Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Thomas B Acton"'
Autor:
Alexander Eletsky, Karolina Michalska, Scott Houliston, Qi Zhang, Michael D Daily, Xiaohui Xu, Hong Cui, Adelinda Yee, Alexander Lemak, Bin Wu, Maite Garcia, Meagan C Burnet, Kristen M Meyer, Uma K Aryal, Octavio Sanchez, Charles Ansong, Rong Xiao, Thomas B Acton, Joshua N Adkins, Gaetano T Montelione, Andrzej Joachimiak, Cheryl H Arrowsmith, Alexei Savchenko, Thomas Szyperski, John R Cort
Publikováno v:
PLoS ONE, Vol 9, Iss 7, p e101787 (2014)
Bacterial species in the Enterobacteriaceae typically contain multiple paralogues of a small domain of unknown function (DUF1471) from a family of conserved proteins also known as YhcN or BhsA/McbA. Proteins containing DUF1471 may have a single or th
Externí odkaz:
https://doaj.org/article/86d6bee1feac4e90bbb12b0e86a9a3f7
Autor:
Shuang-yong Xu, Alexandre P Kuzin, Jayaraman Seetharaman, Alice Gutjahr, Siu-Hong Chan, Yang Chen, Rong Xiao, Thomas B Acton, Gaetano T Montelione, Liang Tong
Publikováno v:
PLoS ONE, Vol 8, Iss 9, p e72114 (2013)
The crystal structure of a putative HNH endonuclease, Gmet_0936 protein from Geobacter metallireducens GS-15, has been determined at 2.6 Å resolution using single-wavelength anomalous dispersion method. The structure contains a two-stranded anti-par
Externí odkaz:
https://doaj.org/article/635f297fe2ca4bb4ae1613b8a9560c15
Autor:
Yibing Wu, Marco Punta, Rong Xiao, Thomas B Acton, Bharathwaj Sathyamoorthy, Fabian Dey, Markus Fischer, Arne Skerra, Burkhard Rost, Gaetano T Montelione, Thomas Szyperski
Publikováno v:
PLoS ONE, Vol 7, Iss 6, p e37404 (2012)
The soluble monomeric domain of lipoprotein YxeF from the Gram positive bacterium B. subtilis was selected by the Northeast Structural Genomics Consortium (NESG) as a target of a biomedical theme project focusing on the structure determination of the
Externí odkaz:
https://doaj.org/article/75854a80aed04bf4a7b9adb71cf253d4
Autor:
Luca Mazzei, Rebecca Greene-Cramer, Khushboo Bafna, Aleksandar Jovanovic, Anna De Falco, Thomas B. Acton, Catherine Ann Royer, Stefano Ciurli, Gaetano T. Montelione
Publikováno v:
STAR Protocols, Vol 4, Iss 2, Pp 102326- (2023)
Summary: 3CLpro protease from SARS-CoV-2 is a primary target for COVID-19 antiviral drug development. Here, we present a protocol for 3CLpro production in Escherichia coli. We describe steps to purify 3CLpro, expressed as a fusion with the Saccharomy
Externí odkaz:
https://doaj.org/article/de67ec972ab7404e8418b641877bf219
Autor:
Khushboo Bafna, Kris White, Balasubramanian Harish, Romel Rosales, Theresa A. Ramelot, Thomas B. Acton, Elena Moreno, Thomas Kehrer, Lisa Miorin, Catherine A. Royer, Adolfo García-Sastre, Robert M. Krug, Gaetano T. Montelione
Publikováno v:
Cell Reports, Vol 35, Iss 7, Pp 109133- (2021)
Summary: Effective control of COVID-19 requires antivirals directed against SARS-CoV-2. We assessed 10 hepatitis C virus (HCV) protease-inhibitor drugs as potential SARS-CoV-2 antivirals. There is a striking structural similarity of the substrate bin
Externí odkaz:
https://doaj.org/article/f487dc0be1e94d1382aa92c5a7ce55f1
Autor:
Rebecca Greene-Cramer, Khushboo Bafna, Kris White, Balasubramanian Harish, Romel Rosales, Theresa Ramelot, Thomas B. Acton, Elena Moreno Del Olmo, Thomas Kehrer, Lisa Miorin, Catherine A. Royer, Adolfo Garcia-Sastre, Robert Krug, Gaetano T. Montelione
Publikováno v:
Biophysical Journal. 121:30a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b871cd980716404460fea626fa88e215
https://doi.org/10.1016/j.bpj.2021.11.2568
https://doi.org/10.1016/j.bpj.2021.11.2568
Autor:
Catherine A. Royer, Gaetano T. Montelione, Khushboo Bafna, Kris M. White, Lisa Miorin, Thomas Kehrer, Elena Moreno, Thomas B. Acton, Robert M. Krug, Romel Rosales, Adolfo García-Sastre, T.A. Ramelot, Balasubramanian Harish
Publikováno v:
Cell Reports, Vol 35, Iss 7, Pp 109133-(2021)
Cell Reports
Cell Reports
Effective control of COVID-19 requires antivirals directed against SARS-CoV-2. We assessed ten hepatitis C virus (HCV) protease-inhibitor drugs as potential SARS-CoV-2 antivirals. There is a striking structural similarity of the substrate binding cle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c84d441747f7a650b4e094221b05e22
https://doi.org/10.1016/j.celrep.2021.109133
https://doi.org/10.1016/j.celrep.2021.109133
Autor:
Rongjin, Guan, Sriram, Aiyer, Marie L, Cote, Rong, Xiao, Mei, Jiang, Thomas B, Acton, Monica J, Roth, Gaetano T, Montelione
Publikováno v:
Proteins. 85(4)
The retroviral integrase (IN) carries out the integration of a dsDNA copy of the viral genome into the host DNA, an essential step for viral replication. All IN proteins have three general domains, the N-terminal domain (NTD), the catalytic core doma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5329391bf22d2c7f2061bd8fc0aff5a3
https://pubmed.ncbi.nlm.nih.gov/28066922
https://pubmed.ncbi.nlm.nih.gov/28066922
Autor:
David A, Snyder, James M, Aramini, Bomina, Yu, Yuanpeng J, Huang, Rong, Xiao, John R, Cort, Ritu, Shastry, Li-Chung, Ma, Jinfeng, Liu, Burkhard, Rost, Thomas B, Acton, Michael A, Kennedy, Gaetano T, Montelione
Publikováno v:
Proteins. 80(7)
The ribosome consists of small and large subunits each composed of dozens of proteins and RNA molecules. However, the functions of many of the individual protomers within the ribosome are still unknown. In this article, we describe the solution NMR s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1772b324c94cbb743fe37efbe5235995
https://pubmed.ncbi.nlm.nih.gov/22422653
https://pubmed.ncbi.nlm.nih.gov/22422653
Autor:
James M, Aramini, Paolo, Rossi, Markus, Fischer, Rong, Xiao, Thomas B, Acton, Gaetano T, Montelione
Publikováno v:
Proteins. 79(10)
Protein domain family PF09905 (DUF2132) is a family of small domains of unknown function that are conserved in a wide range of bacteria. Here we describe the solution NMR structure of the 80-residue VF0530 protein from Vibrio fischeri, the first stru
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4b33eab683b94361e774a7e946f92847
https://pubmed.ncbi.nlm.nih.gov/21905121
https://pubmed.ncbi.nlm.nih.gov/21905121