Subcellular Fractionation Analysis of the Extraction of Ubiquitinated Polytopic Membrane Substrate during ER-Associated Degradation
about
Lipid disequilibrium disrupts ER proteostasis by impairing ERAD substrate glycan trimming and dislocation.Establishing the lipid droplet proteome: Mechanisms of lipid droplet protein targeting and degradation.Lipid droplet functions beyond energy storage.Transmembrane helix hydrophobicity is an energetic barrier during the retrotranslocation of integral membrane ERAD substratesA Cdc48 "Retrochaperone" Function Is Required for the Solubility of Retrotranslocated, Integral Membrane Endoplasmic Reticulum-associated Degradation (ERAD-M) Substrates.The Dfm1 Derlin Is Required for ERAD Retrotranslocation of Integral Membrane Proteins.
P2860
Subcellular Fractionation Analysis of the Extraction of Ubiquitinated Polytopic Membrane Substrate during ER-Associated Degradation
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
Subcellular Fractionation Anal ...... ring ER-Associated Degradation
@ast
Subcellular Fractionation Anal ...... ring ER-Associated Degradation
@en
type
label
Subcellular Fractionation Anal ...... ring ER-Associated Degradation
@ast
Subcellular Fractionation Anal ...... ring ER-Associated Degradation
@en
prefLabel
Subcellular Fractionation Anal ...... ring ER-Associated Degradation
@ast
Subcellular Fractionation Anal ...... ring ER-Associated Degradation
@en
P2860
P1433
P1476
Subcellular Fractionation Anal ...... ring ER-Associated Degradation
@en
P2093
Kunio Nakatsukasa
Takumi Kamura
P2860
P304
P356
10.1371/JOURNAL.PONE.0148327
P407
P577
2016-02-05T00:00:00Z