CACAO Spring 2017
My Annotations
Status | Page | Date/Time | GO Term (Aspect) | Reference | Evidence | Notes | Links |
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acceptable | SCHPO:RAD32 | 2017-04-06 21:46:17 CDT | GO:0006303 double-strand break repair via nonhomologous end joining (P) | PMID:28292918 | ECO:0000315 mutant phenotype evidence used in manual assertion | Mre11, a protein required for double stranded break repair via non homologous end joining, forms a dimer to bridge the gap between the two broken ends of the double-stranded DNA. Figure 6 proves how dimerization of mre11 ( or rad32 in S. pombe) needs to occur for efficient non homologous end joining since the introduced mutations in the Mre11 dimerization domain, but not the nuclease domain, reduce NHEJ. This data is represented by the drastic decrease in PCR products since the bands for PCR products would indicate successful repair by non homologous end-joining. Therefore, mre11 dimerization is essential for NHEJ since there were no excision products from PCR.
| challenge |
updatedbyinstructor | XENLA:PRKDC | 2017-04-08 09:17:06 CDT | GO:0006303 double-strand break repair via nonhomologous end joining (P) | PMID:27324260 | ECO:0000315 mutant phenotype evidence used in manual assertion | Figure 2B shows how DNA -PKcs is required for efficient non homologous end repair activity, as evidenced with the assay on repair activity with or without DNA-PKcs inhibitor NU7441. When DNA-PKcs was inhibited, the activity of repair of double stranded breaks via NHEJ was significantly decreased. Xenopus laevis.
| challenge |
updatedbyinstructor | CANLF:F6UNA4 | 2017-04-08 10:05:53 CDT | GO:0035861 site of double-strand break (C) | PMID:27644316 | ECO:0000314 direct assay evidence used in manual assertion | Figure 4C shows how XRCC4 quickly accumulates at the sites of double-stranded breaks in the DNA since the merged image of XRCC4 localization and antibody detection of γH2AX, a marker of DSBs, indicates that XRCC4 is heavily present at the site of DSBs. The regulation of XRCC4 localizations might play a key role in regulating NHEJ activity since the XRCC4/DNA Ligase IV complex is crucial for the final ligation of DSBs through NHEJ.
| challenge |
acceptable:1
unacceptable:0
requires_changes:0
flagged:0
Annotations challenged by MFeeley
Status | Author,Group | Page | GO Term (Aspect) | Reference | Evidence | Links | Page history |
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0 annotations fixed by MFeeley
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