Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Caralyn E Sein"'
Autor:
Alam García-Heredia, Takehiro Kado, Caralyn E Sein, Julia Puffal, Sarah H Osman, Julius Judd, Todd A Gray, Yasu S Morita, M Sloan Siegrist
Publikováno v:
eLife, Vol 10 (2021)
Many antibiotics target the assembly of cell wall peptidoglycan, an essential, heteropolymeric mesh that encases most bacteria. In rod-shaped bacteria, cell wall elongation is spatially precise yet relies on limited pools of lipid-linked precursors t
Externí odkaz:
https://doaj.org/article/5e854a09122b4a0eb05a1616a3d7f3aa
Autor:
Guillaume B.E. Stewart-Jones, Sayda M. Elbashir, Kai Wu, Diana Lee, Isabella Renzi, Baoling Ying, Matthew Koch, Caralyn E. Sein, Angela Choi, Bradley Whitener, Dario Garcia-Dominguez, Carole Henry, Angela Woods, LingZhi Ma, Daniela Montes Berrueta, Laura E. Avena, Julian Quinones, Samantha Falcone, Chiaowen J. Hsiao, Suzanne M. Scheaffer, Larissa B. Thackray, Phil White, Michael S. Diamond, Darin K. Edwards, Andrea Carfi
Publikováno v:
bioRxiv
With the success of mRNA vaccines against coronavirus disease 2019 (COVID-19), strategies can now focus on improving vaccine potency, breadth, and stability. We present the design and preclinical evaluation of domain-based mRNA vaccines encoding the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bfe8958c3e87fbf6d9c9bca9931512ac
https://europepmc.org/articles/PMC9558437/
https://europepmc.org/articles/PMC9558437/
Autor:
Yasu S. Morita, Benjamin M. Swarts, M. Sloan Siegrist, Herbert W. Kavunja, Kyle J. Biegas, Jessica M. Groenevelt, Brent F. Piligian, Jessica A. Stewart, Caralyn E Sein, Nicholas Banahene, Michael Niederweis
Publikováno v:
J Am Chem Soc
Mycobacteria have a distinctive glycolipid-rich outer membrane, the mycomembrane, which is a critical target for tuberculosis drug development. However, proteins that associate with the mycomembrane, or that are involved in its metabolism and host in
Autor:
M. Sloan Siegrist, Yasu S. Morita, Todd A. Gray, Sarah H Osman, Alam García-Heredia, Julius Judd, Takehiro Kado, Julia Puffal, Caralyn E Sein
Publikováno v:
eLife, Vol 10 (2021)
eLife
eLife
Many antibiotics target the assembly of cell wall peptidoglycan, an essential, heteropolymeric mesh that encases most bacteria. In rod-shaped bacteria, cell wall elongation is spatially precise yet relies on limited pools of lipid-linked precursors t
Boosting with variant-matched or historical mRNA vaccines protects against Omicron infection in mice
Autor:
Baoling Ying, Suzanne M. Scheaffer, Bradley Whitener, Chieh-Yu Liang, Oleksandr Dmytrenko, Samantha Mackin, Kai Wu, Diana Lee, Laura E. Avena, Zhenlu Chong, James Brett Case, LingZhi Ma, Thu T.M. Kim, Caralyn E. Sein, Angela Woods, Daniela Montes Berrueta, Gwo-Yu Chang, Guillaume Stewart-Jones, Isabella Renzi, Yen-Ting Lai, Agata Malinowski, Andrea Carfi, Sayda M. Elbashir, Darin K. Edwards, Larissa B. Thackray, Michael S. Diamond
Publikováno v:
Cell. 185:1572-1587.e11
The large number of spike substitutions in Omicron lineage variants (BA.1, BA.1.1., and BA.2) could jeopardize the efficacy of SARS-CoV-2 vaccines. We evaluated in mice the protective efficacy of the Moderna mRNA-1273 vaccine against BA.1 before or a
Publikováno v:
Cytoskeleton (Hoboken, N.j.)
In many model organisms, diffuse patterning of cell wall peptidoglycan synthesis by the actin homolog MreB enables the bacteria to maintain their characteristic rod shape. InCaulobacter crescentusandEscherichia coli, MreB is also required to sculpt t
Autor:
Alam García-Heredia, Sarah H Osman, Yasu S. Morita, Julia Puffal, Todd A. Gray, Julius Judd, Caralyn E Sein, Takehiro Kado, Siegrist Ms
Many antibiotics target the assembly of cell wall peptidoglycan, an essential, heteropolymeric mesh that encases most bacteria. Different species have characteristic subcellular sites of peptidoglycan synthesis that they must carefully maintain for s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d1e4aea3d56f7d2ddbee19265fc60e53
https://doi.org/10.1101/544338
https://doi.org/10.1101/544338