Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Cody Aplin"'
Autor:
Cody Aplin, Kara A. Zielinski, Suzette Pabit, Deborah Ogunribido, William P. Katt, Lois Pollack, Richard A. Cerione, Shawn K. Milano
Publikováno v:
Communications Biology, Vol 7, Iss 1, Pp 1-16 (2024)
Abstract Transglutaminase 2 (TG2) is a GTP-binding, protein-crosslinking enzyme that has been investigated as a therapeutic target for Celiac disease, neurological disorders, and aggressive cancers. TG2 has been suggested to adopt two conformational
Externí odkaz:
https://doaj.org/article/c30285b37bdd4cb1aa637ea1b450312e
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-14 (2024)
Abstract The glutaminase enzymes GAC and GLS2 catalyze the hydrolysis of glutamine to glutamate, satisfying the ‘glutamine addiction’ of cancer cells. They are the targets of anti-cancer drugs; however, their mechanisms of activation and catalyti
Externí odkaz:
https://doaj.org/article/0e74d97efe8c4ed9bbc126d24beb796e
Autor:
Kara A. Zielinski, Andrea M. Katz, George D. Calvey, Suzette A. Pabit, Shawn K. Milano, Cody Aplin, Josue San Emeterio, Richard A. Cerione, Lois Pollack
Publikováno v:
IUCrJ, Vol 10, Iss 3, Pp 363-375 (2023)
Advances in time-resolved structural techniques, mainly in macromolecular crystallography and small-angle X-ray scattering (SAXS), allow for a detailed view of the dynamics of biological macromolecules and reactions between binding partners. Of parti
Externí odkaz:
https://doaj.org/article/845924a548ac481394f8df26f15ff8be
Publikováno v:
J Phys Chem B
Structure-based drug design (SBDD) is a prominent method in rational drug development and has traditionally benefitted from the atomic models of protein targets obtained using X-ray crystallography at cryogenic temperatures. In this perspective, we h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8acbcac93ef619ffbf4cc6eda8a0534e
https://doi.org/10.1021/acs.jpcb.2c04344
https://doi.org/10.1021/acs.jpcb.2c04344
Publikováno v:
OncoTargets and Therapy. 15:277-290
Tissue transglutaminase (tTG) is a rather unique GTP-binding/protein crosslinking enzyme that has been shown to play important roles in a number of cellular processes that impact both normal physiology and disease states. This is especially the case
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38b84133929aa168d87f6cd0fe5e1718
https://doi.org/10.2147/ott.s329262
https://doi.org/10.2147/ott.s329262
Publikováno v:
bioRxiv
The mitochondrial glutaminase enzymes initiate glutaminolysis by catalyzing the hydrolysis of glutamine to glutamate, satisfying the metabolic requirements of aggressive cancers and thus representing potential therapeutic targets. However, the mechan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae886e5b92e897dfd5da27042a826771
https://europepmc.org/articles/PMC9949068/
https://europepmc.org/articles/PMC9949068/
