Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Bridget P. Belcher"'
Autor:
Bridget P Belcher, Paulo A Machicao, Binqi Tong, Emily Ho, Julia Friedli, Brian So, Helen Bui, Yosuke Isobe, Thomas J Maimone, Daniel K Nomura
Publikováno v:
ChemBioChem.
Autor:
Bridget P. Belcher, Paulo A. Machicao, Binqi Tong, Emily Ho, Julia Friedli, Brian So, Helen Bui, Yosuke Isobe, Thomas J. Maimone, Daniel K. Nomura
Publikováno v:
bioRxiv
Chlorinated gymnastatin and dankastatin alkaloids derived from the fungal strainGymnascella dankaliensishave been reported to possess significant anti-cancer activity but their mode of action is unknown. These members possess electrophilic functional
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8b21dcfcdb4248953ae2570b22c4526
https://doi.org/10.1101/2023.02.11.528139
https://doi.org/10.1101/2023.02.11.528139
Autor:
Annika C. S. Page, Spencer O. Scholz, Katherine N. Keenan, Jessica N. Spradlin, Bridget P. Belcher, Scott M. Brittain, John A. Tallarico, Jeffrey M. McKenna, Markus Schirle, Daniel K. Nomura, F. Dean Toste
Publikováno v:
Chemical science, vol 13, iss 13
Photoaffinity labeling (PAL) is a powerful tool for the identification of non-covalent small molecule-protein interactions that are critical to drug discovery and medicinal chemistry, but this approach is limited to only a small subset of robust phot
Publikováno v:
Biochemistry
Targeted protein degradation (TPD) using Proteolysis Targeting Chimeras (PROTACs) and molecular glue degraders has arisen as a powerful therapeutic modality for eliminating disease-causing proteins from cells. PROTACs and molecular glue degraders emp
Publikováno v:
Chemical science, vol 12, iss 25
Chemical Science
Chemical Science
Electrophilic natural products have provided fertile ground for understanding how nature inhibits protein function using covalent bond formation. The fungal strain Gymnascella dankaliensis has provided an especially interesting collection of halogena
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d26ea5bbee08728738771daf439c175a
https://escholarship.org/uc/item/8gk0k7xx
https://escholarship.org/uc/item/8gk0k7xx
Autor:
Nathaniel J. Henning, Scott M. Brittain, Lynn M. McGregor, John A. Tallarico, Hesse M, Carl C. Ward, Bridget P. Belcher, Lydia Boike, Jessica N. Spradlin, Markus Schirle, Jeffery M. McKenna, Dustin Dovala, Daniel K. Nomura
Targeted protein degradation is a powerful therapeutic modality that uses heterobifunctional small-molecules to induce proximity between E3 ubiquitin ligases and target proteins to ubiquitinate and degrade specific proteins of interest. However, many
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::38f2a0ff703641e9a40022f756281844
https://doi.org/10.1101/2021.04.30.441959
https://doi.org/10.1101/2021.04.30.441959
Autor:
Nathaniel J. Henning, Lydia Boike, Jessica N. Spradlin, Carl C. Ward, Gang Liu, Erika Zhang, Bridget P. Belcher, Scott M. Brittain, Matthew J. Hesse, Dustin Dovala, Lynn M. McGregor, Rachel Valdez Misiolek, Lindsey W. Plasschaert, David J. Rowlands, Feng Wang, Andreas O. Frank, Daniel Fuller, Abigail R. Estes, Katelyn L. Randal, Anoohya Panidapu, Jeffrey M. McKenna, John A. Tallarico, Markus Schirle, Daniel K. Nomura
Publikováno v:
Nature chemical biology, vol 18, iss 4
Many diseases are driven by proteins that are aberrantly ubiquitinated and degraded. These diseases would be therapeutically benefited by targeted protein stabilization (TPS). Here we present deubiquitinase-targeting chimeras (DUBTACs), heterobifunct