SARS-CoV-2 antibodies specific to the mesa and inner side of spike protein receptor binding domain maintain high affinities for both D614G and b.1.351 variants
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Li, K; Huntwork, RHC; Horn, GQ; Feeney, E; Hastie, KM; Li, H; Rayaprolu, V; Olmedillas, O; Schendel, SL; Heise, M; Baric, RS; Alam, SM ...
Published in: BIOPHYSICAL JOURNAL
2022
Duke Scholars
Published In
BIOPHYSICAL JOURNAL
EISSN
1542-0086
ISSN
0006-3495
Publication Date
2022
Volume
121
Issue
3
Start / End Page
38 / 38
Related Subject Headings
- Biophysics
- 51 Physical sciences
- 34 Chemical sciences
- 31 Biological sciences
- 06 Biological Sciences
- 03 Chemical Sciences
- 02 Physical Sciences
Citation
APA
Chicago
ICMJE
MLA
NLM
Li, K., Huntwork, R. H. C., Horn, G. Q., Feeney, E., Hastie, K. M., Li, H., … Dennison, S. M. (2022). SARS-CoV-2 antibodies specific to the mesa and inner side of spike protein receptor binding domain maintain high affinities for both D614G and b.1.351 variants. In BIOPHYSICAL JOURNAL (Vol. 121, pp. 38–38).
Li, Kan, Richard H. C. Huntwork, Gillian Q. Horn, Elizabeth Feeney, Kathryn M. Hastie, Haoyang Li, Vamseedhar Rayaprolu, et al. “SARS-CoV-2 antibodies specific to the mesa and inner side of spike protein receptor binding domain maintain high affinities for both D614G and b.1.351 variants.” In BIOPHYSICAL JOURNAL, 121:38–38, 2022.
Li K, Huntwork RHC, Horn GQ, Feeney E, Hastie KM, Li H, et al. SARS-CoV-2 antibodies specific to the mesa and inner side of spike protein receptor binding domain maintain high affinities for both D614G and b.1.351 variants. In: BIOPHYSICAL JOURNAL. 2022. p. 38–38.
Li, Kan, et al. “SARS-CoV-2 antibodies specific to the mesa and inner side of spike protein receptor binding domain maintain high affinities for both D614G and b.1.351 variants.” BIOPHYSICAL JOURNAL, vol. 121, no. 3, 2022, pp. 38–38.
Li K, Huntwork RHC, Horn GQ, Feeney E, Hastie KM, Li H, Rayaprolu V, Olmedillas O, Schendel SL, Heise M, Baric RS, Alam SM, Saphire EO, Tomaras GD, Dennison SM. SARS-CoV-2 antibodies specific to the mesa and inner side of spike protein receptor binding domain maintain high affinities for both D614G and b.1.351 variants. BIOPHYSICAL JOURNAL. 2022. p. 38–38.
Published In
BIOPHYSICAL JOURNAL
EISSN
1542-0086
ISSN
0006-3495
Publication Date
2022
Volume
121
Issue
3
Start / End Page
38 / 38
Related Subject Headings
- Biophysics
- 51 Physical sciences
- 34 Chemical sciences
- 31 Biological sciences
- 06 Biological Sciences
- 03 Chemical Sciences
- 02 Physical Sciences