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Sökning: WFRF:(Dzhambazov Balik) > Design of glycopept...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00004158naa a2200433 4500
001oai:DiVA.org:umu-41050
003SwePub
008110317s2011 | |||||||||||000 ||eng|
009oai:prod.swepub.kib.ki.se:122247909
024a https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-410502 URI
024a https://doi.org/10.1371/journal.pone.00178812 DOI
024a http://kipublications.ki.se/Default.aspx?queryparsed=id:1222479092 URI
040 a (SwePub)umud (SwePub)ki
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
100a Andersson, Ida E,d 1982-u Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)idaann02
2451 0a Design of glycopeptides used to investigate class II MHC binding and T-Cell responses associated with autoimmune arthritis
264 c 2011-03-15
264 1b Public Library of Science,c 2011
338 a electronic2 rdacarrier
500 a Vid avhandlingens utgivning manuskript med annan titel: "Design of glycopeptide chemical probes used to investigate multiresponses associated with autoimmune arthritis"
520 a The glycopeptide fragment CII259–273 from type II collagen (CII) binds to the murine Aq and human DR4 class II Major Histocompatibility Complex (MHC II) proteins, which are associated with development of murine collagen-induced arthritis (CIA) and rheumatoid arthritis (RA), respectively. It has been shown that CII259–273 can be used in therapeutic vaccination of CIA. This glycopeptide also elicits responses from T-cells obtained from RA patients, which indicates that it has an important role in RA as well. We now present a methodology for studies of (glyco)peptide-receptor interactions based on a combination of structure-based virtual screening, ligand-based statistical molecular design and biological evaluations. This methodology included the design of a CII259–273 glycopeptide library in which two anchor positions crucial for binding in pockets of Aq and DR4 were varied. Synthesis and biological evaluation of the designed glycopeptides provided novel structure-activity relationship (SAR) understanding of binding to Aq and DR4. Glycopeptides that retained high affinities for these MHC II proteins and induced strong responses in panels of T-cell hybridomas were also identified. An analysis of all the responses revealed groups of glycopeptides with different response patterns that are of high interest for vaccination studies in CIA. Moreover, the SAR understanding obtained in this study provides a platform for the design of second-generation glycopeptides with tuned MHC affinities and T-cell responses.
650 7a NATURVETENSKAPx Kemi0 (SwePub)1042 hsv//swe
650 7a NATURAL SCIENCESx Chemical Sciences0 (SwePub)1042 hsv//eng
700a Andersson, C David,d 1978-u Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)dadaon01
700a Batsalova, Tsvetelinau Medicinal Inflammation Research, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm4 aut
700a Dzhambazov, Baliku Medicinal Inflammation Research, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm4 aut
700a Holmdahl, Rikardu Karolinska Institutet4 aut
700a Kihlberg, Jan,d 1957-u Umeå universitet,Kemiska institutionen,AstraZeneca R&D Mölndal, Mölndal, Sweden4 aut0 (Swepub:umu)jaki0001
700a Linusson, Anna,d 1970-u AstraZeneca R&D Mölndal, Mölndal4 aut0 (Swepub:umu)analin99
710a Umeå universitetb Kemiska institutionen4 org
773t PLOS ONEd : Public Library of Scienceg 6:3, s. e17881-q 6:3<e17881-x 1932-6203
856u https://umu.diva-portal.org/smash/get/diva2:404410/FULLTEXT03.pdfx primaryx Raw objecty fulltext:print
856u https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0017881&type=printable
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-41050
8564 8u https://doi.org/10.1371/journal.pone.0017881
8564 8u http://kipublications.ki.se/Default.aspx?queryparsed=id:122247909

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