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VERSION:2.0
CALSCALE:GREGORIAN
PRODID:iCalendar-Ruby
BEGIN:VEVENT
LAST-MODIFIED:20071029T161916
SEQUENCE:0
ORGANIZER:University College London
DTEND:20071102T140000
UID:2008-09-07T18:40:37-0400_816092556@socialweb1
DESCRIPTION:Host: Steve Wilson\n\nCell surface and secreted proteins are 
 centrally involved in initiating intercellular communication and are encode
 d by around a fifth of our genes. Despite their importance and abundance\, 
 many extracellular proteins have no known binding partners because they are
  biochemically difficult to manipulate\; these proteins are therefore large
 ly absent from recent large-scale interactome datasets. \n\nTo address th
 is problem\, we have developed an in vitro binding assay called AVEXIS (for
  AVidity-based EXtracellular Interaction Screen)\, which circumvents the ma
 in biochemical difficulties associated with the identification of extracell
 ular interactions. Using this assay and a library of over 250 zebrafish ect
 odomain fragments - mainly from the immunoglobulin and leucine-rich-repeat 
 superfamilies - we have identified over 100 novel receptor:ligand pairs. \
 n\nWholemount in situ expression patterns of genes encoding interacting pr
 oteins revealed that most are expressed in a restricted tissue-specific man
 ner. In addition\, interacting pairs are usually expressed in overlapping o
 r adjacent tissues\, immediately suggesting potential biological roles. \n
 \nThe in vivo function of selected interactions is being determined by per
 forming loss-of-function experiments on both genes encoding a pair of inter
 acting proteins. Using this approach\, we aim to identify novel signalling 
 pathways important for early vertebrate development.\n
SUMMARY:Large Scale Screening for Novel Low Affinity Extracellular Receptor
 -Ligand Pairs and Functional Analysis in Zebrafish
DTSTART:20071102T130000
CREATED:20071029T115415
DTSTAMP:20080907T184037
LOCATION:University College London Anatomy Building Room 106\, 1st Floor
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