SGTA interacts with the proteasomal ubiquitin receptor Rpn13 via a carboxylate clamp mechanism.
about
Structure and Interactions of the TPR Domain of Sgt2 with Yeast Chaperones and Ybr137wp.Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control.identification and biochemical characterization of the human dicarboxylate clamp TPR protein interaction network
P2860
SGTA interacts with the proteasomal ubiquitin receptor Rpn13 via a carboxylate clamp mechanism.
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
2016年论文
@zh
2016年论文
@zh-cn
name
SGTA interacts with the protea ...... a carboxylate clamp mechanism.
@en
SGTA interacts with the protea ...... a carboxylate clamp mechanism.
@nl
type
label
SGTA interacts with the protea ...... a carboxylate clamp mechanism.
@en
SGTA interacts with the protea ...... a carboxylate clamp mechanism.
@nl
prefLabel
SGTA interacts with the protea ...... a carboxylate clamp mechanism.
@en
SGTA interacts with the protea ...... a carboxylate clamp mechanism.
@nl
P2093
P2860
P50
P356
P1433
P1476
SGTA interacts with the protea ...... a carboxylate clamp mechanism
@en
P2093
Ewelina M Krysztofinska
Isabelle L Terry
Nicola J Evans
Yvonne Nyathi
P2860
P2888
P356
10.1038/SREP36622
P407
P577
2016-11-09T00:00:00Z