Live cell imaging of protein dislocation from the endoplasmic reticulum.
about
Recent technical developments in the study of ER-associated degradationThe C-terminal domain of Nrf1 negatively regulates the full-length CNC-bZIP factor and its shorter isoform LCR-F1/Nrf1β; both are also inhibited by the small dominant-negative Nrf1γ/δ isoforms that down-regulate ARE-battery gene expressionPlant Virus Infection and the Ubiquitin Proteasome Machinery: Arms Race along the Endoplasmic ReticulumCleaning up in the endoplasmic reticulum: ubiquitin in chargeA palette of fluorescent proteins optimized for diverse cellular environmentsNuclear export of misfolded SOD1 mediated by a normally buried NES-like sequence reduces proteotoxicity in the nucleus.Selective inhibition of p97 by chlorinated analogues of dehydrocurvularinDeglycosylation-dependent fluorescent proteins provide unique tools for the study of ER-associated degradation.Approaches to imaging unfolded secretory protein stress in living cells.Transcription factor Nrf1 is topologically repartitioned across membranes to enable target gene transactivation through its acidic glucose-responsive domainsA dynamic study of protein secretion and aggregation in the secretory pathway.The selective post-translational processing of transcription factor Nrf1 yields distinct isoforms that dictate its ability to differentially regulate gene expressiongp78 functions downstream of Hrd1 to promote degradation of misfolded proteins of the endoplasmic reticulumEnterovirus 71 protease 2Apro and 3Cpro differentially inhibit the cellular endoplasmic reticulum-associated degradation (ERAD) pathway via distinct mechanisms, and enterovirus 71 hijacks ERAD component p97 to promote its replication.Losing pieces without disintegrating: Contractile protein loss during muscle atrophy.ER-associated degradation regulates Alzheimer's amyloid pathology and memory function by modulating γ-secretase activity.
P2860
Q26823514-FEB362FE-FA9F-4387-9390-4A74000BAC14Q27341433-D89B759A-C62B-4265-ACFC-3154A8FAFF7BQ28076795-1C555616-AC78-4066-B7EC-6E32BBF2EF8CQ28237362-1AD0B224-0589-4B59-8B3B-A887D272C725Q28647200-58B47001-2398-4DAB-82F1-69908F5D32FFQ33740006-DA6FBA51-5072-4995-9BAE-82136F86B5CDQ33785301-300E232B-011F-4575-A923-78E4032E3295Q34327353-BF7BC4F0-3968-4E86-B063-7045AE19FC84Q34546956-A0EC7D61-0A67-4714-ADB4-7FB9AECE9913Q35138471-E9D42F6F-9D40-406F-9BC7-C737C1459ACEQ35298457-2F47CF7F-1BB9-4286-BC28-43FFD9FA4922Q35947852-9CDD854F-8B80-4359-B8C9-7732B1125E89Q36337039-9DF52CC2-6B3E-4DB0-8E03-8558E23F44B1Q41922848-8C32B340-2917-414B-9B94-64A585C27A73Q42318146-1587ACC4-3F8F-43A8-B530-324D8F12736FQ43405940-E15F77D7-F995-40B0-AB92-AB6E835D7548
P2860
Live cell imaging of protein dislocation from the endoplasmic reticulum.
description
2012 nî lūn-bûn
@nan
2012 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Live cell imaging of protein dislocation from the endoplasmic reticulum.
@ast
Live cell imaging of protein dislocation from the endoplasmic reticulum.
@en
type
label
Live cell imaging of protein dislocation from the endoplasmic reticulum.
@ast
Live cell imaging of protein dislocation from the endoplasmic reticulum.
@en
prefLabel
Live cell imaging of protein dislocation from the endoplasmic reticulum.
@ast
Live cell imaging of protein dislocation from the endoplasmic reticulum.
@en
P2860
P356
P1476
Live cell imaging of protein dislocation from the endoplasmic reticulum.
@en
P2093
Shengyun Fang
Yongwang Zhong
P2860
P304
28057-28066
P356
10.1074/JBC.M112.381798
P407
P577
2012-06-21T00:00:00Z