Journal article
Cyclin f-mediated degradation of ribonucleotide reductase m2 controls genome integrity and DNA repair
- Abstract:
-
F-box proteins are the substrate binding subunits of SCF (Skp1-Cul1-F-box protein) ubiquitin ligase complexes. Using affinity purifications and mass spectrometry, we identified RRM2 (the ribonucleotide reductase family member 2) as an interactor of the F-box protein cyclin F. Ribonucleotide reductase (RNR) catalyzes the conversion of ribonucleotides to deoxyribonucleotides (dNTPs), which are necessary for both replicative and repair DNA synthesis. We found tha...
Expand abstract
- Publication status:
- Published
- Peer review status:
- Peer reviewed
Actions
Access Document
- Publisher copy:
- 10.1016/j.cell.2012.03.043
Why is the content I wish to access not available via ORA?
Bibliographic data (the information relating to research outputs) and full-text items (e.g. articles, theses, reports, etc.) arrive in ORA from several different sources. Unfortunately we are not able to make available the full-text for every research output.
Please contact the ORA team (
) if you have queries regarding unavailable content OR if you are aware of a full-text copy we can make available.
) if you have queries regarding unavailable content OR if you are aware of a full-text copy we can make available.
Content may be unavailable for the following four reasons
-
Version unsuitable
-
We have not obtained a suitable full-text for a given research output. See this page for more information.
-
Recently completed
-
Sometimes content is held in ORA but is unavailable for a fixed period of time to comply with the policies and wishes of rights holders.
-
Permissions
-
All content made available in ORA should comply with relevant rights, such as copyright. See this page for more information.
-
Clearance
-
Some thesis volumes scanned as part of the digitisation scheme funded by Dr Leonard Polonsky are currently unavailable due to sensitive material or uncleared third-party copyright content. We are attempting to contact authors whose theses are affected.
Alternative access to the full-text
You may be able to access the full-text directly from the publisher's website using the 'Publisher Copy' link in the 'Links & Downloads' box from a research output's ORA record page. This method may require an institutional or individual subscription to the journal/resource.
Authors
Funding
Howard Hughes Medical Institute
More from this funder
Expand funders...
Bibliographic Details
- Publisher:
- Elsevier Publisher's website
- Journal:
- Cell Journal website
- Volume:
- 149
- Issue:
- 5
- Pages:
- 1023-1034
- Publication date:
- 2012-05-24
- Acceptance date:
- 2012-03-24
- DOI:
- EISSN:
-
1097-4172
- ISSN:
-
0092-8674
- Pmid:
-
22632967
- Source identifiers:
-
383498
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:383498
- UUID:
-
uuid:3c34ad79-22a4-4d5d-9084-ae9385458a66
- Local pid:
- pubs:383498
- Deposit date:
- 2018-02-02
Terms of use
- Copyright holder:
- Elsevier
- Copyright date:
- 2012
- Notes:
- © 2012 Elsevier Inc. All rights reserved.
If you are the owner of this record, you can report an update to it here: Report update to this record