Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0014-5793(96)01156-8
DC FieldValue
dc.titleLocalisation of the C1q binding site within C1q receptor/calreticulin
dc.contributor.authorStuart, G.R.
dc.contributor.authorLynch, N.J.
dc.contributor.authorLu, J.
dc.contributor.authorGeick, A.
dc.contributor.authorMoffatt, B.E.
dc.contributor.authorSim, R.B.
dc.contributor.authorSchwaeble, W.J.
dc.date.accessioned2014-12-01T06:55:38Z
dc.date.available2014-12-01T06:55:38Z
dc.date.issued1996-11-18
dc.identifier.citationStuart, G.R., Lynch, N.J., Lu, J., Geick, A., Moffatt, B.E., Sim, R.B., Schwaeble, W.J. (1996-11-18). Localisation of the C1q binding site within C1q receptor/calreticulin. FEBS Letters 397 (2-3) : 245-249. ScholarBank@NUS Repository. https://doi.org/10.1016/S0014-5793(96)01156-8
dc.identifier.issn00145793
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/113540
dc.description.abstractC1q receptor (C1qR/colectin receptor) is located on many cell types. Binding of C1q to these cells elicits numerous responses. Protein sequencing has shown that C1qR is almost identical to calreticulin (CaR), an abundant multifunctional protein. Radioiodinated C1qR and CaR bind to C1q with identical characteristics. Three recombinant C1qR/CaR domains (N-, C-terminal domains and central P-domain) were expressed using the Thiofusion system, and used to study the interaction with C1q. Both the N- and P-domains were implicated in C1q binding. A region, termed the S-domain, spanning the N and P intersection was expressed, and showed concentration-dependent binding to C1q, demonstrating that the C1q binding site lies within this region.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/S0014-5793(96)01156-8
dc.sourceScopus
dc.subjectC1q binding site
dc.subjectC1q receptor
dc.subjectCalreticulin
dc.subjectCollagen
dc.subjectComplement
dc.typeArticle
dc.contributor.departmentBIOCHEMISTRY
dc.description.doi10.1016/S0014-5793(96)01156-8
dc.description.sourcetitleFEBS Letters
dc.description.volume397
dc.description.issue2-3
dc.description.page245-249
dc.description.codenFEBLA
dc.identifier.isiutA1996VV17100025
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