Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Rebecca L. Newcomer"'
Autor:
Rebecca L Newcomer, Jason R Schrad, Eddie B Gilcrease, Sherwood R Casjens, Michael Feig, Carolyn M Teschke, Andrei T Alexandrescu, Kristin N Parent
Publikováno v:
eLife, Vol 8 (2019)
The major coat proteins of dsDNA tailed phages (order Caudovirales) and herpesviruses form capsids by a mechanism that includes active packaging of the dsDNA genome into a precursor procapsid, followed by expansion and stabilization of the capsid. Th
Externí odkaz:
https://doaj.org/article/a94a86477c72462ea6b6085239e80eb8
Publikováno v:
Biomolecular NMR Assignments. 12:339-343
Phage L encodes a trimeric 43 kDa decoration protein (Dec) that noncovalently binds and stabilizes the capsids of the homologous phages L and P22 in vitro. At physiological pH Dec was unsuitable for NMR. We were able to obtain samples amenable for NM
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e091a21370b2910713654a21c54fffdc
https://doi.org/10.1007/s12104-018-9836-1
https://doi.org/10.1007/s12104-018-9836-1
Autor:
Andrei T. Alexandrescu, Michael Feig, Carolyn M. Teschke, Sherwood R. Casjens, Kristin N. Parent, Jason R. Schrad, Rebecca L. Newcomer, Eddie B. Gilcrease
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::77fb901e3fc34b83e74f3a0d0fd405d7
https://doi.org/10.7554/elife.45345.025
https://doi.org/10.7554/elife.45345.025
Autor:
Jason R. Schrad, Kristin N. Parent, Michael Feig, Sherwood Casjens, Carolyn M. Teschke, Rebecca L. Newcomer, Eddie B. Gilcrease, Andrei T. Alexandrescu
Publikováno v:
eLife, Vol 8 (2019)
eLife
eLife
The major coat proteins of dsDNA tailed phages and herpesviruses form capsids by a mechanism that includes active packaging of the dsDNA genome into a precursor procapsid, followed by expansion and stabilization of the capsid. These viruses have evol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33a3d1fb392fcfff6bdba3d7ad83c70a
Publikováno v:
ChemInform. 47
Previous work has demonstrated that alkylated benzene sulfonanilides undergo sulfuric acid (98%)–catalyzed rearrangement to alkylamino diaryl sulfones. Similar treatment of their unalkylated analogs typically leads only to hydrolysis. Surprisingly,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::afd52504a4feff6b09faaedfede47e6c
https://doi.org/10.1002/chin.201645031
https://doi.org/10.1002/chin.201645031
Previous work has demonstrated that alkylated benzene sulfonanilides undergo sulfuric acid (98%)–catalyzed rearrangement to alkylamino diaryl sulfones. Similar treatment of their unalkylated analogs typically leads only to hydrolysis. Surprisingly,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26cd2ebf7a8ae737be3d144795671769
The I-domain is an insertion domain of the bacteriophage P22 coat protein that drives rapid folding and accounts for over half of the stability of the full-length protein. We sought to determine the role of hydrogen bonds (H-bonds) in the unfolding o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ab9a9b2347274e4be3ed13475e570b8
https://europepmc.org/articles/PMC4699920/
https://europepmc.org/articles/PMC4699920/
Autor:
Sónia Cruz, João Serôdio, Gisela Dionísio, Mary E. Rumpho, Ricardo Calado, Rebecca L. Newcomer, Karen N. Pelletreau, Paulo Cartaxana
Publikováno v:
Scientific Reports
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Some sea slugs are capable of retaining functional sequestered chloroplasts (kleptoplasts) for variable periods of time. The mechanisms supporting the maintenance of these organelles in animal hosts are still largely unknown. Non-photochemical quench
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6009193193c254677daa920814d18df
https://doi.org/10.1038/srep07904
https://doi.org/10.1038/srep07904