The organization of engaged and quiescent translocons in the endoplasmic reticulum of mammalian cells.
about
Subunits of the translocon interact with components of the oligosaccharyl transferase complex.Human ribosomal protein L7 displays an ER binding property and is involved in ribosome-ER associationERdj4 protein is a soluble endoplasmic reticulum (ER) DnaJ family protein that interacts with ER-associated degradation machineryHomodimerization of the G protein SRbeta in the nucleotide-free state involves proline cis/trans isomerization in the switch II region.Dissecting the molecular organization of the translocon-associated protein complex.Monitoring chaperone engagement of substrates in the endoplasmic reticulum of live cellsCellular mechanisms of membrane protein folding.Evolutionary gain of function for the ER membrane protein Sec62 from yeast to humansRational design and evaluation of FRET experiments to measure protein proximities in cellsApproaches to imaging unfolded secretory protein stress in living cells.Defining the BK channel domains required for beta1-subunit modulation.Cotranslational stabilization of Sec62/63 within the ER Sec61 translocon is controlled by distinct substrate-driven translocation events.Effect of membrane microheterogeneity and domain size on fluorescence resonance energy transfer.Bacterial protein translocation requires only one copy of the SecY complex in vivo.Yeast viral killer toxins: lethality and self-protection.ERdj3 regulates BiP occupancy in living cells.Sequence-specific retention and regulated integration of a nascent membrane protein by the endoplasmic reticulum Sec61 translocon.Molecular mechanism of action of pharmacoperone rescue of misrouted GPCR mutants: the GnRH receptor.Nuclear pore complex proteins mark the implantation window in human endometrium.A new congenital disorder of glycosylation caused by a mutation in SSR4, the signal sequence receptor 4 protein of the TRAP complexCryo-electron microscopy of ribosomal complexes in cotranslational folding, targeting, and translocation.The safety dance: biophysics of membrane protein folding and misfolding in a cellular contextSubnuclear development of the zebrafish habenular nuclei requires ER translocon function.The use of calnexin and calreticulin by cellular and viral glycoproteins.Recognition of transmembrane helices by the endoplasmic reticulum translocon.A functional link between the co-translational protein translocation pathway and the UPR.The structural and functional coupling of two molecular machines, the ribosome and the transloconA trans-membrane segment inside the ribosome exit tunnel triggers RAMP4 recruitment to the Sec61p translocase.Sequential triage of transmembrane segments by Sec61alpha during biogenesis of a native multispanning membrane protein.An Update on Sec61 Channel Functions, Mechanisms, and Related Diseases.Escherichia coli signal recognition particle receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix.Gene expression profiling of periodontitis-affected gingival tissue by spatial transcriptomics.
P2860
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P2860
The organization of engaged and quiescent translocons in the endoplasmic reticulum of mammalian cells.
description
2004 nî lūn-bûn
@nan
2004 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի մարտին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
The organization of engaged an ...... reticulum of mammalian cells.
@ast
The organization of engaged an ...... reticulum of mammalian cells.
@en
type
label
The organization of engaged an ...... reticulum of mammalian cells.
@ast
The organization of engaged an ...... reticulum of mammalian cells.
@en
prefLabel
The organization of engaged an ...... reticulum of mammalian cells.
@ast
The organization of engaged an ...... reticulum of mammalian cells.
@en
P2860
P50
P356
P1476
The organization of engaged an ...... reticulum of mammalian cells.
@en
P2093
Brigitte A Bogert
Gretchen A Reinhart
P2860
P304
P356
10.1083/JCB.200312079
P407
P577
2004-03-01T00:00:00Z