Chemogenomic profiling of human and microbial fk506-binding proteins
FK506-binding proteins (FKBPs) are evolutionarily conserved proteins that display peptidyl-prolyl isomerase activities and act as coreceptors for immunosuppressants. Microbial macrophage-infectivity-potentiator (Mip)-type FKBPs can enhance infectivity. However, developing druglike ligands for FKBPs...
Saved in:
Main Authors: | Pomplun, Sebastian, Sippel, Claudia, Hähle, Andreas, Tay, Donald, Shima, Kensuke, Klages, Alina, Ünal, Can Murat, Rieß, Benedikt, Toh, Hui Ting, Hansen, Guido, Yoon, Ho Sup, Bracher, Andreas, Preiser, Peter, Rupp, Jan, Steinert, Michael, Hausch, Felix |
---|---|
Other Authors: | School of Biological Sciences |
Format: | Article |
Language: | English |
Published: |
2019
|
Subjects: | |
Online Access: | https://hdl.handle.net/10356/88940 http://hdl.handle.net/10220/48345 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Institution: | Nanyang Technological University |
Language: | English |
Similar Items
-
Crystal structure of the FK506 binding domain of plasmodium falciparum FKBP35 in complex with FK506
by: Kotaka, Masayo, et al.
Published: (2012) -
NMR assignments of the FK506-binding domain of FK506-binding protein 35 from Plasmodium vivax
by: Shin, Joon, et al.
Published: (2012) -
Solution structure of FK506 binding domain (FKBD) of Plasmodium falciparum FK506 binding protein 35 (PfFKBP35)
by: Kang, Cong Bao, et al.
Published: (2012) -
The immunosuppressive antagonism of low doses of FK506 and cyclosporine
by: Vathsala, A, et al.
Published: (2022) -
Betamethasone administration during pregnancy is associated with placental epigenetic changes with implications for inflammation
by: Czamara, Darina, et al.
Published: (2022)