Isotype switching converts anti-CD40 antagonism to agonism to elicit potent antitumor activity
- Submitting institution
-
University of Southampton
- Unit of assessment
- 5 - Biological Sciences
- Output identifier
- 59010555
- Type
- D - Journal article
- DOI
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10.1016/j.ccell.2020.04.013
- Title of journal
- Cancer Cell
- Article number
- -
- First page
- 850
- Volume
- 37
- Issue
- 6
- ISSN
- 1535-6108
- Open access status
- Compliant
- Month of publication
- May
- Year of publication
- 2020
- URL
-
-
- Supplementary information
-
-
- Request cross-referral to
- -
- Output has been delayed by COVID-19
- No
- COVID-19 affected output statement
- -
- Forensic science
- No
- Criminology
- No
- Interdisciplinary
- No
- Number of additional authors
-
15
- Research group(s)
-
-
- Citation count
- 4
- Proposed double-weighted
- No
- Reserve for an output with double weighting
- No
- Additional information
- -
- Author contribution statement
- Tews - My group contributed a Small Angle Xray Scattering (SAXS) analysis of an antibody (F(ab) fragment) receptor complex and provided a homology model based on a crystallographic structure determined earlier by us (PBD: 6FAX, Cancer Cell 33, 664–675) that was experimentally validated by the SAXS analysis. The interpretation is shown in Figure 1 of the paper, and together with epitope mapping data lays the foundation for the ensuing work and analysis presented in this manuscript. The data we contributed here was instrumental in building a model for antibody receptor recognition.
- Non-English
- No
- English abstract
- -