Structural mechanisms of interaction of triphosphorylated 2`-5`-triadenylates with S100A1 protein
Saved in:
| Date: | 2020 |
|---|---|
| Main Authors: | Yu. Skorobohatov, Yu. Zhukov, Yu. Tkachuk |
| Format: | Article |
| Language: | English |
| Published: |
2020
|
| Series: | Reports of the National Academy of Sciences of Ukraine |
| Online Access: | http://jnas.nbuv.gov.ua/article/UJRN-0001082660 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| Journal Title: | Library portal of National Academy of Sciences of Ukraine | LibNAS |
Institution
Library portal of National Academy of Sciences of Ukraine | LibNASSimilar Items
-
2′,5′ oligoadenylates change the secondary structure and the functional activity of human S100A1 protein
by: Yu. Skorobohatov, et al.
Published: (2015) -
Study of dephosphorylated 2'-5'-linked oligoadenylates impact on apo-S100A1 protein conformation by heteronuclear NMR and circular dichroism
by: Skorobogatov, O.Yu., et al.
Published: (2014) -
Study of dephosphorylated 2'-5'-linked oligoadenylates impact on apo -S100A1 protein conformation by heteronuclear NMR and circular dichroism
by: Yu. Skorobogatov, et al.
Published: (2014) -
Investigation of the interaction of "core” 2′,5′-oligoadenylates with some proteins by fluorescence spectroscopy
by: V. V. Tkachuk, et al.
Published: (2015) -
Interaction of serine/threonine protein phosphatase 5 with the protein products of tumour suppressor gene Tsc2
by: Malanchuk, O.M., et al.
Published: (2007)