Zobrazeno 1 - 10
of 28
pro vyhledávání: '"James A. Baber"'
Autor:
Louise Murdoch, Karen Quan, James A. Baber, Agnes W. Y. Ho, Ying Zhang, Xia Xu, Claire Lu, David Cooper, Kenneth Koury, Stephen P. Lockhart, Annaliesa S. Anderson, Özlem Türeci, Uğur Şahin, Kena A. Swanson, William C. Gruber, Nicholas Kitchin, the C4591030 Clinical Trial Group
Publikováno v:
Infectious Diseases and Therapy, Vol 12, Iss 9, Pp 2241-2258 (2023)
Abstract Introduction Vaccination is a critical tool for preventing coronavirus disease 2019 (COVID-19) and influenza illnesses. Coadministration of the COVID-19 vaccine, BNT162b2, with seasonal inactivated influenza vaccine (SIIV) can provide substa
Externí odkaz:
https://doaj.org/article/c10e41db0b574d23af185c6952e55029
Publikováno v:
Journal of Biomolecular NMR.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::929d4cea0f4d94115088f9e71793aecc
https://doi.org/10.1007/s10858-023-00413-8
https://doi.org/10.1007/s10858-023-00413-8
Publikováno v:
PLoS ONE, Vol 11, Iss 8, p e0160597 (2016)
The transitioning of the ectodomain of gp41 from a pre-hairpin to a six-helix bundle conformation is a crucial aspect of virus-cell fusion. To gain insight into the intermediary steps of the fusion process we have studied the pH and dodecyl phosphoch
Externí odkaz:
https://doaj.org/article/2b9902b48a1649afa656f6d933c16d97
Publikováno v:
Angewandte Chemie International Edition. 57:5674-5678
Efficient and accurate models to predict the fitness of a sequence would be extremely valuable in protein design. We have explored the use of statistical potentials for the coevolutionary fitness landscape, extracted from known protein sequences, in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23f54938d2441991d0598c549725cddb
https://doi.org/10.1002/anie.201713220
https://doi.org/10.1002/anie.201713220
Publikováno v:
Journal of the American Chemical Society. 140:34-37
Cryo-electron microscopy and X-ray crystallography have shown that the pre- and post-fusion states of the HIV-1 gp41 viral coat protein, although very different from one another, each adopt C3 symmetric structures. A stable homotrimeric structure for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24529f4709106aa7f15a031a3802cccf
https://doi.org/10.1021/jacs.7b10245
https://doi.org/10.1021/jacs.7b10245
Publikováno v:
Angewandte Chemie (International ed. in English)
Current distance measurements between spin-labels on multimeric protonated proteins using double electron–electron resonance (DEER) EPR spectroscopy are generally limited to the 15–60 A range. Here we show how DEER experiments can be extended to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2de52a3654f799ed611eb101b9977650
https://doi.org/10.1002/ange.201609617
https://doi.org/10.1002/ange.201609617
Publikováno v:
Angewandte Chemie International Edition. 54:5336-5339
Pulsed double electron-electron resonance (DEER) provides pairwise P(r) distance distributions in doubly spin-labeled proteins. We report that in protonated proteins P(r) is dependent on the length of the second echo period T owing to local environme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3245782dec05aa479a339c70230abeb8
https://doi.org/10.1002/anie.201500640
https://doi.org/10.1002/anie.201500640
Autor:
Charles D. Schwieters, Lalit Deshmukh, G. Clore, Alexander Grishaev, Rodolfo Ghirlando, James L. Baber
Publikováno v:
Journal of the American Chemical Society. 135:16133-16147
The HIV-1 capsid protein plays a crucial role in viral infectivity, assembling into a cone that encloses the viral RNA. In the mature virion, the N-terminal domain of the capsid protein forms hexameric and pentameric rings, while C-terminal domain ho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b96c1fc3919c7e1224c7a865a739cd9
https://doi.org/10.1021/ja406246z
https://doi.org/10.1021/ja406246z
Publikováno v:
Chemphyschem : a European journal of chemical physics and physical chemistry. 17(19)
A simple method, based on inversion modulated double electron-electron resonance electron paramagnetic resonance (DEER EPR) spectroscopy, is presented for determining populations of monomer and dimer in proteins (as well as any other biological macro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5582fc69c3aa88530e281fb70129ca6
https://pubmed.ncbi.nlm.nih.gov/27442455
https://pubmed.ncbi.nlm.nih.gov/27442455
Publikováno v:
Angewandte Chemie International Edition. 57:5953-5953
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a71ba29723bf7d7fa7f5a75a1d605417
https://doi.org/10.1002/anie.201803004
https://doi.org/10.1002/anie.201803004