dc.contributor |
Казанский федеральный университет |
|
dc.contributor.author |
Bulatov Emil Rafaelevich |
|
dc.contributor.author |
Chatterjee Sneha |
|
dc.contributor.author |
Ciulli Alessio |
|
dc.contributor.author |
Grandi Paola |
|
dc.contributor.author |
Johnson Clare |
|
dc.contributor.author |
Knebel Axel |
|
dc.contributor.author |
Konijnenberg Albert |
|
dc.contributor.author |
Martin Esther |
|
dc.contributor.author |
Shimamura Satoko |
|
dc.contributor.author |
Sobott Frank |
|
dc.contributor.author |
Zinn Nico |
|
dc.date.accessioned |
2017-03-21T13:12:12Z |
|
dc.date.available |
2017-03-21T13:12:12Z |
|
dc.date.issued |
2015 |
|
dc.identifier.citation |
Bulatov, E. R. Biophysical studies on interactions and assembly of full-size E3 ubiquitin ligase: suppressor of cytokine signaling 2 (SOCS2):ElonginBC:Cullin5:RING-box protein 2 (Rbx2) / Е. R. Bulatov, Е. М. Martin, S. Сhatterjee, А. Knebel, S. Shimamura, А. Konijnenberg, С. Johnson, N. Zinn, Р. Grandi, F. Sobott, А. Ciulli // The Journal of Biological Chemistry. - 2015. - Vol. 290. - № 7. - Р. 4178-4191. |
|
dc.identifier.uri |
http://dspace.kpfu.ru/xmlui/handle/net/110273 |
|
dc.description.abstract |
|
|
dc.language.iso |
en |
|
dc.relation.ispartofseries |
The Journal of Biological Chemistry |
|
dc.rights |
только для КФУ |
|
dc.subject |
Biophysics |
|
dc.subject |
E3 Ubiquitin Ligase |
|
dc.subject |
Isothermal Titration Calorimetry (ITC |
|
dc.subject |
) Mass Spectrometry (MS) |
|
dc.subject |
Post-translational Modification (PTM) |
|
dc.subject |
Protein Assembly |
|
dc.subject |
Protein Complex |
|
dc.subject |
Protein-Protein Interaction |
|
dc.subject |
Cullin |
|
dc.title |
Biophysical Studies on Interactions and Assembly of Full-size E3 Ubiquitin Ligase
SUPPRESSOR OF CYTOKINE SIGNALING 2 (SOCS2)-ELONGIN BC-CULLIN 5-RING BOX PROTEIN 2 (RBX2) |
|
dc.type |
Article |
|
dc.contributor.org |
Институт фундаментальной медицины и биологии |
|
dc.description.pages |
|
|
dc.relation.ispartofseries-issue |
7 |
|
dc.relation.ispartofseries-volume |
290 |
|
dc.pub-id |
103896 |
|