Entry ID | Original Release date | Data summary | Entry Title | Citation Title | Authors |
---|---|---|---|---|---|
30861 | 2021-03-01 | Chemical Shifts: 1 set Spectral_peak_list: 3 sets |
Solution NMR structure of the PNUTS amino-terminal Domain fused to Myc Homology Box 0 |
The MYC oncoprotein directly interacts with its chromatin cofactor PNUTS to recruit PP1 phosphatase
|
Aaliya Tamachi, Alexander Lemak, Alexandra Ahlner, Bjorn Wallner, Cheryl H Arrowsmith, Cornelia Redel, David W Andrews, Isak Johansson-Akhe, Linda Z Penn, Maria Sunnerhagen, Scott Houliston, Shili Duan, Tristan Kenney, Vivian Morad, Yong Wei |
30722 | 2020-02-21 | Chemical Shifts: 1 set |
Solution NMR structure of the N-terminal domain of the Serine/threonine-protein phosphatase 1 regulatory subunit 10, PPP1R10 |
The MYC oncoprotein directly interacts with its chromatin cofactor PNUTS to recruit PP1 phosphatase
|
Aaliya Tamachi, Alexander Lemak, Alexandra Ahlner, Bjorn Wallner, Cheryl H Arrowsmith, Cornelia Redel, David W Andrews, Isak Johansson-Akhe, Linda Z Penn, Maria Sunnerhagen, Scott Houliston, Shili Duan, Tristan Kenney, Vivian Morad, Yong Wei |
18176 | 2012-06-18 | Chemical Shifts: 1 set |
Backbone chemical shift assignments for the oxidized form of cVIMP-Cys |
The human selenoprotein VCP-interacting membrane protein (VIMP) is non-globular and harbors a reductase function in an intrinsically disordered region.
|
Andrea Vala, Jakob Rahr Winther, Jurate Kamarauskaite, Kaare Teilum, Kay Hofmann, Lars Ellgaard, Lea Cecilie Christensen, Linda Johansson, Njal Winther Jensen |
18177 | 2012-06-18 | Chemical Shifts: 1 set |
Backbone chemical shift assignments for the reduced form of cVIMP-Cys |
The human selenoprotein VCP-interacting membrane protein (VIMP) is non-globular and harbors a reductase function in an intrinsically disordered region.
|
Andrea Vala, Jakob Rahr Winther, Jurate Kamarauskaite, Kaare Teilum, Kay Hofmann, Lars Ellgaard, Lea Cecilie Christensen, Linda Johansson, Njal Winther Jensen |