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| { | |
| "evidence-collection": [ | |
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| "evidence": { | |
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| { | |
| "evidence": { | |
| "bel_statement": "kin(p(HGNC:AKT1)) directlyIncreases p(HGNC:FOXO3,pmod(P,T,32))", | |
| "citation": { | |
| "type": "PubMed", | |
| "name": "Biochem J 2001 Mar 15 354(Pt 3) 605-12", | |
| "id": "11237865", | |
| "date": "", | |
| "authors": [ | |
| ], | |
| "comment": "" | |
| }, | |
| "summary_text": "FKHR, FKHRL1 and AFX are each phosphorylated by PKB at three residues in vitro, and, in co-transfection experiments with FKHR, these were shown to be Thr-24, Ser-256 and Ser-319 [9-14]. The half time for phosphorylation of each site was 2-5 min. In contrast, the mutation S256A completely prevented phosphorylation at Thr-24 and Ser-319 ... but the mutation T24A did not prevent phosphorylation at Ser-256 or Ser-319 ..., and the mutation S319A did not prevent the phosphorylation of Thr-24 and Ser-256...", | |
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| "Description": "Approximately 61,000 statements.", | |
| "Version": "20150611", | |
| "Copyright": "Copyright (c) 2011-2015, Selventa. All rights reserved.", | |
| "Authors": "Selventa", | |
| "Licenses": "Creative Commons Attribution-Non-Commercial-ShareAlike 3.0 Unported License", | |
| "ContactInfo": "[email protected]" | |
| } | |
| } | |
| ] | |
| }, | |
| "_links": { | |
| "self": { | |
| "type": "evidence", | |
| "href": "http://localhost:9000/api/evidence/560154bf8a4cca1317001fba" | |
| }, | |
| "collection": { | |
| "type": "evidence-collection", | |
| "href": "http://localhost:9000/api/evidence" | |
| } | |
| } | |
| } |
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