Structures of complexes formed by H5 influenza hemagglutinin with a potent broadly neutralizing human monoclonal antibody
- Submitting institution
-
The University of Kent
(joint submission with University of Greenwich)
- Unit of assessment
- 3 - Allied Health Professions, Dentistry, Nursing and Pharmacy
- Output identifier
- 2848
- Type
- D - Journal article
- DOI
-
10.1073/pnas.1510816112
- Title of journal
- Proceedings of the National Academy of Sciences
- Article number
- -
- First page
- 9430
- Volume
- 112
- Issue
- 30
- ISSN
- 0027-8424
- Open access status
- Out of scope for open access requirements
- Month of publication
- July
- Year of publication
- 2015
- URL
-
https://kar.kent.ac.uk/49599/
- 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
-
17
- Research group(s)
-
B - Biological Sciences
- Citation count
- 34
- Proposed double-weighted
- No
- Reserve for an output with double weighting
- No
- Additional information
- -
- Author contribution statement
- Dr Temperton produced a comprehensive panel of 13 H5N1 pseudotypes from multiple clades, and associated serological assays for the detailed analysis of monoclonal antibody specificity and potency. This obviated the need to work with containment level 4 wildtype viruses, many of which would be impossible to obtain.
- Non-English
- No
- English abstract
- -
