Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Nicholas Fredette"'
Autor:
Brian Cunniff, Gregg W. Snider, Nicholas Fredette, Jason Stumpff, Robert J. Hondal, Nicholas H. Heintz
Publikováno v:
Redox Biology, Vol 2, Iss C, Pp 475-484 (2014)
Thioredoxin reductase (TR) catalyzes the reduction of thioredoxin (TRX), which in turn reduces mammalian typical 2-Cys peroxiredoxins (PRXs 1–4), thiol peroxidases implicated in redox homeostasis and cell signaling. Typical 2-Cys PRXs are inactivat
Externí odkaz:
https://doaj.org/article/a2ab729a78a9419497152b76959de25c
Autor:
Sharon Shacham, Yosef Landesman, Leah Henegar, Kathleen Martyn, Christopher James Walker, Hua Chang, Trinayan Kashyap, Nicholas Fredette
Publikováno v:
Cancer Research. 81:1049-1049
Background: Decitabine (DEC) is a hypomethylating agent approved to treat acute myeloid leukemia (AML) that can reactivate tumor suppressor genes that are epigenetically silenced by DNA methylation. Selinexor (SEL) is a selective inhibitor of nuclear
Autor:
Yongfei Cai, Andrea Carfi, Bing Chen, Kshitij Wagh, James Theiler, Michael S. Seaman, Stephen C. Harrison, Sophia Rits-Volloch, Selen Karaca-Griffin, Christine E. Linton, Nicholas Fredette, Sai Tian, Jia Chen, Jianming Lu, Bette T. Korber
Publikováno v:
Proceedings of the National Academy of Sciences. 114:4477-4482
The extraordinary genetic diversity of the HIV-1 envelope spike [Env; trimeric (gp160)3, cleaved to (gp120/gp41)3] poses challenges for vaccine development. Envs of different clinical isolates exhibit different sensitivities to antibody-mediated neut
Autor:
Jason Stumpff, Robert J. Hondal, Nicholas Fredette, Gregg W. Snider, Brian Cunniff, Nicholas H. Heintz
Publikováno v:
Redox Biology, Vol 2, Iss C, Pp 475-484 (2014)
Redox Biology
Redox Biology
Thioredoxin reductase (TR) catalyzes the reduction of thioredoxin (TRX), which in turn reduces mammalian typical 2-Cys peroxiredoxins (PRXs 1–4), thiol peroxidases implicated in redox homeostasis and cell signaling. Typical 2-Cys PRXs are inactivat
Publikováno v:
Analytical Biochemistry. 443:34-40
Thioredoxin reductase (TR) is an oxidoreductase responsible for maintaining thioredoxin in the reduced state, thereby contributing to proper cellular redox homeostasis. The C-terminal active site of mammalian TR contains the rare amino acid selenocys
Autor:
Nicholas Fredette, Michael Rist, Janina M. Benoit, Meg E. Kirkpatrick, Wyll Everett, Jennifer M. Gibson
Publikováno v:
Neurotoxicology. 50
Methylmercury (MeHg) is a widely distributed environmental neurotoxin with established effects on locomotor behaviors and cognition in both human populations and animal models. Despite well-described neurobehavioral effects, the mechanisms of MeHg to