Glycosylation can influence topogenesis of membrane proteins and reveals dynamic reorientation of nascent polypeptides within the translocon.
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The concept of translocational regulationProcessing of surfactant protein C requires a type II transmembrane topology directed by juxtamembrane positively charged residuesMembrane topography and topogenesis of prenylated Rab acceptor (PRA1)Membrane topology of mouse stearoyl-CoA desaturase 1Yeast genes controlling responses to topogenic signals in a model transmembrane protein.Control of translocation through the Sec61 translocon by nascent polypeptide structure within the ribosome.Cellular mechanisms of membrane protein folding.Lipids and topological rules governing membrane protein assembly.Positive charges of translocating polypeptide chain retrieve an upstream marginal hydrophobic segment from the endoplasmic reticulum lumen to the translocon.Evidence in support of a four transmembrane-pore-transmembrane topology model for the Arabidopsis thaliana Na+/K+ translocating AtHKT1 protein, a member of the superfamily of K+ transportersMembrane protein insertion at the endoplasmic reticulum.Cotranslational partitioning of nascent prion protein into multiple populations at the translocation channel.Topogenesis of membrane proteins: determinants and dynamics.Lipid-dependent membrane protein topogenesis.Transcription factor Nrf1 is topologically repartitioned across membranes to enable target gene transactivation through its acidic glucose-responsive domainsMolecular mechanism of signal sequence orientation in the endoplasmic reticulum.Stepwise insertion and inversion of a type II signal anchor sequence in the ribosome-Sec61 translocon complex.A transmembrane form of the prion protein contains an uncleaved signal peptide and is retained in the endoplasmic Reticulum.Cotranslational membrane protein biogenesis at the endoplasmic reticulum.Versatility of the endoplasmic reticulum protein folding factory.In vivo kinetics of protein targeting to the endoplasmic reticulum determined by site-specific phosphorylationIn vitro reconstitution of lipid-dependent dual topology and postassembly topological switching of a membrane protein.The membrane-topogenic vectorial behaviour of Nrf1 controls its post-translational modification and transactivation activity.Reorientation of the first signal-anchor sequence during potassium channel biogenesis at the Sec61 complex.Adaptation of low-resolution methods for the study of yeast microsomal polytopic membrane proteins: a methodological review.The Sec translocon mediated protein transport in prokaryotes and eukaryotes.The adenovirus E3-6.7K protein adopts diverse membrane topologies following posttranslational translocationTopology of transmembrane segments 1-4 in the human chloride/bicarbonate anion exchanger 1 (AE1) by scanning N-glycosylation mutagenesisDifferential stability of biogenesis intermediates reveals a common pathway for aquaporin-1 topological maturation.Membrane topology of the murine fatty acid transport protein 1.Cooperativity and flexibility of cystic fibrosis transmembrane conductance regulator transmembrane segments participate in membrane localization of a charged residue.UT-B1 proteins in rat: tissue distribution and regulation by antidiuretic hormone in kidney.A basic cluster determines topology of the cytoplasmic M3-M4 loop of the glycine receptor alpha1 subunit.Signal sequences initiate the pathway of maturation in the endoplasmic reticulum lumen.Sequential triage of transmembrane segments by Sec61alpha during biogenesis of a native multispanning membrane protein.Roles of individual N-glycans for ATP potency and expression of the rat P2X1 receptor.Integration of deletion mutants of bovine rhodopsin into the membrane of the endoplasmic reticulum.Identification of sequence determinants that direct different intracellular folding pathways for aquaporin-1 and aquaporin-4.A six-membrane-spanning topology for yeast and Arabidopsis Tsc13p, the enoyl reductases of the microsomal fatty acid elongating system.The Topogenic Contribution of Uncharged Amino Acids on Signal Sequence Orientation in the Endoplasmic Reticulum
P2860
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P2860
Glycosylation can influence topogenesis of membrane proteins and reveals dynamic reorientation of nascent polypeptides within the translocon.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh
1999年學術文章
@zh-hant
name
Glycosylation can influence to ...... eptides within the translocon.
@ast
Glycosylation can influence to ...... eptides within the translocon.
@en
type
label
Glycosylation can influence to ...... eptides within the translocon.
@ast
Glycosylation can influence to ...... eptides within the translocon.
@en
prefLabel
Glycosylation can influence to ...... eptides within the translocon.
@ast
Glycosylation can influence to ...... eptides within the translocon.
@en
P2860
P356
P1476
Glycosylation can influence to ...... eptides within the translocon.
@en
P2093
P2860
P304
P356
10.1083/JCB.147.2.257
P407
P577
1999-10-01T00:00:00Z