Difference between revisions of "Category:ECO:0000025 ! hybrid interaction evidence"
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'''name:''' hybrid interaction evidence<br> | '''name:''' hybrid interaction evidence<br> | ||
'''def:''' "A type of affinity evidence where proteins of interest (bait and prey) are covalently linked to incomplete fragments of a third protein (reporter) and expressed in vivo, at which time interaction between bait and prey proteins brings reporter fragments in close enough proximity to allow them to reform and become a functional reporter protein." [ECO:MCC, PSI-MI:MI\:0090]<br> | '''def:''' "A type of affinity evidence where proteins of interest (bait and prey) are covalently linked to incomplete fragments of a third protein (reporter) and expressed in vivo, at which time interaction between bait and prey proteins brings reporter fragments in close enough proximity to allow them to reform and become a functional reporter protein." [ECO:MCC, PSI-MI:MI\:0090]<br> | ||
| − | '''xref:''' [ PSI-MI:MI\:0090 "protein complementation assay"]<br> | + | '''xref:''' [http://psidev.sourceforge.net/mi/xml/doc/user/index.html PSI-MI:MI\:0090 "protein complementation assay"]<br> |
'''is_a:''' [[:Category:ECO:0000023 ! affinity evidence|ECO:0000023 ! affinity evidence]][[Category:ECO:0000023 ! affinity evidence|ECO:0000023 ! affinity evidence]]<br> | '''is_a:''' [[:Category:ECO:0000023 ! affinity evidence|ECO:0000023 ! affinity evidence]][[Category:ECO:0000023 ! affinity evidence|ECO:0000023 ! affinity evidence]]<br> | ||
'''comment:''' Typically enzymes which confer resistance to antibiotics, such as Dihydrofolate reductase or Beta-lactamase, or proteins that give colorimetric or fluorescent signals are used. The Bait protein is generally the protein under study and the methods are readily adaptable to highthroughput mode.<br> | '''comment:''' Typically enzymes which confer resistance to antibiotics, such as Dihydrofolate reductase or Beta-lactamase, or proteins that give colorimetric or fluorescent signals are used. The Bait protein is generally the protein under study and the methods are readily adaptable to highthroughput mode.<br> | ||
Revision as of 12:49, 23 April 2013
| id: ECO:0000025 name: hybrid interaction evidence |
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