Zobrazeno 1 - 10
of 58
pro vyhledávání: '"Michael R. Duff"'
Autor:
Rupesh Agarwal, Pawat Pattarawat, Michael R. Duff, Hwa-Chain Robert Wang, Jerome Baudry, Jeremy C. Smith
Publikováno v:
Pharmaceuticals, Vol 17, Iss 7, p 867 (2024)
Histone deacetylases (HDACs) are important cancer drug targets. Existing FDA-approved drugs target the catalytic pocket of HDACs, which is conserved across subfamilies (classes) of HDAC. However, engineering specificity is an important goal. Herein,
Externí odkaz:
https://doaj.org/article/8c72edc793fc47ea81c5a0326e30330a
Autor:
Jasmina S. Redzic, Michael R. Duff, Ashley Blue, Todd M. Pitts, Pratul Agarwal, Elan Zohar Eisenmesser
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
The biliverdin reductase B (BLVRB) class of enzymes catalyze the NADPH-dependent reduction of multiple flavin substrates and are emerging as critical players in cellular redox regulation. However, the role of dynamics and allostery have not been addr
Externí odkaz:
https://doaj.org/article/ee672be1a0f340ee8b3426730e2bf8ca
Autor:
Gabriel J. Fuente‐Gómez, Alexis C. Miranda, Creighton L. Kellum, Elizabeth E. Howell, Michael R. Duff
Publikováno v:
Protein Science. 30:477-484
R67 dihydrofolate reductase (R67 DHFR) is a plasmid-encoded enzyme that confers resistance to the antibacterial drug trimethoprim. R67 DHFR is a tetramer with a single active site that is unusual as both cofactor and substrate are recognized by symme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7a4e1c907b98b5f43f8cc6671bff3430
https://doi.org/10.1002/pro.4007
https://doi.org/10.1002/pro.4007
Autor:
Rupesh Agarwal, Pawat Pattarawat, Michael R. Duff, Hwa-Chain Robert Wang, Jerome Baudry, Jeremy C. Smith
Histone deacetylases (HDACs) are important cancer drug targets. Existing FDA-approved drugs target the catalytic pocket of HDACs, which is conserved across subfamilies (classes) of HDAC. Here, we use molecular modeling approaches to identify and targ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0b00127d9b4c7cd16108081d50a770ce
https://doi.org/10.1101/2022.05.31.494169
https://doi.org/10.1101/2022.05.31.494169
Autor:
Lars C. Pedersen, Robert E. London, Elizabeth E. Howell, Scott A. Gabel, Juno M. Krahn, Michael R. Duff, Eugene F. DeRose
Publikováno v:
J Med Chem
Although nonsteroidal anti-inflammatory drugs (NSAIDs) target primarily cyclooxygenase enzymes, a subset of NSAIDs containing carboxylate groups also has been reported to competitively inhibit dihydrofolate reductase (DHFR). In this study, we have ch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87856884455707440c1eaf986117e32f
https://doi.org/10.1021/acs.jmedchem.0c00546
https://doi.org/10.1021/acs.jmedchem.0c00546
Publikováno v:
The Journal of Physical Chemistry B. 124:6212-6224
Osmolyte interactions with ligands can affect their affinity for proteins and are dependent upon the cosolute and the functional groups of the ligand. Here, we explored ligand binding to Bacillus anthracis dihydropteroate synthase (BaDHPS) under osmo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::577c7cc014c749c94c7fa7ff856b4469
https://doi.org/10.1021/acs.jpcb.0c03311
https://doi.org/10.1021/acs.jpcb.0c03311
Publikováno v:
Biochemistry. 58:1198-1213
Dihydrofolate reductase (DHFR) reduces dihydrofolate (DHF) to tetrahydrofolate using NADPH as a cofactor. Due to its role in one carbon metabolism, chromosomal DHFR is the target of the antibacterial drug, trimethoprim. Resistance to trimethoprim has
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3fc763969f1e2982bd4ab312cb86eee7
https://doi.org/10.1021/acs.biochem.8b01110
https://doi.org/10.1021/acs.biochem.8b01110
Autor:
Pratul K Agarwal, Michael R. Duff, Ashley Blue, Todd M. Pitts, Elan Z. Eisenmesser, Jasmina S. Redzic
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
Frontiers in Molecular Biosciences
Frontiers in Molecular Biosciences
The biliverdin reductase B (BLVRB) class of enzymes catalyze the NADPH-dependent reduction of multiple flavin substrates and are emerging as critical players in cellular redox regulation. However, the role of dynamics and allostery have not been addr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abba513b762f5f1c12e6a70f608fb066
https://doi.org/10.3389/fmolb.2021.691208
https://doi.org/10.3389/fmolb.2021.691208
Publikováno v:
The journal of physical chemistry. B. 124(29)
Osmolyte interactions with ligands can affect their affinity for proteins and are dependent upon the cosolute and the functional groups of the ligand. Here, we explored ligand binding to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::fb6e3c09854a931612130dc3720b1196
https://pubmed.ncbi.nlm.nih.gov/32580556
https://pubmed.ncbi.nlm.nih.gov/32580556
Autor:
Michael R. Duff, Todd M. Pitts, Elan Z. Eisenmesser, Natasia Paukovich, Jasmina S. Redzic, Jay C. Nix, Pratul K. Agarwal, Lucas P Ryan, Rui Zhao
Publikováno v:
Journal of biochemistry. 168(2)
Biliverdin reductase B (BLVRB) family members are general flavin reductases critical in maintaining cellular redox with recent findings revealing that BLVRB alone can dictate cellular fate. However, as opposed to most enzymes, the BLVRB family remain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae016a6acbd4bbb2545e7de2815dd0ab
https://pubmed.ncbi.nlm.nih.gov/32246827
https://pubmed.ncbi.nlm.nih.gov/32246827