Zobrazeno 1 - 10
of 94
pro vyhledávání: '"Monica J, Roth"'
Autor:
Arup Mondal, G.V.T. Swapna, Maria M. Lopez, Laura Klang, Jingzhou Hao, LiChung Ma, Monica J. Roth, Gaetano T. Montelione, Alberto Perez
Publikováno v:
J Chem Inf Model
Intrinsically disordered regions of proteins often mediate important protein–protein interactions. However, the folding-upon-binding nature of many polypeptide–protein interactions limits the ability of modeling tools to predict the three-dimensi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2896313d0e69f68fd897e44cc63cc0a1
https://doi.org/10.1021/acs.jcim.2c01595
https://doi.org/10.1021/acs.jcim.2c01595
Autor:
Lorenz Loyola, Vasudevan Achuthan, Kathryn Gilroy, Gillian Borland, Anna Kilbey, Nancy Mackay, Margaret Bell, Jodie Hay, Sriram Aiyer, Dylan Fingerman, Rodrigo A Villanueva, Ewan Cameron, Christine A Kozak, Alan N Engelman, James Neil, Monica J Roth
Publikováno v:
PLoS Pathogens, Vol 15, Iss 12, p e1008154 (2019)
Murine leukemia virus (MLV) integrase (IN) lacking the C-terminal tail peptide (TP) loses its interaction with the host bromodomain and extraterminal (BET) proteins and displays decreased integration at promoter/enhancers and transcriptional start si
Externí odkaz:
https://doaj.org/article/91ca4810555048f5889c474b6985f372
Autor:
Arup Mondal, G.V.T. Swapna, Jingzhou Hao, LiChung Ma, Monica J. Roth, Gaetano T. Montelione, Alberto Perez
Intrinsically disordered regions of proteins often mediate important protein-protein interactions. However, the folding upon binding nature of many polypeptide-protein interactions limits the ability of modeling tools to predict structures of such co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::437c1f879b5a5633d2bcd6fb1babd36c
https://doi.org/10.1101/2021.12.31.474671
https://doi.org/10.1101/2021.12.31.474671
Autor:
Jingzhou Hao, Li-Chung Ma, Gaetano T. Montelione, G. V. T. Swapna, Monica J. Roth, Gaohua Liu, Brian C. Jacobs, Gordon Chalmers, Sriram Aiyer
Publikováno v:
SSRN Electronic Journal.
SummaryThe extra-terminal (ET) domain of BRD3 is conserved among BET proteins (BRD2, BRD3, BRD4), interacting with multiple host and viral protein-protein networks. Solution NMR structures of complexes formed between BRD3-ET domain with either the 79
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18a1b5b0e8eb62f5a4b0a9c9a9652679
https://doi.org/10.2139/ssrn.3708513
https://doi.org/10.2139/ssrn.3708513
Publikováno v:
PLoS ONE, Vol 7, Iss 4, p e34778 (2012)
The identification of stem cells within a mixed population of cells is a major hurdle for stem cell biology--in particular, in the identification of induced pluripotent stem (iPS) cells during the reprogramming process. Based on the selective express
Externí odkaz:
https://doaj.org/article/69d57c6374964ba6904da7aa54841279
Autor:
Monica J. Roth, G. V. T. Swapna, Brian C. Jacobs, Jingzhou Hao, Gordon Chalmers, Gaohua Liu, Gaetano T. Montelione, Li-Chung Ma, Sriram Aiyer
Publikováno v:
Structure. 29:886-898.e6
The extraterminal (ET) domain of BRD3 is conserved among BET proteins (BRD2, BRD3, BRD4), interacting with multiple host and viral protein-protein networks. Solution NMR structures of complexes formed between the BRD3 ET domain and either the 79-resi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2df5ac04ee9ab966f366e9dce98b5add
https://doi.org/10.1016/j.str.2021.01.010
https://doi.org/10.1016/j.str.2021.01.010
Autor:
Marie L. Coté, Rongjin Guan, Monica J. Roth, Gaetano T. Montelione, Thomas Acton, Sriram Aiyer, Rong Xiao, Mei Jiang
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 85:647-656
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=doi_________::a93a90847cfd1559c60b27862c4bbd6c
https://doi.org/10.1002/prot.25245
https://doi.org/10.1002/prot.25245
Autor:
Jodie Hay, Margaret Bell, Nancy Mackay, Sriram Aiyer, Alan Engelman, Anna Kilbey, Gillian Borland, Christine A. Kozak, James C. Neil, Rodrigo A. Villanueva, Vasudevan Achuthan, Dylan Fingerman, Monica J. Roth, Kathryn Gilroy, Lorenz Loyola, Ewan R. Cameron
Publikováno v:
PLoS Pathogens, Vol 15, Iss 12, p e1008154 (2019)
PLoS Pathogens
PLoS Pathogens
Murine leukemia virus (MLV) integrase (IN) lacking the C-terminal tail peptide (TP) loses its interaction with the host bromodomain and extraterminal (BET) proteins and displays decreased integration at promoter/enhancers and transcriptional start si
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f9faf7ec2328b7b72ba13b0eda83ce3
https://doi.org/10.1371/journal.ppat.1008154
https://doi.org/10.1371/journal.ppat.1008154
Autor:
Frederic D. Bushman, Paolo Rossi, Sriram Aiyer, Monica J. Roth, William M. Schneider, Nirav Malani, Ashwin Chandar, Gaetano T. Montelione
Publikováno v:
Nucleic Acids Research
Target-site selection by retroviral integrase (IN) proteins profoundly affects viral pathogenesis. We describe the solution nuclear magnetic resonance structure of the Moloney murine leukemia virus IN (M-MLV) C-terminal domain (CTD) and a structural
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e36ce0c119cd7edab6a11c1cd6ba0506
https://doi.org/10.1093/nar/gkv410
https://doi.org/10.1093/nar/gkv410
Autor:
G. V. T. Swapna, Sriram Aiyer, Nirav Malani, Frederic D. Bushman, Matthew R. Plumb, James M. Aramini, William M. Schneider, Monica J. Roth, Mustafa H. Ghanem, Barbara Studamire, Ross C. Larue, Amit Sharma, Mamuka Kvaratskhelia, Gaetano T. Montelione
Publikováno v:
Nucleic Acids Research
We report alterations to the murine leukemia virus (MLV) integrase (IN) protein that successfully result in decreasing its integration frequency at transcription start sites and CpG islands, thereby reducing the potential for insertional activation.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed26c5edf75f7ea23d034e1b3a715a52
https://doi.org/10.1093/nar/gku175
https://doi.org/10.1093/nar/gku175