltext-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.languageiso639-1en-
crisitem.author.deptMolecular Imaging and Therapy-
crisitem.author.deptOlivia Newton-John Cancer Research Institute-
crisitem.author.deptSurgery (University of Melbourne)-
Appears in Collections:Journal articles
Show simple item record

Page view(s)

58
checked on Jun 17, 2024

Google ScholarTM

Check


Items in AHRO are protected by copyright, with all rights reserved, unless otherwise indicated.